HGNC approved symbol Status of entry HGNC ID HGNC approved name Entrez gene ID UniProt AC (human)
UniProt ID (human)
Pfam domains MGI symbol MGI ID UniProt AC (mouse)
UniProt ID (mouse)
HGNC gene family tag HGNC gene family description Function Modification PMID for information on function Protein complex Target molecule Target entity Product UniProt ID of targets PMID for information on target Comment
#
(details)
# # # 84717 Q7Z4V5 HDGR2_HUMAN LEDGF PF11467 472-578, PWWP PF00855 5-87, Pfam-B_32406 PB032406 111-159 Hdgfrp2 1194492 Q3UMU9 HDGR2_MOUSE # # Histone modification read # 217205545 # histone H3K79me3, H4K20me3, H3K36me3 # # 217205545 The crystal structures of the PWWP domains from seven different human proteins and three PWWP domain complex structures with histone peptides, i.e., BRPF1-H3K36me3, HDGF2-H3K79me3 and HDGF2-H4K20me3 shows that the PWWP domain can not only bind DNA but also histones.
A1CF
(details)
# 24086 APOBEC1 complementation factor 29974 Q9NQ94 A1CF_HUMAN DND1_DSRM PF14709 445-523, RRM_1 PF00076 58-127 138-203, RRM_6 PF14259 233-297 A1cf 1917115 Q5YD48 A1CF_MOUSE RBM RNA binding motif (RRM) containing RNA modification RNA deamination 10781591 APOB_mRNA_editosome RNA mRNA, mC U # 10781591 ASP=A1CF has three RNA-binding domains with homologies to poly(A)-binding proteins. Recombinant ASP complements recombinant APOBEC-1 to edit apoB RNA in vitro. Therefore, APOBEC-1 and ASP represent the minimal requirements for apoB mRNA editing in vitro.
ACTB
(details)
# 132 actin, beta 60 P60709 ACTB_HUMAN Actin PF00022 2-375 Actb 87904 P60710 ACTB_MOUSE # # Chromatin remodelling cofactor # 10966108 BAF, nBAF, npBAF, PBAF, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1, NuA4, NuA4-related complex chromatin # # # 10966108 β-actin=ACTB and actin-related proteins appear to have weak ATPase activities, which contribute ∼1% of the total activity in the BAF remodeling complex (Zhao et al. 1998). Results of experiments using the actin monomer sequestering product latrunculin B suggest that β-actin and BAF53 are required for stimulation of the ATPase activity of the BAF complex by chromatin
ACTL6A
(details)
# 24124 actin-like 6A 86 O96019 ACL6A_HUMAN Actin PF00022 8-429 Actl6a 1861453 Q9Z2N8 ACL6A_MOUSE INO80 INO80 complex subunits Chromatin remodelling cofactor # 9845365 BAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, SWI/SNF BRM-BRG1, Ino80, NuA4, NuA4-related complex, SRCAP chromatin # # # 9845365 β-actin and BAF53 =ACTL6A are required for maximal ATPase activity of BRG1 and are also required with BRG1 for association of the complex with chromatin/matrix.
ACTL6B
(details)
# 160 actin-like 6B 51412 O94805 ACL6B_HUMAN Actin PF00022 8-426 Actl6b 1933548 Q99MR0 ACL6B_MOUSE # # Chromatin remodelling cofactor # 11726552 BAF, nBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF BRM-BRG1 chromatin # # # 11726552 Belongs to the chromatin remodeling brain-specific BAF (bBAF) complex, as such plays a role in remodeling mononucleosomes in an ATP-dependent fashion.
ACTR3B
(details)
# 17256 ARP3 actin-related protein 3 homolog B (yeast) 57180 Q9P1U1 ARP3B_HUMAN Actin PF00022 3-412 Actr3b 2661120 Q641P0 ARP3B_MOUSE # # Chromatin remodelling # 10911987 # histone H2A, H3, H4 # # 10911987 Act3/Arp4 can interact through the N-terminal domains of histones H3, H4, and H2A. Since Esa1 can only acetylate nucleosomal histones as part of theNuA4 complex, it has been proposed that the Act3/Arp4 subunit functions by promoting the binding of NuA4 to chromatin.
ACTR5
(details)
# 14671 ARP5 actin-related protein 5 homolog (yeast) 79913 Q9H9F9 ARP5_HUMAN Actin PF00022 30-570 Actr5 1924748 Q80US4 ARP5_MOUSE INO80 INO80 complex subunits Chromatin remodelling # 19014934 Ino80 chromatin # # # 19014934 hArp5 binds to chromatin as a component of the hINO80 complex in a DSB-independent manner.
ACTR6
(details)
# 24025 ARP6 actin-related protein 6 homolog (yeast) 64431 Q9GZN1 ARP6_HUMAN Actin PF00022 1-395 Actr6 1914269 Q9D864 ARP6_MOUSE # # Chromatin remodelling cofactor # 11368909 SRCAP chromatin # # # 11368909 The Arp6 subfamily might regulate heterochromatin formation induced by the HP1 family.
ACTR8
(details)
# 14672 ARP8 actin-related protein 8 homolog (yeast) 93973 Q9H981 ARP8_HUMAN Actin PF00022 43-621 Actr8 1860775 Q8R2S9 ARP8_MOUSE INO80 INO80 complex subunits Histone modification read # 22977180 Ino80 histone # # # 22977180 Arp8 and the Arp8-Arp4-actin-HSA sub-complex of INO80 strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting that Arp8 functions as a nucleosome recognition module.
ADNP
(details)
New 15766 activity-dependent neuroprotector homeobox 23394 Q9H2P0 ADNP_HUMAN Homeobox PF00046 765-813, Pfam-B_10803 PB010803 691-762, Pfam-B_21724 PB021724 921-1100, Pfam-B_29916 PB029916 615-646 Adnp 1338758 Q9Z103 ADNP_MOUSE ZFHX Homeoboxes / ZF class Chromatin remodelling cofactor # 17878164 # chromatin # # # # Identified as a member of SWI/SNF chromatin remodeling complex. UniProt: Potential transcription factor.
AEBP2
(details)
# 24051 AE binding protein 2 121536 Q6ZN18 AEBP2_HUMAN Pfam-B_22101 PB022101 1-79, Pfam-B_8048 PB008048 401-515, zf-H2C2_2 PF13465 315-341 Aebp2 1338038 Q9Z248 AEBP2_MOUSE # # Histone modification write cofactor Histone methylation 15225548 PRC2 DNA # # # 15225548 The HMTase activity requires a minimum of three components-EZH2, EED, and SUZ12-while AEBP2 is required for optimal enzymatic activity. Using a stable SUZ12 knockdown cell line, SUZ12 knockdown results in cell growth defects, which correlate with genome-wide alteration on H3-K27 methylation as well as upregulation of a number of Hox genes.
AICDA
(details)
# 13203 activation-induced cytidine deaminase 57379 Q9GZX7 AICDA_HUMAN APOBEC_N PF08210 11-181 Aicda 1342279 Q9WVE0 AICDA_MOUSE APOBEC Apolipoprotein B mRNA editing enzymes DNA modification DNA demethylation 21496894 APOB_mRNA_editosome DNA ssDNA, hmC hmU # 21496894 AICDA or AID is required for OCT4 and NANOG promoter demethylation, 5mCs are first oxidized to 5hmCs by TET proteins. 5hmCs are then deaminated by AID/APOBEC deaminases into 5hmU. Finally, 5hmU can be excised by 5hmU glycosylases and repaired by the BER pathway with unmethylated cytosines
AIRE
(details)
# 360 autoimmune regulator 326 O43918 AIRE_HUMAN PHD PF00628 298-343, Pfam-B_9104 PB009104 481-543, SAND PF01342 189-249, Sp100 PF03172 1-106 Aire 1338803 Q9Z0E3 AIRE_MOUSE PHF Zinc fingers, PHD-type Histone modification read, TF #, # 18292755 # histone, DNA H3K4, H3K4me3, DNA motif # # 18292755 AIRE selectively interacts with histone H3 through its first plant homeodomain (PHD) finger (AIRE–PHD1) and preferentially binds to non-methylated H3K4 (H3K4me0). Accordingly, in vivo AIRE binds to and activates promoters containing low levels of H3K4me3 in human embryonic kidney 293 cells. AIRE–PHD1 is an important member of a newly identified class of PHD fingers that specifically recognize H3K4me0, thus providing a new link between the status of histone modifications.
ALKBH1
(details)
New 17911 alkB, alkylation repair homolog 1 (E. coli) 8846 Q13686 ALKB1_HUMAN 2OG-FeII_Oxy_2 PF13532 98-344 Alkbh1 2384034 P0CB42 ALKB1_MOUSE ALKB Alkylation repair homologs Histone modification # 22961808 # histone H2A # # # ALKBH1 is a histone H2A dioxygenase involved in neural differentiation.
ANKRD32
(details)
# 25408 ankyrin repeat domain 32 84250 Q9BQI6 ANR32_HUMAN Ank_2 PF12796 783-871 845-931, Pfam-B_101142 PB101142 932-1056, Pfam-B_12624 PB012624 231-430, Pfam-B_18156 PB018156 1-229, Pfam-B_81366 PB081366 641-782 Ankrd32 2145448 Q8R3P9 ANR32_MOUSE ANKRD Ankyrin repeat domain containing Histone modification read # 21423274 # histone H2AXS139 # # 21423274 Table 1 in the reference (ANKRD32=BRCT repeat)
ANP32A
(details)
# 13233 acidic (leucine-rich) nuclear phosphoprotein 32 family, member A 8125 P39687 AN32A_HUMAN LRR_9 PF14580 17-166 Anp32a 108447 O35381 AN32A_MOUSE ANP32 ANP32 acidic nuclear phosphoproteins Chromatin remodelling cofactor # 11163245 # chromatin # # # 11163245 pp32 = ANP32A is a member of a family of leucine-rich acidic nuclear proteins ( 7 and 19). Results suggest potential roles of INHAT subunits in chromatin remodeling and transcriptional regulation; INHAT complex including pp32 inhibits the HAT activity of p300/CBP and PCAF by binding to their substrate, histones.
ANP32B
(details)
# 16677 acidic (leucine-rich) nuclear phosphoprotein 32 family, member B 10541 Q92688 AN32B_HUMAN LRR_4 PF12799 88-136, Pfam-B_30686 PB030686 171-249 Anp32b 1914878 Q9EST5 AN32B_MOUSE ANP32 ANP32 acidic nuclear phosphoproteins Histone chaperone # 20538007 # histone H3, H4 # # 20538007 The LRR domain of ANP32B possesses histone chaperone activity and forms a curved structure with a parallel beta-sheet on the concave side and mostly helical elements on the convex side. Analyses revealed that the interaction of ANP32B with the core histones H3-H4 occurs on its concave side
ANP32E
(details)
# 16673 acidic (leucine-rich) nuclear phosphoprotein 32 family, member E 81611 Q9BTT0 AN32E_HUMAN LRR_4 PF12799 88-133, LRR_8 PF13855 65-125, Pfam-B_38005 PB038005 215-262, Pfam-B_94319 PB094319 171-200 Anp32e 1913721 P97822 AN32E_MOUSE ANP32 ANP32 acidic nuclear phosphoproteins Histone chaperone, Histone modification read #, # 24463511 SWR histone H2A.Z # # 24463511 ANP32E interacts with a short region of the docking domain of H2A.Z through a new motif termed H2A.Z interacting domain (ZID).
APBB1
(details)
New 581 amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65) 322 O00213 APBB1_HUMAN PID PF00640 370-509 543-664, Pfam-B_23321 PB023321 1-215, WW PF00397 255-283 Apbb1 107765 Q9QXJ1 APBB1_MOUSE # # Histone modification # 21403922 # histone H2AX # # # Chromatin acetylation, β-amyloid precursor protein and its binding partner FE65 in DNA double strand break repair. UniProt: May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs).
APEX1
(details)
New 587 APEX nuclease (multifunctional DNA repair enzyme) 1 328 P27695 APEX1_HUMAN Exo_endo_phos PF03372 65-309, Pfam-B_21616 PB021616 1-39 Apex1 88042 P28352 APEX1_MOUSE # # DNA modification cofactor DNA demethylation # # DNA # # # # UniProt: May play a role in the epigenetic regulation of gene expression by participating in DNA demethylation.
APOBEC1
(details)
# 604 apolipoprotein B mRNA editing enzyme, catalytic polypeptide 1 339 P41238 ABEC1_HUMAN APOBEC_N PF08210 17-186 Apobec1 103298 P51908 ABEC1_MOUSE APOBEC Apolipoprotein B mRNA editing enzymes DNA modification, RNA modification DNA demethylation, mRNA editing 22001110 APOB_mRNA_editosome DNA, RNA ssDNA, mRNA, mC U # 22001110 Fig. A2 in the reference (APOBEC1 or A1 has no known mammalian DNA substrate but it has DNA deaminase activity sufficient to induce reversion mutations when overexpressed in E. coli. In addition, A1 expressed in neurons may have a protective function against HSV (Herpers simplex virus) that involves ssDNA deamination of the viral genome).
APOBEC2
(details)
# 605 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2 10930 Q9Y235 ABEC2_HUMAN APOBEC_C PF05240 159-216, Pfam-B_38491 PB038491 1-39 Apobec2 1343178 Q9WV35 ABEC2_MOUSE APOBEC Apolipoprotein B mRNA editing enzymes DNA modification, RNA modification DNA demethylation, mRNA editing 21496894, 22001110 # DNA, RNA ssDNA, mRNA, mC hmU # 22001110, 21496894 Fig. A2 in the reference
APOBEC3A
(details)
# 17343 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A 200315 P31941 ABC3A_HUMAN APOBEC_C PF05240 133-187 # # # # APOBEC Apolipoprotein B mRNA editing enzymes DNA modification, RNA modification DNA demethylation, mRNA editing 22001110 # DNA, RNA ssDNA, mRNA, mC dhU # 22001110 Fig. A2 in the reference (Targets are exogenous retroviruses ssDNA like HIV, DNA viruses or transposable elements/ endogenous retroelements e.g. LINEs, SINEs and LTR).
APOBEC3B
(details)
# 17352 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3B 9582 Q9UH17 ABC3B_HUMAN APOBEC_C PF05240 316-370, APOBEC_N PF08210 11-190 Apobec3 1933111 Q99J72 ABEC3_MOUSE APOBEC Apolipoprotein B mRNA editing enzymes DNA modification, RNA modification DNA demethylation, mRNA editing 22001110 # DNA, RNA ssDNA, mRNA, mC dhU # 22001110 Fig. A2 in the reference (Targets are DNA viruses or transposable elements/ endogenous retroelements e.g. LINEs, SINEs and LTR).
APOBEC3C
(details)
# 17353 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C 27350 Q9NRW3 ABC3C_HUMAN APOBEC_C PF05240 128-182 # # # # APOBEC Apolipoprotein B mRNA editing enzymes DNA modification, RNA modification DNA demethylation, mRNA editing 22001110 # DNA, RNA ssDNA, mRNA, mC dhU # 22001110 Fig. A2 in the reference (Targets are transposable elements/ endogenous retroelements e.g. LINEs, SINEs and LTR).
APOBEC3D
(details)
# 17354 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3D 140564 Q96AK3 ABC3D_HUMAN APOBEC_C PF05240 140-194 324-378 # # # # APOBEC Apolipoprotein B mRNA editing enzymes DNA modification, RNA modification DNA demethylation, mRNA editing 21835787 # DNA, RNA ssDNA, mRNA, mC dhU # 22001110 Fig. A2 in the reference (Targets are exogenous retroviruses ssDNA like HIV or transposable elements/ endogenous retroelements e.g. LINEs and SINEs).
APOBEC3F
(details)
# 17356 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3F 200316 Q8IUX4 ABC3F_HUMAN APOBEC_N PF08210 3-189 199-373 # # # # APOBEC Apolipoprotein B mRNA editing enzymes DNA modification, RNA modification DNA demethylation, mRNA editing 22001110 APOB_mRNA_editosome DNA, RNA ssDNA, mRNA, mC dhU # 22001110 Fig. A2 in the reference (Targets are exogenous retroviruses ssDNA like HIV, DNA viruses or transposable elements/ endogenous retroelements e.g. LINEs, SINEs and LTR).
APOBEC3G
(details)
# 17357 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G 60489 Q9HC16 ABC3G_HUMAN APOBEC_N PF08210 3-182 202-380 # # # # APOBEC Apolipoprotein B mRNA editing enzymes DNA modification, RNA modification DNA demethylation, mRNA editing 22001110 APOB_mRNA_editosome DNA, RNA ssDNA, mRNA, mC dhU # 22001110 Fig. A2 in the reference (Targets are exogenous retroviruses ssDNA like HIV, DNA viruses or transposable elements/ endogenous retroelements e.g. SINEs and LTR).
APOBEC3H
(details)
# 24100 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3H 164668 Q6NTF7 ABC3H_HUMAN APOBEC_C PF05240 116-174, dCMP_cyt_deam_1 PF00383 24-99 # # # # APOBEC Apolipoprotein B mRNA editing enzymes DNA modification, RNA modification DNA demethylation, mRNA editing 22001110 APOB_mRNA_editosome DNA, RNA ssDNA, mRNA, mC dhU # 22001110 Fig. A2 in the reference (Targets are exogenous retroviruses ssDNA like HIV or transposable elements/ endogenous retroelements e.g. LINEs, SINEs and LTR).
ARID1A
(details)
# 11110 AT rich interactive domain 1A (SWI-like) 8289 O14497 ARI1A_HUMAN ARID PF01388 1015-1104, DUF3518 PF12031 1975-2231, Pfam-B_16906 PB016906 451-499, Pfam-B_1854 PB001854 281-379 Arid1a 1935147 A2BH40 ARI1A_MOUSE ARID # Chromatin remodelling cofactor # 18448678 BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, WINAC, bBAF, SWI/SNF BRM-BRG1 DNA DNA motif # # 18448678 BAF250a=ARID1A mediated chromatin remodeling plays a critical role in maintaining a particular chromatin configuration of its target genes that is essential for ES pluripotency and mesoderm formation.
ARID1B
(details)
# 18040 AT rich interactive domain 1B (SWI1-like) 57492 Q8NFD5 ARI1B_HUMAN ARID PF01388 1050-1140, DUF3518 PF12031 1926-2182, Pfam-B_60945 PB060945 291-369, Pfam-B_7257 PB007257 371-449 Arid1b 1926129 # # ARID # Histone modification write Histone ubiquitination 20086098 BAF, nBAF, npBAF, PBAF, SWI/SNF-like_EPAFa, SWI/SNF-like EPAFB, SWI/SNF BRM-BRG1 histone, DNA H2BK120, DNA motif # # 20086098 The characteristic member of human SWI/SNF-A is BAF250/ARID1, of which there are two isoforms, BAF250a/ARID1a and BAF250b/ARID1b. The immunopurified BAF250b E3 ubiquitin ligase was found to target histone H2B at lysine 120 for monoubiquitination in vitro.
ARID2
(details)
# 18037 AT rich interactive domain 2 (ARID, RFX-like) 196528 Q68CP9 ARID2_HUMAN ARID PF01388 10-101, Pfam-B_11884 PB011884 1660-1747, Pfam-B_14804 PB014804 1051-1098, Pfam-B_649 PB000649 1529-1658, Pfam-B_6603 PB006603 1239-1268, RFX_DNA_binding PF02257 517-604 Arid2 1924294 # # ARID # Chromatin remodelling cofactor # 15640446 PBAF DNA DNA motif # # 15640446 Extends the role of ARID-containing subunits as components of SWI/SNF-related chromatin-remodeling complexes. Analysis of ARID2 in the DNA pull-down assay (Figure 4) indicates that it binds DNA without sequence specificity, like all other known ARID-containing components of SWI/SNF-related complexes.
ARID4A
(details)
# 9885 AT rich interactive domain 4A (RBP1-like) 5926 P29374 ARI4A_HUMAN ARID PF01388 306-397, Pfam-B_1988 PB001988 1071-1111 1166-1240, RBB1NT PF08169 168-263, Tudor-knot PF11717 573-630 Arid4a 2444354 # # ARID # Histone modification write cofactor Histone acetylation 15640446 mSin3A DNA DNA motif # # 15640446 ARID4 subfamily DNA-binding activity is represented here by RBP1 (ARID4A). Amino acid identity within the ARID consensus is 75% between RBP1 (ARID4A) and RBP1L1 (ARID4B), the only other member of this class. Both RBP1 and RBP1L1/SAP180 have been found in association with the mSIN3-histone deacetylase complex.
ARID4B
(details)
# 15550 AT rich interactive domain 4B (RBP1-like) 51742 Q4LE39 ARI4B_HUMAN ARID PF01388 304-394, Pfam-B_15110 PB015110 771-828, RBB1NT PF08169 166-264, Tudor-knot PF11717 569-626 Arid4b 2137512 A2CG63 ARI4B_MOUSE ARID # Histone modification write cofactor Histone acetylation 15640446 mSin3A DNA DNA motif # # 15640446 ARID4 subfamily DNA-binding activity is represented here by RBP1 (ARID4A). Amino acid identity within the ARID consensus is 75% between RBP1 (ARID4A) and RBP1L1 (ARID4B), the only other member of this class. Both RBP1 and RBP1L1/SAP180 have been found in association with the mSIN3-histone deacetylase complex.
ARNTL
(details)
# 701 aryl hydrocarbon receptor nuclear translocator-like 406 O00327 BMAL1_HUMAN HLH PF00010 73-126, PAS PF00989 146-253, PAS_11 PF14598 337-444, Pfam-B_2781 PB002781 455-619 Arntl 1096381 Q9WTL8 BMAL1_MOUSE bHLH Basic helix-loop-helix proteins Histone modification write cofactor, TF #, TF activator 14645221, 24395244 # histone # # # 14645221, 24395244 The coincidence of a rhythm in histone H3 and histone H4 acetylation on the proximal E-box of hPer1 with transcriptional activation of per1 and per2 is consistent with the heterodimeric complexes of CLOCK, NPAS2 and BMAL1 = ARNTL recruiting a histone acetyltransferase (HAT)-containing transcriptional co-activation complex to achieve maximal target gene activation; CLOCK:BMAL1 functions like pioneer transcription factors and regulates the DNA accessibility of other transcription factors.
ARRB1
(details)
New 711 arrestin, beta 1 408 P49407 ARRB1_HUMAN Arrestin_C PF02752 193-356, Arrestin_N PF00339 18-174 Arrb1 99473 Q8BWG8 ARRB1_MOUSE # # Histone modification # 17618287, 16325578 # histone # # # # Recruits acetylase p300. Regulates histone acetylation and gene transcription. UniProt: Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes.
ASF1A
(details)
# 20995 anti-silencing function 1A histone chaperone 25842 Q9Y294 ASF1A_HUMAN ASF1_hist_chap PF04729 1-154 Asf1a 1913653 Q9CQE6 ASF1A_MOUSE # # Histone chaperone # 10759893 # histone H3, H4 # # 10759893 CIA=ASF1A binds to histones H3/H4 in vitro, and the interacting region of histone H3 is located in the C-terminal helices. Human CIA, whose yeast homologue ASF1 is an anti-silencing factor, possesses histone chaperone activity
ASF1B
(details)
# 20996 anti-silencing function 1B histone chaperone 55723 Q9NVP2 ASF1B_HUMAN ASF1_hist_chap PF04729 1-154 Asf1b 1914179 Q9DAP7 ASF1B_MOUSE # # Histone chaperone # 12842904 # histone H3, H4 # # 12842904 hCIA-II=ASF1B interacts with histone H3 in vivo and with histones H3/H4 in vitro and that it facilitates supercoiling of circular DNA when it is incubated with core histones and topoisomerase I in vitro. These data suggest that CIA-II is a histone chaperone and is implicated in the regulation of mammalian spermatogenesis.
ASH1L
(details)
# 19088 ash1 (absent, small, or homeotic)-like (Drosophila) 55870 Q9NR48 ASH1L_HUMAN BAH PF01426 2661-2798, Bromodomain PF00439 2453-2538, PHD PF00628 2587-2631, Pfam-B_14208 PB014208 1818-1847, Pfam-B_18246 PB018246 2310-2419, Pfam-B_25586 PB025586 1473-1507, Pfam-B_4663 PB004663 1023-1054 1180-1377, Pfam-B_6310 PB006310 1509-1554, SET PF00856 2156-2261 Ash1l 2183158 Q99MY8 ASH1L_MOUSE KMT, PHF Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type Histone modification write Histone methylation 21239497 # histone H3K36 H3K36me # 21239497 Human ASH1L specifically methylates histone H3 Lys-36. Implicates that there may be a regulatory mechanism of ASH1L histone methyltransferases.
ASH2L
(details)
# 744 ash2 (absent, small, or homeotic)-like (Drosophila) 9070 Q9UBL3 ASH2L_HUMAN Pfam-B_11232 PB011232 499-622, Pfam-B_12412 PB012412 361-417, SPRY PF00622 418-497 Ash2l 1344416 Q91X20 ASH2L_MOUSE PHF Zinc fingers, PHD-type Histone modification write cofactor Histone methylation 21285357 COMPASS, Menin-associated_HMT, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7, COMPASS-like MLL3,4 histone # # # 21285357 The oncoprotein Ash2L is a component of the mixed lineage leukemia (MLL) family members 1–4, Setd1A, and Setd1B mammalian histone H3K4 methyltransferase complexes and is essential to maintain global trimethylation of histone H3K4.
ASXL1
(details)
# 18318 additional sex combs like transcriptional regulator 1 171023 Q8IXJ9 ASXL1_HUMAN ASXH PF13919 231-362, HARE-HTH PF05066 11-83, PHD_3 PF13922 1475-1539, Pfam-B_4087 PB004087 970-1084 Asxl1 2684063 P59598 ASXL1_MOUSE # # Histone modification erase, Polycomb group (PcG) protein Histone deubiquitination, # 20436459 PR-DUB histone H2AK119 H2AK119ub1 # 20436459 Reconstituted recombinant Drosophila and human PR-DUB=ASXL1 complexes remove monoubiquitin from H2A but not from H2B in nucleosomes.
ASXL2
(details)
# 23805 additional sex combs like transcriptional regulator 2 55252 Q76L83 ASXL2_HUMAN ASXH PF13919 249-381, HARE-HTH PF05066 11-83, PHD_3 PF13922 1370-1433, Pfam-B_4087 PB004087 944-1090 Asxl2 1922552 Q8BZ32 ASXL2_MOUSE # # Histone modification read # 21047783 # histone H3K4, H3K9 # # 21047783 ASXL2 occupies the aP2 promoter together with histone-lysine N-methyltransferase MLL1 and Lys-9-acetylated and Lys-4-methylated H3 histones. Microarray analysis demonstrated that ASXL1 represses, whereas ASXL2 increases, the expression of adipogenic genes.
ASXL3
(details)
# 29357 additional sex combs like transcriptional regulator 3 80816 Q9C0F0 ASXL3_HUMAN ASXH PF13919 229-361, HARE-HTH PF05066 10-81, PHD_3 PF13922 2183-2246, Pfam-B_17129 PB017129 941-1279, Pfam-B_20113 PB020113 751-939, Pfam-B_27498 PB027498 1341-1411, Pfam-B_34336 PB034336 1281-1339, Pfam-B_6874 PB006874 601-669 Asxl3 2685175 Q8C4A5 ASXL3_MOUSE # # Scaffold protein, Polycomb group (PcG) protein #, # 23736028 # histone # # # 23736028 ASXL family members are epigenetic scaffolding proteins that assemble epigenetic regulators and transcription factors to specific genomic loci with histone modifications, contain PHD domain.
ATAD2
(details)
# 30123 ATPase family, AAA domain containing 2 29028 Q6PL18 ATAD2_HUMAN AAA PF00004 463-598, Bromodomain PF00439 993-1075, Pfam-B_11064 PB011064 870-958, Pfam-B_23116 PB023116 1-56, Pfam-B_40477 PB040477 57-79 Atad2 1917722 Q8CDM1 ATAD2_MOUSE AATP ATPases / AAA-type Chromatin remodelling # 17998543 # chromatin # # # 17998543 Although ANCCA=ATAD2 may not be critical for ERα recruitment to its target genes, it plays an important role in the recruitment or assembly of ERα–CBP complex at the chromatin and hence the histone modifications mediated by the complex.
ATAD2B
(details)
# 29230 ATPase family, AAA domain containing 2B 54454 Q9ULI0 ATD2B_HUMAN AAA PF00004 437-572, Bromodomain PF00439 967-1050, Pfam-B_11064 PB011064 896-932, Pfam-B_130965 PB130965 330-388 Atad2b 2444798 # # AATP ATPases / AAA-type Histone modification read # 15308210 # histone H1.4, H2A, H2B, H3 and H4 # # 15308210 Binds acetylated lysine residues in histone H1.4, H2A, H2B, H3 and H4 (in vitro).
ATF2
(details)
# 784 activating transcription factor 2 1386 P15336 ATF2_HUMAN bZIP_1 PF00170 349-413 Atf2 109349 P16951 ATF2_MOUSE bZIP Basic leucine zipper proteins Histone modification write, TF Histone acetylation, TF activator 10821277 # histone, DNA H2B, H4, DNA motif # # 10821277 ATF-2 is a histone acetyltransferase (HAT), which specifically acetylates histones H2B and H4 in vitro, exhibits histone acetyltransferase (HAT) activity.
ATF7IP
(details)
# 20092 activating transcription factor 7 interacting protein 55729 Q6VMQ6 MCAF1_HUMAN Pfam-B_2570 PB002570 450-518 Atf7ip 1858965 Q7TT18 MCAF1_MOUSE # # Histone modification write cofactor Histone methylation 14536086 # histone # # # 14536086 Promoter H3-K9 trimethylation is the cause of transcriptional repression and that mAM/hAM facilitates conversion of H3-K9 dimethyl to trimethyl by ESET/SETDB1.
ATM
(details)
# 795 ATM serine/threonine kinase 472 Q13315 ATM_HUMAN FAT PF02259 2096-2489, FATC PF02260 3024-3056, PI3_PI4_kinase PF00454 2711-2962, Pfam-B_10220 PB010220 1575-1713, Pfam-B_13450 PB013450 602-830, Pfam-B_16049 PB016049 1715-1818, Pfam-B_17604 PB017604 1819-1953, Pfam-B_3386 PB003386 861-1458, TAN PF11640 5-166 Atm 107202 Q62388 ATM_MOUSE # # Histone modification write Histone phosphorylation 19261749 # histone H2AXS139 # # 19261749 Damage-induced ATM/ATR phosphorylation on S139 of histone H2AX directly recruits MDC1 through MDC1’s BRCT domains. MDC1 itself is a substrate of ATM/ATR.
ATN1
(details)
# 3033 atrophin 1 1822 P54259 ATN1_HUMAN Atrophin-1 PF03154 1-163 349-1190 Atn1 104725 O35126 ATN1_MOUSE # # Histone modification erase cofactor # 10973986 # histone # # # 10973986 When cotransfected into Neuro-2a cells, atrophin-1 and ETO/MTG8 colocalize.
ATR
(details)
# 882 ATR serine/threonine kinase 545 Q13535 ATR_HUMAN FAT PF02259 1771-2092, FATC PF02260 2612-2644, PI3_PI4_kinase PF00454 2321-2567, Pfam-B_15857 PB015857 1226-1489, Pfam-B_17853 PB017853 1-129, Pfam-B_20071 PB020071 291-659, Pfam-B_21066 PB021066 131-289, Pfam-B_21726 PB021726 661-1009, Pfam-B_22672 PB022672 1011-1079, UME PF08064 1119-1225 Atr 108028 Q9JKK8 ATR_MOUSE # # Histone modification write Histone phosphorylation 11673449 # histone H2AX # # 11673449 While H2AX phosphorylation requires ATR, this phosphorylation event is independent of Hus1. Thus, the phosphorylated H2AX may function upstream of Hus1 in the transduction of DNA damage.
ATRX
(details)
# 886 alpha thalassemia/mental retardation syndrome X-linked 546 P46100 ATRX_HUMAN Helicase_C PF00271 2076-2155, Pfam-B_12326 PB012326 1906-2016, Pfam-B_14952 PB014952 1242-1362, Pfam-B_16104 PB016104 2368-2490, Pfam-B_16400 PB016400 1424-1474, Pfam-B_17163 PB017163 1364-1422, Pfam-B_19720 PB019720 751-889, Pfam-B_24253 PB024253 1181-1239, Pfam-B_3534 PB003534 45-304, SNF2_N PF00176 1563-1889 Atrx 103067 Q61687 ATRX_MOUSE # # Chromatin remodelling # 9499421 # histone H3K9me2, H3K9me3, H3K4 # # 9499421, 21666677 The characteristics of the helicase domains make the XNP protein a new member of the SNF2/SWI DNA helicase family. XNP could regulate gene expression by direct interaction with heterochromatin-associated proteins.A yeast two-hybrid analysis using XNP and several human heterochromatin-associated proteins showed a specific interaction between the XNP and the EZH2 proteins.
ATXN7
(details)
# 10560 ataxin 7 6314 O15265 ATX7_HUMAN Pfam-B_15485 PB015485 781-879, Pfam-B_23658 PB023658 129-174, Pfam-B_6735 PB006735 491-579, SCA7 PF08313 318-397 Atxn7 2179277 Q8R4I1 ATX7_MOUSE ATXN Ataxins Histone modification write cofactor Histone acetylation 16494529 SAGA histone # # # 16494529 Ataxin-7 (ATXN7) is a subunit of the GCN5 histone acetyltransferase–containing coactivator complexes TFTC/STAGA. TFTC/STAGA complexes purified from SCA7 mice have normal TRRAP, GCN5, TAF12, and SPT3 levels and that their histone or nucleosomal acetylation activities are unaffected.
ATXN7L3
(details)
# 25416 ataxin 7-like 3 56970 Q14CW9 AT7L3_HUMAN Pfam-B_25595 PB025595 276-345, SCA7 PF08313 201-239, Sgf11 PF08209 80-112 Atxn7l3 3036270 A2AWT3 AT7L3_MOUSE # # Histone modification erase cofactor Histone deubiquitination 18206972 SAGA histone # # # 18206972 ATXN7L3, USP22, and ENY2 are the human orthologs of yeast Sgf11, Ubp8, and Sus1, respectively, and they are integral components of TFTC/STAGA complex. These three proteins together form a module of the TFTC/STAGA complex, which specifically removes the ubiquitin moiety from monoubiquitinated histones H2A and H2B.
AURKA
(details)
# 11393 aurora kinase A 6790 O14965 AURKA_HUMAN Pfam-B_20489 PB020489 1-59, Pkinase PF00069 133-383 Aurka 894678 P97477 AURKA_MOUSE PPP1R Serine/threonine phosphatases / Protein phosphatase 1, regulatory subunits Histone modification write Histone phosphorylation 12576638 # histone H3 H3S10ph # 12576638 Xenopus Aurora-A = AURKA, pEg2, phosphorylate specifically H3 at Serine10 in vitro.
AURKB
(details)
# 11390 aurora kinase B 9212 Q96GD4 AURKB_HUMAN Pfam-B_34716 PB034716 1-46, Pkinase PF00069 77-327 Aurkb 107168 O70126 AURKB_MOUSE PPP1R Serine/threonine phosphatases / Protein phosphatase 1, regulatory subunits Histone modification write Histone phosphorylation 11856369 # histone H3S10, H3S28 # # 11856369 Aurora-B=AURKB directly phosphorylated H3, not only at Ser10 but also at Ser28.
AURKC
(details)
# 11391 aurora kinase C 6795 Q9UQB9 AURKC_HUMAN Pkinase PF00069 43-293 Aurkc 1321119 O88445 AURKC_MOUSE # # Histone modification write Histone phosphorylation 15499654 # histone H3S10, H3S28 # # 15499654 Aurora-C=AURKC, like Aurora-B kinase, is a chromosomal passenger protein localizing first to centromeres and then to the midzone of mitotic cells. Aurora-C transcript is expressed at a moderate level albeit about an order of magnitude lower than Aurora-B transcript in diploid human fibroblasts.
BABAM1
(details)
# 25008 BRISC and BRCA1 A complex member 1 29086 Q9NWV8 BABA1_HUMAN Pfam-B_4074 PB004074 1-327 Babam1 1915501 Q3UI43 BABA1_MOUSE # # Histone modification erase cofactor Histone deubiquitination 19261746 BRISC, BRCA1-A histone # # # 19261746 MERIT40 (Mediator of Rap80 Interactions and Targeting 40 kD)/(C19orf62) is a Rap80-associated protein. MERIT40 is required for Rap80-associated lysine63–ubiquitin DUB activity, a critical component of BRCA1–Rap80 G2 checkpoint and viability responses to ionizing radiation. Thus, MERIT40 represents a novel factor that links BRCA1–Rap80 complex integrity, DSB recognition, and ubiquitin chain hydrolytic activities to the DNA damage response.
BAHD1
(details)
# 29153 bromo adjacent homology domain containing 1 22893 Q8TBE0 BAHD1_HUMAN BAH PF01426 623-779 Bahd1 2139371 Q497V6 BAHD1_MOUSE # # Chromatin remodelling # 19666599 # histone H3K27me3 # # 19666599 Two-hybrid screen suggest that BAHD1 could link chromatin condensation activities to DNA-binding transcription factors. The BAH domain does not bind H3K27me3 in vitro but is required for BAHD1 colocalization with H3K27me3 in vivo.
BANP
(details)
# 13450 BTG3 associated nuclear protein 54971 Q8N9N5 BANP_HUMAN BEN PF10523 249-322 Banp 1889023 Q8VBU8 BANP_MOUSE BEND BEN domain containing Histone modification write Histone acetylation 16166625 # histone H3K9, H4K8 # # 16166625 SMAR1 (=BANP) directs the histone modifications at a distance. Overexpression of SMAR1 deacetylates the histones in the probe II and III region and depletion of SMAR1 increases acetylation in this region. Possibly SMAR1 controls the histone acetylation status at a distance.
BAP1
(details)
# 950 BRCA1 associated protein-1 (ubiquitin carboxy-terminal hydrolase) 8314 Q92560 BAP1_HUMAN Peptidase_C12 PF01088 4-217, Pfam-B_14567 PB014567 441-579, Pfam-B_16218 PB016218 271-439, Pfam-B_4660 PB004660 581-693 Bap1 1206586 Q99PU7 BAP1_MOUSE # # Histone modification erase, Polycomb group (PcG) protein Histone deubiquitination, # 20436459 PR-DUB histone H2AK119ub1 H2AK119 # 19815555, 19188440, 20436459 The Polycomb group proteins BAP1 and ASX form a conserved complex in vivo and in vitro.
BARD1
(details)
# 952 BRCA1 associated RING domain 1 580 Q99728 BARD1_HUMAN Ank PF00023 427-459 460-491 493-525, BRCT PF00533 568-640, Pfam-B_30184 PB030184 161-239, Pfam-B_32178 PB032178 241-290, Pfam-B_32432 PB032432 291-339, Pfam-B_33025 PB033025 723-775, zf-RING_6 PF14835 41-105 Bard1 1328361 O70445 BARD1_MOUSE ANKRD Ankyrin repeat domain containing Histone modification write Histone ubiquitination 19916563 BRCC, BRCA1-A histone H2AX, H2A, H2B, H3, H4 H2AXub, H2Aub, H2Bub, H3ub, H4ub # 19916563, 12485996 BARD1, like CstF-50, also interacts with RNA polymerase II. BARD1-mediated inhibition of polyadenylation may prevent inappropriate RNA processing during transcription,
BAZ1A
(details)
# 960 bromodomain adjacent to zinc finger domain, 1A 11177 Q9NRL2 BAZ1A_HUMAN Bromodomain PF00439 1438-1521, DDT PF02791 422-487, PHD PF00628 1150-1198, Pfam-B_18021 PB018021 670-767, Pfam-B_18567 PB018567 769-877, Pfam-B_19398 PB019398 1210-1430, WAC_Acf1_DNA_bd PF10537 22-122, WHIM1 PF15612 592-640 Baz1a 1309478 O88379 BAZ1A_MOUSE PHF Zinc fingers, PHD-type Histone chaperone # 14759371 ACF, CHRAC histone # # # 14759371 ACF1-ISWI complex (ATP-dependent chromatin assembly and remodeling factor [ACF]) associates with histone-fold proteins (CHRAC-15 and CHRAC-17 in the human chromatin accessibility complex [CHRAC]). These histone-fold proteins facilitate ATP-dependent nucleosome sliding by ACF. Direct interaction of the CHRAC-15/17 complex with the ACF1 subunit is essential for this process.
BAZ1B
(details)
# 961 bromodomain adjacent to zinc finger domain, 1B 9031 Q9UIG0 BAZ1B_HUMAN Bromodomain PF00439 1348-1431, PHD PF00628 1186-1234, WAC_Acf1_DNA_bd PF10537 20-120, WHIM1 PF15612 724-773, WHIM2 PF15613 899-936, WHIM3 PF15614 991-1031 Baz1b 1353499 Q9Z277 BAZ1B_MOUSE PHF Zinc fingers, PHD-type Histone modification write Histone phosphorylation 19092802 B-WICH, WINAC histone H2AXT142, H3 H2AXY142ph # 19092802 WSTF=BAZ1B phosphorylates Tyr 142 of H2A.X, and WSTF activity has an important role in regulating several events that are critical for the DNA damage response.
BAZ2A
(details)
# 962 bromodomain adjacent to zinc finger domain, 2A 11176 Q9UIF9 BAZ2A_HUMAN Bromodomain PF00439 1802-1885, DDT PF02791 848-910, MBD PF01429 546-620, PHD PF00628 1678-1726, Pfam-B_14139 PB014139 1518-1541, Pfam-B_1702 PB001702 2-228, Pfam-B_25722 PB025722 1211-1279, Pfam-B_3124 PB003124 701-789 1085-1136, Pfam-B_32186 PB032186 1484-1516, Pfam-B_6766 PB006766 331-489, WHIM1 PF15612 950-999, WHIM3 PF15614 1439-1480 Baz2a 2151152 Q91YE5 BAZ2A_MOUSE PHF Zinc fingers, PHD-type Chromatin remodelling, Histone modification erase #, Histone deacetylation 11532953 NoRC histone, DNA H4K16ac, DNA motif H4K5, H4K8, H4K12 # 11532953 TIP5=BAZ2A is a member of a family of chromatin remodeling factors. Fig. 1 in the reference.
BAZ2B
(details)
# 963 bromodomain adjacent to zinc finger domain, 2B 29994 Q9UIF8 BAZ2B_HUMAN Bromodomain PF00439 2069-2151, DDT PF02791 1087-1149, MBD PF01429 739-813, PHD PF00628 1933-1981, Pfam-B_10350 PB010350 521-649, Pfam-B_12038 PB012038 1200-1479, Pfam-B_13066 PB013066 91-399, Pfam-B_1587 PB001587 401-519, Pfam-B_17078 PB017078 1618-1728, Pfam-B_17427 PB017427 1-89, Pfam-B_9375 PB009375 1481-1616 Baz2b 2442782 # # PHF Zinc fingers, PHD-type Histone modification read # 22464331 # histone, DNA H1.4ac, H2Aac, H2Bac, H3ac, H4Kac # # 22464331 Fig. 5 in the reference.
BCOR
(details)
# 20893 BCL6 corepressor 54880 Q6W2J9 BCOR_HUMAN Ank_2 PF12796 1460-1560, Pfam-B_11277 PB011277 41-289, Pfam-B_26758 PB026758 300-329, Pfam-B_27995 PB027995 1241-1359, Pfam-B_30654 PB030654 1361-1419, Pfam-B_5207 PB005207 421-1239 Bcor 1918708 Q8CGN4 BCOR_MOUSE ANKRD Ankyrin repeat domain containing Polycomb group (PcG) protein # 16943429 BCOR # # # # 16943429 The recruitment of BCOR complex PcG proteins to target genes by BCL6=BCOR in B cells suggests that BCL6 functions as a PcG-targeting factor.
BCORL1
(details)
# 25657 BCL6 corepressor-like 1 63035 Q5H9F3 BCORL_HUMAN Ank_2 PF12796 1410-1486 1426-1519, Pfam-B_1109 PB001109 110-149, Pfam-B_16739 PB016739 560-637, Pfam-B_20248 PB020248 740-800, Pfam-B_31169 PB031169 1-76, Pfam-B_8912 PB008912 383-533 Bcorl1 2443910 A2AQH4 BCORL_MOUSE ANKRD Ankyrin repeat domain containing Histone modification erase cofactor Histone deacetylation 23523425, 17379597 BCOR histone H3K36me2 # # 23523425 Homologous to BCOR; which is a component of a complex (dRAF-like complex) in companion with KDM2B, a H3K36me2 demethylase.
BMI1
(details)
# 1066 BMI1 proto-oncogene, polycomb ring finger 648 P35226 BMI1_HUMAN zf-C3HC4 PF00097 18-56 Bmi1 88174 P25916 BMI1_MOUSE RNF, PCGF RING-type (C3HC4) zinc fingers, Polycomb group ring fingers Polycomb group (PcG) protein # 15386022 PRC1 # # # # 15386022 The complex, termed hPRC1L (human Polycomb repressive complex 1-like), is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2.
BPTF
(details)
# 3581 bromodomain PHD finger transcription factor 2186 Q12830 BPTF_HUMAN Bromodomain PF00439 2936-3019, DDT PF02791 240-300, PHD PF00628 392-437 2869-2918, Pfam-B_14861 PB014861 2113-2229, Pfam-B_26081 PB026081 91-205, Pfam-B_911 PB000911 1922-2111, Pfam-B_94218 PB094218 1-89, WHIM1 PF15612 339-388 Bptf 2444008 # # PHF Zinc fingers, PHD-type Chromatin remodelling # 18974875 NuRF chromatin # # # 18974875 Chromatin remodeling protein Bptf (Bromodomain PHD-finger Transcription Factor), the largest subunit of NURF (Nucleosome Remodeling Factor) in a mammal.
BRCA1
(details)
# 1100 breast cancer 1, early onset 672 P38398 BRCA1_HUMAN BRCT PF00533 1648-1723 1756-1842, BRCT_assoc PF12820 344-508, EIN3 PF04873 648-978, Pfam-B_17893 PB017893 1404-1493, zf-C3HC4 PF00097 24-64 Brca1 104537 P48754 BRCA1_MOUSE RNF, PPP1R RING-type (C3HC4) zinc fingers, Serine/threonine phosphatases / Protein phosphatase 1, regulatory subunits Histone modification write cofactor, Histone modification write cofactor, Histone modification write cofactor, TF, TF Histone acetylation, Histone methylation, Histone ubiquitination, TF activator, TF repressor 20820192 BRCC, BRCA1-A DNA DNA motif # # 20820192 BRCA1 acts as a transcription factor, which regulates expression of many genes involved in many biological processes. DNMT1, the methylation maintenance enzyme, is a transcriptional target of BRCA1. Impaired function of BRCA1 leads to global DNA hypomethylation, loss of genomic imprinting, and an open chromatin configuration in several types of tissues examined in a BRCA1 mutant mouse model at premaligant stages. BRCA1 deficiency is also associated with significantly increased expression levels of several protooncogenes.
BRCA2
(details)
# 1101 breast cancer 2, early onset 675 P51587 BRCA2_HUMAN BRCA-2_OB1 PF09103 2670-2800, BRCA-2_OB3 PF09104 3052-3190, BRCA-2_helical PF09169 2479-2667, BRCA2 PF00634 1002-1036 1212-1246 1421-1455 1517-1551 1664-1698 1837-1871 1971-2005 2051-2085, Pfam-B_13057 PB013057 2141-2448, Pfam-B_47717 PB047717 2449-2478, Pfam-B_8258 PB008258 651-989, Tower PF09121 2831-2872 Brca2 109337 P97929 BRCA2_MOUSE FANC Fanconi anemia, complementation groups Histone modification write Histone acetylation 9619837 BRCC histone, DNA H3, H4, ssDNA # # 9619837 BRCA2 proteins acetylate primarily H3 and H4 of free histones. This suggests that HAT activity of BRCA2 may play an important role in the regulation of transcription and tumor suppressor function.
BRCC3
(details)
# 24185 BRCA1/BRCA2-containing complex, subunit 3 79184 P46736 BRCC3_HUMAN JAB PF01398 7-148 Brcc3 2389572 P46737 BRCC3_MOUSE # # Histone modification erase Histone deubiquitination 19202061 BRISC, BRCA1-A histone H2AK63, H2AXK63 H2A, H2AX # 19202061 Involved in DNA damage response and reverses RNF8 ubiquitination activity. Rap80-BRCC36 DUB Activity and γH2AX hydrolysis Ubiquitination. Rap80 is required for BRCA1 and BRCC36 localization to DSBs.
BRD1
(details)
# 1102 bromodomain containing 1 23774 O95696 BRD1_HUMAN Bromodomain PF00439 571-654, EPL1 PF10513 46-196, PHD_2 PF13831 228-262, PWWP PF00855 927-1042, zf-HC5HC2H_2 PF13832 269-388 Brd1 1924161 # # # # Histone modification read # 21720545 MOZ/MORF histone H3K36me3, H3 # # 21720545 The PWWP domains in BRPF1, BRPF2=BRD1, HDGF2, MUM1 and the N-terminal PWWP domains of WHSC1 and WHSC1L1 show weak binding affinity to histones with H3K36, K3K79 or H4K20 methylation.
BRD2
(details)
# 1103 bromodomain containing 2 6046 P25440 BRD2_HUMAN Bromodomain PF00439 84-168 353-441, Pfam-B_12618 PB012618 624-776, Pfam-B_14336 PB014336 541-613 Brd2 99495 Q7JJ13 BRD2_MOUSE # # Histone modification read # 18406326 # histone H3K9me2, H3K14me2, H4K5ac, H4K12ac # # 18406326 Brd2- and Brd3-associated chromatin is significantly enriched in H4K5, H4K12, and H3K14 acetylation and contains relatively little dimethylated H3K9. Both Brd2 and Brd3 allowed RNA polymerase II to transcribe through nucleosomes in a defined transcription system. Such activity depended on specific histone H4 modifications known to be recognized by the Brd proteins.
BRD3
(details)
# 1104 bromodomain containing 3 8019 Q15059 BRD3_HUMAN Bromodomain PF00439 42-128 315-403 Brd3 1914632 Q8K2F0 BRD3_MOUSE # # Histone modification read # 18406326 # histone H3K9me2, H3K14me2, H4K5ac, H4K12ac # # 18406326 Brd2- and Brd3-associated chromatin is significantly enriched in H4K5, H4K12, and H3K14 acetylation and contains relatively little dimethylated H3K9. Both Brd2 and Brd3 allowed RNA polymerase II to transcribe through nucleosomes in a defined transcription system. Such activity depended on specific histone H4 modifications known to be recognized by the Brd proteins.
BRD4
(details)
# 13575 bromodomain containing 4 23476 O60885 BRD4_HUMAN Bromodomain PF00439 67-152 357-445, Pfam-B_14896 PB014896 1187-1263, Pfam-B_15118 PB015118 509-647, Pfam-B_18611 PB018611 648-667, Pfam-B_24632 PB024632 833-892, Pfam-B_29595 PB029595 1283-1311, Pfam-B_35798 PB035798 1136-1185, Pfam-B_361 PB000361 1324-1357 Brd4 1888520 Q9ESU6 BRD4_MOUSE # # Histone modification read # 12840145 # histone H3K9, H3K14, H4K5, H4K12 # # 12840145 Brd4 avidly binds to di- and tetraacetylated histone H4 and diacetylated H3, but weakly or not at all to mono- and unacetylated H3 and H4.
BRD7
(details)
# 14310 bromodomain containing 7 29117 Q9NPI1 BRD7_HUMAN Bromodomain PF00439 140-223, DUF3512 PF12024 286-534, Pfam-B_1543 PB001543 591-649, Pfam-B_64177 PB064177 1-49 Brd7 1349766 O88665 BRD7_MOUSE # # Histone modification read # 17498659 SWI/SNF BRM-BRG1 histone H3K9ac, H3K14ac, H3K8ac # # 17498659 BRD7 bromodomain contains the typical left-handed four-helix bundle topology, and can bind with weak affinity to lysine-acetylated peptides derived from histone H3 with K9 or K14 acetylated and from histone H4 with K8, K12 or K16 acetylated.
BRD8
(details)
# 19874 bromodomain containing 8 10902 Q9H0E9 BRD8_HUMAN Bromodomain PF00439 713-799 1112-1195, Pfam-B_19676 PB019676 1-69, Pfam-B_55933 PB055933 71-109 Brd8 1925906 Q8R3B7 BRD8_MOUSE # # Histone modification read # 14966270 SWR, NuA4, NuA4-related complex histone # # # 14966270 Part of the NuA4 histone acetyltransferase complex.
BRD9
(details)
# 25818 bromodomain containing 9 65980 Q9H8M2 BRD9_HUMAN Bromodomain PF00439 143-228, DUF3512 PF12024 268-505, Pfam-B_8260 PB008260 511-595 Brd9 2145317 Q3UQU0 BRD9_MOUSE # # Histone modification read # 22464331 SWI/SNF BRM-BRG1 histone H3 # # 22464331 Fig. 5 in the reference.
BRDT
(details)
# 1105 bromodomain, testis-specific 676 Q58F21 BRDT_HUMAN Bromodomain PF00439 36-121 276-364, Pfam-B_11430 PB011430 710-791 Brdt 1891374 Q91Y44 BRDT_MOUSE # # Histone modification read # 22901802 # histone H4K5ac, H4K8ac # # 22901802 Biochemical and crystallographic studies confirm that occupancy of the BRDT acetyl-lysine binding pocket by JQ1 prevents recognition of acetylated histone H4.
BRE
(details)
# 1106 brain and reproductive organ-expressed (TNFRSF1A modulator) 9577 Q9NXR7 BRE_HUMAN BRE PF06113 1-333 Bre 1333875 Q8K3W0 BRE_MOUSE # # Histone modification write cofactor Histone ubiquitination 14636569 BRISC, BRCC, BRCA1-A histone # # # 14636569 BRCC36 and BRCC45 are novel components of the complex with sequence homology to a subunit of the signalosome and proteasome complexes. Reconstitution of a recombinant four-subunit complex containing BRCA1/BARD1/BRCC45/BRCC36 revealed an enhanced E3 ligase activity compared to that of BRCA1/BARD1 heterodimer. Furthermore, a recent report describes the ability of BRCA1-BARD1 heterodimer to autoubiquitinate BRCA1 and BARD1 and transubiquitinate the histone H2A(X).
BRMS1
(details)
# 17262 breast cancer metastasis suppressor 1 25855 Q9HCU9 BRMS1_HUMAN Sds3 PF08598 58-229 Brms1 2388804 Q99N20 BRMS1_MOUSE # # Chromatin remodelling # 17000776 mSin3A chromatin # # # 17000776 As a corepressor, BRMS1 can function as a more global regulator of chromatin structure, as evidenced by its ability to decrease promoter occupancy of Ac-H3 and Ac-H4 on both the cIAP2 and the Bfl-1/A1 promoters.
BRMS1L
(details)
# 20512 breast cancer metastasis-suppressor 1-like 84312 Q5PSV4 BRM1L_HUMAN Sds3 PF08598 59-227 Brms1l 1196337 Q3U1T3 BRM1L_MOUSE # # Histone modification erase Histone deacetylation 15451426 mSin3A histone # # # 15451426 p40-associated Sin3A/HDAC1 complex can deacetylate histone peptides in vitro. p40 can also repress transcription when tethered to the Gal-regulated promoter by the Gal-DNA binding domain.
BRPF1
(details)
# 14255 bromodomain and PHD finger containing, 1 7862 P55201 BRPF1_HUMAN Bromodomain PF00439 637-720, EPL1 PF10513 105-255, PHD_2 PF13831 287-321, PWWP PF00855 1083-1198, zf-HC5HC2H_2 PF13832 328-447 Brpf1 1926033 # # # # Histone modification read # 20400950 MOZ/MORF histone H3K36me3 # # 20400950 Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1.
BRPF3
(details)
# 14256 bromodomain and PHD finger containing, 3 27154 Q9ULD4 BRPF3_HUMAN Bromodomain PF00439 598-681, EPL1 PF10513 47-194, PHD_2 PF13831 226-260, PWWP PF00855 1074-1189, Pfam-B_5327 PB005327 751-829, zf-HC5HC2H_2 PF13832 267-386 Brpf3 2146836 # # # # Histone modification write cofactor Histone acetylation 18794358 MOZ/MORF histone # # # 18794358 Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. BRPF proteins bridge the association of MOZ and MORF with ING5 and EAF6.
BRWD1
(details)
# 12760 bromodomain and WD repeat domain containing 1 54014 Q9NSI6 BRWD1_HUMAN Bromodomain PF00439 1166-1252 1322-1405, Pfam-B_18973 PB018973 859-924, Pfam-B_22078 PB022078 2089-2186, Pfam-B_27858 PB027858 1900-2087, Pfam-B_71 PB000071 2238-2318, Pfam-B_8184 PB008184 1821-1898, WD40 PF00400 177-214 218-256 260-302 358-396 458-497 Brwd1 1890651 Q921C3 BRWD1_MOUSE WDR WD repeat domain containing Histone modification read # 22464331 # histone H3 # # 22464331 Fig. 5 in the reference.
BRWD3
(details)
# 17342 bromodomain and WD repeat domain containing 3 254065 Q6RI45 BRWD3_HUMAN Bromodomain PF00439 1147-1233 1345-1418, Pfam-B_12397 PB012397 1669-1710, Pfam-B_2569 PB002569 9-97, WD40 PF00400 171-208 212-250 254-296 352-392 455-494 507-540 Brwd3 3029414 A2AHJ4 BRWD3_MOUSE WDR WD repeat domain containing Histone modification read # 22464331 # histone H3 # # 22464331 Fig. 5 in the reference.
BUB1
(details)
# 1148 BUB1 mitotic checkpoint serine/threonine kinase 699 O43683 BUB1_HUMAN Mad3_BUB1_I PF08311 4-126, Pkinase PF00069 787-1033 Bub1 1100510 O08901 BUB1_MOUSE # # Histone modification write Histone phosphorylation 20929775 # histone H2AS121 H2AS121ph # 20929775 Bub1 mediates histone 2A-serine 121 (H2A-S121) phosphorylation.
C11orf30
(details)
New 18071 chromosome 11 open reading frame 30 56946 Q7Z589 EMSY_HUMAN ENT PF03735 16-88, Pfam-B_10468 PB010468 695-833, Pfam-B_10943 PB010943 985-1113 2210018M11Rik 1924203 Q8BMB0 EMSY_MOUSE # # Histone modification write cofactor Histone methylation 19131338 # histone # # # # Part of a complex with histone methyltranferase activity. UniProt: Regulator which is able to repress transcription, possibly via its interaction with a multiprotein chromatin remodeling complex that modifies the chromatin.
C14orf169
(details)
# 20968 # # Q9H6W3 NO66_HUMAN Cupin_4 PF08007 215-557, Pfam-B_41208 PB041208 71-139, Pfam-B_47541 PB047541 1-69 - - Q9JJF3 NO66_MOUSE # # Histone modification erase Histone methylation 23160351 # histone H3K4me3, H3K4me1, H3K36me2 H3K4me2, H3K4, H3K36me1 # 23160351 H3K4me3 demethylase Rbp2 (Kdm5a). In addition to NO66=C14orf169, at least four other H3K36me3 demethylases are known.
C17orf49
(details)
# 28737 chromosome 17 open reading frame 49 124944 Q8IXM2 BAP18_HUMAN # 0610010K14Rik 1915609 Q9DCT6 BAP18_MOUSE # # Histone modification read # 20850016 CHD8, MLL2/3, MLL4/WBP7 histone H3K4me3 # # 20850016 H3K4me3 readers Sgf29, TRRAP, PHF8, GATAD1, and BAP18=C17orf49, are associated mainly with promoters (Figures S3A and S3B) and coincide with H3K4me3 marking.
CARM1
(details)
# 23393 coactivator-associated arginine methyltransferase 1 10498 Q86X55 CARM1_HUMAN CARM1 PF11531 26-139, PRMT5 PF05185 143-446, Pfam-B_10255 PB010255 449-469, Pfam-B_13059 PB013059 511-606 Carm1 1913208 Q9WVG6 CARM1_MOUSE PRMT Protein arginine methyltransferases Histone modification write Histone methylation 12237300 # histone H3R17 H3R17me, H3R17me2a # 16497732, 19405910 Methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. CARM1-directed arginine methylation of histone H3 in the promoters of steroid hormone-responsive genes is induced by steroid hormone treatment of cells.
CBX1
(details)
# 1551 chromobox homolog 1 10951 P83916 CBX1_HUMAN Chromo PF00385 21-70, Chromo_shadow PF01393 115-172 Cbx1 105369 P83917 CBX1_MOUSE # # Histone modification read # 21047797 # histone H3K9me3, H3K27me3 # # 21047797 Binding data indicate that Cbx1, -3, and -5 bind with greater affinity to H3K9me3.
CBX2
(details)
# 1552 chromobox homolog 2 84733 Q14781 CBX2_HUMAN Chromo PF00385 12-61, Pfam-B_1400 PB001400 249-295 Cbx2 88289 P30658 CBX2_MOUSE # # Histone modification read # 21047797 PRC1 histone H3K9me3, H3K27me3 # # 21047797 Cbx2 and Cbx7 recognized both H3K9me3 and H3K27me3, whereas Cbx4 preferred H3K9me3.
CBX3
(details)
# 1553 chromobox homolog 3 11335 Q13185 CBX3_HUMAN Chromo PF00385 30-79, Chromo_shadow PF01393 119-176 Cbx3 108515 P23198 CBX3_MOUSE # # Histone modification read # 21047797 RING2-L3MBTL2, L3MBTL1 histone H3K9me3 # # 21047797 Cbx3 chromodomain binds to H3K9me3 but not to H3K27me3.
CBX4
(details)
# 1554 chromobox homolog 4 8535 O00257 CBX4_HUMAN Chromo PF00385 11-60, Pfam-B_16393 PB016393 481-531, Pfam-B_26041 PB026041 401-479, Pfam-B_8537 PB008537 82-281 Cbx4 1195985 O55187 CBX4_MOUSE # # Histone modification read # 21047797 PRC1 histone H3K9me3 # # 21047797 Cbx2 and Cbx7 recognizes both H3K9me3 and H3K27me3, whereas Cbx4 prefers H3K9me3.
CBX5
(details)
# 1555 chromobox homolog 5 23468 P45973 CBX5_HUMAN Chromo PF00385 20-69, Chromo_shadow PF01393 119-176 Cbx5 109372 Q61686 CBX5_MOUSE # # Histone modification read # 21047797 # histone H3K9me, H3K27me3 # # 21047797 Excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph).
CBX6
(details)
# 1556 chromobox homolog 6 23466 O95503 CBX6_HUMAN Chromo PF00385 11-60, Pfam-B_41557 PB041557 291-379, Pfam-B_49897 PB049897 381-410 Cbx6 3512628 Q9DBY5 CBX6_MOUSE # # Histone modification read # 21047797 PRC1 histone H3K9me3, H3K27me3 # # 21047797 Cbx6 and Cbx8 have functional aromatic cages and hydrophobic fingers very similar to those of Cbx2, -4, and -7, but the former bind to H3K9me3 and H3K27me3 peptides with much lower affinity.
CBX7
(details)
# 1557 chromobox homolog 7 23492 O95931 CBX7_HUMAN Chromo PF00385 11-60 Cbx7 1196439 Q8VDS3 CBX7_MOUSE # # Histone modification read # 21047797 PRC1 histone H3K9me3, H3K27me3 # # 21047797 Cbx2 and Cbx7 recognize both H3K9me3 and H3K27me3, whereas Cbx4 prefers H3K9me3.
CBX8
(details)
# 15962 chromobox homolog 8 57332 Q9HC52 CBX8_HUMAN Chromo PF00385 11-60 Cbx8 1353589 Q9QXV1 CBX8_MOUSE # # Histone modification read # 21047797 PRC1 histone H3K9me3, H3K27me3 # # 21047797 Cbx6 and Cbx8 have functional aromatic cages and hydrophobic fingers very similar to those of Cbx2, -4, and -7, but the former bind to H3K9me3 and H3K27me3 peptides with much lower affinity.
CCDC101
(details)
# 25156 coiled-coil domain containing 101 112869 Q96ES7 SGF29_HUMAN DUF1325 PF07039 157-289 Ccdc101 1922815 Q9DA08 SGF29_MOUSE # # Histone modification read # 21685874 ATAC histone H3K4me, H3K4me3 # # 21685874 The crystal structures of the tandem Tudor domains of Saccharomyces cerevisiae and human Sgf29=CCDC101 and their complexes with H3K4me2 and H3K4me3 peptides, respectively, shows that Sgf29 selectively binds H3K4me2/3 marks.
CDC6
(details)
New 1744 cell division cycle 6 990 Q99741 CDC6_HUMAN AAA_22 PF13401 190-322, Cdc6_C PF09079 465-545 Cdc6 1345150 O89033 CDC6_MOUSE # # Chromatin remodelling # 22358331 # chromatin # # # # CDC6 interacts with the HP1 chromoshadow domain.
CDC73
(details)
New 16783 cell division cycle 73 79577 Q6P1J9 CDC73_HUMAN CDC73 PF05179 233-525 Cdc73 2384876 Q8JZM7 CDC73_MOUSE # # Histone modification write cofactor Histone methylation # # histone # # # # UniProt: PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1).
CDK1
(details)
# 1722 cyclin-dependent kinase 1 983 P06493 CDK1_HUMAN Pkinase PF00069 4-287 Cdk1 88351 P11440 CDK1_MOUSE CDK Cyclin-dependent kinases Histone modification write Histone phosphorylation 22509284 # histone H1 H1ph # 22509284 Histone H1, a known CDKs target protein, was strongly phosphorylated by CDK1/cyclin B, illustrating the normal activity of CDK1/cyclin B.
CDK17
(details)
# 8750 cyclin-dependent kinase 17 5128 Q00537 CDK17_HUMAN Pkinase PF00069 192-473 Cdk17 97517 Q8K0D0 CDK17_MOUSE CDK Cyclin-dependent kinases Histone modification write Histone phosphorylation # # histone H1 # # # Has a Ser/Thr-phosphorylating activity for histone H1. (Annotated by similarity.)
CDK2
(details)
# 1771 cyclin-dependent kinase 2 1017 P24941 CDK2_HUMAN Pkinase PF00069 4-286 Cdk2 104772 P97377 CDK2_MOUSE CDK Cyclin-dependent kinases Histone modification write Histone phosphorylation 15753125 # histone H1S, H1T H1Sph, H1Tph # 15753125 Cdk2 is one of the enzymes recruited to replication foci (by Cdc45 or other fork proteins), followed by H1 phosphorylation and chromatin unfolding.
CDK3
(details)
# 1772 cyclin-dependent kinase 3 1018 Q00526 CDK3_HUMAN Pkinase PF00069 4-286 Cdk3-ps 1916931 Q80YP0 CDK3_MOUSE CDK Cyclin-dependent kinases Histone modification write Histone phosphorylation # # histone H1 # # # Cdk3 is supposed to phosphorylate histone H1, but have found no good reference to document it.
CDK5
(details)
# 1774 cyclin-dependent kinase 5 1020 Q00535 CDK5_HUMAN Pkinase PF00069 4-286 Cdk5 101765 P49615 CDK5_MOUSE CDK Cyclin-dependent kinases Histone modification write Histone phosphorylation 19729834 # histone H1 # # 19729834 Reciprocal coimmunoprecipitation studies with antibodies to either myc or Cdk5 revealed that cyclin I bound to and activated endogenous Cdk5, as analyzed by histone H1 phosphorylation.
CDK7
(details)
# 1778 cyclin-dependent kinase 7 1022 P50613 CDK7_HUMAN Pfam-B_20206 PB020206 301-344, Pkinase PF00069 12-295 Cdk7 102956 Q03147 CDK7_MOUSE CDK, TFIIH Cyclin-dependent kinases, General transcription factor IIH complex subunits Histone modification write Histone phosphorylation 10722743 # histone H1 # # 10722743 Cdk7, is able to phosphorylate histone H1, and the basal activity is increased 2-fold in the presence of recombinant human cyclin H (the activating partner of Cdk7).
CDK9
(details)
New 1780 cyclin-dependent kinase 9 1025 P50750 CDK9_HUMAN Pkinase PF00069 19-315 Cdk9 1328368 Q99J95 CDK9_MOUSE CDK Cyclin-dependent kinases Histone modification cofactor # 19844166 # histone # # # # CDK9 functions to guide a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3. UniProt: Protein kinase involved in the regulation of transcription. Part of the complex P-TEFb involved in cotranscriptional histone modification.
CDY1
(details)
# 1809 chromodomain protein, Y-linked, 1 9085 Q9Y6F8 CDY1_HUMAN Chromo PF00385 6-57, ECH PF00378 287-535, Pfam-B_51834 PB051834 101-148 # # # # # # Histone modification write Histone acetylation 12072557 # histone H4 # # 12072557 Human CDY and mouse CDYL=CDY1 proteins exhibit histone acetyltransferase activity in vitro, with a strong preference for histone H4.
CDY1B
(details)
# 23920 chromodomain protein, Y-linked, 1B 253175 Q9Y6F8 CDY1_HUMAN Chromo PF00385 6-57, ECH PF00378 287-535, Pfam-B_51834 PB051834 101-148 # # # # # # Histone modification write Histone acetylation 12072557 # histone H4 # # 12072557 Human CDY and mouse CDYL=CDY1B proteins exhibit histone acetyltransferase activity in vitro, with a strong preference for histone H4.
CDY2A
(details)
# 1810 chromodomain protein, Y-linked, 2A 9426 Q9Y6F7 CDY2_HUMAN Chromo PF00385 6-57, ECH PF00378 288-536, Pfam-B_51834 PB051834 101-149 # # # # # # Histone modification write Histone acetylation # # histone # # # # May have histone acetyltransferase activity. (Annotated by similarity.)
CDY2B
(details)
New 23921 chromodomain protein, Y-linked, 2B 203611 Q9Y6F7 CDY2_HUMAN Chromo PF00385 6-57, ECH PF00378 288-536, Pfam-B_51834 PB051834 101-149 # # # # # # Histone modification write Histone acetylation 22498752 # histone # # # # CDY2B annotated as histone acetyltransferase in UniProt.
CDYL
(details)
# 1811 chromodomain protein, Y-like 9425 Q9Y232 CDYL1_HUMAN Chromo PF00385 61-112, ECH PF00378 345-593, Pfam-B_14969 PB014969 136-234 Cdyl 1339956 Q9WTK2 CDYL_MOUSE # # Histone modification write Histone acetylation 12072557 # histone H4 # # 12072557 Human CDY and mouse CDYL proteins exhibit histone acetyltransferase activity in vitro, with a strong preference for histone H4.
CDYL2
(details)
# 23030 chromodomain protein, Y-like 2 124359 Q8N8U2 CDYL2_HUMAN Chromo PF00385 7-57, ECH PF00378 253-501 Cdyl2 1923046 Q9D5D8 CDYL2_MOUSE # # Histone modification read # 23455924 # histone H3K9me3 # # 21774827 Many mouse chromodomain proteins are reported to bind H3K9me3 in vitro, including CDYL, CDYL2, CBX2, CBX4, CBX7 and M-phase phosphoprotein 8 (MPP8).
CECR2
(details)
# 1840 cat eye syndrome chromosome region, candidate 2 27443 Q9BXF3 CECR2_HUMAN Bromodomain PF00439 443-526, Pfam-B_13010 PB013010 1-329, Pfam-B_18245 PB018245 800-968, Pfam-B_20164 PB020164 331-419 Cecr2 1923799 # # # # Histone modification read # 22464331 CERF, CERF histone H2A, H3 # # 22464331 Fig. 5 in the reference.
CENPC
(details)
# 1854 centromere protein C 1060 Q03188 CENPC_HUMAN CENP-C_C PF11699 856-940, CENP-C_mid PF15620 296-552, CENP_C_N PF15622 7-292 Cenpc1 99700 P49452 CENPC_MOUSE # # DNA modification DNA methylation 19482874 # DNA C 5mC # 19482874 CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions.
CHAF1A
(details)
# 1910 chromatin assembly factor 1, subunit A (p150) 10036 Q13111 CAF1A_HUMAN CAF-1_p150 PF11600 266-479, CAF1-p150_C2 PF15539 665-956, CAF1-p150_N PF15557 1-229, CAF1A PF12253 557-635 Chaf1a 1351331 Q9QWF0 CAF1A_MOUSE # # Chromatin remodelling # 7600578 CAF-1 histone H3, H4 # # 7600578 p150=CHAF1A and p60 directly interact and are both required for DNA replication-dependent assembly of nucleosomes. Deletion of the p60-binding domain from the p150 protein prevents chromatin assembly. p150 and p60 form complexes with newly synthesized histones H3 and acetylated H4 in human cell extracts, suggesting that such complexes are intermediates between histone synthesis and assembly onto replicating DNA.
CHAF1B
(details)
# 1911 chromatin assembly factor 1, subunit B (p60) 8208 Q13112 CAF1B_HUMAN CAF-1_p60_C PF15512 381-558, WD40 PF00400 10-45 57-94 119-157 161-199 339-372 Chaf1b 1314881 Q9D0N7 CAF1B_MOUSE WDR WD repeat domain containing Chromatin remodelling # 7600578 WINAC, CAF-1 histone H3, H4 # # 7600578 p150 and p60==CHAF1B directly interact and are both required for DNA replication-dependent assembly of nucleosomes. Deletion of the p60-binding domain from the p150 protein prevents chromatin assembly. p150 and p60 form complexes with newly synthesized histones H3 and acetylated H4 in human cell extracts, suggesting that such complexes are intermediates between histone synthesis and assembly onto replicating DNA.
CHD1
(details)
# 1915 chromodomain helicase DNA binding protein 1 1105 O14646 CHD1_HUMAN Chromo PF00385 273-355 389-443, DUF4208 PF13907 1400-1500, Helicase_C PF00271 822-902, Pfam-B_182 PB000182 1646-1708, Pfam-B_91833 PB091833 121-162, SNF2_N PF00176 484-765 Chd1 88393 P40201 CHD1_MOUSE # # Chromatin remodelling # 12592387 # DNA # # # 12592387 These proteins have a DNA-binding domain as well as a chromodomain motif that can directly effect chromatin structure and gene transcription. There are currently four known members of this gene family in humans (CHD1–CHD4).
CHD1L
(details)
# 1916 chromodomain helicase DNA binding protein 1-like 9557 Q86WJ1 CHD1L_HUMAN Helicase_C PF00271 381-459, Pfam-B_2492 PB002492 468-549, SNF2_N PF00176 49-328 Chd1l 1915308 Q9CXF7 CHD1L_MOUSE # # Chromatin remodelling # 19661379 # DNA # # # 19661379 A chromatin-remodeling enzyme, ALC1 (Amplified in Liver Cancer 1, also known as CHD1L), that interacts with poly(ADP-ribose) and catalyzes PARP1-stimulated nucleosome sliding.
CHD2
(details)
# 1917 chromodomain helicase DNA binding protein 2 1106 O14647 CHD2_HUMAN Chromo PF00385 261-344 378-447, DUF4208 PF13907 1455-1555, Helicase_C PF00271 825-905, Pfam-B_19320 PB019320 1231-1309, Pfam-B_761 PB000761 1111-1229, SNF2_N PF00176 487-768 Chd2 2448567 E9PZM4 CHD2_MOUSE # # Chromatin remodelling # 12592387 # DNA # # # 12592387 These proteins have a DNA-binding domain as well as a chromodomain motif that can directly effect chromatin structure and gene transcription. There are currently four known members of this gene family in humans (CHD1–CHD4).
CHD3
(details)
# 1918 chromodomain helicase DNA binding protein 3 1107 Q12873 CHD3_HUMAN CHDCT2 PF08074 1735-1907, CHDNT PF08073 147-201, Chromo PF00385 539-574 631-683, DUF1086 PF06461 1363-1519, DUF1087 PF06465 1293-1357, Helicase_C PF00271 1094-1174, PHD PF00628 381-426 458-503, SNF2_N PF00176 739-1035 Chd3 1344395 # # PHF Zinc fingers, PHD-type Chromatin remodelling # 12592387 NuRD DNA # # # 12592387 These proteins have a DNA-binding domain as well as a chromodomain motif that can directly effect chromatin structure and gene transcription. There are currently four known members of this gene family in humans (CHD1–CHD4).
CHD4
(details)
# 1919 chromodomain helicase DNA binding protein 4 1108 Q14839 CHD4_HUMAN CHDCT2 PF08074 1724-1896, CHDNT PF08073 163-217, Chromo PF00385 531-577 622-674, DUF1086 PF06461 1366-1523, DUF1087 PF06465 1289-1353, Helicase_C PF00271 1084-1164, PHD PF00628 372-417 451-496, SNF2_N PF00176 729-1025 Chd4 1344380 Q6PDQ2 CHD4_MOUSE PHF Zinc fingers, PHD-type Chromatin remodelling # 12592387 NuRD DNA # # # 12592387 These proteins have a DNA-binding domain as well as a chromodomain motif that can directly effect chromatin structure and gene transcription. There are currently four known members of this gene family in humans (CHD1–CHD4).
CHD5
(details)
# 16816 chromodomain helicase DNA binding protein 5 26038 Q8TDI0 CHD5_HUMAN CHDCT2 PF08074 1731-1903, CHDNT PF08073 146-200, Chromo PF00385 499-537 592-643, DUF1086 PF06461 1377-1531, DUF1087 PF06465 1295-1359, Helicase_C PF00271 1058-1138, PHD PF00628 345-390 418-463, Pfam-B_20089 PB020089 201-334, SNF2_N PF00176 703-999 Chd5 3036258 A2A8L1 CHD5_MOUSE PHF Zinc fingers, PHD-type Chromatin remodelling # 12592387 # histone H3K27me3, H3K4 # # 12592387, 23948251 A novel gene encoding a protein with chromatin remodeling, helicase and DNA-binding motifs. This gene (CHD5) is the fifth member of the CHD gene family identified in humans.
CHD6
(details)
# 19057 chromodomain helicase DNA binding protein 6 # Q8TD26 CHD6_HUMAN BRK PF07533 2400-2441, Chromo PF00385 292-354 375-429, Helicase_C PF00271 817-897, Pfam-B_18962 PB018962 1-49, Pfam-B_23619 PB023619 1691-1909, Pfam-B_71010 PB071010 1911-1953, Pfam-B_761 PB000761 1271-1333 1361-1519, SNF2_N PF00176 464-751 Chd6 1918639 A3KFM7 CHD6_MOUSE # # Chromatin remodelling # 12592387 # chromatin # # # 12592387 A novel gene encoding a protein with chromatin remodeling, helicase and DNA-binding motifs. This gene (CHD5=CHD6) is the fifth member of the CHD gene family identified in humans.
CHD7
(details)
# 20626 chromodomain helicase DNA binding protein 7 55636 Q9P2D1 CHD7_HUMAN BRK PF07533 2562-2612 2640-2685, Chromo PF00385 800-862 882-935, Helicase_C PF00271 1324-1404, Pfam-B_19729 PB019729 1-188, Pfam-B_19848 PB019848 2351-2469, Pfam-B_2227 PB002227 281-449, Pfam-B_2565 PB002565 1722-1920, Pfam-B_6146 PB006146 2041-2259, Pfam-B_761 PB000761 1622-1720 1966-2035, SNF2_N PF00176 971-1258 Chd7 2444748 A2AJK6 CHD7_MOUSE # # Chromatin remodelling # 5201778 # chromatin # # # 5201778 CHD7 protein counts several functional domains: two chromo (chromatin organization modifier), one SNF2/SWI, one helicase and two BRK domains (Figure 4). Chromo domains are implicated in the recognition of lysine-methylated histone tails and of DNA (and RNA) targets.
CHD8
(details)
# 20153 chromodomain helicase DNA binding protein 8 57680 Q9HCK8 CHD8_HUMAN BRK PF07533 2308-2353, Chromo PF00385 642-704 724-778, Helicase_C PF00271 1167-1247, Pfam-B_10410 PB010410 1-109, Pfam-B_12479 PB012479 1721-1779, Pfam-B_13819 PB013819 2211-2279, Pfam-B_20709 PB020709 2031-2169, Pfam-B_2565 PB002565 1781-2029, Pfam-B_6146 PB006146 2171-2209, Pfam-B_6192 PB006192 1481-1669, Pfam-B_7386 PB007386 311-493, Pfam-B_8182 PB008182 1411-1479, Pfam-B_8545 PB008545 111-309, SNF2_N PF00176 814-1101 Chd8 1915022 Q09XV5 CHD8_MOUSE # # Chromatin remodelling # 18378692 CHD8, MLL2/3, MLL4/WBP7 chromatin H1 # # 19151705, 18378692 CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes.
CHD9
(details)
# 25701 chromodomain helicase DNA binding protein 9 80205 Q3L8U1 CHD9_HUMAN BRK PF07533 2480-2530 2554-2599, Chromo PF00385 690-752 773-827, Helicase_C PF00271 1216-1296, Pfam-B_10410 PB010410 1-89, Pfam-B_1107 PB001107 2701-2729, Pfam-B_15117 PB015117 371-579, Pfam-B_24836 PB024836 1774-1901, Pfam-B_6192 PB006192 1530-1675, Pfam-B_7386 PB007386 231-369, Pfam-B_8182 PB008182 1460-1528, Pfam-B_8545 PB008545 91-229, SNF2_N PF00176 863-1150 Chd9 1924001 Q8BYH8 CHD9_MOUSE # # Chromatin remodelling # 16554032 # DNA # # # 16554032 PRIC320=CHD9 is similar to a recently described chromodomain helicase DNA-binding protein [27]. The recognition of this chromatin remodeling function and nuclear receptor coactivator function is suggestive of the multiple roles played by these nuclear receptor cofactors.
CHEK1
(details)
New 1925 checkpoint kinase 1 1111 O14757 CHK1_HUMAN Pkinase PF00069 9-265 Chek1 1202065 O35280 CHK1_MOUSE # # Histone modification write Histone phosphorylation # # histone H3.1 H3.1ph # # UniProt: May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes.
CHRAC1
(details)
# 13544 chromatin accessibility complex 1 54108 Q9NRG0 CHRC1_HUMAN CBFD_NFYB_HMF PF00808 17-80 Chrac1 2135796 Q9JKP8 CHRC1_MOUSE # # Histone chaperone # 10880450 CHRAC DNA # # # 10880450 Human homologues of two novel putative histone-fold proteins in Drosophila CHRAC are present in HuCHRAC. The two human histone-fold proteins form a stable complex that binds naked DNA but not nucleosomes.
CHTOP
(details)
New 24511 chromatin target of PRMT1 26097 Q9Y3Y2 CHTOP_HUMAN FoP_duplication PF13865 171-245 Chtop 1913761 Q9CY57 CHTOP_MOUSE # # # # 25284789 # DNA # # # # 5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex.
CHUK
(details)
# 1974 conserved helix-loop-helix ubiquitous kinase 1147 O15111 IKKA_HUMAN IKKbetaNEMObind PF12179 706-743, Pfam-B_15051 PB015051 300-415, Pkinase PF00069 15-297 Chuk 99484 Q60680 IKKA_MOUSE # # Histone modification write Histone phosphorylation 17434128 # histone H3 # # 17434128 In the nucleus, IKKα=CHUK is recruited to the promoter region of the NF-κB-regulated genes by interacting with CBP, and contributes to NF-κB-mediated gene expressions through phosphorylation of histone H3.
CIR1
(details)
# 24217 corepressor interacting with RBPJ, 1 9541 Q86X95 CIR1_HUMAN Cir_N PF10197 13-49, Pfam-B_16354 PB016354 52-448 Cir1 1914185 Q9DA19 CIR1_MOUSE # # Histone modification read # 9874765 # histone # # # 9874765 CIR binds to histone deacetylase and to SAP30 and serves as a linker between CBF1 and the histone deacetylase complex.
CIT
(details)
# 1985 citron rho-interacting serine/threonine kinase 11113 O14578 CTRO_HUMAN CNH PF00780 1597-1868, Pfam-B_11694 PB011694 483-521, Pfam-B_387 PB000387 1354-1412, Pkinase PF00069 97-360, Pkinase_C PF00433 378-424 Cit 105313 P49025 CTRO_MOUSE # # Histone modification write cofactor, Histone modification write cofactor Histone methylation, Histone phosphorylation 18245345 # histone H3K9 H3K9me # 18245345 Drosophila sticky/citron kinase (=CIT) is a regulator of cell-cycle progression, genetically interacts with Argonaute 1 and modulates epigenetic gene silencing.
CLNS1A
(details)
New 2080 chloride channel, nucleotide-sensitive, 1A 1207 P54105 ICLN_HUMAN Pfam-B_77655 PB077655 1-34, Voldacs PF03517 35-165 Clns1a 109638 Q61189 ICLN_MOUSE # # Histone modification write cofactor Histone methylation # methylosome # # # # # Part of the methylosome complex
CLOCK
(details)
# 2082 clock circadian regulator 9575 O15516 CLOCK_HUMAN HLH PF00010 35-85, PAS PF00989 109-188, PAS_11 PF14598 273-381, Pfam-B_3081 PB003081 721-839, Pfam-B_7827 PB007827 571-719, Pfam-B_8264 PB008264 382-429 Clock 99698 O08785 CLOCK_MOUSE KAT, bHLH Chromatin-modifying enzymes / K-acetyltransferases, Basic helix-loop-helix proteins Histone modification write Histone acetylation # # histone H3, H4 # # # Acetylates primarily histones H3 and H4. (Annotated by similarity.)
CRB2
(details)
# 18688 crumbs family member 2 286204 Q5IJ48 CRUM2_HUMAN EGF PF00008 112-142 150-180 227-257 324-354 362-392 811-841 1060-1090, Laminin_G_2 PF02210 465-588 900-1033, Pfam-B_3557 PB003557 1199-1283, Pfam-B_79172 PB079172 1119-1197, hEGF PF12661 305-317 Crb2 2679260 Q80YA8 CRUM2_MOUSE # # Histone modification read # 21423274 # histone H4K20 # # 21423274 Table 1 in the reference.
CREBBP
(details)
# 2348 CREB binding protein 1387 Q92793 CBP_HUMAN Bromodomain PF00439 1094-1180, Creb_binding PF09030 2016-2115, DUF902 PF06001 1191-1232, KAT11 PF08214 1342-1648, KIX PF02172 587-667, Pfam-B_2669 PB002669 2188-2217, Pfam-B_817 PB000817 2353-2401, ZZ PF00569 1701-1742, zf-TAZ PF02135 352-432 1770-1843 Crebbp 1098280 P45481 CBP_MOUSE KAT Chromatin-modifying enzymes / K-acetyltransferases Histone modification write Histone acetylation 8945521 # histone # # # 8945521 The transcriptional coactivators p300 and CBP=CREBBP are histone acetyltransferases.
CSNK2A1
(details)
New 2457 casein kinase 2, alpha 1 polypeptide 1457 P68400 CSK21_HUMAN Pkinase PF00069 39-324 Csnk2a1 88543 Q60737 CSK21_MOUSE # # Histone modification # 24217316, 22325352 RING2-FBRS histone # # # 24217316, 22325352 Part of a RING2 complex.
CSRP2BP
(details)
# 15904 CSRP2 binding protein 57325 Q9H8E8 CSR2B_HUMAN Acetyltransf_1 PF00583 678-752, Pfam-B_6449 PB006449 351-435, Pfam-B_8520 PB008520 1-129 Csrp2bp 1917264 Q8CID0 CSR2B_MOUSE # # Histone modification write Histone acetylation 19103755 ATAC histone H4 # # 19103755 The SANT domains in ADA2a and ZZZ3/ATAC1 might enable the complex to associate with nucleosome tails in order to potentiate the catalytic activities of GCN5 and ATAC2, similar to what has been shown for the SANT domains in yeast Ada2 and Swi3.
CTBP1
(details)
# 2494 C-terminal binding protein 1 1487 Q13363 CTBP1_HUMAN 2-Hacid_dh PF00389 30-352, 2-Hacid_dh_C PF02826 133-317 Ctbp1 1201685 O88712 CTBP1_MOUSE # # Chromatin remodelling # 21102443 LSD-CoREST chromatin # # # 21102443 CtBP is a homodimer or heterodimer of CtBP1 and CtBP2 that assembles with a diverse array of factors that regulate chromatin structure.
CTBP2
(details)
# 2495 C-terminal binding protein 2 1488 P56545 CTBP2_HUMAN 2-Hacid_dh PF00389 36-358, 2-Hacid_dh_C PF02826 139-323 Ctbp2 1201686 P56546 CTBP2_MOUSE # # Histone modification write cofactor Histone methylation 16702210 # histone H3K9 H3K9me, H3K9me2 # 16702210 It is possible that CtBPs or CtBP-interacting molecules have various impacts on the G9a/GLP-mediated (a SET-domain mammalian histone methyltransferase responsible for mono- and dimethylation of lysine 9 in histone H3 (H3K9)) functions through Wiz interaction.
CTCF
(details)
# 13723 CCCTC-binding factor (zinc finger protein) 10664 P49711 CTCF_HUMAN Pfam-B_18810 PB018810 671-725, zf-C2H2 PF00096 437-460, zf-C2H2_4 PF13894 555-578, zf-H2C2_2 PF13465 280-305 308-333 336-362 365-389 393-418 481-506 507-534 Ctcf 109447 Q61164 CTCF_MOUSE ZNF Zinc fingers, C2H2-type Chromatin remodelling, TF #, TF activator 16949368 # DNA DNA motif # # 16949368 A CTCF-CHD8 complex is involved in both enhancer blocking and epigenetic remodeling at chromatin boundary in vivo.
CTCFL
(details)
# 16234 CCCTC-binding factor (zinc finger protein)-like 140690 Q8NI51 CTCFL_HUMAN Pfam-B_37192 PB037192 1-49, Pfam-B_59982 PB059982 611-659, zf-C2H2 PF00096 428-451 546-568, zf-H2C2_2 PF13465 271-296 299-324 327-353 356-380 384-409 472-497 500-525 Ctcfl 3652571 A2APF3 CTCFL_MOUSE ZNF Zinc fingers, C2H2-type Chromatin remodelling # 18765639 # DNA # # # 18765639 BORIS=CTCFL acts as a scaffold upon which BAT3 and SET1A assemble and through which BAT3 and SET1A exert their effects upon chromatin structure and gene expression. In contrast to CTCF, BORIS appears to be a methylation-independent DNA-binding protein (28b) that activates, rather than inhibits, gene expression.
CTR9
(details)
New 16850 CTR9, Paf1/RNA polymerase II complex component 9646 Q6PD62 CTR9_HUMAN Pfam-B_9491 PB009491 5-42, TPR_1 PF00515 163-196 198-231 306-339 342-374 498-530 531-564 681-710, TPR_2 PF07719 451-483 Ctr9 109345 Q62018 CTR9_MOUSE TTC Tetratricopeptide (TTC) repeat domain containing Histone modification cofactor # 24036311 # histone H3K36 # # # CTR9/PAF1c regulates molecular lineage identity, histone H3K36 trimethylation and genomic imprinting during preimplantation development.
CUL1
(details)
# 2551 cullin 1 8454 Q13616 CUL1_HUMAN Cullin PF00888 21-707, Cullin_Nedd8 PF10557 703-770 Cul1 1349658 Q9WTX6 CUL1_MOUSE # # Chromatin remodelling cofactor # 9663463 # histone H3K9me3, H3K36me3, H1.4K26me3 H3K9, H3K36, H1.4K26 # 21757720 The SKP1-Cul1-F-box and leucine-rich repeat protein 4 (SCF-FbxL4) ubiquitin ligase regulates lysine demethylase 4A (KDM4A)/Jumonji domain-containing 2A (JMJD2A) protein. The JMJD2/KDM43 histone demethylase family removes trimethylated H3K9, H3K36, and H1.4K26 .
CUL2
(details)
# 2552 cullin 2 8453 Q13617 CUL2_HUMAN Cullin PF00888 14-645, Cullin_Nedd8 PF10557 672-739 Cul2 1918995 Q9D4H8 CUL2_MOUSE # # Chromatin remodelling cofactor # # # chromatin HP1 (Heterochromatin protein 1) # # 9122164 The VHL-HP1 (heterochromatin protein 1) interaction recruits VHL to chromatin. VHL interacts with elongin B, elongin C, and cullin 2 through its α domain and these proteins form an E3 ubiquitin ligase complex.
CUL3
(details)
# 2553 cullin 3 8452 Q13618 CUL3_HUMAN Cullin PF00888 34-666, Cullin_Nedd8 PF10557 695-762 Cul3 1347360 Q9JLV5 CUL3_MOUSE # # Histone modification write Histone ubiquitination 15897469 # histone MACROH2A # # 15897469 E3 ubiquitin ligase consisting of SPOP and CULLIN3=CUL3 is able to ubiquitinate the Polycomb group protein BMI1 and the variant histone MACROH2A.
CUL4A
(details)
# 2554 cullin 4A 8451 Q13619 CUL4A_HUMAN Cullin PF00888 63-661, Cullin_Nedd8 PF10557 688-753 Cul4a 1914487 Q3TCH7 CUL4A_MOUSE # # Histone modification write Histone ubiquitination 16678110 # histone H3, H4 # # 16678110 Results shown in Figure 4A demonstrate that knockdown of CUL4A or CUL4B significantly reduces H3 and H4 ubiquitylation levels, indicating that both CUL4A and CUL4B contribute to histone H3 and H4 ubiquitylation in vivo.
CUL4B
(details)
# 2555 cullin 4B 8450 Q13620 CUL4B_HUMAN Cullin PF00888 217-815, Cullin_Nedd8 PF10557 842-907 Cul4b 1919834 A2A432 CUL4B_MOUSE # # Histone modification write Histone ubiquitination 16678110 # histone H3, H4 # # 16678110 Results shown in Figure 4A demonstrate that knockdown of CUL4A or CUL4B significantly reduces H3 and H4 ubiquitylation levels, indicating that both CUL4A and CUL4B contribute to histone H3 and H4 ubiquitylation in vivo.
CUL5
(details)
# 2556 cullin 5 8065 Q93034 CUL5_HUMAN Cullin PF00888 19-673, Cullin_Nedd8 PF10557 707-774 Cul5 1922967 Q9D5V5 CUL5_MOUSE # # DNA modification cofactor DNA methylation 20847044 # DNA # # # 20847044 In cancer cells, many promoters become aberrantly methylated through the activity of the de novo DNA methyltransferases DNMT3a and DNMT3b and acquire repressive chromatin marks, and, indeed, DNMT3b interacted with CUL1, CUL2, CUL3, CUL4A, and CUL5.
CXXC1
(details)
# 24343 CXXC finger protein 1 30827 Q9P0U4 CXXC1_HUMAN PHD PF00628 28-76, zf-CXXC PF02008 160-208, zf-CpG_bind_C PF12269 400-636 Cxxc1 1921572 Q9CWW7 CXXC1_MOUSE PHF Zinc fingers, PHD-type Chromatin remodelling, TF #, # 21407193 COMPASS DNA CG, DNA motif # # 21407193 CFP1=CXXC1 is a CXXC domain-containing protein. CXXC domain proteins direct different chromatin-modifying activities to various chromatin regions.
DAPK3
(details)
# 2676 death-associated protein kinase 3 1613 O43293 DAPK3_HUMAN Pkinase PF00069 13-275 Dapk3 1203520 O54784 DAPK3_MOUSE # # Histone modification write Histone phosphorylation 12560483 # histone H3T11 # # 12560483 Dlk/ZIP=DAPK3 kinase phosphorylates histone H3 at a novel site, Thr11, rather than Ser10, which is characteristic of mitotic chromosomes.
DAXX
(details)
New 2681 death-domain associated protein 1616 Q9UER7 DAXX_HUMAN Daxx PF03344 1-740 Daxx 1197015 O35613 DAXX_MOUSE # # # # 23075851 # histone H3.3 # # # DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition.
DDB1
(details)
# 2717 damage-specific DNA binding protein 1, 127kDa 1642 Q16531 DDB1_HUMAN CPSF_A PF03178 788-1099, MMS1_N PF10433 75-546, Pfam-B_431 PB000431 585-732 Ddb1 1202384 Q3U1J4 DDB1_MOUSE # # Histone modification write Histone ubiquitination 16678110 # histone H2A # # 16678110 DDB1-CUL4ADDB2 E3 in vivo targets histone H2A for ubiquitination at UV-damage DNA sites, where DDB2 serves as the substrate receptor.
DDB2
(details)
# 2718 damage-specific DNA binding protein 2, 48kDa 1643 Q92466 DDB2_HUMAN WD40 PF00400 112-140 232-271 284-316 Ddb2 1355314 Q99J79 DDB2_MOUSE WDR WD repeat domain containing Histone modification write cofactor Histone ubiquitination 16678110 # histone # # # 16678110 DDB1-CUL4ADDB2 E3 in vivo targets histone H2A for ubiquitination at UV-damage DNA sites, where DDB2 serves as the substrate receptor.
DDX21
(details)
# 2744 DEAD (Asp-Glu-Ala-Asp) box helicase 21 9188 Q9NR30 DDX21_HUMAN DEAD PF00270 210-385, GUCT PF08152 620-716, Helicase_C PF00271 458-532, Pfam-B_47445 PB047445 1-39 Ddx21 1860494 Q9JIK5 DDX21_MOUSE DDX DEAD-boxes RNA modification # 11237763 B-WICH RNA # # # 11237763 Human RNA helicase II/Gu (hRH II/Gu) protein unwinds double-stranded RNA, folds single-stranded RNA, and may play important roles in ribosomal RNA biogenesis, RNA editing, RNA transport, and general transcription.
DDX50
(details)
# 17906 DEAD (Asp-Glu-Ala-Asp) box polypeptide 50 79009 Q9BQ39 DDX50_HUMAN DEAD PF00270 161-336, GUCT PF08152 571-666, Helicase_C PF00271 409-483 Ddx50 2182303 Q99MJ9 DDX50_MOUSE DDX DEAD-boxes RNA modification # 11823437 # RNA # # # 11823437 In addition to the proposed role of DEAD-box RNA helicases in transcription, some of these enzymes promote mRNA translation.
DEK
(details)
# 2768 DEK proto-oncogene 7913 P35659 DEK_HUMAN DEK_C PF08766 321-375, Pfam-B_10960 PB010960 191-269, SAP PF02037 149-183 Dek 1926209 Q7TNV0 DEK_MOUSE # # Chromatin remodelling # 17524367 B-WICH histone H4 # # 17524367 It has been suggested that DEK functions as an “architectural” protein in chromatin. This is because DEK changes the structure of the DNA to which it is bound and could therefore influence gene activity.
DMAP1
(details)
# 18291 DNA methyltransferase 1 associated protein 1 55929 Q9NPF5 DMAP1_HUMAN DMAP1 PF05499 243-407 Dmap1 1913483 Q9JI44 DMAP1_MOUSE # # Chromatin remodelling # 14966270 NuA4, NuA4-related complex, SRCAP chromatin # # # 14966270 SANT-domain protein DMAP1 links NuA4 to DNA replication and is also present in distinct proteins
DNAJC1
(details)
# 20090 DnaJ (Hsp40) homolog, subfamily C, member 1 64215 Q96KC8 DNJC1_HUMAN DnaJ PF00226 65-126, Myb_DNA-binding PF00249 494-543, Pfam-B_8255 PB008255 367-413 Dnajc1 103268 Q61712 DNJC1_MOUSE DNAJ Heat shock proteins / DNAJ (HSP40) Histone modification write cofactor, Histone modification erase cofactor Histone acetylation, Histone deacetylation 16271702 # histone # # # 16271702 HTJ1=DNAJC1 consists of two SANT domains separated by a spacer region. SANT domains can also mediate protein–protein interaction, particularly with histone deacetylases and histone acetyl transferases.
DNAJC2
(details)
# 13192 DnaJ (Hsp40) homolog, subfamily C, member 2 27000 Q99543 DNJC2_HUMAN DnaJ PF00226 88-158, Myb_DNA-binding PF00249 451-506 552-600, Pfam-B_24524 PB024524 28-59, Pfam-B_30652 PB030652 1-27 Dnajc2 99470 P54103 DNJC2_MOUSE DNAJ Heat shock proteins / DNAJ (HSP40) Histone modification read # 21179169 # histone H2A # # 21179169 The ubiquitin mark at histone H2A may be a docking site for ZRF1.
DND1
(details)
# 23799 DND microRNA-mediated repression inhibitor 1 373863 Q8IYX4 DND1_HUMAN DND1_DSRM PF14709 253-333, RRM_1 PF00076 60-126 Dnd1 2447763 Q6VY05 DND1_MOUSE RBM RNA binding motif (RRM) containing RNA modification # 23890083 # RNA # # # 23890083 The RNA binding protein DEAD-END (DND1) is one of the few proteins known to regulate microRNA (miRNA) activity at the level of miRNA-mRNA interaction. APOBEC3G may bind mRNAs (maybe together with DND1) and subsequently interact with components of the miRISC to activate translation repression or interact with translation initiation factors to inhibit them. APOBEC3G may bind to DND1 and sequester it away from mRNAs and miRNAs, the cytidine deaminase activity of APOBEC3 may allow it to edit the 3′-UTR sequences of P27, LATS2 and CX43 to inhibit DND1 binding.
DNMT1
(details)
# 2976 DNA (cytosine-5-)-methyltransferase 1 1786 P26358 DNMT1_HUMAN BAH PF01426 755-880 931-1100, DMAP_binding PF06464 16-105, DNA_methylase PF00145 1139-1594, DNMT1-RFD PF12047 399-534, zf-CXXC PF02008 645-691 Dnmt1 94912 P13864 DNMT1_MOUSE # # DNA modification DNA methylation 18754681 # DNA dhC dhU # 18754681 The CXXC region (C is cysteine; X is any amino acid) of DNMT1 binds specifically to unmethylated CpG dinucleotides. Thus, the CXXC domain encompassing the amino terminus region of DNMT1 cooperates with the catalytic domain for DNA methyltransferase activity.
DNMT3A
(details)
# 2978 DNA (cytosine-5-)-methyltransferase 3 alpha 1788 Q9Y6K1 DNM3A_HUMAN DNA_methylase PF00145 634-776, PWWP PF00855 290-375 Dnmt3a 1261827 O88508 DNM3A_MOUSE # # DNA modification DNA methylation 12138111 # DNA dhC dhU # 12138111 One form of Dnmt3a has been identified and shown to be capable of methylating DNA bothin vitro and in vivo.
DNMT3B
(details)
# 2979 DNA (cytosine-5-)-methyltransferase 3 beta 1789 Q9UBC3 DNM3B_HUMAN DNA_methylase PF00145 575-725, PWWP PF00855 223-308 Dnmt3b 1261819 O88509 DNM3B_MOUSE # # DNA modification DNA methylation 10325416 # DNA dhC dhU # 10325416 DNA methyltransferases (Dnmt3a and Dnmt3b) in mouse methylate hemimethylated and unmethylated templates with equal efficiencies and are candidates for de novo methyltransferases.
DNMT3L
(details)
# 2980 DNA (cytosine-5-)-methyltransferase 3-like 29947 Q9UJW3 DNM3L_HUMAN Pfam-B_139748 PB139748 181-229, Pfam-B_41249 PB041249 91-179 Dnmt3l 1859287 Q9CWR8 DNM3L_MOUSE # # Histone modification read # 17687327 # histone H3K4 # # 17687327 DNMT3L specifically interacts with the extreme amino terminus of histone H3, this interaction is strongly inhibited by methylation at lysine 4 of histone H3.
DNTTIP2
(details)
# 24013 deoxynucleotidyltransferase, terminal, interacting protein 2 30836 Q5QJE6 TDIF2_HUMAN Fcf2 PF08698 635-731 Dnttip2 1923173 Q8R2M2 TDIF2_MOUSE # # Chromatin remodelling # 12786946 # histone H2A, H2B # # 12786946 TdIF2 would function as a chromatin remodeling protein at the N region synthesis.
DOT1L
(details)
# 24948 DOT1-like histone H3K79 methyltransferase 84444 Q8TEK3 DOT1L_HUMAN DOT1 PF08123 115-317, Pfam-B_30738 PB030738 501-539 Dot1l 2143886 - - KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation 12123582 # histone H3K79 # # 12123582 Human DOT1-like (DOT1L) protein possesses intrinsic H3-K79-specific histone methyltransferase (HMTase) activity in vitro and in vivo.
DPF1
(details)
# 20225 D4, zinc and double PHD fingers family 1 # Q92782 DPF1_HUMAN PHD PF00628 256-311 310-368, Pfam-B_77905 PB077905 1-37, Requiem_N PF14051 38-111 Dpf1 1352748 Q9QX66 DPF1_MOUSE PHF Zinc fingers, PHD-type Chromatin remodelling cofactor # 21931736 nBAF, SWI/SNF BRM-BRG1 chromatin # # # 21931736 Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). Baf45b=DPF1 and Baf53b are both brain specific components of the SWI/SNF complex varaint nBAF.
DPF2
(details)
# 9964 D4, zinc and double PHD fingers family 2 5977 Q92785 REQU_HUMAN PHD PF00628 272-330 329-376, Requiem_N PF14051 12-85 Dpf2 109529 Q61103 REQU_MOUSE PHF Zinc fingers, PHD-type Chromatin remodelling # 21888896 SWI/SNF BRM-BRG1 histone, DNA # # # 21888896 The different domains of DPF2 may function in a cooperative manner in some intracellular processes, which could bind histone and DNA via tandem PHD domain and C2H2 ZF domain, respectively in the context of nucleosome.
DPF3
(details)
# 17427 D4, zinc and double PHD fingers, family 3 8110 Q92784 DPF3_HUMAN PHD PF00628 261-319 318-366, Requiem_N PF14051 12-85 Dpf3 1917377 P58269 DPF3_MOUSE PHF Zinc fingers, PHD-type Chromatin remodelling # 21423274 BAF, nBAF, SWI/SNF BRM-BRG1 histone H3, H4 # # 21423274 Table 1 in the reference. DPF3 is associated with the BAF chromatin remodeling complex and binds methylated and acetylated lysine residues of histone 3 and 4.
DPPA3
(details)
# 19199 developmental pluripotency associated 3 359787 Q6W0C5 DPPA3_HUMAN PGC7_Stella PF15549 1-155 Dppa3 1920958 Q8QZY3 DPPA3_MOUSE # # Histone modification read # # # histone H3K9me2 # # # Specifically recognizes and binds histone H3 dimethylated at 'Lys-9' (H3K9me2) on maternal genome,
DPY30
(details)
# 24590 dpy-30 homolog (C. elegans) 84661 Q9C005 DPY30_HUMAN Dpy-30 PF05186 52-93, Pfam-B_28037 PB028037 1-51 Dpy30 1913560 Q99LT0 DPY30_MOUSE # # Histone modification write cofactor Histone methylation 19556245 COMPASS, Menin-associated_HMT, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7, COMPASS-like MLL3,4 histone # # # 19556245 The isolated MLL1 SET domain is an H3K4 monomethyltransferase. When the MLL1 SET domain fragment is assembled with a complex containing WDR5, RbBP5, Ash2L, and DPY-30, the rate of lysine methylation is dramatically increased, but only to the dimethyl form of H3K4, suggesting that the MLL1 core complex is predominantly a dimethyltransferase.
DR1
(details)
# 3017 down-regulator of transcription 1, TBP-binding (negative cofactor 2) 1810 Q01658 NC2B_HUMAN CBFD_NFYB_HMF PF00808 11-75 Dr1 1100515 Q91WV0 NC2B_MOUSE # # Histone chaperone # 18838386 ATAC histone # # # 18838386 YEATS2-NC2beta=DR1 histone fold module that interacts with the TATA-binding protein (TBP) and negatively regulates transcription when recruited to a promoter.
DTX3L
(details)
# 30323 deltex 3 like, E3 ubiquitin ligase 151636 Q8TDB6 DTX3L_HUMAN Pfam-B_11420 PB011420 311-389 706-737, zf-RING_2 PF13639 559-600 Dtx3l 2656973 Q3UIR3 DTX3L_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write Histone ubiquitination 19818714 # histone H4K91 # # 19818714 BBAP=DTX3L selectively monoubiquitylates histone H4 lysine 91 and protects cells exposed to DNA-damaging agents.
DZIP3
(details)
# 30938 DAZ interacting zinc finger protein 3 9666 Q86Y13 DZIP3_HUMAN Pfam-B_10362 PB010362 531-619, Pfam-B_5525 PB005525 201-419, Pfam-B_5636 PB005636 1-199, Pfam-B_8501 PB008501 621-773, Pfam-B_8729 PB008729 421-529, zf-RING_2 PF13639 1146-1188 Dzip3 1917433 Q7TPV2 DZIP3_MOUSE RNF, PPP1R RING-type (C3HC4) zinc fingers, Serine/threonine phosphatases / Protein phosphatase 1, regulatory subunits Histone modification write Histone ubiquitination 18206970 # histone, RNA H2AK119 H2AK119ub # 18206970 The N-CoR/HDAC1/3 complex specifically recruits a previously-unidentified specific histone H2A ubiquitin ligase, 2A-HUB/hRUL138 = DZIP3, to a subset of regulated gene promoters.
E2F6
(details)
# 3120 E2F transcription factor 6 1876 O75461 E2F6_HUMAN E2F_TDP PF02319 63-128 E2f6 1354159 O54917 E2F6_MOUSE # # TF TF repressor # RING2-L3MBTL2, CHD8, MLL2/3, MLL4/WBP7 DNA DNA motif # # # Epigenetic complex (MLL) partner.
EED
(details)
# 3188 embryonic ectoderm development 8726 O75530 EED_HUMAN Pfam-B_26038 PB026038 1-39, Pfam-B_6684 PB006684 265-359, WD40 PF00400 180-219 231-264 Eed 95286 Q921E6 EED_MOUSE WDR WD repeat domain containing Polycomb group (PcG) protein # 9584199 PRC2 # # # # 9584199 Enx1/EZH2 and EED are members of a class of PcG proteins that is distinct from previously described human PcG proteins.
EHMT1
(details)
# 24650 euchromatic histone-lysine N-methyltransferase 1 79813 Q9H9B1 EHMT1_HUMAN Ank_2 PF12796 742-836 810-903 910-998, Ank_4 PF13637 773-826 839-893, Pfam-B_28560 PB028560 1-98, Pre-SET PF05033 1013-1118, SET PF00856 1137-1243 Ehmt1 1924933 Q5DW34 EHMT1_MOUSE KMT, ANKRD Chromatin-modifying enzymes / K-methyltransferases, Ankyrin repeat domain containing Histone modification write Histone methylation 18264113 # histone H3K9 H3K9me1, H3K9me2 # 18264113 G9a and G9a-like protein (GLP)=EHMT1 are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9).
EHMT2
(details)
# 14129 euchromatic histone-lysine N-methyltransferase 2 10919 Q96KQ7 EHMT2_HUMAN Ank PF00023 684-716 717-748 750-783 784-816 818-849 850-882, Pfam-B_9355 PB009355 34-359, Pre-SET PF05033 925-1030, SET PF00856 1049-1155 Ehmt2 2148922 Q9Z148 EHMT2_MOUSE KMT, ANKRD Chromatin-modifying enzymes / K-methyltransferases, Ankyrin repeat domain containing Histone modification write Histone methylation 18264113 # histone H3K9 H3K9me1, H3K9me2 # 18264113 G9a=EHMT2 and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9).
EID1
(details)
# 1191 EP300 interacting inhibitor of differentiation 1 23741 Q9Y6B2 EID1_HUMAN Pfam-B_5729 PB005729 1-159 Eid1 1889651 Q9DCR4 EID1_MOUSE # # Histone modification write cofactor Histone acetylation 11073990 # histone # # # 11073990 Inhibition of MyoD may be explained by EID-1's ability to bind and inhibit p300's histone acetylase activity, an essential MyoD coactivator. Thus, EID-1 binds both Rb and p300 and is a novel repressor of MyoD function.
EID2
(details)
# 28292 EP300 interacting inhibitor of differentiation 2 163126 Q8N6I1 EID2_HUMAN Pfam-B_42536 PB042536 111-199, Pfam-B_7728 PB007728 1-109 201-234 Eid2 2681174 Q6X7S9 EID2_MOUSE # # Histone modification write cofactor Histone acetylation 14585496 # histone # # # 14585496 Overexpression of EID-2 inhibits muscle-specific gene expression through inhibition of MyoD-dependent transcription. This inhibitory effect on gene expression can be explained by EID-2's ability to associate with and inhibit the acetyltransferase activity of p300. These data suggest that EID-1 and -2 represent a novel family of proteins that negatively regulate differentiation through a p300-dependent mechanism.
EID2B
(details)
# 26796 EP300 interacting inhibitor of differentiation 2B 126272 Q96D98 EID2B_HUMAN # Eid2b 1924095 # # # # Histone modification erase cofactor Histone acetylation 15970276 # histone # # # 15970276 The transrepressional function of EID-2 depends on recruitment of class I histone deacetylases (HDACs). HDACs participate in the dynamic process of chromatin remodeling, forming corepressor complexes that repress transcription by deacetylating histones and transcription factors.
ELP2
(details)
# 18248 elongator acetyltransferase complex subunit 2 55250 Q6IA86 ELP2_HUMAN WD40 PF00400 48-91 99-143 197-237 274-320 378-416 557-587 604-642 662-697 Elp2 1889642 Q91WG4 ELP2_MOUSE ELP, WDR Elongator acetyltransferase complex subunits, WD repeat domain containing Histone modification write cofactor Histone acetylation 11818576 Pol2 elongator histone # # # 11818576 Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation.
ELP3
(details)
# 20696 elongator acetyltransferase complex subunit 3 55140 Q9H9T3 ELP3_HUMAN Acetyltransf_1 PF00583 441-536, Pfam-B_13823 PB013823 1-49, Radical_SAM PF04055 96-305 Elp3 1921445 Q9CZX0 ELP3_MOUSE KAT, ELP Chromatin-modifying enzymes / K-acetyltransferases, Elongator acetyltransferase complex subunits Histone modification write Histone acetylation 11818576 Pol2 elongator histone H3, H4? # # 11818576 Elp3 contains domains characteristic of proteins with acetyltransferase activity, and its complex was found to acetylate histones, with specificity to H3 and to a much lesser extent H4.
ELP4
(details)
# 1171 elongator acetyltransferase complex subunit 4 26610 Q96EB1 ELP4_HUMAN PAXNEB PF05625 27-424 Elp4 1925016 Q9ER73 ELP4_MOUSE ELP Elongator acetyltransferase complex subunits Histone modification write cofactor Histone acetylation 11714725 Pol2 elongator histone # # # 11714725 The three small holo-Elongator subunits, hELP4, p38, and p30, are required to activate the HAT activity of hELP3, or one of these proteins may have intrinsic HAT activity.
ELP5
(details)
# 30617 elongator acetyltransferase complex subunit 5 23587 Q8TE02 ELP5_HUMAN Elong_Iki1 PF10483 17-298 Elp5 1859017 Q99L85 ELP5_MOUSE ELP Elongator acetyltransferase complex subunits Histone modification write cofactor Histone acetylation 11904415 Pol2 elongator histone H3K14, H4K8 # # 11904415 The elongating, hyperphosphorylated form of RNA polymerase II is associated with the Elongator complex, which has the histone acetyltransferase (HAT) Elp3 as a subunit. The three smallest Elongator subunits--Elp4, Elp5, and Elp6--are required for HAT activity, and Elongator binds to both naked and nucleosomal DNA. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4.
ELP6
(details)
# 25976 elongator acetyltransferase complex subunit 6 54859 Q0PNE2 ELP6_HUMAN DUF2348 PF09807 1-251 Elp6 1919349 Q8BK75 ELP6_MOUSE ELP Elongator acetyltransferase complex subunits Histone modification write cofactor Histone acetylation 22854966 Pol2 elongator histone # # # 22854966 The Elongator complex is composed of 6 subunits (Elp1-Elp6) and promotes RNAPII transcript elongation through histone acetylation in the nucleus as well as tRNA modification in the cytoplasm. DERP6/ELP5 and C3ORF75/ELP6 are key players for migration, invasion and tumorigenicity of melanoma cells, as integral subunits of Elongator.
ENY2
(details)
# 24449 enhancer of yellow 2 homolog (Drosophila) 56943 Q9NPA8 ENY2_HUMAN EnY2 PF10163 11-96 Eny2 1919286 Q9JIX0 ENY2_MOUSE # # Histone modification erase cofactor Histone ubiquitination 18206972 SAGA histone # # # 18206972 ATXN7L3, USP22, and ENY2 are required as cofactors for the full transcriptional activity by nuclear receptors. Thus, the deubiquitinase activity of the TFTC/STAGA HAT complex is necessary to counteract heterochromatin silencing and acts as a positive cofactor for activation by nuclear receptors in vivo.
EP300
(details)
# 3373 E1A binding protein p300 2033 Q09472 EP300_HUMAN Bromodomain PF00439 1058-1144, Creb_binding PF09030 1990-2099, DUF902 PF06001 1155-1196, KAT11 PF08214 1306-1612, KIX PF02172 566-646, Pfam-B_15526 PB015526 1-129, Pfam-B_817 PB000817 2317-2349, ZZ PF00569 1664-1705, zf-TAZ PF02135 336-416 1733-1806 Ep300 1276116 B2RWS6 EP300_MOUSE KAT Chromatin-modifying enzymes / K-acetyltransferases Histone modification write Histone acetylation 17065153 # histone H2A, H2B, H3, H4 # # 17065153 Acetylation of proteins by p300=EP300 histone acetyltransferase plays a critical role in the regulation of gene expression.
EP400
(details)
# 11958 E1A binding protein p400 57634 Q96L91 EP400_HUMAN HSA PF07529 800-871, Helicase_C PF00271 1932-2014, Pfam-B_18422 PB018422 1887-1923, SNF2_N PF00176 1094-1374 Ep400 1276124 Q8CHI8 EP400_MOUSE # # Chromatin remodelling, Histone modification write #, Histone acetylation 20876283 SWR, NuA4, NuA4-related complex histone # # # 20876283 p400 is a novel DNA damage response protein and p400-mediated alterations in nucleosome and chromatin structure promote both chromatin ubiquitination and the accumulation of brca1 and 53BP1 at sites of DNA damage.
EPC1
(details)
# 19876 enhancer of polycomb homolog 1 (Drosophila) 80314 Q9H2F5 EPC1_HUMAN EPL1 PF10513 6-149, E_Pc_C PF06752 582-836 Epc1 1278322 Q8C9X6 EPC1_MOUSE # # Polycomb group (PcG) protein # 14966270 NuA4, Piccolo_NuA4, NuA4-related complex histone # # # 14966270 The Enhancer of Polycomb homology domain of human EPC1, like Epl1 in yeast (7), is a conserved functional key for histone acetylation since it bridges the MYST HAT with the ING protein to enable potent nucleosome histone acetyltransferase activity.
EPC2
(details)
New 24543 enhancer of polycomb homolog 2 (Drosophila) 26122 Q52LR7 EPC2_HUMAN EPL1 PF10513 6-149, E_Pc_C PF06752 577-807, Pfam-B_18248 PB018248 432-544, Pfam-B_19406 PB019406 370-415 Epc2 1278321 Q8C0I4 EPC2_MOUSE # # Chromatin remodelling # 19898529 # chromatin # # # # NuA4 and SWR1-C: two chromatin-modifying complexes with overlapping functions and components
ERBB4
(details)
# 3432 v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4 2066 Q15303 ERBB4_HUMAN Furin-like PF00757 176-335, GF_recep_IV PF14843 502-634, Pfam-B_10445 PB010445 1236-1306, Pkinase_Tyr PF07714 718-974, Recep_L_domain PF01030 55-167 358-478 Erbb4 104771 Q61527 ERBB4_MOUSE # # Histone modification cofactor # 23230144 # histone H3K9me3 # # 23230144 ErbB4 intracellular domain (4ICD) that translocates into the nucleus to control gene expression through inhibiting an increase of H3K9me3.
ERCC6
(details)
# 3438 excision repair cross-complementation group 6 2074 Q03468 ERCC6_HUMAN Helicase_C PF00271 873-952, Pfam-B_58020 PB058020 1-49, SNF2_N PF00176 510-812 Ercc6 1100494 # # # # Chromatin remodelling # 15226310 B-WICH chromatin # # # 15226310 CSB=ERCC6 is a DNA-dependent ATPase and is able to remodel chromatin at the expense of ATP.
EXOSC1
(details)
# 17286 exosome component 1 51013 Q9Y3B2 EXOS1_HUMAN ECR1_N PF14382 7-41, EXOSC1 PF10447 64-135 Exosc1 1913833 Q9DAA6 EXOS1_MOUSE # # Scaffold protein, RNA modification #, RNA degradation 17174896 RNA exosome RNA # # # 17174896 RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA.
EXOSC2
(details)
# 17097 exosome component 2 23404 Q13868 EXOS2_HUMAN ECR1_N PF14382 26-64 Exosc2 2385133 Q8VBV3 EXOS2_MOUSE # # Scaffold protein, RNA modification #, RNA degradation 17174896 RNA exosome RNA # # # 17174896 RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA.
EXOSC3
(details)
# 17944 exosome component 3 51010 Q9NQT5 EXOS3_HUMAN Pfam-B_7181 PB007181 221-267 Exosc3 1913612 Q7TQK4 EXOS3_MOUSE # # Scaffold protein, RNA modification #, RNA degradation 17174896 RNA exosome RNA # # # 17174896 RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA.
EXOSC4
(details)
# 18189 exosome component 4 54512 Q9NPD3 EXOS4_HUMAN Pfam-B_25613 PB025613 221-243, RNase_PH PF01138 21-152, RNase_PH_C PF03725 155-220 Exosc4 1923576 Q921I9 EXOS4_MOUSE # # Scaffold protein, RNA modification #, RNA degradation 17174896 RNA exosome RNA # # # 17174896 RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA.
EXOSC5
(details)
# 24662 exosome component 5 56915 Q9NQT4 EXOS5_HUMAN RNase_PH PF01138 27-147, RNase_PH_C PF03725 150-216 Exosc5 107889 Q9CRA8 EXOS5_MOUSE # # Scaffold protein, RNA modification #, RNA degradation 17174896 RNA exosome RNA # # # 17174896 RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA.
EXOSC6
(details)
# 19055 exosome component 6 118460 Q5RKV6 EXOS6_HUMAN RNase_PH PF01138 35-175 Exosc6 1919794 Q8BTW3 EXOS6_MOUSE # # Scaffold protein, RNA modification #, RNA degradation 17174896 RNA exosome RNA # # # 17174896 RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA.
EXOSC7
(details)
# 28112 exosome component 7 23016 Q15024 EXOS7_HUMAN RNase_PH PF01138 31-166, RNase_PH_C PF03725 196-262 Exosc7 1913696 Q9D0M0 EXOS7_MOUSE # # Scaffold protein, RNA modification #, RNA degradation 17174896 RNA exosome RNA # # # 17174896 RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA.
EXOSC8
(details)
# 17035 exosome component 8 11340 Q96B26 EXOS8_HUMAN RNase_PH PF01138 31-166, RNase_PH_C PF03725 191-258 Exosc8 1916889 Q9D753 EXOS8_MOUSE # # Scaffold protein, RNA modification #, RNA degradation 17174896 RNA exosome RNA # # # 17174896 RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA.
EXOSC9
(details)
# 9137 exosome component 9 5393 Q06265 EXOS9_HUMAN RNase_PH PF01138 31-163, RNase_PH_C PF03725 189-256 Exosc9 1355319 Q9JHI7 EXOS9_MOUSE # # Scaffold protein, RNA modification #, RNA degradation 17174896 RNA exosome RNA # # # 17174896 RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA.
EYA1
(details)
# 3519 EYA transcriptional coactivator and phosphatase 1 2138 Q99502 EYA1_HUMAN Pfam-B_10178 PB010178 530-586, Pfam-B_3150 PB003150 209-513 Eya1 109344 P97767 EYA1_MOUSE PTPE Protein tyrosine phosphatases / Asp-based PTPs Histone modification erase Histone phosphorylation 19234442 # histone H2AXT142 # # 19234442 Eya effectively removes the phosphotyrosine mark from H2AX, while the phosphatase-inactive mutant Eya proteins (Eya1 D323A or Eya3 D246A) have little or no effect.
EYA2
(details)
# 3520 EYA transcriptional coactivator and phosphatase 2 2139 O00167 EYA2_HUMAN # Eya2 109341 O08575 EYA2_MOUSE PTPE Protein tyrosine phosphatases / Asp-based PTPs Histone modification erase Histone phosphorylation 19351884 # histone H2AXT142 # # 19351884 EYA2 and EYA3 display specificity (dephosphorylation) for Tyr-142 of H2A.X in assays in vitro.
EYA3
(details)
# 3521 EYA transcriptional coactivator and phosphatase 3 2140 Q99504 EYA3_HUMAN # Eya3 109339 P97480 EYA3_MOUSE PTPE Protein tyrosine phosphatases / Asp-based PTPs Histone modification erase Histone phosphorylation 19351884 # histone H2AXT142 # # 19351884 EYA2 and EYA3 display specificity (dephosphorylation) for Tyr-142 of H2A.X in assays in vitro.
EYA4
(details)
# 3522 EYA transcriptional coactivator and phosphatase 4 2070 O95677 EYA4_HUMAN Pfam-B_6035 PB006035 96-142 Eya4 1337104 Q9Z191 EYA4_MOUSE PTPE Protein tyrosine phosphatases / Asp-based PTPs Histone modification erase Histone phosphorylation # # histone H2AXY142ph H2AXY142 # 24096489 In response to double-stranded breaks, EYA4 dephosphorylates the Tyr-142 residue of H2AX facilitating phosphorylation of Ser-139 of H2AX (forming γH2AX), leading to the recruitment of DNA repair complex components to sites of double-stranded break.
EZH1
(details)
# 3526 enhancer of zeste 1 polycomb repressive complex 2 subunit 2145 Q92800 EZH1_HUMAN EZH2_WD-Binding PF11616 39-68, SET PF00856 624-728 Ezh1 1097695 P70351 EZH1_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write, Polycomb group (PcG) protein Histone methylation, # 19026781 PRC2 histone H3K27 H3K27me1, H3K27me2, H3K27me3 # 19026781 Polycomb group proteins are critical to maintaining gene repression established during Drosophila development. Part of this group forms the PRC2 complex containing Ez that catalyzes di- and trimethylation of histone H3 lysine 27 (H3K37me2/3), marks repressive to transcription. The mammalian homologs Ezh1 and Ezh2 form similar PRC2 complexes but exhibit contrasting repressive roles. While PRC2-Ezh2 catalyzes H3K27me2/3 and its knockdown affects global H3K27me2/3 levels, PRC2-Ezh1 performs this function weakly.
EZH2
(details)
# 3527 enhancer of zeste 2 polycomb repressive complex 2 subunit 2146 Q15910 EZH2_HUMAN EZH2_WD-Binding PF11616 39-68, SET PF00856 623-727 Ezh2 107940 Q61188 EZH2_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write, Polycomb group (PcG) protein Histone methylation, # 19026781 PRC2 histone H3K27 H3K27me1, H3K27me2, H3K27me3 # 19026781 Polycomb group proteins are critical to maintaining gene repression established during Drosophila development. Part of this group forms the PRC2 complex containing Ez that catalyzes di- and trimethylation of histone H3 lysine 27 (H3K37me2/3), marks repressive to transcription. The mammalian homologs Ezh1 and Ezh2 form similar PRC2 complexes, but exhibit contrasting repressive roles. While PRC2-Ezh2 catalyzes H3K27me2/3 and its knockdown affects global H3K27me2/3 levels, PRC2-Ezh1 performs this function weakly.
FAM175A
(details)
# 25829 family with sequence similarity 175, member A 84142 Q6UWZ7 F175A_HUMAN Pfam-B_8506 PB008506 1-175 Fam175a 1917931 Q8BPZ8 F175A_MOUSE # # Scaffold protein # 19261749 BRCA1-A TF # # # 19261749 Abra1=FAM175A protein, which appears to act as a scaffold for the A complex. Abra1 is known to mediate the interaction of Rap80 with BRCA1.
FAM175B
(details)
# 28975 family with sequence similarity 175, member B 23172 Q15018 F175B_HUMAN Pfam-B_24421 PB024421 331-390 Fam175b 1926116 Q3TCJ1 F175B_MOUSE # # Histone modification erase cofactor Histone ubiquitination 20656690 BRISC histone H2AK63 H2AK63ub # 20656690 #
FBL
(details)
# 3599 fibrillarin 2091 P22087 FBRL_HUMAN Fibrillarin PF01269 88-315 Fbl 95486 P35550 FBRL_MOUSE # # Histone modification write Histone methylation 24352239 # histone H2AQ104 H2AQ104me # 24352239 Nop1 is a methyltransferase in yeast, and fibrillarin is the orthologue enzyme in human cells. The modification is exclusively enriched over the 35S ribosomal DNA transcriptional unit. Glutamine methylation of H2A is the first histone epigenetic mark dedicated to a specific RNA polymerase and define its function as a regulator of FACT interaction with nucleosomes.
FBRS
(details)
New 20442 fibrosin 64319 Q9HAH7 FBRS_HUMAN Auts2 PF15336 82-282, Pfam-B_58582 PB058582 283-359 Fbrs 104648 Q8R089 FBRS_MOUSE # # Histone modification # 24217316, 22325352 RING2-FBRS histone # # # 24217316, 22325352 Part of a RING2 complex.
FBRSL1
(details)
New 29308 fibrosin-like 1 57666 Q9HCM7 FBSL_HUMAN Auts2 PF15336 587-791, Pfam-B_17807 PB017807 439-487, Pfam-B_187339 PB187339 41-131, Pfam-B_52362 PB052362 164-412 Fbrsl1 1920907 # # # # Histone modification # 24217316, 22325352 RING2-FBRS histone # # # 24217316, 22325352 Part of a RING2 complex.
FOXA1
(details)
New 5021 forkhead box A1 3169 P55317 FOXA1_HUMAN Fork_head PF00250 170-265, Fork_head_N PF08430 17-169, HNF_C PF09354 397-461 Foxa1 1347472 P35582 FOXA1_MOUSE FOX Forkhead boxes Chromatin remodelling, TF #, # 22406422 # chromatin, DNA DNA motif # # # FOXA1 functions in organizing nucleosome positioning.
FOXO1
(details)
New 3819 forkhead box O1 2308 Q12778 FOXO1_HUMAN Fork_head PF00250 127-268, Pfam-B_12765 PB012765 601-653, Pfam-B_39024 PB039024 1-49 Foxo1 1890077 Q9R1E0 FOXO1_MOUSE FOX Forkhead boxes TF # 22406422 # histone, DNA DNA motif, H3, H4 # # # FOXO1 interacts with core histones H3 and H4.
FOXP1
(details)
New 3823 forkhead box P1 27086 Q9H334 FOXP1_HUMAN Fork_head PF00250 465-555, Pfam-B_24123 PB024123 1-79 Foxp1 1914004 P58462 FOXP1_MOUSE FOX Forkhead boxes TF # 22406422 # histone, DNA DNA motif # # # Recruitment of specific chromatin-modifying complexes with HDAC activity.
FOXP2
(details)
New 13875 forkhead box P2 93986 O15409 FOXP2_HUMAN Fork_head PF00250 504-593, Pfam-B_4008 PB004008 240-308 Foxp2 2148705 P58463 FOXP2_MOUSE FOX Forkhead boxes TF # 22406422 # histone, DNA DNA motif # # # Recruitment of specific chromatin-modifying complexes with HDAC activity.
FOXP3
(details)
New 6106 forkhead box P3 50943 Q9BZS1 FOXP3_HUMAN Fork_head PF00250 337-426 Foxp3 1891436 Q99JB6 FOXP3_MOUSE FOX Forkhead boxes TF # 22406422 # histone, DNA DNA motif # # # Recruitment of specific chromatin-modifying complexes with HDAC activity.
FOXP4
(details)
New 20842 forkhead box P4 116113 Q8IVH2 FOXP4_HUMAN Fork_head PF00250 467-555, Pfam-B_22084 PB022084 1-155, Pfam-B_23482 PB023482 569-647, Pfam-B_4008 PB004008 201-230 Foxp4 1921373 Q9DBY0 FOXP4_MOUSE FOX Forkhead boxes TF # 22406422 # histone, DNA DNA motif # # # Recruitment of specific chromatin-modifying complexes with HDAC activity.
GADD45A
(details)
# 4095 growth arrest and DNA-damage-inducible, alpha 1647 P24522 GA45A_HUMAN Ribosomal_L7Ae PF01248 21-123 Gadd45a 107799 P48316 GA45A_MOUSE # # Chromatin remodelling # 21986581 # histone H2A, H2B, H3, H4 # # 21986581 Active DNA demethylation is partially attributed to the ability of Gadd45(A, B, C) proteins to bind histones and modify accessibility of DNA on damaged chromatin.
GADD45B
(details)
# 4096 growth arrest and DNA-damage-inducible, beta 4616 O75293 GA45B_HUMAN Ribosomal_L7Ae PF01248 21-121 Gadd45b 107776 P22339 GA45B_MOUSE # # Chromatin remodelling # 21986581 # histone H2A, H2B, H3, H4 # # 21986581 Active DNA demethylation is partially attributed to the ability of Gadd45(A, B, C) proteins to bind histones and modify accessibility of DNA on damaged chromatin.
GADD45G
(details)
# 4097 growth arrest and DNA-damage-inducible, gamma 10912 O95257 GA45G_HUMAN Ribosomal_L7Ae PF01248 24-113 Gadd45g 1346325 Q9Z111 GA45G_MOUSE # # Chromatin remodelling # 21986581 # histone H2A, H2B, H3, H4 # # 21986581 Active DNA demethylation is partially attributed to the ability of Gadd45(A, B, C) proteins to bind histones and modify accessibility of DNA on damaged chromatin.
GATAD1
(details)
New 29941 GATA zinc finger domain containing 1 57798 Q8WUU5 GATD1_HUMAN GATA PF00320 9-36, Pfam-B_13145 PB013145 175-216, Pfam-B_17231 PB017231 235-263 Gatad1 1914460 Q920S3 GATD1_MOUSE GATAD GATA zinc finger domain containing Histone modification read # 20850016 # histone H3K4me3 # # # GATA zinc finger domain containing 1 (GATAD1) has been identified as a H3K4me3 interactor.
GATAD2A
(details)
# 29989 GATA zinc finger domain containing 2A 54815 Q86YP4 P66A_HUMAN Pfam-B_2058 PB002058 1-79 Gatad2a 2384585 Q8CHY6 P66A_MOUSE GATAD GATA zinc finger domain containing Histone modification read # 16415179 NuRD histone H2A, H2B, H3, H4 # # 16415179 In vitro translated p66α=GATAD2A and p66β showed a strong affinity for all histone tails tested.
GATAD2B
(details)
# 30778 GATA zinc finger domain containing 2B 57459 Q8WXI9 P66B_HUMAN GATA PF00320 420-454 Gatad2b 2443225 Q8VHR5 P66B_MOUSE GATAD GATA zinc finger domain containing Histone modification read # 16415179 NuRD histone H2A, H2B, H3, H4 # # 16415179 In vitro translated p66α and p66β=GATAD2B showed a strong affinity for all histone tails tested.
GFI1
(details)
New 4237 growth factor independent 1 transcription repressor 2672 Q99684 GFI1_HUMAN LIM PF00412 228-283 287-342 346-401 405-460, Paxillin PF03535 6-135 Gfi1 103170 P70338 GFI1_MOUSE ZNF Zinc fingers, C2H2-type Chromatin remodelling # 16287849 # # # # # # Gfi1 coordinates epigenetic repression of p21Cip/WAF1 by recruitment of histone lysine methyltransferase G9a and histone deacetylase 1.
GFI1B
(details)
New 4238 growth factor independent 1B transcription repressor 8328 Q5VTD9 GFI1B_HUMAN zf-C2H2 PF00096 220-242, zf-H2C2_2 PF13465 177-203 262-287 290-314 Gfi1b 1276578 O70237 GFI1B_MOUSE ZNF Zinc fingers, C2H2-type Histone modification cofactor # 24395799 # # # # # # The principal hematopoietic regulator T-cell acute lymphocytic leukemia-1 (TAL1) is involved in regulating H3K27me3 variations in collaboration with the transcription factor growth factor independent 1B (GFI1B).
GLYR1
(details)
# 24434 glyoxylate reductase 1 homolog (Arabidopsis) 84656 Q49A26 GLYR1_HUMAN NAD_binding_11 PF14833 430-551, NAD_binding_2 PF03446 267-429, PWWP PF00855 6-89 Glyr1 1921272 Q922P9 GLYR1_MOUSE # # Histone modification read # 20850016 # histone H3K4me3 # # 20850016 N-PAC=GLYR1, MSH-6, and NSD1 as well as NSD2 were identified as H3K36me3 interactors (Figure 1C; Table S2). Interestingly, these four proteins share a PWWP domain which is part of the Tudor domain “Royal Family” and includes the Tudor, chromo and MBT domains that can interact with methylated lysine residues.
GSE1
(details)
# 28979 Gse1 coiled-coil protein 23199 Q14687 GSE1_HUMAN DUF3736 PF12540 70-203 731-874 Gse1 1098275 Q3U3C9 GSE1_MOUSE # # Histone modification erase Histone acetylation 8724849 BHC, LSD-CoREST RNA # # # 8724849 A novel repeat composed of alternating Arg and Glu (RE repeat) was observed in KIAA0182. Alternating Arg-Asp tracts have been found in many RNA-binding proteins as a characteristic sequence. The presence of the RE repeat with structural similarity to the RD repeat strongly suggests that KIAA0182=GSE1 exhibits an RNA-binding activity.
GSG2
(details)
# 19682 germ cell associated 2 (haspin) 83903 Q8TF76 HASP_HUMAN DUF3635 PF12330 708-797, Pfam-B_41097 PB041097 111-310, Pfam-B_49843 PB049843 1-109, Pkinase PF00069 484-699 Gsg2 1194498 Q9Z0R0 HASP_MOUSE # # Histone modification write Histone phosphorylation 20705812 # histone H3T3 H3T3ph # 20705812 Phosphorylation of histone H3 threonine 3 (H3T3ph) by Haspin=GSG2 is necessary for CPC accumulation at centromeres and that CPC subunit Survivin binds directly to H3T3ph.
GTF2I
(details)
# 4659 general transcription factor IIi 2969 P78347 GTF2I_HUMAN GTF2I PF02946 112-187 361-436 466-541 571-646 733-808 868-943 Gtf2i 1202722 Q9ESZ8 GTF2I_MOUSE # # TF # 9334314 BHC DNA DNA motif # # # Added because it is a complex partner.
GTF3C4
(details)
# 4667 general transcription factor IIIC, polypeptide 4, 90kDa 9329 Q9UKN8 TF3C4_HUMAN TFIIIC_delta PF12657 61-254, zf-TFIIIC PF12660 733-822 Gtf3c4 2138937 Q8BMQ2 TF3C4_MOUSE KAT, GTF Chromatin-modifying enzymes / K-acetyltransferases, General transcription factors Histone modification write Histone acetylation 10523658 # histone H3 # # 10523658 hTFIIIC90=GTF3C4 has an intrinsic histone acetyltransferase activity with a substrate specificity for histone H3.
HAT1
(details)
# 4821 histone acetyltransferase 1 8520 O14929 HAT1_HUMAN Hat1_N PF10394 26-187 Hat1 96013 Q8BY71 HAT1_MOUSE KAT Chromatin-modifying enzymes / K-acetyltransferases Histone modification write Histone acetylation 9427644 # histone H4, H2A # # 9427644 The human holoenzyme consists of two subunits: a catalytic subunit, Hat1, and a subunit that binds core histones, p46, which greatly stimulates the acetyltransferase activity of Hat1. On the other hand, given that the Hat1 holoenzyme bound weakly to H2A and also acetylated the H2A
HCFC1
(details)
# 4839 host cell factor C1 3054 P51610 HCFC1_HUMAN Kelch_1 PF01344 32-71, Kelch_3 PF13415 91-145 146-208 215-263 264-330, Pfam-B_49758 PB049758 381-598 Hcfc1 105942 Q61191 HCFC1_MOUSE # # Chromatin remodelling # 12670868 NSL, COMPASS, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7 chromatin # # # 12670868 A series of molecular activities are associated with the N-terminal subunit of HCF-1 in HSV uninfected cells. Two of these activities are associated with opposing roles in the regulation of transcription through the modulation of chromatin structure: Sin3 HDAC and a novel human Set1/Ash2 HMT.
HCFC2
(details)
# 24972 host cell factor C2 29915 Q9Y5Z7 HCFC2_HUMAN Kelch_1 PF01344 244-301, Kelch_3 PF13415 205-253, Kelch_5 PF13854 312-356 Hcfc2 1915183 Q9D968 HCFC2_MOUSE # # Histone modification write cofactor, Histone modification write cofactor Histone methylation, Histone acetylation 15199122 MLL-HCF, CHD8, MLL2/3, MLL4/WBP7 histone H3 # # 15199122 HCF-2 (HCFC2), which specifically interact with a conserved binding motif in the MLL(N) (p300) subunit of MLL (histone methyltransferase ) and provide a potential mechanism for regulating its antagonistic transcriptional properties.
HDAC1
(details)
# 4852 histone deacetylase 1 3065 Q13547 HDAC1_HUMAN Hist_deacetyl PF00850 18-320, Pfam-B_22185 PB022185 444-478 Hdac1 108086 O09106 HDAC1_MOUSE # # Histone modification erase Histone acetylation 10220385 SWI/SNF_Brm, NuRD, BHC, MeCP1, mSin3A, core HDAC, mSin3A-like complex, RING2-L3MBTL2, CREST-BRG1, LSD-CoREST histone H3, H4 # # 10220385 HDAC1, HDAC4, HDAC5, and HDAC6 deacetylate all four core histones equally well, though deacetylation by HDAC4 and HDAC5 is incomplete.
HDAC10
(details)
# 18128 histone deacetylase 10 83933 Q969S8 HDA10_HUMAN Hist_deacetyl PF00850 13-322 Hdac10 2158340 Q6P3E7 HDA10_MOUSE # # Histone modification erase Histone acetylation 11861901 # histone H2AKac, H2BKac, H3Kac, H4Kac H2AK, H2BK, H3K, H4K # 11861901 HDAC10 can deacetylate histones.
HDAC11
(details)
# 19086 histone deacetylase 11 79885 Q96DB2 HDA11_HUMAN Hist_deacetyl PF00850 23-320 Hdac11 2385252 Q91WA3 HDA11_MOUSE # # Histone modification erase Histone acetylation 9346952 # histone H2AKac, H2BKac, H3Kac, H4Kac H2AK, H2BK, H3K, H4K # 9346952 HDAC11 is a bona fide histone deacetylase.
HDAC2
(details)
# 4853 histone deacetylase 2 3066 Q92769 HDAC2_HUMAN Hist_deacetyl PF00850 19-321, Pfam-B_46198 PB046198 351-449 Hdac2 1097691 P70288 HDAC2_MOUSE # # Histone modification erase Histone acetylation 9346952 SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, NuRD, BHC, MeCP1, mSin3A, core HDAC, mSin3A-like complex, RING2-L3MBTL2, LSD-CoREST histone H2AKac, H2BKac, H3Kac, H4Kac H2AK, H2BK, H3K, H4K # 9346952 HDAC1, HDAC2, and HDAC3 constitute a human HDAC family. All three proteins possess histone deacetylase activity, and repress transcription when bound to a promoter.
HDAC3
(details)
# 4854 histone deacetylase 3 8841 O15379 HDAC3_HUMAN Hist_deacetyl PF00850 11-315, Pfam-B_3137 PB003137 353-383 Hdac3 1343091 O88895 HDAC3_MOUSE # # Histone modification erase Histone acetylation 10655483 # histone H2AKac, H2BKac, H3Kac, H4Kac H2AK, H2BK, H3K, H4K # 10655483 HDAC1, HDAC2, and HDAC3 constitute a human HDAC family. All three proteins possess histone deacetylase activity, and repress transcription when bound to a promoter.
HDAC4
(details)
# 14063 histone deacetylase 4 9759 P56524 HDAC4_HUMAN Arb2 PF09757 1000-1059, HDAC4_Gln PF12203 61-152, Hist_deacetyl PF00850 664-993 Hdac4 3036234 Q6NZM9 HDAC4_MOUSE # # Histone modification erase Histone acetylation 10220385 # histone H2AKac, H2BKac, H3Kac, H4Kac H2AK, H2BK, H3K, H4K # 10220385 HDAC1, HDAC4, HDAC5, and HDAC6 deacetylate all four core histones equally well, though deacetylation by HDAC4 and HDAC5 is incomplete.
HDAC5
(details)
# 14068 histone deacetylase 5 10014 Q9UQL6 HDAC5_HUMAN HDAC4_Gln PF12203 66-133, Hist_deacetyl PF00850 693-1023 Hdac5 1333784 Q9Z2V6 HDAC5_MOUSE # # Histone modification erase Histone acetylation 10220385 # histone H2AKac, H2BKac, H3Kac, H4Kac H2AK, H2BK, H3K, H4K # 10220385 HDAC1, HDAC4, HDAC5, and HDAC6 deacetylate all four core histones equally well, though deacetylation by HDAC4 and HDAC5 is incomplete.
HDAC6
(details)
# 14064 histone deacetylase 6 10013 Q9UBN7 HDAC6_HUMAN Hist_deacetyl PF00850 95-403 489-799, zf-UBP PF02148 1133-1195 Hdac6 1333752 Q9Z2V5 HDAC6_MOUSE # # Histone modification erase Histone acetylation 10220385 # histone H2AKac, H2BKac, H3Kac, H4Kac H2AK, H2BK, H3K, H4K # 10220385 HDAC1, HDAC4, HDAC5, and HDAC6 deacetylate all four core histones equally well, though deacetylation by HDAC4 and HDAC5 is incomplete. (HDAC6 is possibly not involved in epigenetic signalling, but it deacetylates microtubules and heat shock protein 90; PMID:22498752)
HDAC7
(details)
# 14067 histone deacetylase 7 51564 Q8WUI4 HDAC7_HUMAN Hist_deacetyl PF00850 530-860, Pfam-B_5922 PB005922 1-148 Hdac7 1891835 Q8C2B3 HDAC7_MOUSE # # Histone modification erase Histone acetylation 18285338 # histone H2AKac, H2BKac, H3Kac, H4Kac H2AK, H2BK, H3K, H4K # 18285338 The isolated and purified catalytic domain of the human class IIa HDAC, cdHDAC7, has an intrinsic low level of deacetylase activity in the absence of any complex partner which can be inhibited by known HDAC inhibitors such as the hydroxamic acid TSA. It has been showen that the isolated catalytic domain of class IIa HDACs have weak but measurable intrinsic catalytic activity on chemically acetylated core histones.
HDAC8
(details)
# 13315 histone deacetylase 8 55869 Q9BY41 HDAC8_HUMAN Hist_deacetyl PF00850 21-323, Pfam-B_15628 PB015628 324-375 Hdac8 1917565 Q8VH37 HDAC8_MOUSE # # Histone modification erase Histone acetylation 10748112 # histone H2AKac, H2BKac, H3Kac, H4Kac H2AK, H2BK, H3K, H4K # 10748112 HDAC8 exhibited deacetylase activity toward acetylated histone, indicating that this protein is a bona fide histone deacetylase.
HDAC9
(details)
# 14065 histone deacetylase 9 9734 Q9UKV0 HDAC9_HUMAN HDAC4_Gln PF12203 36-124, Hist_deacetyl PF00850 643-973, Pfam-B_5353 PB005353 577-624 Hdac9 1931221 Q99N13 HDAC9_MOUSE # # Histone modification erase Histone acetylation 12590135 # histone H3Kac, H4Kac H3K, H4K # 12590135 A new member of the Class II HDAC family, HDAC9. The enzyme contains a conserved deacetylase domain, represses reporter activity when recruited to a promoter, and utilizes histones H3 and H4 as substrates in vitro and in vivo.
HDGF
(details)
# 4856 hepatoma-derived growth factor 3068 P51858 HDGF_HUMAN PWWP PF00855 10-92 Hdgf 1194494 P51859 HDGF_MOUSE # # Chromatin remodelling, TF #, TF repressor 18331345, 17974029 # DNA DNA motif # # 18331345 SUMOylated HDGF is not bound to chromatin.
HELLS
(details)
# 4861 helicase, lymphoid-specific 3070 Q9NRZ9 HELLS_HUMAN Helicase_C PF00271 633-712, SNF2_N PF00176 226-577 Hells 106209 Q60848 HELLS_MOUSE # # Chromatin remodelling # 14612388 # chromatin # # # 14517253, 14612388 Lymphoid-specific helicase (Lsh=HELLS) is another member of the SNF2 family of chromatin remodeling proteins.
HIF1AN
(details)
# 17113 hypoxia inducible factor 1, alpha subunit inhibitor 55662 Q9NWT6 HIF1N_HUMAN Cupin_8 PF13621 48-302 Hif1an 2442345 Q8BLR9 HIF1N_MOUSE # # Histone modification erase cofactor Histone acetylation 11641274 # histone # # # 11641274 VHL and FIH-1=HIF1AN interact with histone deacetylases in vitro.
HINFP
(details)
# 17850 histone H4 transcription factor 25988 Q9BQA5 HINFP_HUMAN Pfam-B_17110 PB017110 1-103, zf-C2H2 PF00096 255-278 345-368, zf-C2H2_4 PF13894 229-254, zf-H2C2_2 PF13465 185-210 Hinfp 2429620 Q8K1K9 HINFP_MOUSE ZNF Zinc fingers, C2H2-type Histone modification read, TF, TF #, TF activator, TF repressor 14585971 # histone, DNA H4, DNA motif # # 14585971 HiNF-P interacts with conserved H4 cell cycle regulatory sequences in vivo.
HIRA
(details)
# 4916 histone cell cycle regulator 7290 P54198 HIRA_HUMAN HIRA_B PF09453 448-471, Hira PF07569 763-962, Pfam-B_18560 PB018560 963-1015, WD40 PF00400 5-44 60-98 121-159 164-202 258-312 Hira 99430 Q61666 HIRA_MOUSE WDR WD repeat domain containing Histone modification read # 9710638 # histone H2B, H4 # # 9710638 HIRA interacts with core histone H4. H2B- and H4-binding domains are overlapping but distinguishable in the carboxy-terminal region of HIRA, and the region for HIRA interaction has been mapped to the amino-terminal tail of H2B and the second alpha helix of H4.
HIRIP3
(details)
# 4917 HIRA interacting protein 3 8479 Q9BW71 HIRP3_HUMAN CHZ PF09649 484-520 Hirip3 2142364 Q8BLH7 HIRP3_MOUSE # # Histone modification read # 9710638 # histone H2A, H3 # # 9710638 In vitro, HIRIP3 directly interacted with HIRA but also with core histones H2B and H3, suggesting that a HIRA-HIRIP3-containing complex could function in some aspects of chromatin and histone metabolism.
HJURP
(details)
# 25444 Holliday junction recognition protein 55355 Q8NCD3 HJURP_HUMAN HJURP_C PF12347 409-471 554-614, HJURP_mid PF12346 271-386, Pfam-B_631 PB000631 682-746, Scm3 PF10384 16-77 Hjurp 2685821 Q6PG16 HJURP_MOUSE # # Histone chaperone # 21478274 # histone H4 # # 21478274 Deposition of CENP-A to the centromere requires histone chaperone HJURP (Holliday junction recognition protein). The crystal structure of an HJURP–CENP-A–histone H4 complex shows that HJURP binds a CENP-A–H4 heterodimer.
HLCS
(details)
# 4976 holocarboxylase synthetase (biotin-(proprionyl-CoA-carboxylase (ATP-hydrolysing)) ligase) 3141 P50747 BPL1_HUMAN BPL_C PF02237 669-718, BPL_LplA_LipB PF03099 471-603, Pfam-B_33359 PB033359 244-405, Pfam-B_35799 PB035799 407-469 Hlcs 894646 Q920N2 BPL1_MOUSE # # Histone modification write # 14613969 # histone H1, H2A, H2B, H4 # # 14613969 Nuclear HCS =HLCS retains its biotinylating activity and has been shown to biotinylate purified histones in vitro.
HLTF
(details)
# 11099 helicase-like transcription factor 6596 Q14527 HLTF_HUMAN HIRAN PF08797 60-155, Helicase_C PF00271 870-950, SNF2_N PF00176 243-722, zf-RING_2 PF13639 758-801 Hltf 1196437 Q6PCN7 HLTF_MOUSE RNF RING-type (C3HC4) zinc fingers Chromatin remodelling cofactor # 18719106 # chromatin # # # 18719106 Acts as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA.
HMG20A
(details)
# 5001 high mobility group 20A 10363 Q9NP66 HM20A_HUMAN HMG_box PF00505 103-171 Hmg20a 1914117 Q9DC33 HM20A_MOUSE HMGX High mobility group / Non-canonical Chromatin remodelling cofactor # 24227653 LSD-CoREST histone H3K4 # # 24227653 Involved in the recruitment of the histone methyltransferase KMT2A/MLL1 and consequent increased methylation of histone H3 lysine 4.
HMG20B
(details)
# 5002 high mobility group 20B 10362 Q9P0W2 HM20B_HUMAN HMG_box PF00505 70-138, Pfam-B_10576 PB010576 211-315 Hmg20b 1341190 Q9Z104 HM20B_MOUSE HMGX High mobility group / Non-canonical Chromatin remodelling # 11997092 BHC, LSD-CoREST DNA # # # 11997092 The high-mobility-group (HMG) proteins are chromatin-associated proteins that are common to all higher organisms. They bind DNA in a sequence-specific or non-sequence-specific way to induce DNA bending, and regulate chromatin function and gene expression.
HMGB1
(details)
New 4983 high mobility group box 1 3146 P09429 HMGB1_HUMAN HMG_box PF00505 95-163, HMG_box_2 PF09011 6-79 Hmgb1 96113 P63158 HMGB1_MOUSE HMG High-mobility group / Canonical Chromatin remodelling # 19158276 # chromatin # # # # Chromatin-specific remodeling by HMGB1 and linker histone H1 silences proinflammatory genes during endotoxin tolerance.
HMGN1
(details)
New 4984 high mobility group nucleosome binding domain 1 3150 P05114 HMGN1_HUMAN HMG14_17 PF01101 2-96 Hmgn1 96120 P18608 HMGN1_MOUSE HMG High-mobility group / Canonical Chromatin remodelling # 22395460, 20123071 # histone H1 # # # HMGB1-4 proteins are believed to dock to the H1 linker.
HMGN2
(details)
New 4986 high mobility group nucleosomal binding domain 2 3151 P05204 HMGN2_HUMAN HMG14_17 PF01101 2-90 Hmgn2 96136 P09602 HMGN2_MOUSE HMG High-mobility group / Canonical Chromatin remodelling # 22395460, 20123071 # histone H1 # # # HMGB1-4 proteins are believed to dock to the H1 linker.
HMGN3
(details)
New 12312 high mobility group nucleosomal binding domain 3 9324 Q15651 HMGN3_HUMAN HMG14_17 PF01101 2-98 Hmgn3 2138069 Q9DCB1 HMGN3_MOUSE HMG High-mobility group / Canonical Chromatin remodelling # 22395460, 20123071 # histone H1 # # # HMGB1-4 proteins are believed to dock to the H1 linker.
HMGN4
(details)
New 4989 high mobility group nucleosomal binding domain 4 10473 O00479 HMGN4_HUMAN HMG14_17 PF01101 2-90 # # # # HMG High-mobility group / Canonical Chromatin remodelling # 22395460, 20123071 # histone H1 # # # HMGB1-4 proteins are believed to dock to the H1 linker.
HMGN5
(details)
New 8013 high mobility group nucleosome binding domain 5 79366 P82970 HMGN5_HUMAN HMG14_17 PF01101 2-102 Hmgn5 1355295 Q9JL35 HMGN5_MOUSE HMG High-mobility group / Canonical Chromatin remodelling # 22395460, 20123071 # histone H1 # # # HMGB1-4 proteins are believed to dock to the H1 linker.
HP1BP3
(details)
New 24973 heterochromatin protein 1, binding protein 3 50809 Q5SSJ5 HP1B3_HUMAN Linker_histone PF00538 157-232 260-330 341-412 Hp1bp3 109369 Q3TEA8 HP1B3_MOUSE # # Chromatin remodelling # 25100860 # chromatin # # # # Chromatin organizer protein HP1BP3 is mediating chromatin condensation during hypoxia.
HR
(details)
# 5172 hair growth associated 55806 O43593 HAIR_HUMAN JmjC PF02373 1026-1140, Pfam-B_40014 PB040014 312-431, Pfam-B_80075 PB080075 181-289 Hr 96223 Q61645 HAIR_MOUSE # # Histone modification erase Histone methylation 24334705 # histone H3K9me1, H3K9me2 H3K9 # 24334705 HR can demethylate monomethylated or dimethylated histone H3 lysine 9 (H3K9me1 or me2).
HSPA1A
(details)
# 5232 heat shock 70kDa protein 1A 3303 P08107 HSP71_HUMAN HSP70 PF00012 6-612 Hspa1a 96244 Q61696 HS71A_MOUSE HSP70 Heat shock proteins / HSP70 Histone modification write cofactor, Histone modification write cofactor Histone methylation, Histone acetylation 22123078 CHD8, MLL2/3, MLL4/WBP7 histone # # # 22123078 #
HSPA1B
(details)
# 5233 heat shock 70kDa protein 1B 3304 P08107 HSP71_HUMAN HSP70 PF00012 6-612 Hspa1a 96244 Q61696 HS71A_MOUSE HSP70 Heat shock proteins / HSP70 Histone modification write cofactor, Histone modification write cofactor Histone methylation, Histone acetylation 22123078 CHD8, MLL2/3, MLL4/WBP7 histone # # # 22123078 #
HUWE1
(details)
# 30892 HECT, UBA and WWE domain containing 1, E3 ubiquitin protein ligase 10075 Q7Z6Z7 HUWE1_HUMAN DUF4414 PF14377 2968-3079, DUF908 PF06012 89-370, DUF913 PF06025 429-815, HECT PF00632 4067-4374, Pfam-B_13571 PB013571 3944-3965, Pfam-B_15798 PB015798 3091-3191, Pfam-B_20712 PB020712 2429-2459, Pfam-B_6870 PB006870 3966-4021, UBA PF00627 1317-1352, WWE PF02825 1611-1679 Huwe1 1926884 Q7TMY8 HUWE1_MOUSE # # Histone modification write Histone ubiquitination 15767685 # histone H3K9 # # 15767685 A HECT=HUWE1 domain-containing E3 that ubiquitinates histones.
IKBKAP
(details)
# 5959 inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase complex-associated protein 8518 O95163 ELP1_HUMAN IKI3 PF04762 1-954, Pfam-B_8846 PB008846 1048-1212 Ikbkap 1914544 Q7TT37 ELP1_MOUSE ELP Elongator acetyltransferase complex subunits Scaffold protein # 11818576, 11714725 Pol2 elongator # RNA # # 11818576, 11714725 The human Elongator facilitates transcription by RNA polymerase II in a chromatin- and acetyl-CoA-dependent manner. Several human homologues of the yeast Elongator subunits have been identified as subunits of the human Elongator complex, including StIP1 (STAT-interacting protein 1) and IKAP (IKK complex-associated protein) =IKBKAP.
IKZF1
(details)
# 13176 IKAROS family zinc finger 1 (Ikaros) 10320 Q13422 IKZF1_HUMAN zf-H2C2_2 PF13465 131-156 159-184 187-212 Ikzf1 1342540 Q03267 IKZF1_MOUSE ZNF, IKZF Zinc fingers, C2H2-type, IKAROS zinc fingers Chromatin remodelling, TF #, # 19141594 # DNA DNA motif # # 19141594 Ikaros=IKZF1 forms dimers and multimers efficiently, and it has been proposed that Ikaros induces heterochromatization or chromatin remodeling of mouse DNA, resulting in repression or activation of target genes. The results provide insight into possible structural and functional roles of pericentromeric regions in mouse and human chromosomes.
IKZF3
(details)
# 13178 IKAROS family zinc finger 3 (Aiolos) 22806 Q9UKT9 IKZF3_HUMAN Pfam-B_2031 PB002031 67-110, zf-C2H2_4 PF13894 480-504, zf-H2C2_2 PF13465 132-157 160-183 188-213 Ikzf3 1342542 O08900 IKZF3_MOUSE ZNF, IKZF Zinc fingers, C2H2-type, "IKAROS zinc fingers" TF # # # DNA DNA motif # # # Associates with histone deacetylase complexes containing HDAC1, MTA2 and SIN3A. (UniProt)
ING1
(details)
# 6062 inhibitor of growth family, member 1 3621 Q9UK53 ING1_HUMAN ING PF12998 173-256, PHD PF00628 355-402, Pfam-B_837 PB000837 51-89 Ing1 1349481 Q9QXV3 ING1_MOUSE PHF Zinc fingers, PHD-type Histone modification read # 18533182 # histone H3K4me3 # # 18533182 Both DNA repair and apoptotic activities of ING1 require the interaction of the C-terminal plant homeodomain (PHD) finger with histone H3 trimethylated at Lys4 (H3K4me3). The ING1 PHD finger recognizes methylated H3K4 but not other histone modifications as revealed by peptide microarrays.
ING2
(details)
# 6063 inhibitor of growth family, member 2 3622 Q9H160 ING2_HUMAN ING PF12998 26-125, PHD PF00628 214-261 Ing2 1916510 Q9ESK4 ING2_MOUSE PHF Zinc fingers, PHD-type Histone modification read # 16728974 mSin3A-like complex histone H3K4me3 # # 16728974 ING2, a native subunit of a repressive mSin3a-HDAC1 histone deacetylase complex, binds with high affinity to the trimethylated species. In response to DNA damage, recognition of H3K4me3 by the ING2 PHD domain stabilizes the mSin3a-HDAC1 complex at the promoters of proliferation genes.
ING3
(details)
# 14587 inhibitor of growth family, member 3 54556 Q9NXR8 ING3_HUMAN ING PF12998 2-104, PHD PF00628 362-409 Ing3 1919027 Q8VEK6 ING3_MOUSE PHF Zinc fingers, PHD-type Chromatin remodelling, Histone modification write cofactor #, Histone acetylation 12545155 SWR, NuA4, Piccolo_NuA4 histone H2A, H4 # # 12545155 p47ING3 has a PHD-finger motif at its C-terminal region similar to p33ING1 and p33ING2. Although the precise function of the PHD-finger motif is not fully clarified, it is found in proteins involved in chromatin remodeling.
ING4
(details)
# 19423 inhibitor of growth family, member 4 51147 Q9UNL4 ING4_HUMAN ING PF12998 5-107, PHD PF00628 198-245 Ing4 107307 Q8C0D7 ING4_MOUSE PHF Zinc fingers, PHD-type Histone modification read # 18381289 HBO1 histone H3K4me3 # # 18381289 Crystal structure of ING4-PHD bound to H3K4me3.
ING5
(details)
# 19421 inhibitor of growth family, member 5 84289 Q8WYH8 ING5_HUMAN ING PF12998 5-107, PHD PF00628 188-235 Ing5 1922816 Q9D8Y8 ING5_MOUSE PHF Zinc fingers, PHD-type Histone modification read # 18623064 HBO1, MOZ/MORF histone H3K4me3, H3K4me2 # # 18623064 Crystal structure of the ING5 PHD finger in complex with its histone target (H3K4me3). Binding affinities for unmodified, mono-, di-, and tri-methylated histone peptides showed that both full-length ING5 and methylated H3K4 are essential for the acetyltransferase activity of the MOZ/MORF and HBO1 complexes.
INO80
(details)
# 26956 INO80 complex subunit 54617 Q9ULG1 INO80_HUMAN DBINO PF13892 270-410, Helicase_C PF00271 1135-1214, Pfam-B_16799 PB016799 1435-1475, SNF2_N PF00176 521-822 Ino80 1915392 Q6ZPV2 INO80_MOUSE INO80 INO80 complex subunits Chromatin remodelling # 16298340 Ino80 DNA # # # 16298340 The proteins belonging to SWI2/SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. Functional activity of the domains from hINO80 gene both in terms of the DNA dependent ATPase as well as DNA binding activity.
INO80B
(details)
# 13324 INO80 complex subunit B 83444 Q9C086 IN80B_HUMAN PAPA-1 PF04795 211-293, zf-HIT PF04438 305-336 Ino80b 1917270 Q99PT3 IN80B_MOUSE ZNHIT, INO80 Zinc fingers, HIT-type, INO80 complex subunits Chromatin remodelling cofactor # 21303910 Ino80 chromatin # # # 21303910 Composed of the hIno80 Snf2 ATPase domain, the Ies2=INO80B and Ies6 proteins, the AAA+ ATPases Tip49a and Tip49b, and the actin-related protein Arp5.
INO80C
(details)
# 26994 INO80 complex subunit C 125476 Q6PI98 IN80C_HUMAN YL1_C PF08265 141-170 Ino80c 2443014 Q8BHA0 IN80C_MOUSE INO80 INO80 complex subunits Chromatin remodelling cofactor # 16230350 Ino80, CHD8, MLL2/3, MLL4/WBP7 chromatin # # # 16230350 FLAG-tagged PAPA-1, C18orf37, Amida, FLJ20309, and FLJ90652 each copurified with the hINO80 helicase and the Tip49a, Tip49b, PAPA-1, C18orf37, Arp4, Arp5, Arp8, Amida, NFRKB, MCRS1, FLJ90652, and FLJ20309 proteins, which argues that they are all components of a multiprotein hINO80-containing complex.
INO80D
(details)
# 25997 INO80 complex subunit D 54891 Q53TQ3 IN80D_HUMAN Pfam-B_14282 PB014282 588-622, zf-C3Hc3H PF13891 16-80 446-512 Ino80d 3027003 Q66JY2 IN80D_MOUSE INO80 INO80 complex subunits Chromatin remodelling cofactor # 21303910 Ino80 chromatin # # # 21303910 Component of the chromatin remodeling INO80 complex.
INO80E
(details)
# 26905 INO80 complex subunit E 283899 Q8NBZ0 IN80E_HUMAN # Ino80e 2141881 # # INO80 INO80 complex subunits Chromatin remodelling cofactor # 21303910 # chromatin # # # 21303910 Component of the chromatin remodeling INO80 complex.
JADE1
(details)
# 30027 jade family PHD finger 1 79960 Q6IE81 JADE1_HUMAN EPL1 PF10513 29-181, PHD_2 PF13831 217-251, zf-HC5HC2H_2 PF13832 256-368 Jade1 1925835 Q6ZPI0 JADE1_MOUSE PHF Zinc fingers, PHD-type Histone modification write Histone acetylation 16387653 HBO1 histone H3, H4 H3ac, H4ac # 16387653 HBO1-JADE(1,2,3=PHF15,PHF16,PHF17)-ING-hEAF6 tetramer complexes are likely responsible for the majority of histone H4 acetylation higher eukaryotes.
JADE2
(details)
# 22984 jade family PHD finger 2 23338 Q9NQC1 JADE2_HUMAN EPL1 PF10513 39-177, PHD_2 PF13831 213-247, Pfam-B_23296 PB023296 631-669, zf-HC5HC2H_2 PF13832 252-364 Jade2 1924151 Q6ZQF7 JADE2_MOUSE PHF Zinc fingers, PHD-type Histone modification write Histone acetylation 16387653 HBO1 histone H3, H4 H3ac, H4ac # 16387653 HBO1-JADE(1,2,3=PHF15,PHF16,PHF17)-ING-hEAF6 tetramer complexes are likely responsible for the majority of histone H4 acetylation higher eukaryotes.
JADE3
(details)
# 22982 jade family PHD finger 3 9767 Q92613 JADE3_HUMAN EPL1 PF10513 30-178, PHD PF00628 202-249, zf-HC5HC2H_2 PF13832 253-365 Jade3 2148019 Q6IE82 JADE3_MOUSE PHF Zinc fingers, PHD-type Histone modification write Histone acetylation 14612400 HBO1 histone H3, H4 H3ac, H4ac # 14612400 Jade1 =PHF17 may function in the activation and/or repression of Hox complex genes via modulation of chromatin structure.
JAK2
(details)
# 6192 Janus kinase 2 3717 O60674 JAK2_HUMAN Pkinase_Tyr PF07714 545-805 849-1123, SH2 PF00017 400-481 Jak2 96629 Q62120 JAK2_MOUSE SH2D SH2 domain containing Histone modification write Histone phosphorylation 19783980 # histone H3T41 H3T41ph # 19783980 Human JAK2 is present in the nucleus of haematopoietic cells and directly phosphorylates Tyr 41 (Y41) on histone H3.
JARID2
(details)
# 6196 jumonji, AT rich interactive domain 2 3720 Q92833 JARD2_HUMAN ARID PF01388 618-709, JmjC PF02373 916-1031, JmjN PF02375 558-591, Pfam-B_728 PB000728 1-122, zf-C5HC2 PF02928 1139-1193 Jarid2 104813 Q62315 JARD2_MOUSE # # Histone modification write cofactor Histone methylation 20075857 PRC2 histone H3K27, H3K9 # # 20075857 JARID2 is sufficient to recruit PcG proteins to a heterologous promoter, and inhibition of JARID2 expression leads to a major loss of PcG binding and to a reduction of H3K27me3 levels on target genes.
JDP2
(details)
# 17546 Jun dimerization protein 2 122953 Q8WYK2 JDP2_HUMAN bZIP_1 PF00170 70-131 Jdp2 1932093 P97875 JDP2_MOUSE bZIP basic leucine zipper proteins Chromatin remodelling, Histone modification erase cofactor #, Histone acetylation 16518400 # DNA # # # 16518400 JDP2 has histone-chaperone activity in vitro. The sequence-specific DNA-binding protein JDP2 may control transcription via direct regulation of the modification of histones and the assembly of chromatin.
JMJD1C
(details)
# 12313 jumonji domain containing 1C 221037 Q15652 JHD2C_HUMAN JmjC PF02373 2381-2481, Pfam-B_14856 PB014856 2090-2122, Pfam-B_15350 PB015350 2148-2224, Pfam-B_16501 PB016501 1889-1927, Pfam-B_17329 PB017329 541-947, Pfam-B_19453 PB019453 1929-2023, Pfam-B_2770 PB002770 220-524, Pfam-B_63706 PB063706 1-119 Jmjd1c 1918614 Q69ZK6 JHD2C_MOUSE # # Histone modification erase Histone methylation 17549425 # histone H3K9me H3K9 # 17549425 JMJD1A (TSGA), JMJD1B (5qNCA) and JMJD1C with the common domain architecture are histone H3K9 demethylases implicated in the nuclear hormone receptor-based transcriptional regulation.
JMJD6
(details)
# 19355 jumonji domain containing 6 23210 Q6NYC1 JMJD6_HUMAN JmjC PF02373 174-288, Pfam-B_22969 PB022969 1-39 Jmjd6 1858910 Q9ERI5 JMJD6_MOUSE # # Histone modification erase Histone methylation 17947579 # histone H3R2me, H4R3me H3R2, H4R3 # 17947579 The Jumonji domain-containing 6 protein (JMJD6) is a JmjC-containing iron- and 2-oxoglutarate-dependent dioxygenase that demethylates histone H3 at arginine 2 (H3R2) and histone H4 at arginine 3 (H4R3) in both biochemical and cell-based assays.
KANSL1
(details)
# 24565 KAT8 regulatory NSL complex subunit 1 284058 Q7Z3B3 KANL1_HUMAN PEHE PF15275 885-1035, Pfam-B_14811 PB014811 571-639, Pfam-B_19390 PB019390 431-469, Pfam-B_2194 PB002194 135-403, Pfam-B_6892 PB006892 471-569 Kansl1 1923969 Q80TG1 KANL1_MOUSE # # Histone modification write cofactor, Histone modification write cofactor Histone methylation, Histone acetylation 20018852 NSL, CHD8, MLL2/3, MLL4/WBP7 histone H4 H4ac # 20018852 As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.
KANSL2
(details)
# 26024 KAT8 regulatory NSL complex subunit 2 54934 Q9H9L4 KANL2_HUMAN Pfam-B_21577 PB021577 1-25, zf-C3Hc3H PF13891 27-93 300-365 Kansl2 1916862 Q8BQR4 KANL2_MOUSE # # Histone modification write cofactor Histone acetylation 20018852 NSL histone H5 H4ac # 20018852 As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.
KANSL3
(details)
# 25473 KAT8 regulatory NSL complex subunit 3 55683 Q9P2N6 KANL3_HUMAN Abhydrolase_5 PF12695 287-436, Pfam-B_10092 PB010092 521-544, Pfam-B_8995 PB008995 545-589 Kansl3 1918055 A2RSY1 KANL3_MOUSE # # Histone modification write cofactor Histone acetylation 20018852 NSL histone H6 H4ac # 20018852 As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.
KAT2A
(details)
# 4201 K(lysine) acetyltransferase 2A 2648 Q92830 KAT2A_HUMAN Acetyltransf_1 PF00583 553-628, Bromodomain PF00439 737-820, PCAF_N PF06466 86-337, Pfam-B_10717 PB010717 1-67 Kat2a 1343101 Q9JHD2 KAT2A_MOUSE KAT Chromatin-modifying enzymes / K-acetyltransferases Histone modification write Histone acetylation 10611234 TFTC-HAT, SAGA, ATAC, STAGA histone # # # 10611234 Current models of HAT protein activity suggest that one hypothesis for the role of hGCN5=KAT2A in c-Myc's activities might be due to the relaxing of chromatin packaging at target genes following histone acetylation by hGCN5.
KAT2B
(details)
# 8638 K(lysine) acetyltransferase 2B 8850 Q92831 KAT2B_HUMAN Acetyltransf_7 PF13508 541-624, Bromodomain PF00439 732-815, PCAF_N PF06466 74-327, Pfam-B_358817 PB358817 339-381 Kat2b 1343094 Q9JHD1 KAT2B_MOUSE KAT Chromatin-modifying enzymes / K-acetyltransferases Histone modification write Histone acetylation 8945521 # histone # # # 8945521 The cellular p300/CBP associated factor (PCAF=KAT2B) possesses intrinsic histone acetyltransferase activity.
KAT5
(details)
# 5275 K(lysine) acetyltransferase 5 10524 Q92993 KAT5_HUMAN MOZ_SAS PF01853 285-477, Tudor-knot PF11717 7-65 Kat5 1932051 Q8CHK4 KAT5_MOUSE KAT, ZC2HC Chromatin-modifying enzymes / K-acetyltransferases, Zinc fingers, C2HC-type containing Histone modification write Histone acetylation 10096020 SWR, NuA4, Piccolo_NuA4 histone H2AK5, H3K14, H4K5,H4K8, H4K12, H4K16 H2AK5ac, H3K14ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac # 10096020 Tip60=KAT5 significantly acetylates amino-terminal tail peptides of histones H2A, H3 and H4, but not H2B, consistent with substrate preference on intact histones. Preferred acetylation sites for Tip60 are the Lys-5 of histone H2A, the Lys-14 of histone H3, and the Lys-5, -8, -12, -16 of histone H4.
KAT6A
(details)
# 13013 K(lysine) acetyltransferase 6A 7994 Q92794 KAT6A_HUMAN MOZ_SAS PF01853 562-749, PHD PF00628 208-265 264-313, Pfam-B_19382 PB019382 1-84, Pfam-B_21350 PB021350 1011-1048, Pfam-B_25985 PB025985 1056-1116, Pfam-B_3468 PB003468 1648-1699, Pfam-B_6470 PB006470 1487-1601 Kat6a 2442415 Q8BZ21 KAT6A_MOUSE KAT, ZC2HC, PHF Chromatin-modifying enzymes / K-acetyltransferases, Zinc fingers, C2HC-type containing, Zinc fingers, PHD-type Histone modification write Histone acetylation 11313971 MOZ/MORF histone H3, H4 H3ac, H4ac # 11313971 The monocytic leukemia zinc finger protein MOZ=KAT6A is a histone acetyltransferase.
KAT6B
(details)
# 17582 K(lysine) acetyltransferase 6B 23522 Q8WYB5 KAT6B_HUMAN Linker_histone PF00538 106-175, MOZ_SAS PF01853 773-960, PHD PF00628 271-320, Pfam-B_6470 PB006470 1604-1717 Kat6b 1858746 Q8BRB7 KAT6B_MOUSE KAT, ZC2HC, PHF Chromatin-modifying enzymes / K-acetyltransferases, Zinc fingers, C2HC-type containing, Zinc fingers, PHD-type Histone modification write Histone acetylation 10497217 MOZ/MORF histone H3 H3ac # 10497217 A novel human histone acetyltransferase, termed MORF=KAT6B (monocytic leukemia zinc finger protein-related factor).
KAT7
(details)
# 17016 K(lysine) acetyltransferase 7 11143 O95251 KAT7_HUMAN MOZ_SAS PF01853 390-577, zf-C2HC PF01530 182-212 Kat7 2182799 Q5SVQ0 KAT7_MOUSE KAT, ZC2HC Chromatin-modifying enzymes / K-acetyltransferases, Zinc fingers, C2HC-type containing Histone modification write Histone acetylation 10438470 HBO1 histone H4 H4ac # 10438470 A novel protein, HBO1=KAT7 (histone acetyltransferase binding to ORC), that interacts with human ORC1 protein.
KAT8
(details)
# 17933 K(lysine) acetyltransferase 8 84148 Q9H7Z6 KAT8_HUMAN MOZ_SAS PF01853 232-418, Tudor-knot PF11717 55-111 Kat8 1915023 Q9D1P2 KAT8_MOUSE KAT, ZC2HC Chromatin-modifying enzymes / K-acetyltransferases, Zinc fingers, C2HC-type containing Histone modification write Histone acetylation 10786633 NSL, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7 histone H2A, H3, H4 H2Aac, H3ac, H4ac # 10786633 A recombinant C-terminal portion of hMOF=KAT8 has histone acetyltransferase activity directed toward histones H3, H2A and H4, a specificity characteristic of other MYST family histone acetyltransferases.
KDM1A
(details)
# 29079 lysine (K)-specific demethylase 1A 23028 O60341 KDM1A_HUMAN Amino_oxidase PF01593 288-826, SWIRM PF04433 174-264 Kdm1a 1196256 Q6ZQ88 KDM1A_MOUSE KDM Chromatin-modifying enzymes / K-demethylases Histone modification erase Histone methylation 16223729 NuRD, BHC, SCL histone H3K4me1, H3K4me2, H3K9me H3K4, H3K9 # 16223729 Human histone demethylase LSD1=KDM1A is a flavin-dependent amine oxidase that catalyzes the specific removal of methyl groups from mono- and dimethylated Lys4 of histone H3.
KDM1B
(details)
# 21577 lysine (K)-specific demethylase 1B 221656 Q8NB78 KDM1B_HUMAN Amino_oxidase PF01593 392-820, zf-CW PF07496 137-192 Kdm1b 2145261 Q8CIG3 KDM1B_MOUSE KDM Chromatin-modifying enzymes / K-demethylases Histone modification erase Histone methylation 19727073 # histone H3K4me1, H3K4me2 H3K4 # 19727073 KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints.
KDM2A
(details)
# 13606 lysine (K)-specific demethylase 2A 22992 Q9Y2K7 KDM2A_HUMAN F-box PF00646 889-935, JmjC PF02373 199-299, Pfam-B_11167 PB011167 362-470, Pfam-B_6618 PB006618 951-1149, Pfam-B_9841 PB009841 686-744, zf-CXXC PF02008 563-609 Kdm2a 1354736 P59997 KDM2A_MOUSE FBXL, KDM F-boxes / Leucine-rich repeats, Chromatin-modifying enzymes / K-demethylases Histone modification erase Histone methylation 20417597 # histone H3K36me2 H3K36 # 20417597 CpG islands directly recruit the H3K36-specific lysine demethylase enzyme KDM2A. Nucleation of KDM2A at these elements results in removal of H3K36 methylation, creating CpG island chromatin that is uniquely depleted of this modification.
KDM2B
(details)
# 13610 lysine (K)-specific demethylase 2B 84678 Q8NHM5 KDM2B_HUMAN Cupin_8 PF13621 23-335, F-box PF00646 1050-1107, Pfam-B_23456 PB023456 441-519, Pfam-B_33113 PB033113 1235-1289, zf-CXXC PF02008 605-651 Kdm2b 1354737 Q6P1G2 KDM2B_MOUSE FBXL, KDM F-boxes / Leucine-rich repeats, Chromatin-modifying enzymes / K-demethylases Histone modification erase Histone methylation 17994099 BCOR histone H3K4me3, H3K36me2 H3K4, H3K36 # 17994099 JHDM1B =KDM2B is a histone demethylase that catalyses the demethylation of H3K4me3.
KDM3A
(details)
# 20815 lysine (K)-specific demethylase 3A 55818 Q9Y4C1 KDM3A_HUMAN JmjC PF02373 1151-1264, Pfam-B_14772 PB014772 851-889, Pfam-B_17027 PB017027 351-439, Pfam-B_6147 PB006147 441-539, Pfam-B_7111 PB007111 781-849 Kdm3a 98847 Q6PCM1 KDM3A_MOUSE KDM Chromatin-modifying enzymes / K-demethylases Histone modification erase Histone methylation 16603237 # histone H3K9me1, H3K9me2 H3K9 # 16603237 JHDM2A =KDM3A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor.
KDM3B
(details)
# 1337 lysine (K)-specific demethylase 3B 51780 Q7LBC6 KDM3B_HUMAN JmjC PF02373 1594-1704, Pfam-B_16202 PB016202 1548-1593, Pfam-B_16670 PB016670 1497-1546, Pfam-B_19299 PB019299 351-469, Pfam-B_22020 PB022020 711-779, Pfam-B_3525 PB003525 571-639, Pfam-B_38652 PB038652 1-39, Pfam-B_6147 PB006147 471-569, Pfam-B_7111 PB007111 781-839 Kdm3b 1923356 Q6ZPY7 KDM3B_MOUSE KDM Chromatin-modifying enzymes / K-demethylases Histone modification erase Histone methylation 16603237 # histone H3K9me1, H3K9me2 H3K9 # 16603237 A JmjC domain-containing protein (KDM3B=JmjC domain-containing histone demethylation protein 2B), JHDM2A, which specifically demethylates mono- and dimethyl-H3K9.
KDM4A
(details)
# 22978 lysine (K)-specific demethylase 4A 9682 O75164 KDM4A_HUMAN JmjC PF02373 175-291, JmjN PF02375 15-49, PHD_2 PF13831 732-767, zf-HC5HC2H_2 PF13832 773-884 Kdm4a 2446210 Q8BW72 KDM4A_MOUSE KDM, TDRD Chromatin-modifying enzymes / K-demethylases, Tudor domain containing Histone modification erase Histone methylation 16603238 # histone H3K4me3, H3K36me3 H3K4me2, H3K36me2 # 16603238 The JmjC domain-containing protein JMJD2A =KDM4A reverses trimethylated H3-K9/K36 to di- but not mono- or unmethylated products. Overexpression of JMJD2A (but not a catalytically inactive mutant) reduces H3-K9/K36 trimethylation levels in cultured cells.
KDM4B
(details)
# 29136 lysine (K)-specific demethylase 4B 23030 O94953 KDM4B_HUMAN JmjC PF02373 176-292, JmjN PF02375 16-50, PHD_2 PF13831 754-789, Pfam-B_12059 PB012059 1021-1094, zf-HC5HC2H_2 PF13832 795-906 Kdm4b 2442355 Q91VY5 KDM4B_MOUSE KDM, TDRD Chromatin-modifying enzymes / K-demethylases, Tudor domain containing Histone modification erase Histone methylation 16603238 # histone H3K9me3 H3K9me1, H3K9me2 # 16603238 Human JMJD2(B, C, D) =KDM4(B, C, D) subfamily members function as trimethylation-specific demethylases, converting H3-K9Me3 to H3-K9Me2 and H3-K9Me1, respectively.
KDM4C
(details)
# 17071 lysine (K)-specific demethylase 4C 23081 Q9H3R0 KDM4C_HUMAN JmjC PF02373 177-293, JmjN PF02375 17-51, PHD_2 PF13831 712-747, Pfam-B_10616 PB010616 1021-1054, Pfam-B_14467 PB014467 422-670, Pfam-B_5109 PB005109 891-1019, zf-HC5HC2H_2 PF13832 753-864 Kdm4c 1924054 Q8VCD7 KDM4C_MOUSE KDM, TDRD Chromatin-modifying enzymes / K-demethylases, Tudor domain containing Histone modification erase Histone methylation 16603238 # histone H3K9me3, H3K36me3 H3K9me1, H3K9me2 # 16603238 Human JMJD2(B, C, D) =KDM4(B, C, D) subfamily members function as trimethylation-specific demethylases, converting H3-K9Me3 to H3-K9Me2 and H3-K9Me1, respectively.
KDM4D
(details)
# 25498 lysine (K)-specific demethylase 4D 55693 Q6B0I6 KDM4D_HUMAN JmjC PF02373 179-295, JmjN PF02375 19-53, Pfam-B_45485 PB045485 324-356, Pfam-B_84013 PB084013 451-521 Kdm4d 3606484 Q3U2K5 KDM4D_MOUSE KDM Chromatin-modifying enzymes / K-demethylases Histone modification erase Histone methylation 16603238 # histone H3K9me3 H3K9me1, H3K9me2 # 16603238 Human JMJD2(B, C, D) =KDM4(B, C, D) subfamily members function as trimethylation-specific demethylases, converting H3-K9Me3 to H3-K9Me2 and H3-K9Me1, respectively.
KDM4E
(details)
# 37098 lysine (K)-specific demethylase 4E 390245 B2RXH2 KDM4E_HUMAN JmjC PF02373 176-292, JmjN PF02375 16-50 # # # # KDM Chromatin-modifying enzymes / K-demethylases Histone modification erase Histone methylation 21914792 # histone H3K9me2, H3K9me3 H3K9 # 21914792 KDM4D and KDM4E (which is catalytically active) catalyze demethylation of H3K9me3/me2.
KDM5A
(details)
# 9886 lysine (K)-specific demethylase 5A 5927 P29375 KDM5A_HUMAN ARID PF01388 81-170, JmjC PF02373 470-586, JmjN PF02375 20-53, PHD PF00628 295-343 1163-1218, PLU-1 PF08429 740-1072, zf-C5HC2 PF02928 676-729 Kdm5a 2136980 Q3UXZ9 KDM5A_MOUSE KDM, PHF Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type Histone modification erase Histone methylation 17320163 # histone H3K4me3 H3K4 # 17320163 The retinoblastoma binding protein RBP2 =KDM5A is an H3K4 demethylase.
KDM5B
(details)
# 18039 lysine (K)-specific demethylase 5B 10765 Q9UGL1 KDM5B_HUMAN ARID PF01388 94-183, JmjC PF02373 486-602, JmjN PF02375 33-66, PHD PF00628 311-359 1178-1224 1486-1538, PLU-1 PF08429 756-1088, zf-C5HC2 PF02928 692-745 Kdm5b 1922855 Q80Y84 KDM5B_MOUSE KDM, PHF Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type Histone modification erase Histone methylation 17363312 # histone H3K4me3 H3K4 # 17363312 PLU-1 =KDM5B, a transcriptional repressor implicated in breast cancer, is a histone demethylase enzyme that has the ability to reverse the trimethyl H3K4 modification state.
KDM5C
(details)
# 11114 lysine (K)-specific demethylase 5C 8242 P41229 KDM5C_HUMAN ARID PF01388 76-165, JmjC PF02373 501-617, JmjN PF02375 15-48, PHD PF00628 326-374 1187-1250, PLU-1 PF08429 771-1100, Pfam-B_12821 PB012821 1417-1482, zf-C5HC2 PF02928 707-760 Kdm5c 99781 P41230 KDM5C_MOUSE KDM, PHF Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type Histone modification erase Histone methylation 17320160 # histone H3K4me3 H3K4me2, H3K4me1 # 17320160 The X-linked mental retardation (XLMR) gene SMCX (JARID1C)=KDM5C, which encodes a JmjC-domain protein, reverses H3K4me3 to di- and mono- but not unmethylated products.
KDM5D
(details)
# 11115 lysine (K)-specific demethylase 5D 8284 Q9BY66 KDM5D_HUMAN ARID PF01388 76-165, JmjC PF02373 491-607, JmjN PF02375 15-48, PHD PF00628 316-364 1174-1237, PLU-1 PF08429 761-1087, Pfam-B_12821 PB012821 1401-1443, zf-C5HC2 PF02928 697-750 Kdm5d 99780 Q62240 KDM5D_MOUSE KDM, PHF Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type Histone modification erase Histone methylation 17320160 # histone H3K4me3, H3K4me2 H3K4 # 17320160 SMCX family members, including SMCY=KDM5D, RBP2, and PLU-1, demethylate H3K4me3.
KDM6A
(details)
# 12637 lysine (K)-specific demethylase 6A 7403 O15550 KDM6A_HUMAN JmjC PF02373 1133-1241, Pfam-B_604 PB000604 631-769, Pfam-B_972 PB000972 771-1109, TPR_1 PF00515 130-163 318-351 352-380, TPR_17 PF13431 272-304, TPR_8 PF13181 205-238 Kdm6a 1095419 O70546 KDM6A_MOUSE KDM, TTC Chromatin-modifying enzymes / K-demethylases, Tetratricopeptide (TTC) repeat domain containing Histone modification erase Histone methylation 17851529 CHD8, MLL2/3, MLL4/WBP7, COMPASS-like MLL3,4 histone H3K27me2. H3K27me3 H3K27 # 17851529 The JmjC-domain-containing proteins UTX=KDM6A and JMJD3 catalyse demethylation of H3K27me3/2.
KDM6B
(details)
# 29012 lysine (K)-specific demethylase 6B 23135 O15054 KDM6B_HUMAN JmjC PF02373 1377-1485, Pfam-B_5108 PB005108 101-843, Pfam-B_992 PB000992 1-99 Kdm6b 2448492 Q5NCY0 KDM6B_MOUSE KDM Chromatin-modifying enzymes / K-demethylases Histone modification erase Histone methylation 17851529 # histone H3K27me2. H3K27me4 H3K28 # 17851529 The JmjC-domain-containing proteins UTX=KDM6A and JMJD3=KDM6B catalyse demethylation of H3K27me3/2.
KDM7A
(details)
# 22224 lysine (K)-specific demethylase 7A 80853 Q6ZMT4 KDM7A_HUMAN PHD PF00628 39-88, JmjC PF02373 269-369, Pfam-B_18122 PB018122 381-538, Pfam-B_13686 PB013686 541-639, Pfam-B_1060 PB001060 853-939 Kdm7a 2443388 Q3UWM4 KDM7A_MOUSE KDM, PHF Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type Histone modification erase Histone methylation 20194436 # histone H3K9me2, H3K27me2, H4K20me1 H3K9, H3K27, H4K20 # 20194436 KDM7 (also known as JHDM1D) is a dual demethylase for H3K9 and H3K27 that functions as an eraser of silencing marks on chromatin during brain development. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: in presence of H3K4me3, it has no demethylase activity toward H3K9me2, while it has high activity toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate.
KDM8
(details)
# 25840 lysine (K)-specific demethylase 8 79831 Q8N371 KDM8_HUMAN Cupin_8 PF13621 192-416 Kdm8 1924285 Q9CXT6 KDM8_MOUSE KDM Chromatin-modifying enzymes / K-demethylases Histone modification erase Histone methylation 20457893 # histone H3K36me2 H3K36 # 20457893 JMJD5 (now renamed KDM8), a JmjC family member, demethylates H3K36me2 and is required for cell cycle progression.
KEAP1
(details)
New 23177 kelch-like ECH-associated protein 1 9817 Q14145 KEAP1_HUMAN BACK PF07707 184-286, BTB PF00651 67-179, Kelch_1 PF01344 317-359 361-410 412-457 459-504 506-551 553-598 Keap1 1858732 Q9Z2X8 KEAP1_MOUSE KLHL, BTBD Kelch-like, "BTB/POZ domain containing" Chromatin remodelling # 21920360 # chromatin # # # # Interacts with the NURF Nucleosome Remodeling Factor complex.
KMT2A
(details)
# 7132 lysine (K)-specific methyltransferase 2A 4297 Q03164 KMT2A_HUMAN FYRC PF05965 3666-3749, FYRN PF05964 2023-2073, PHD PF00628 1481-1533 1568-1627, Pfam-B_11202 PB011202 1021-1086, SET PF00856 3840-3945, zf-CXXC PF02008 1147-1194, zf-HC5HC2H PF13771 1900-1978 Kmt2a 96995 P55200 KMT2A_MOUSE KMT, PHF Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type Histone modification write Histone methylation 19187761 MLL-HCF, CHD8, COMPASS-like MLL1,2 histone H3K4 H3K4me # 19187761 MLL1 SET domain can incorporate methyl groups into unmodified or H3K4me1 substrates, signifying both mono- and dimethylation activity.
KMT2B
(details)
# 15840 lysine (K)-specific methyltransferase 2B 9757 Q9UMN6 KMT2B_HUMAN FYRC PF05965 2411-2494, FYRN PF05964 1732-1782, PHD PF00628 1251-1303 1337-1396, Pfam-B_25060 PB025060 1783-1849, Pfam-B_25524 PB025524 1168-1202, Pfam-B_26440 PB026440 701-839, Pfam-B_27348 PB027348 2191-2289, Pfam-B_3353 PB003353 1981-2079, Pfam-B_6332 PB006332 1401-1479, Pfam-B_85509 PB085509 345-387, SET PF00856 2586-2691, zf-CXXC PF02008 958-1005, zf-HC5HC2H PF13771 1608-1686 Kmt2b 109565 O08550 KMT2B_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation 17707229 Menin-associated_HMT, MLL2/3, COMPASS-like MLL3,4 histone H3K4 H3K4me3 # 17707229 MLL (=KMT2B)-containing complexes methylate histone H3 at lysine 4 (H3K4) and have been implicated in the regulation of transcription.
KMT2C
(details)
# 13726 lysine (K)-specific methyltransferase 2C 58508 Q8NEZ4 KMT2C_HUMAN FYRC PF05965 4606-4693, FYRN PF05964 4550-4604, PHD PF00628 390-438 959-1010 1009-1060, Pfam-B_16694 PB016694 2536-2572, Pfam-B_19991 PB019991 1874-1906, Pfam-B_43 PB000043 3044-3095, Pfam-B_49476 PB049476 1-159, SET PF00856 4782-4887, zf-HC5HC2H PF13771 252-331 4429-4507 Kmt2c 2444959 Q8BRH4 KMT2C_MOUSE KMT, PHF Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type Histone modification write Histone methylation 20937768 MLL2/3, COMPASS-like MLL3,4 histone H3K4 H3K4me # 20937768 In humans, multiple Set1-like HMT complexes with H3K4 HMT activities have been identified. Each of these complexes contains the SET domain-containing homologs of yeast Set1, including human Set1 (hSet1), MLL1 (mixed lineage leukemia 1, also known as MLL, HRX, ALL1, or KMT2A), MLL2 (mixed-lineage leukemia 2, also known as HRX2 or KMT2B), MLL3 (mixed-lineage leukemia 3, also known as HALR or KMT2C), and MLL4 (mixed-lineage leukemia 4, also known as ALR or KMT2D), which carry the enzymatic activity for the associated complexes.
KMT2D
(details)
# 7133 lysine (K)-specific methyltransferase 2D 8085 O14686 KMT2D_HUMAN FYRC PF05965 5236-5323, FYRN PF05964 5180-5234, PHD PF00628 275-323 1379-1429 1429-1477, Pfam-B_26489 PB026489 5016-5050, Pfam-B_29065 PB029065 423-678, Pfam-B_2976 PB002976 1682-1717, Pfam-B_33020 PB033020 3681-3767, SET PF00856 5408-5513, zf-HC5HC2H PF13771 139-218 5059-5137 Kmt2d 2682319 Q6PDK2 KMT2D_MOUSE KMT, PHF Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type Histone modification write Histone methylation 20937768 COMPASS-like MLL1,2, MLL4/WBP7, COMPASS-like MLL3,4 histone H3K4 H3K4me # 20937768 In humans, multiple Set1-like HMT complexes with H3K4 HMT activities have been identified. Each of these complexes contains the SET domain-containing homologs of yeast Set1, including human Set1 (hSet1), MLL1 (mixed lineage leukemia 1, also known as MLL, HRX, ALL1, or KMT2A), MLL2 (mixed-lineage leukemia 2, also known as HRX2 or KMT2B), MLL3 (mixed-lineage leukemia 3, also known as HALR or KMT2C), and MLL4 (mixed-lineage leukemia 4, also known as ALR or KMT2D), which carry the enzymatic activity for the associated complexes.
KMT2E
(details)
# 18541 lysine (K)-specific methyltransferase 2E 55904 Q8IZD2 KMT2E_HUMAN PHD PF00628 120-166, Pfam-B_13611 PB013611 1791-1856, Pfam-B_19470 PB019470 1301-1369, Pfam-B_19601 PB019601 1131-1179, Pfam-B_20626 PB020626 961-1129, Pfam-B_22469 PB022469 871-959, Pfam-B_24586 PB024586 1261-1299, Pfam-B_7010 PB007010 1651-1789, Pfam-B_7713 PB007713 731-869, SET PF00856 342-447 Kmt2e 1924825 Q3UG20 KMT2E_MOUSE KMT, PHF Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type Histone modification write Histone methylation 19377461 # histone H3K4 H3K4me1, H3K4me2 # 19377461 Nuclear GlcNAcylation of the histone lysine methyltransferase (HKMT), MLL5, by O-GlcNAc transferase facilitates retinoic-acid-induced granulopoiesis in human HL60 promyelocytes through methylation of H3K4.
L3MBTL1
(details)
# 15905 l(3)mbt-like 1 (Drosophila) 26013 Q9Y468 LMBL1_HUMAN MBT PF02820 242-314 349-421 453-525, SAM_1 PF00536 681-745, zf-C2HC PF01530 551-581 L3mbtl1 2676663 A2A5N8 LMBL1_MOUSE ZC2HC, SAMD Zinc fingers, C2HC-type containing, Sterile alpha motif (SAM) domain containing Histone modification read # 18026117 L3MBTL1 histone H1BK26, H4K20 # # 18026117 Crystal structures of the L3MBTL1 MBT repeats in complex with histone H4 peptides dimethylated on Lys20 (H4K20me2). Only the second of the three MBT repeats can bind mono- and dimethylated histone peptides. Its binding pocket has similarities to that of 53BP1 and is able to recognize the degree of histone lysine methylation.
L3MBTL2
(details)
# 18594 l(3)mbt-like 2 (Drosophila) 83746 Q969R5 LMBL2_HUMAN MBT PF02820 214-290 327-395 432-508 540-610 L3mbtl2 2443584 P59178 LMBL2_MOUSE # # Histone modification read # 19233876 RING2-L3MBTL2 histone H3K4, H3K9, H3K27, H4K20 # # 19233876 Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2.
L3MBTL3
(details)
# 23035 l(3)mbt-like 3 (Drosophila) 84456 Q96JM7 LMBL3_HUMAN MBT PF02820 268-340 375-447 479-548, Pfam-B_29190 PB029190 1-79, SAM_1 PF00536 706-770 L3mbtl3 2143628 Q8BLB7 LMBL3_MOUSE SAMD Sterile alpha motif (SAM) domain containing Histone modification read # 23292653 # histone H4K20me # # 23292653 Binds L3MBTL3 with a similar affinity to H4K20me histone
L3MBTL4
(details)
# 26677 l(3)mbt-like 4 (Drosophila) 91133 Q8NA19 LMBL4_HUMAN MBT PF02820 88-160 196-268 300-371, SAM_1 PF00536 541-605, zf-C2HC PF01530 376-407 L3mbtl4 2444889 B1B1A0 LMBL4_MOUSE SAMD Sterile alpha motif (SAM) domain containing Histone modification read # 20698951 # histone HKme # # 20698951 The L3MBTL4 protein contains three "malignant brain tumor" (MBT) domains. The MBT domain binds methylated histone residues.
LAS1L
(details)
# 25726 LAS1-like (S. cerevisiae) 81887 Q9Y4W2 LAS1L_HUMAN Las1 PF04031 42-188, Pfam-B_28535 PB028535 671-732 Las1l 1923380 A2BE28 LAS1L_MOUSE # # Histone modification write cofactor, Histone modification write cofactor Histone methylation, Histone acetylation 20442285 CHD8, MLL2/3, MLL4/WBP7 histone H3K4, H3,H4,H2A H3K4me, H3K4me2, H3Ac, H4Ac, H2AAc # 15960975 Facultative member of the MLL1/MLL complex.
LBR
(details)
New 6518 lamin B receptor 3930 Q14739 LBR_HUMAN ERG4_ERG24 PF01222 183-615, LBR_tudor PF09465 1-55 Lbr 2138281 Q3U9G9 LBR_MOUSE TDRD Tudor domain containing # # 22498752 # chromatin # # # # Anchors the lamina and the heterochromatin to the inner nuclear membrane.
LEO1
(details)
New 30401 Leo1, Paf1/RNA polymerase II complex component, homolog (S. cerevisiae) 123169 Q8WVC0 LEO1_HUMAN Leo1 PF04004 373-537, Pfam-B_17842 PB017842 1-105, Pfam-B_20153 PB020153 171-239, Pfam-B_6431 PB006431 241-309 Leo1 2685031 Q5XJE5 LEO1_MOUSE # # Histone modification write cofactor Histone ubiquitination 24038468 # histone # # # # Part of the PAF1 complex, which may be involved in recruitment of ubiquitination complexes. Important for PAF1 binding to H3.
LRWD1
(details)
# 21769 leucine-rich repeats and WD repeat domain containing 1 222229 Q9UFC0 LRWD1_HUMAN LRR_1 PF00560 48-69, Pfam-B_28625 PB028625 274-344, Pfam-B_39252 PB039252 191-239, WD40 PF00400 382-421 Lrwd1 1918985 Q8BUI3 LRWD1_MOUSE WDR WD repeat domain containing Chromatin remodelling # 20932478 # histone, DNA H3K9me3, H3K27me3 # # 20932478 A highly conserved, leucine-rich repeats and WD40 repeat domain-containing protein 1 (LRWD1) or ORC-associated (ORCA) in human cells that interacts with ORC and modulates chromatin association of ORC. ORCA colocalizes with ORC and shows similar cell-cycle dynamics. ORCA efficiently recruits ORC to chromatin.
MAP3K7
(details)
New 6859 mitogen-activated protein kinase kinase kinase 7 6885 O43318 M3K7_HUMAN Pfam-B_11880 PB011880 521-569, Pkinase_Tyr PF07714 36-284 Map3k7 1346877 Q62073 M3K7_MOUSE MAP3K Mitogen-activated protein kinase cascade / Kinase kinase kinases Histone modification write # 18838386 # histone # # # # A member of the ATAC complex.
MAPKAPK3
(details)
# 6888 mitogen-activated protein kinase-activated protein kinase 3 7867 Q16644 MAPK3_HUMAN Pkinase PF00069 44-304 Mapkapk3 2143163 Q3UMW7 MAPK3_MOUSE # # Chromatin remodelling # 15563468 # chromatin # # # 15563468 MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1.
MASTL
(details)
# 19042 microtubule associated serine/threonine kinase-like 84930 Q96GX5 GWL_HUMAN Pfam-B_24677 PB024677 271-369, Pfam-B_8409 PB008409 371-489, Pkinase PF00069 35-203 733-835 Mastl 1914371 Q8C0P0 GWL_MOUSE # # Histone modification write Histone phosphorylation 20818157 # histone H1, H3 H1p, H3p # 20818157 Phosphorylates histone protein in vitro; however such activity is unsure in vivo (UniProt).
MAX
(details)
# 6913 MYC associated factor X 4149 P61244 MAX_HUMAN HLH PF00010 24-75 Max 96921 P28574 MAX_MOUSE bHLH Basic helix-loop-helix proteins Histone modification write cofactor, Histone modification write cofactor, TF, TF Histone methylation, Histone acetylation, TF activator, TF repressor 18271930, 12004135 CHD8, MLL2/3, MLL4/WBP7 DNA DNA motif # # 18271930, 12004135 Part of a multimeric protein complex that contains E2F6, Mga and Max. The complex contains chromatin modifiers such as a novel histone methyltransferase that modifies lysine 9 of histone H3, HP1gamma, and Polycomb group (PcG) proteins.
MAZ
(details)
New 6914 MYC-associated zinc finger protein (purine-binding transcription factor) 4150 P56270 MAZ_HUMAN zf-C2H2 PF00096 337-360, zf-C2H2_4 PF13894 190-213 366-388, zf-H2C2_2 PF13465 293-318 Maz 1338823 P56671 MAZ_MOUSE ZNF Zinc fingers, C2H2-type Chromatin remodelling # 21920360 # chromatin # # # # Interacts with the NURF Nucleosome Remodeling Factor complex.
MBD1
(details)
# 6916 methyl-CpG binding domain protein 1 4152 Q9UIS9 MBD1_HUMAN MBD PF01429 1-85, Pfam-B_12306 PB012306 468-526, Pfam-B_9691 PB009691 528-587, zf-CXXC PF02008 168-215 217-262 330-377 Mbd1 1333811 Q9Z2E2 MBD1_MOUSE # # Histone modification write cofactor, TF Histone methylation, TF repressor 15327775 # DNA mCG, DNA motif # # 15327775 MBD1 recruits SETDB1 to the large subunit of chromatin assembly factor CAF-1 to form an S phase-specific CAF-1/MBD1/SETDB1 complex that facilitates methylation of H3-K9 during replication-coupled chromatin assembly. In the absence of MBD1, H3-K9 methylation is lost at multiple genomic loci and results in activation of p53BP2 gene, normally repressed by MBD1 in HeLa cells. Data suggest a model in which H3-K9 methylation by SETDB1 is dependent on MBD1 and is heritably maintained through DNA replication to support the formation of stable heterochromatin at methylated DNA.
MBD2
(details)
# 6917 methyl-CpG binding domain protein 2 8932 Q9UBB5 MBD2_HUMAN MBD PF01429 145-216, MBD_C PF14048 294-387 Mbd2 1333813 Q9Z2E1 MBD2_MOUSE # # Histone modification write cofactor, Histone modification erase cofactor, TF Histone methylation, Histone acetylation, TF repressor 16415179 NuRD, MeCP1 DNA mCG, DNA motif # # 16415179 Wild-type subnuclear distribution of p66alpha and p66beta depends on the presence of MBD2. Both proteins interact with the tails of all octamer histones in vitro, and acetylation of histone tails interferes with p66 binding.
MBD3
(details)
# 6918 methyl-CpG binding domain protein 3 53615 O95983 MBD3_HUMAN MBD PF01429 1-72, MBD_C PF14048 150-243 Mbd3 1333812 Q9Z2D8 MBD3_MOUSE # # Histone modification erase cofactor Histone acetylation 12124384 NuRD histone # # # 12124384 MBD3 has been identified as a component of the NuRD/Mi2 complex that shows chromatin remodeling and histone deacetylase activities. MBD3 MBD is necessary and sufficient for binding to HDAC1 and MTA2, two components of the NuRD/Mi2 complex. It has been suggested that mCpG-binding-defective MBD3 has evolutionarily conserved its MBD because of the secondary role played by the MBD in protein-protein interactions.
MBD4
(details)
# 6919 methyl-CpG binding domain protein 4 8930 O95243 MBD4_HUMAN HhH-GPD PF00730 461-575, MBD PF01429 76-151, Pfam-B_47325 PB047325 409-460 Mbd4 1333850 Q9Z2D7 MBD4_MOUSE # # DNA modification # 10930409 # DNA G:T, G:U # # 10930409 MED1 functions as a mismatch-specific DNA repair enzyme. MED1 lacks uracil glycosylase activity on single-strand DNA and abasic site lyase activity. The glycosylase activity of MED1 prefers substrates containing a G:T mismatch within methylated or unmethylated CpG sites; since G:T mismatches can originate via deamination of 5-methylcytosine to thymine, MED1 may act as a caretaker of genomic fidelity at CpG sites.
MBD5
(details)
# 20444 methyl-CpG binding domain protein 5 55777 Q9P267 MBD5_HUMAN Pfam-B_1400 PB001400 981-1140, Pfam-B_19258 PB019258 499-567, Pfam-B_41495 PB041495 438-497, Pfam-B_51737 PB051737 1-119, Pfam-B_5417 PB005417 121-219, Pfam-B_7705 PB007705 221-410 Mbd5 2138934 B1AYB6 MBD5_MOUSE # # Chromatin remodelling # 20700456 # chromatin # # # 20700456 MBD5 and MBD6 may contribute to the unique epigenetic machinery of neurons or to the global reorganization of chromatin during spermatogenesis.
MBD6
(details)
# 20445 methyl-CpG binding domain protein 6 114785 Q96DN6 MBD6_HUMAN Pfam-B_28044 PB028044 161-209 Mbd6 106378 Q3TY92 MBD6_MOUSE # # Chromatin remodelling # 20700456 # chromatin # # # 20700456 MBD5 and MBD6 may contribute to the unique epigenetic machinery of neurons or to the global reorganization of chromatin during spermatogenesis.
MBIP
(details)
# 20427 MAP3K12 binding inhibitory protein 1 51562 Q9NS73 MBIP1_HUMAN Pfam-B_15854 PB015854 191-249, Pfam-B_276 PB000276 251-342 Mbip 1918320 Q99LQ1 MBIP1_MOUSE # # Histone modification write cofactor Histone acetylation 19103755 ATAC histone # # # 19103755 Novel proteins identified as STAGA/ TFTC subunits, such as ATAC2, DR1, MBIP, WDR5, YEATS2, and ZZZ3/ATAC1.
MBTD1
(details)
# 19866 mbt domain containing 1 54799 Q05BQ5 MBTD1_HUMAN MBT PF02820 183-253 289-360 388-464 496-568, Pfam-B_45320 PB045320 1-59 Mbtd1 2143977 Q6P5G3 MBTD1_MOUSE # # Polycomb group (PcG) protein # 19841675 # histone H4K20me1, H4K20me2 # # 19841675 MBTD1, Malignant Brain Tumor domain-containing protein 1, is a PcG protein.
MCRS1
(details)
# 6960 microspherule protein 1 10445 Q96EZ8 MCRS1_HUMAN FHA PF00498 363-436, MCRS_N PF13325 134-331 Mcrs1 1858420 Q99L90 MCRS1_MOUSE INO80 INO80 complex subunits Histone modification write Histone acetylation 20018852 Ino80, NSL, CHD8, MLL2/3, MLL4/WBP7 histone H4K5, H4K8, H4K16 H4K5ac, H4K8ac, H4K16ac # 20018852 Human MOF (MYST1), a member of the MYST (Moz-Ybf2/Sas3-Sas2-Tip60) family of histone acetyltransferases (HATs), is the human ortholog of the Drosophila males absent on the first (MOF) protein.
MDC1
(details)
# 21163 mediator of DNA-damage checkpoint 1 9656 Q14676 MDC1_HUMAN FHA PF00498 54-124, Pfam-B_1811 PB001811 319-407 Mdc1 3525201 Q5PSV9 MDC1_MOUSE # # Histone modification read # 16377563 # histone H2AX # # 16377563 Mammalian MDC1/NFBD1 directly binds to phospho-H2AX (gammaH2AX) by specifically interacting with the phosphoepitope at the gammaH2AX carboxyl terminus.
MEAF6
(details)
# 25674 MYST/Esa1-associated factor 6 64769 Q9HAF1 EAF6_HUMAN NuA4 PF09340 16-97 Meaf6 1917338 Q2VPQ9 EAF6_MOUSE # # Histone modification write cofactor Histone acetylation 18794358 HBO1, NuA4, MOZ/MORF histone H2A, H3K14, H4K5, H4K8, H4K12 H2Aac, H3K14ac, H4K5ac, H4K8ac, H4K12ac # 18794358 BRPF proteins bridge the association of MOZ and MORF with ING5 and EAF6=MEAF6. An N-terminal region of BRPF1 interacts with the acetyltransferases; the enhancer of polycomb (EPc) homology domain in the middle part binds to ING5 and EAF6. The association of BRPF1 with EAF6 is weak, but ING5 increases the affinity. These three proteins form a trimeric core that is conserved from Drosophila melanogaster to humans, although authentic orthologs of MOZ and MORF are absent in invertebrates. Deletion mapping studies revealed that the acetyltransferase domain of MOZ/MORF is sufficient for BRPF1 interaction. At the functional level, complex formation with BRPF1 and ING5 drastically stimulates the activity of the acetyltransferase domain in acetylation of nucleosomal histone H3 and free histones H3 and H4.
MECP2
(details)
# 6990 methyl CpG binding protein 2 4204 P51608 MECP2_HUMAN MBD PF01429 90-164 Mecp2 99918 Q9Z2D6 MECP2_MOUSE # # Histone modification write cofactor, Histone modification write cofactor, TF Histone methylation, Histone acetylation, TF repressor 10773092 # DNA mCG, DNA motif # # 10773092 Methyl-CpG-binding protein 2 (MeCP2) contains a transcriptional repression domain (TRD), which can act by recruitment of a large transcriptional co-repressor complex containing histone deacetylases HDAC1 and 2.
MEN1
(details)
# 7010 multiple endocrine neoplasia I # O00255 MEN1_HUMAN Menin PF05053 1-615 Men1 1316736 O88559 MEN1_MOUSE # # Histone modification write cofactor Histone methylation 14992727 Menin-associated_HMT, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7 histone H3K4 H3K4me # 14992727, 15199122 Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4) (UniProt).
MGA
(details)
# 14010 MGA, MAX dimerization protein 23269 Q8IWI9 MGAP_HUMAN HLH PF00010 2385-2436, Pfam-B_11518 PB011518 378-497, Pfam-B_24878 PB024878 2971-3008, Pfam-B_591 PB000591 979-1080 1332-1376, Pfam-B_7320 PB007320 1791-1938, Pfam-B_80122 PB080122 1-39, Pfam-B_8542 PB008542 653-837, T-box PF00907 76-261 Mga 1352483 A2AWL7 MGAP_MOUSE # # Histone modification write cofactor, Histone modification write cofactor, TF, TF Histone methylation, Histone acetylation, TF activator, TF repressor # RING2-L3MBTL2, CHD8, MLL2/3, MLL4/WBP7 DNA DNA motif # # # Added because it is a complex partner
MGEA5
(details)
# 7056 meningioma expressed antigen 5 (hyaluronidase) 10724 O60502 NCOAT_HUMAN NAGidase PF07555 62-364, Pfam-B_15148 PB015148 851-895 Mgea5 1932139 Q9EQQ9 NCOAT_MOUSE # # Histone modification write Histone acetylation 15485860 # histone H3K14, H4K8 H3K14ac, H4K8ac # 15485860 The HAT domain of NCOAT=MGEA5 has the ability to acetylate all four core histones when either free or bound by DNA in the context of oligonucleosome arrays.
MINA
(details)
# 19441 MYC induced nuclear antigen 84864 Q8IUF8 MINA_HUMAN Cupin_4 PF08007 51-364 Mina 1914264 Q8CD15 MINA_MOUSE # # Histone modification erase Histone methylation 19502796 # histone H3K9me3 H3K9 # 19502796 mdig=MINA is involved in demethylation of tri-methyl lysine 9 on histone H3.
MLLT1
(details)
# 7134 myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 1 4298 Q03111 ENL_HUMAN YEATS PF03366 29-112 Mllt1 1927238 # # # # Chromatin remodelling cofactor # 23623499 SWI/SNF-like_EPAFa, SWI/SNF-like EPAFB chromatin # # # 23623499 MLL-ENL (=MLLT1) inhibits polycomb repressive complex 1.
MLLT10
(details)
# 16063 myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 10 8028 P55197 AF10_HUMAN PHD_2 PF13831 36-72, Pfam-B_12689 PB012689 541-619, Pfam-B_12729 PB012729 821-879, Pfam-B_4074 PB004074 234-538, Pfam-B_6933 PB006933 721-819, Pfam-B_9291 PB009291 621-719, zf-HC5HC2H_2 PF13832 80-197 Mllt10 1329038 O54826 AF10_MOUSE PHF Zinc fingers, PHD-type Histone modification write cofactor Histone methylation 20203130 # histone H3K79 H3K79me3 # 20203130 MLLT10 =AF10 plays an important role in Dot1’s HMTase activity through either DotCom stability, catalytic activity, or the recruitment of the complex to chromatin.
MLLT6
(details)
# 7138 myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 6 4302 P55198 AF17_HUMAN Pfam-B_16181 PB016181 791-1091, Pfam-B_3448 PB003448 551-789, zf-HC5HC2H_2 PF13832 63-180 Mllt6 1935145 # # PHF Zinc fingers, PHD-type Histone modification write cofactor Histone methylation 20203130 # histone H3K79 H3K79me3 # 20203130 MLLT6 =AF17, nucleosomes containing monoubiquitinated H2B are a better substrate for DotCom in the generation of trimethylated H3K79. DotCom requires monoubiquitination of H2B for H3K79 trimethylation.
MORF4L1
(details)
# 16989 mortality factor 4 like 1 10933 Q9UBU8 MO4L1_HUMAN MRG PF05712 166-350, Tudor-knot PF11717 11-53 Morf4l1 1096551 P60762 MO4L1_MOUSE # # Histone modification read # 21423274 NuA4 histone H4 # # 21423274 Table 1 in reference (MRG15 =MORF4L1).
MORF4L2
(details)
# 16849 mortality factor 4 like 2 9643 Q15014 MO4L2_HUMAN MRG PF05712 93-276, Pfam-B_26706 PB026706 1-39 Morf4l2 1927167 Q9R0Q4 MO4L2_MOUSE # # Histone modification erase cofactor Histone acetylation 12963728 NuA4 histone # # # 12963728 The FLJ10914 protein is associated with components of the TRRAP/TIP60 histone acetyltransferase complex and binds directly to the MORF4-related MRG15 and MRGX proteins.
MOV10
(details)
New 7200 Mov10 RISC complex RNA helicase 4343 Q9HCE1 MOV10_HUMAN AAA_11 PF13086 498-605 599-691, AAA_12 PF13087 698-923, Pfam-B_18178 PB018178 1-114 Mov10 97054 P23249 MOV10_MOUSE # # # # 20543829 # histone # # # # MOV10 may be directly involved in transcriptional silencing by PcG complexes.
MPHOSPH8
(details)
# 29810 M-phase phosphoprotein 8 54737 Q99549 MPP8_HUMAN Ank_2 PF12796 570-664 647-730, Chromo PF00385 59-109 Mphosph8 1922589 Q3TYA6 MPP8_MOUSE ANKRD Ankyrin repeat domain containing Histone modification read # 21419134 # histone H3K9me3, H3K9me2 # # 21419134 M-phase phosphoprotein 8 (MPP8=MPHOSPH8) harbors an N-terminal chromodomain and a C-terminal ankyrin repeat domain. MPP8, via its chromodomain, binds histone H3 peptide tri- or di-methylated at lysine 9 (H3K9me3/H3K9me2) in submicromolar affinity.
MRGBP
(details)
# 15866 MRG/MORF4L binding protein 55257 Q9NV56 MRGBP_HUMAN Eaf7 PF07904 34-114 Mrgbp 1920497 Q9DAT2 MRGBP_MOUSE # # Histone modification write cofactor Histone acetylation 12963728 NuA4 histone # # # 12963728 TRCp120, DMAP1, and MRGBP are components of the mammalian TRRAP/TIP60 histone acetyltransferase complex.
MSH6
(details)
# 7329 mutS homolog 6 2956 P52701 MSH6_HUMAN MutS_I PF01624 407-526, MutS_II PF05188 537-703, MutS_III PF05192 737-1065, MutS_IV PF05190 932-1024, MutS_V PF00488 1074-1326, PWWP PF00855 90-182 Msh6 1343961 P54276 MSH6_MOUSE # # Histone modification read # 21423274 # histone H3K36me3 # # 21423274, 23622243 Table 1 in the reference. Via its PWWP domain it specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction.
MSL1
(details)
# 27905 male-specific lethal 1 homolog (Drosophila) 339287 Q68DK7 MSL1_HUMAN PEHE PF15275 473-591, Pfam-B_41610 PB041610 41-129, Pfam-B_70275 PB070275 1-39 Msl1 1921276 Q6PDM1 MSL1_MOUSE # # Histone modification write Histone ubiquitination 21726816 # histone H2BK34 H2BK34ub # 21726816 MSL1/2 ubiquitylates nucleosomal H2B on K34 in vitro.
MSL2
(details)
# 25544 male-specific lethal 2 homolog (Drosophila) 55167 Q9HCI7 MSL2_HUMAN Pfam-B_16851 PB016851 461-575, Pfam-B_19348 PB019348 1-89, Pfam-B_20099 PB020099 211-459, Pfam-B_22844 PB022844 91-209 Msl2 1925103 Q69ZF8 MSL2_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write Histone ubiquitination 21726816 # histone H2BK34 H2BK34ub # 21726816 RING finger protein MSL2 in the MOF-MSL complex is a histone ubiquitin E3 ligase. MSL2, together with MSL1, has robust histone ubiquitylation activity that mainly targets nucleosomal H2B on lysine 34 (H2B K34ub), a site within a conserved basic patch on H2B tail.
MSL3
(details)
# 7370 male-specific lethal 3 homolog (Drosophila) 10943 Q8N5Y2 MS3L1_HUMAN MRG PF05712 136-504, Tudor-knot PF11717 11-74 Msl3 1341851 Q9WVG9 MS3L1_MOUSE # # Histone modification read # 20943666 # histone H4K20me1 # # 20943666 MSL3 plays an important role in targeting the male specific lethal complex to chromatin in both humans and flies by binding to H4K20Me.
MST1
(details)
New 7380 macrophage stimulating 1 (hepatocyte growth factor-like) 4485 P26927 HGFL_HUMAN Kringle PF00051 110-186 191-268 283-361 370-448, PAN_1 PF00024 16-106, Trypsin PF00089 484-704 Mst1 96080 P26928 HGFL_MOUSE # # Histone modification # 17320507 # histone # # # # Classified as histone-modifying enzymes in paper.
MTA1
(details)
# 7410 metastasis associated 1 9112 Q13330 MTA1_HUMAN BAH PF01426 4-164, ELM2 PF01448 167-221, GATA PF00320 393-430 Mta1 2150037 Q8K4B0 MTA1_MOUSE GATAD GATA zinc finger domain containing Chromatin remodelling cofactor # 9885572 NuRD chromatin # # # 9885572 One subunit of NURD was identified as MTA1, a metastasis-associated protein with a region similar to the nuclear receptor corepressor, N-CoR; and antibodies against NURD partially relieve transcriptional repression by thyroid hormone receptor. These results suggest that ATP-dependent chromatin remodeling can participate in transcriptional repression by assisting repressors in gaining access to chromatin.
MTA2
(details)
# 7411 metastasis associated 1 family, member 2 9219 O94776 MTA2_HUMAN BAH PF01426 4-144, ELM2 PF01448 147-201, GATA PF00320 367-404, Pfam-B_3593 PB003593 571-637 Mta2 1346340 Q9R190 MTA2_MOUSE GATAD GATA zinc finger domain containing Histone modification erase cofactor Histone acetylation 10444591 NuRD histone # # # 10444591 MTA2 directs the assembly of an active histone deacetylase complex, and the association of MTA2 with the core HDAC/RbAp complex requires MBD3.
MTA3
(details)
# 23784 metastasis associated 1 family, member 3 57504 Q9BTC8 MTA3_HUMAN BAH PF01426 4-147, ELM2 PF01448 150-204, GATA PF00320 379-416, Pfam-B_11869 PB011869 421-489, Pfam-B_22870 PB022870 491-520 Mta3 2151172 Q924K8 MTA3_MOUSE GATAD GATA zinc finger domain containing Chromatin remodelling cofactor # 12705869 NuRD chromatin # # # 12705869 The product of human MTA3 is an estrogen-dependent component of the Mi-2/NuRD transcriptional corepressor in breast epithelial cells. MTA3 constitutes a key component of an estrogen-dependent pathway regulating growth and differentiation.
MTF2
(details)
New 29535 metal response element binding transcription factor 2 22823 Q9Y483 MTF2_HUMAN Mtf2_C PF14061 542-592, PHD PF00628 104-157 Mtf2 105050 Q02395 MTF2_MOUSE TDRD, PHF Tudor domain containing, "Zinc fingers, PHD-type" Polycomb group (PcG) protein # 21881606 PRC2 histone H3K36me3 # # 21881606 Polycomb group (PcG) that binds histone H3 trimethylated at Lys-36.
MUM1
(details)
# 29641 melanoma associated antigen (mutated) 1 84939 Q2TAK8 MUM1_HUMAN Pfam-B_7774 PB007774 1-232 Mum1 1915364 Q6DID5 MUM1_MOUSE # # Histone modification read # 217205545 # histone H3K36me, K3K79me, H4K20me # # 217205545 The PWWP domains in BRPF1, BRPF2, HDGF2, MUM1 and the N-terminal PWWP domains of WHSC1 and WHSC1L1 show weak binding affinity to histones with H3K36, K3K79 or H4K20
MYBBP1A
(details)
# 7546 MYB binding protein (P160) 1a 10514 Q9BQG0 MBB1A_HUMAN DNA_pol_phi PF04931 70-836 Mybbp1a 106181 Q7TPV4 MBB1A_MOUSE # # Chromatin remodelling cofactor # 16603771 B-WICH chromatin # # # 16603771 The WSTF (Williams syndrome transcription factor) protein is involved in vitamin D-mediated transcription and replication as a component of two distinct ATP-dependent chromatin remodeling complexes, WINAC and WICH, respectively. The WICH complex (WSTF-SNF2h) interacts with several nuclear proteins as follows: Sf3b155/SAP155, RNA helicase II/Guα, Myb-binding protein 1a, CSB.
MYO1C
(details)
# 7597 myosin IC 4641 O00159 MYO1C_HUMAN IQ PF00612 735-755 758-777, Myosin_TH1 PF06017 873-1059, Myosin_head PF00063 48-718 Myo1c 106612 Q9WTI7 MYO1C_MOUSE MYOI Myosins / Myosin superfamily : Class I Chromatin remodelling cofactor # 16603771 B-WICH chromatin # # # 16603771 The WSTF (Williams syndrome transcription factor) protein is involved in vitamin D-mediated transcription and replication as a component of two distinct ATP-dependent chromatin remodeling complexes, WINAC and WICH, respectively. The WICH complex (WSTF-SNF2h) interacts with several nuclear proteins as follows: Sf3b155/SAP155, RNA helicase II/Gualpha, Myb-binding protein 1a, CSB, the proto-oncogene Dek, and nuclear myosin 1 in a large 3-MDa assembly, B-WICH, during active transcription.
MYSM1
(details)
# 29401 Myb-like, SWIRM and MPN domains 1 114803 Q5VVJ2 MYSM1_HUMAN JAB PF01398 572-682, Myb_DNA-binding PF00249 118-163, Pfam-B_30622 PB030622 691-736, SWIRM PF04433 372-461 Mysm1 2444584 Q69Z66 MYSM1_MOUSE # # Histone modification erase Histone ubiquitination 17707232 # histone H2Aub H2A # 17707232 JAMM/MPN(+) domain-containing histone H2A deubiquitinase (2A-DUB, or KIAA1915/MYSM1) is specific for monoubiquitinated H2A (uH2A) that has permitted delineation of a strategy for specific regulatory pathways of gene activation.
NAA60
(details)
# 25875 N(alpha)-acetyltransferase 60, NatF catalytic subunit 79903 Q9H7X0 NAA60_HUMAN Acetyltransf_1 PF00583 57-156 Naa60 1922013 Q9DBU2 NAA60_MOUSE NAA N(alpha)-acetyltransferase subunits Histone modification write Histone acetylation 21981917 # histone H4K20, H4K79, H4K91 H4K20ac, H4K79ac, H4K91ac # 21981917 HAT4 =NAA60 is localized in the Golgi apparatus and displays a substrate preference for lysine residues of free histone H4, including H4K79 and H4K91, that reside in the globular domain of H4.
NAP1L1
(details)
# 7637 nucleosome assembly protein 1-like 1 4673 P55209 NP1L1_HUMAN NAP PF00956 75-346 Nap1l1 1855693 P28656 NP1L1_MOUSE # # Histone chaperone # 18226242 # histone # # # 18226242 Human Nucleosome Assembly Protein-1 (hNAP-1) =NAP1L1 is known to act as a histone chaperone that shuttles histones H2A/H2B into the nucleus, assembles nucleosomes and promotes chromatin fluidity, thereby affecting transcription of several cellular genes.
NAP1L2
(details)
New 7638 nucleosome assembly protein 1-like 2 4674 Q9ULW6 NP1L2_HUMAN NAP PF00956 109-412 Nap1l2 106654 P51860 NP1L2_MOUSE # # Histone modification cofactor # 21333655, 17591696 # histone H3, H4 # # # Interacts with H3 and H4 and may be involved in regulation of acetylation.
NAP1L4
(details)
New 7640 nucleosome assembly protein 1-like 4 4676 Q99733 NP1L4_HUMAN NAP PF00956 64-339 Nap1l4 1316687 Q78ZA7 NP1L4_MOUSE # # Histone modification cofactor # 21333655 # histone H3, H4 # # # Interacts with H3 and H4 and may be involved in regulation of acetylation.
NASP
(details)
# 7644 nuclear autoantigenic sperm protein (histone-binding) 4678 P49321 NASP_HUMAN SHNi-TPR PF10516 542-579, TPR_1 PF00515 584-617 Nasp 1355328 Q99MD9 NASP_MOUSE TTC Tetratricopeptide (TTC) repeat domain containing Chromatin remodelling # 8724350 # histone H1 # # 8724350 Binds to linker H1 histones, but not to core histones.
NAT10
(details)
# 29830 N-acetyltransferase 10 (GCN5-related) 55226 Q9H0A0 NAT10_HUMAN DUF1726 PF08351 107-201, GNAT_acetyltr_2 PF13718 528-753, Helicase_RecD PF05127 281-488, tRNA_bind_2 PF13725 771-892 Nat10 2138939 Q8K224 NAT10_MOUSE # # Histone modification write Histone acetylation 14592445 # histone # # # 14592445 hALP =NAT10 can specifically acetylate free histones in vitro. hALP may influence the activity of histone acetylation and possibly up-regulate telomerase activity through transactivation of hTERT promoter.
NBN
(details)
New 7652 nibrin 4683 O60934 NBN_HUMAN FHA PF00498 24-100, Nbs1_C PF08599 682-746 Nbn 1351625 Q9R207 NBN_MOUSE # # Chromatin remodelling # 19338747 # histone H2AX # # # Interacts with H2AX. UniProt: It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX.
NCL
(details)
# 7667 nucleolin 4691 P19338 NUCL_HUMAN Pfam-B_12581 PB012581 1-59, RRM_1 PF00076 309-377 395-460 488-554 574-641 Ncl 97286 P09405 NUCL_MOUSE RBM RNA binding motif (RRM) containing Histone chaperone # 16601700 # histone, DNA, RNA DNA motif, RNA motif # # 16601700, 15371412 The nuclear protein nucleolin =NCL possesses a histone chaperone activity and this factor greatly enhances the activity of the chromatin remodeling machineries SWI/SNF and ACF.
NCOA1
(details)
# 7668 nuclear receptor coactivator 1 8648 Q15788 NCOA1_HUMAN DUF1518 PF07469 1149-1205 1212-1268, Nuc_rec_co-act PF08815 924-973, PAS PF00989 112-183, PAS_11 PF14598 259-370, SRC-1 PF08832 625-708 Ncoa1 1276523 P70365 NCOA1_MOUSE KAT, bHLH Chromatin-modifying enzymes / K-acetyltransferases, Basic helix-loop-helix proteins Histone modification write Histone acetylation 9296499 # histone H3, H4 # # 9296499 The HAT activity of SRC-1=NCOA1 maps to its carboxy-terminal region and is primarily specific for histones H3 and H4. Acetylation by SRC-1 and PCAF of histones bound at specific promoters may result from ligand binding to steroid receptors and could be a mechanism by which the activation functions of steroid receptors and associated coactivators enhance formation of a stable preinitiation complex, thereby increasing transcription of specific genes from transcriptionally repressed chromatin templates.
NCOA2
(details)
# 7669 nuclear receptor coactivator 2 10499 Q15596 NCOA2_HUMAN DUF1518 PF07469 1281-1338, Nuc_rec_co-act PF08815 1071-1117, PAS PF00989 115-215, PAS_11 PF14598 267-379, SRC-1 PF08832 636-709 Ncoa2 1276533 Q61026 NCOA2_MOUSE KAT, bHLH Chromatin-modifying enzymes / K-acetyltransferases, Basic helix-loop-helix proteins Chromatin remodelling cofactor # 9590696 # chromatin # # # 9590696 GR, SRC-1/NcoA1 and GRIP-1/TIF-2/NcoA2 are known to bind to distinct regions. The chromatin remodelling complexes and coactivators may contribute to the transcriptional activation of organized chromatin templates.
NCOA3
(details)
# 7670 nuclear receptor coactivator 3 8202 Q9Y6Q9 NCOA3_HUMAN DUF1518 PF07469 1291-1348, Nuc_rec_co-act PF08815 1045-1095, PAS PF00989 113-210, PAS_11 PF14598 264-375, Pfam-B_10879 PB010879 1096-1195, Pfam-B_14009 PB014009 794-924, SRC-1 PF08832 616-704 Ncoa3 1276535 O09000 NCOA3_MOUSE KAT, bHLH Chromatin-modifying enzymes / K-acetyltransferases, Basic helix-loop-helix proteins Histone modification write Histone acetylation 9267036 # histone # # # 9267036 ACTR =NCOA3 is a potent histone acetyltransferase and appears to define a distinct evolutionary branch.
NCOA6
(details)
# 15936 nuclear receptor coactivator 6 23054 Q14686 NCOA6_HUMAN Nucleic_acid_bd PF13820 45-195, Pfam-B_14375 PB014375 987-1511, Pfam-B_3537 PB003537 407-669 Ncoa6 1929915 Q9JL19 NCOA6_MOUSE # # Histone modification write cofactor Histone methylation 17500065 CHD8, MLL2/3, COMPASS-like MLL3,4 histone # # # 17500065 Ectopically expressed PTIP is capable of interacting with DNA damage response proteins including 53BP1, while endogenous PTIP, and a novel protein PA1 are both components of a Set1-like histone methyltransferase (HMT) complex that also contains ASH2L, RBBP5, WDR5, hDPY-30, NCOA6, SET domain-containing HMTs MLL3 and MLL4, and substoichiometric amount of JmjC domain-containing putative histone demethylase UTX.
NCOR1
(details)
New 7672 nuclear receptor corepressor 1 9611 O75376 NCOR1_HUMAN Myb_DNA-binding PF00249 625-670, Pfam-B_4054 PB004054 1242-1723, Pfam-B_670 PB000670 1725-1983, Pfam-B_7837 PB007837 1-159 Ncor1 1349717 Q60974 NCOR1_MOUSE # # Histone modification erase cofactor Histone acetylation 14527417 # histone # # # # UniProt: Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors.
NCOR2
(details)
New 7673 nuclear receptor corepressor 2 9612 Q9Y618 NCOR2_HUMAN Myb_DNA-binding PF00249 612-657, Pfam-B_1539 PB001539 271-430 Ncor2 1337080 Q9WU42 NCOR2_MOUSE # # Histone modification erase cofactor Histone acetylation 14527417, 25006126 # # # # # # Ncor2 knockdown upregulates fos transcription by modulating the acetylation level in the fos promoter region.
NEK6
(details)
# 7749 NIMA-related kinase 6 10783 Q9HC98 NEK6_HUMAN Pkinase PF00069 45-306 Nek6 1891638 Q9ES70 NEK6_MOUSE # # Histone modification write Histone phosphorylation 12054534 # histone H1, H3 H1ph, H3ph # 12054534 Recombinant hNek6 protein produced in insect cells effectively phosphorylates histones H1 and H3, but not casein. Thus Nek6 is a mitotic histone kinase which regulates chromatin condensation in mammalian cells.
NEK9
(details)
# 18591 NIMA-related kinase 9 91754 Q8TD19 NEK9_HUMAN Pfam-B_22064 PB022064 309-349, Pkinase PF00069 52-308, RCC1 PF00415 390-441 444-495 499-547 615-665 Nek9 2387995 Q8K1R7 NEK9_MOUSE # # Histone modification write Histone phosphorylation 14660563 # histone H1 H1ph # 14660563 Endogenous, immunoprecipitated Nek9 kinase can become activated (i.e. phosphorylation on histone H1).
NFRKB
(details)
# 7802 nuclear factor related to kappaB binding protein 4798 Q6P4R8 NFRKB_HUMAN NFRKB_winged PF14465 379-478, Pfam-B_18306 PB018306 610-661 Nfrkb 2442410 Q6PIJ4 NFRKB_MOUSE INO80 INO80 complex subunits Chromatin remodelling cofactor, TF #, # 16230350 Ino80 DNA DNA motif # # 16230350 Five proteins appear to be unique to the human INO80 complex. NFRKB is a large (more than 1300 amino acids) protein. The C-terminal half of NFRKB contains low complexity, mucin-like repeats.
NFYB
(details)
# 7805 nuclear transcription factor Y, beta 4801 P25208 NFYB_HUMAN CBFD_NFYB_HMF PF00808 57-122, Pfam-B_17851 PB017851 1-39 Nfyb 97317 P63139 NFYB_MOUSE # # Chromatin remodelling, TF #, TF activator 15243141, 23332751 # DNA DNA motif # # 23332751 NF-Y is a sequence-specific transcription factor with nucleosome-like properties of nonspecific DNA binding and helps establish permissive chromatin modifications at CCAAT promoters.
NFYC
(details)
New 7806 nuclear transcription factor Y, gamma 4802 Q13952 NFYC_HUMAN CBFD_NFYB_HMF PF00808 41-105, Pfam-B_8767 PB008767 141-201 Nfyc 107901 P70353 NFYC_MOUSE # # Histone modification # 21445285 # histone # # # # NF-Y recruits Ash2L to impart H3K4 trimethylation on CCAAT promoters
NIPBL
(details)
New 28862 Nipped-B homolog (Drosophila) 25836 Q6KC79 NIPBL_HUMAN Cohesin_HEAT PF12765 1794-1835, Nipped-B_C PF12830 2274-2457, Pfam-B_338 PB000338 1292-1355, Pfam-B_4450 PB004450 1859-2018, Pfam-B_5032 PB005032 2020-2194 Nipbl 1918425 Q6KCD5 NIPBL_MOUSE # # Histone modification erase cofactor Histone acetylation 25255084, 18854353 # # # # # # Probably involved in cohesin loading and promoter-enhancer interaction. Attracts histone deacetylases.
NOC2L
(details)
# 24517 nucleolar complex associated 2 homolog (S. cerevisiae) 26155 Q9Y3T9 NOC2L_HUMAN Noc2 PF03715 325-623, Pfam-B_22168 PB022168 62-101, Pfam-B_2429 PB002429 644-713, Pfam-B_50064 PB050064 1-31 Noc2l 1931051 Q9WV70 NOC2L_MOUSE # # Chromatin remodelling, TF #, TF repressor 15100215 # histone H3 # # 15100215 INHAT =NOC2L (inhibitor of acetyltransferases) is a specific histone H3 N-terminal tail-binding complex.
NPAS2
(details)
# 7895 neuronal PAS domain protein 2 4862 Q99743 NPAS2_HUMAN HLH PF00010 10-59, PAS PF00989 84-176, PAS_11 PF14598 248-356 Npas2 109232 P97460 NPAS2_MOUSE bHLH Basic helix-loop-helix proteins Chromatin remodelling, TF #, TF activator 14645221, 24196956 # DNA DNA motif # # 14645221 There is a time-dependent recruitment of chromatin remodeling machinery by NPAS2 in vivo.
NPM1
(details)
New 7910 nucleophosmin (nucleolar phosphoprotein B23, numatrin) 4869 P06748 NPM_HUMAN Nucleoplasmin PF03066 13-196 Npm1 106184 Q61937 NPM_MOUSE # # Histone chaperone # 25349213 # histone H3, H2B, H4 # # # Co-immunoprecipitation shows that NPM1 is associated with HP1γ, core and linker histones. Uniprot: Acts as a chaperonin for the core histones H3, H2B and H4.
NPM2
(details)
New 7930 nucleophosmin/nucleoplasmin 2 10361 Q86SE8 NPM2_HUMAN TSP_1 PF00090 161-209 213-267 271-316 319-374 Npm2 1890811 Q80W85 NPM2_MOUSE # # Histone chaperone # 21863821 # histone H2A, H2B # # # Core histone chaperon. In the absence of histone tetramers, these chaperones bind H2A-H2B dimers.
NSD1
(details)
# 14234 nuclear receptor binding SET domain protein 1 64324 Q96L73 NSD1_HUMAN PHD PF00628 1709-1751, PWWP PF00855 321-419 1754-1844, Pfam-B_7228 PB007228 821-937, SET PF00856 1953-2059 Nsd1 1276545 O88491 NSD1_MOUSE KMT, PHF Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type Histone modification write Histone methylation 21196496 # histone H3K36, H4K20 H3K36me, H4K20me # 21196496 NSD1 is a SET domain histone methyltransferase that primarily dimethylates nucleosomal histone H3 lysine 36 (H3K36).
NSL1
(details)
# 24548 NSL1, MIS12 kinetochore complex component 25936 Q96IY1 NSL1_HUMAN Mis14 PF08641 67-211 Nsl1 2685830 Q8K305 NSL1_MOUSE # # Histone modification write cofactor Histone acetylation 20018852 # histone H4K16 H4K16ac # 20018852 Binding of NSL1 to MOF enhances MOF acetylation of histone H4 on lysine 16 and of the DNA binding transcription factor p53.
OGT
(details)
# 8127 O-linked N-acetylglucosamine (GlcNAc) transferase 8473 O15294 OGT1_HUMAN Glyco_transf_41 PF13844 556-1024, TPR_1 PF00515 89-122 191-224 225-258 259-292 293-326 327-360 361-394 395-428 429-462, TPR_11 PF13414 87-154, TPR_8 PF13181 160-190 Ogt 1339639 Q8CGY8 OGT1_MOUSE TTC Tetratricopeptide (TTC) repeat domain containing Histone modification write Histone GlcNAcylation 22121020 NSL histone H2BS112 H2BS112GlcNa # 22121020 Histone H2B is GlcNAcylated at residue S112 by OGT in vitro and in living cells. Histone GlcNAcylation fluctuated in response to extracellular glucose through the hexosamine biosynthesis pathway (HBP).
PADI1
(details)
# 18367 peptidyl arginine deiminase, type I 29943 Q9ULC6 PADI1_HUMAN PAD PF03068 276-663, PAD_M PF08527 115-273, PAD_N PF08526 1-113 Padi1 1338893 Q9Z185 PADI1_MOUSE PADI Peptidyl arginine deiminases Histone modification Histone citrullination 15087120 # histone H2AR, H3R, H4R H2ARci, H3Rci, H4Rci # 15087120 Peptidylarginine deiminases (PADs) convert arginine residues in proteins into citrullines. They are suspected to be involved in multiple sclerosis and rheumatoid arthritis pathophysiology, and they play a role in epidermis homeostasis and possibly in regulation of gene expression through histone modification
PADI2
(details)
# 18341 peptidyl arginine deiminase, type II 11240 Q9Y2J8 PADI2_HUMAN PAD PF03068 279-665, PAD_M PF08527 116-274, PAD_N PF08526 1-114 Padi2 1338892 Q08642 PADI2_MOUSE PADI Peptidyl arginine deiminases Histone modification Histone citrullination 15087120 # histone H2AR, H3R, H4R H2ARci, H3Rci, H4Rci # 15087120 Peptidylarginine deiminases (PADs) convert arginine residues in proteins into citrullines. They are suspected to be involved in multiple sclerosis and rheumatoid arthritis pathophysiology, and they play a role in epidermis homeostasis and possibly in regulation of gene expression through histone modification
PADI3
(details)
# 18337 peptidyl arginine deiminase, type III 51702 Q9ULW8 PADI3_HUMAN PAD PF03068 278-664, PAD_M PF08527 115-273, PAD_N PF08526 1-113 Padi3 1338891 Q9Z184 PADI3_MOUSE PADI Peptidyl arginine deiminases Histone modification Histone citrullination 15087120 # histone H2AR, H3R, H4R H2ARci, H3Rci, H4Rci # 15087120 Peptidylarginine deiminases (PADs) convert arginine residues in proteins into citrullines. They are suspected to be involved in multiple sclerosis and rheumatoid arthritis pathophysiology, and they play a role in epidermis homeostasis and possibly in regulation of gene expression through histone modification
PADI4
(details)
# 18368 peptidyl arginine deiminase, type IV 23569 Q9UM07 PADI4_HUMAN PAD PF03068 278-663, PAD_M PF08527 113-273, PAD_N PF08526 1-111 Padi4 1338898 Q9Z183 PADI4_MOUSE PADI Peptidyl arginine deiminases Histone modification Histone citrullination 15339660 # histone H2AR, H3R2, H3R8, H3R17, H3R26, H4R H2ARci, H3R2ci, H3R8ci, H3R17ci, H3R26ci, H4Rci # 15339660 Deimination converts histone arginine to citrulline and antagonizes arginine methylation. Peptidyl arginine deiminase 4 (PADI4) specifically deiminates, arginine residues R2, R8, R17, and R26 in the H3 tail. Deimination by PADI4 prevents arginine methylation by CARM1.
PAF1
(details)
New 25459 Paf1, RNA polymerase II associated factor, homolog (S. cerevisiae) 54623 Q8N7H5 PAF1_HUMAN Paf1 PF03985 27-446 Paf1 1923988 Q8K2T8 PAF1_MOUSE # # Histone modification write cofactor Histone ubiquitination 16307923 # histone H2, H3 # # # Involved in H2 and H3 ubiquitination. Involved in H2 and H3 ubiquitination. UniProt: PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3).
PAGR1
(details)
# 28707 PAXIP1 associated glutamate-rich protein 1 79447 Q9BTK6 PAGR1_HUMAN PAXIP1_C PF15364 86-221 2900092E17Rik 1914528 Q99L02 PAGR1_MOUSE # # Histone modification write cofactor, Histone modification write cofactor Histone methylation, Histone acetylation 17500065 CHD8, MLL2/3, MLL4/WBP7, COMPASS-like MLL3,4 histone # # # 17500065 Component of the MLL2/MLL3 complex (UniProt).
PAK2
(details)
# 8591 p21 protein (Cdc42/Rac)-activated kinase 2 5062 Q13177 PAK2_HUMAN PBD PF00786 73-131, Pkinase PF00069 249-500 Pak2 1339984 Q8CIN4 PAK2_MOUSE # # Histone modification write Histone phosphorylation 21724829 # histone H4S47 H4S47ph # 21724829 Phosphorylation of histone H4 Ser 47 (H4S47ph), catalyzed by the PAK2 kinase, promotes nucleosome assembly of H3.3-H4 and inhibits nucleosome assembly of H3.1-H4 by increasing the binding affinity of HIRA to H3.3-H4 and reducing association of CAF-1 with H3.1-H4.
PARG
(details)
# 8605 poly (ADP-ribose) glycohydrolase 8505 Q86W56 PARG_HUMAN PARG_cat PF05028 577-912, Pfam-B_14007 PB014007 925-955 Parg 1347094 O88622 PARG_MOUSE # # Chromatin remodelling # 23102699, 21398629 # histone H3K9 # # 23102699, 21398629 Reverses PARP activity. Both PAR and PARP-1 have an influence on PARG recruitment. Also recruitment through a PBD-mediated interaction of PARG with PCNA.
PARP1
(details)
# 270 poly (ADP-ribose) polymerase 1 142 P09874 PARP1_HUMAN BRCT PF00533 385-462, PADR1 PF08063 279-332, PARP PF00644 797-1007, PARP_reg PF02877 662-795, WGR PF05406 549-633, zf-PARP PF00645 12-90 116-200 Parp1 1340806 P11103 PARP1_MOUSE PARP Poly (ADP-ribose) polymerases Chromatin remodelling # 20926656, 17177976, 17396150 # histone H1 # # 20926656 Histone H1 poly[ADP]-ribosylation = PARP1, and its loss at specific loci, may be an epigenetic mechanism involved in the reprogramming of neuronal gene expression required for memory consolidation.
PARP2
(details)
# 272 poly (ADP-ribose) polymerase 2 10038 Q9UGN5 PARP2_HUMAN PARP PF00644 365-577, PARP_reg PF02877 231-363, WGR PF05406 111-195 Parp2 1341112 O88554 PARP2_MOUSE PARP Poly (ADP-ribose) polymerases Chromatin remodelling cofactor # 20092359 # # # # # 20092359 PARP activity is involved in processes such as chromatin remodeling. Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LRIG3. Homo- and heterodimer with PARP1.
PARP3
(details)
# 273 poly (ADP-ribose) polymerase family, member 3 10039 Q9Y6F1 PARP3_HUMAN PARP PF00644 322-533, PARP_reg PF02877 182-320, WGR PF05406 62-144 Parp3 1891258 # # PARP Poly (ADP-ribose) polymerases Polycomb group (PcG) protein # 16924674 # # # # # 16924674 PARP-3 is part of Polycomb group protein complexes.
PAXIP1
(details)
# 8624 PAX interacting (with transcription-activation domain) protein 1 22976 Q6ZW49 PAXI1_HUMAN BRCT PF00533 601-681 701-776 867-934, PTCB-BRCT PF12738 102-165, Pfam-B_13490 PB013490 1009-1064, Pfam-B_16838 PB016838 485-548 Paxip1 1890430 Q6NZQ4 PAXI1_MOUSE # # Histone modification write cofactor Histone methylation 17178841 CHD8, MLL2/3, MLL4/WBP7, COMPASS-like MLL3,4 histone H3K4 H3K4me3 # 17178841 ALR (MLL2) is a member of the human MLL family, which belongs to a larger SET1 family of histone methyltransferases. ALR is present within a stable multiprotein complex containing a cohort of proteins shared with other SET1 family complexes and several unique components, such as PTIP and the jumonji family member UTX.
PBK
(details)
New 18282 PDZ binding kinase 55872 Q96KB5 TOPK_HUMAN Pkinase PF00069 33-318 Pbk 1289156 Q9JJ78 TOPK_MOUSE # # Histone modification write Histone phosphorylation 16982762 # histone H3S10 H3S10ph # # PBK/TOPK can phosphorylate histone H3 at Ser10 in vitro and in vivo, and mediate its growth-promoting effect through histone H3 modification. Can phosphorylate histone H3 at Ser10 in vitro and in vivo.
PBRM1
(details)
# 30064 polybromo 1 55193 Q86U86 PB1_HUMAN BAH PF01426 956-1074 1156-1272, Bromodomain PF00439 54-139 186-275 392-475 532-613 666-750 785-867, HMG_box PF00505 1379-1446 Pbrm1 1923998 Q8BSQ9 PB1_MOUSE # # Histone modification read # 22464331 PBAF, SWI/SNF BRM-BRG1 histone H3 # # 22464331 Fig. 5 in the reference (PBRM1 =PB1).
PCGF1
(details)
# 17615 polycomb group ring finger 1 84759 Q9BSM1 PCGF1_HUMAN zf-C3HC4 PF00097 47-85 Pcgf1 1917087 Q8R023 PCGF1_MOUSE RNF, PCGF RING-type (C3HC4) zinc fingers, Polycomb group ring fingers Polycomb group (PcG) protein # 15620699 PRC1, BCOR # # # # 15620699 Nervous system polycomb 1 (NSPc1=PCGF1) shares high homology with vertebrate PcG proteins Mel-18 and Bmi-1.
PCGF2
(details)
# 12929 polycomb group ring finger 2 7703 P35227 PCGF2_HUMAN zf-C3HC4 PF00097 18-56 Pcgf2 99161 P23798 PCGF2_MOUSE RNF, PCGF RING-type (C3HC4) zinc fingers, Polycomb group ring fingers Polycomb group (PcG) protein # 21282530 PRC1 # # # # 21282530 CBX7 and CBX8, two Polycomb (Pc) homologs that repress INK4a, both participate in PRC1-like complexes with at least two Posterior sex combs (Psc) proteins, MEL18 =PCGF2 and BMI1.
PCGF3
(details)
# 10066 polycomb group ring finger 3 10336 Q3KNV8 PCGF3_HUMAN zf-C3HC4 PF00097 17-55 Pcgf3 1916837 Q8BTQ0 PCGF3_MOUSE RNF, PCGF RING-type (C3HC4) zinc fingers, Polycomb group ring fingers Polycomb group (PcG) protein # 21282530 PRC1, RING2-FBRS # # # # 21282530 There are multiple orthologs of the archetypal PRC1 proteins; five Pc proteins (CBX2, CBX4, CBX6, CBX7 and CBX8), six Psc proteins (BMI1, MEL18, MBLR, NSPC1, RNF159 and RNF3=PCGF3).
PCGF5
(details)
# 28264 polycomb group ring finger 5 84333 Q86SE9 PCGF5_HUMAN zf-C3HC4 PF00097 18-56 Pcgf5 1923505 Q3UK78 PCGF5_MOUSE RNF, PCGF RING-type (C3HC4) zinc fingers, Polycomb group ring fingers Polycomb group (PcG) protein # 21282530 PRC1, RING2-FBRS # # # # 21282530 There are multiple orthologs of the archetypal PRC1 proteins; five Pc proteins (CBX2, CBX4, CBX6, CBX7 and CBX8), six Psc proteins (BMI1, MEL18, MBLR, NSPC1, RNF159==PCGF5 and RNF3).
PCGF6
(details)
# 21156 polycomb group ring finger 6 84108 Q9BYE7 PCGF6_HUMAN zf-C3HC4 PF00097 134-172 Pcgf6 1918291 Q99NA9 PCGF6_MOUSE RNF, PCGF RING-type (C3HC4) zinc fingers, Polycomb group ring fingers Polycomb group (PcG) protein # 21282530 PRC1, RING2-L3MBTL2 # # # # 21282530 There are multiple orthologs of the archetypal PRC1 proteins; five Pc proteins (CBX2, CBX4, CBX6, CBX7 and CBX8), six Psc proteins (BMI1, MEL18, MBLR=PCGF6, NSPC1, RNF159 and RNF3).
PCNA
(details)
# 8729 proliferating cell nuclear antigen 5111 P12004 PCNA_HUMAN PCNA_C PF02747 127-254, PCNA_N PF00705 1-125 Pcna 97503 P17918 PCNA_MOUSE # # Chromatin remodelling # 12786946 # histone H2A, H2B # # 12786946 PCNA forms a ternary complex with DNTTIP2 and core histone.
PDP1
(details)
# 9279 pyruvate dehyrogenase phosphatase catalytic subunit 1 54704 Q9P0J1 PDP1_HUMAN PP2C PF00481 194-487, Pfam-B_13776 PB013776 99-163 Pdp1 2685870 Q3UV70 PDP1_MOUSE PPM Serine/threonine phosphatases / Protein phosphatases, Mg2+/Mn2+ dependent Histone modification read # 22150589 # histone, DNA H4K20me3 # # 22150589 The PWWP domain of Pdp1 binds not only to H4K20me3 (trimethylated Lys(20) of histone H4), but also to dsDNA (double-stranded DNA) via an aromatic cage and a positively charged area respectively. Pdp1 is a PWWP (proline-tryptophan-tryptophan-proline) domain-containing protein, which associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20.
PELP1
(details)
# 30134 proline, glutamate and leucine rich protein 1 27043 Q8IZL8 PELP1_HUMAN NUC202 PF08166 423-489 569-642, RIX1 PF08167 66-226 Pelp1 1922523 Q9DBD5 PELP1_MOUSE # # Histone modification read, Histone modification write cofactor Histone methylation, Histone acetylation 15456770, 11481323 CHD8, MLL2/3, MLL4/WBP7 histone H1, H3, H4 # # 15456770, 15374949 C-terminal glutamic acid-abundant region bound to the hypoacetylated histones H3 and H4 and prevents them from becoming substrates of histone acetyltransferase. Thus PELP1 promotes and maintains the hypoacetylated state of histones at the target genomic site, and ER binding reverses its role to hyperacetylate histones through an as yet unidentified mechanism.
PHC1
(details)
# 3182 polyhomeotic homolog 1 (Drosophila) 1911 P78364 PHC1_HUMAN Pfam-B_4954 PB004954 615-678, Pfam-B_5821 PB005821 430-536, SAM_1 PF00536 938-1002, zf-FCS PF06467 792-827 Phc1 103248 Q64028 PHC1_MOUSE SAMD Sterile alpha motif (SAM) domain containing Polycomb group (PcG) protein # 16024804 PRC1 # # # # 16024804 Phc1 plays a pivotal role in mediating the PcG-dependent bridging of distant chromatin templates.
PHC2
(details)
# 3183 polyhomeotic homolog 2 (Drosophila) 1912 Q8IXK0 PHC2_HUMAN Pfam-B_5669 PB005669 651-679, Pfam-B_6832 PB006832 1-198, SAM_1 PF00536 792-856 Phc2 1860454 Q9QWH1 PHC2_MOUSE SAMD Sterile alpha motif (SAM) domain containing Polycomb group (PcG) protein # 16024804 PRC1 # # # # 16024804 Phc2 is involved in the anterior-posterior (A-P) specification of the vertebral column through the regulation of Hox gene expression, as well as other PcG proteins.
PHC3
(details)
# 15682 polyhomeotic homolog 3 (Drosophila) 80012 Q8NDX5 PHC3_HUMAN Pfam-B_12208 PB012208 689-724, Pfam-B_17091 PB017091 431-487, Pfam-B_19383 PB019383 780-822, Pfam-B_19396 PB019396 1-39, SAM_1 PF00536 917-981 Phc3 2181434 Q8CHP6 PHC3_MOUSE SAMD Sterile alpha motif (SAM) domain containing Polycomb group (PcG) protein # 16024804 PRC1 # # # # 16024804 All known components of the PRC1 protein complex are found stably associated with CBX proteins. In particular, all the human Psc orthologs (BMI1, PCGF1, PCGF2, PCGF3, PCGF5, and PCGF6), the Ph orthologs (PHC1, PHC2, and PHC3).
PHF1
(details)
# 8919 PHD finger protein 1 5252 O43189 PHF1_HUMAN Mtf2_C PF14061 525-566, PHD PF00628 89-142, Pfam-B_18040 PB018040 1-30, Pfam-B_24844 PB024844 331-384 Phf1 98647 Q9Z1B8 PHF1_MOUSE TDRD, PHF Tudor domain containing, Zinc fingers, PHD-type Polycomb group (PcG) protein # 18086877 PRC2 # # # # 18086877 The EED-EZH2 complex, containing the core subunits EZH2, EED, SUZ12, and RbAp48, functions as a histone H3K27-specific methyltransferase. The related EED-EZH2 protein complex is distinguished from the previous complex by the presence of another PcG protein, hPHF1.
PHF10
(details)
# 18250 PHD finger protein 10 55274 Q8WUB8 PHF10_HUMAN PHD PF00628 379-436 435-481, Pfam-B_1316 PB001316 15-230 Phf10 1919307 Q9D8M7 PHF10_MOUSE PHF Zinc fingers, PHD-type Chromatin remodelling # 20068294 npBAF, SWI/SNF BRM-BRG1 chromatin # # # 20068294 PHF10 belongs to a family of plant homeodomain (PHD) containing proteins which play a role in transcription regulation via chromatin remodeling.
PHF12
(details)
# 20816 PHD finger protein 12 57649 Q96QT6 PHF12_HUMAN PHD PF00628 58-105 273-318 Phf12 1924057 Q5SPL2 PHF12_MOUSE PHF Zinc fingers, PHD-type Histone modification erase cofactor Histone acetylation 11390640 # histone # # # 11390640 Pf1 =PHF12 is a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex.
PHF13
(details)
# 22983 PHD finger protein 13 148479 Q86YI8 PHF13_HUMAN PHD PF00628 234-280, Pfam-B_28476 PB028476 1-49 Phf13 2446217 Q8K2W6 PHF13_MOUSE PHF Zinc fingers, PHD-type Histone modification read # 19638409 # histone H3K4me3 # # 19638409 Interacts with histone H3 that is trimethylated at 'Lys-4' (H3K4me3).
PHF14
(details)
# 22203 PHD finger protein 14 9678 O94880 PHF14_HUMAN PHD PF00628 321-380 727-779, Pfam-B_16803 PB016803 175-216, Pfam-B_19012 PB019012 218-295, zf-HC5HC2H_2 PF13832 383-498 Phf14 1923539 Q9D4H9 PHF14_MOUSE PHF Zinc fingers, PHD-type Histone modification read # 23688586 # histone H2A, H2B, H3 H2Aac, H2Bac, H3ac # 23688586 PHF14α is bound to histones. Histone H3, H2A, and H2B can be co-immunoprecipitated with GFP-PHF14α, but not with GFP alone, from total cell lysate. Histones H3, H2A, and H2B can be pulled down together with non-tagged exogenous PHF14α using an anti-PHF14 antibody.
PHF19
(details)
# 24566 PHD finger protein 19 26147 Q5T6S3 PHF19_HUMAN Mtf2_C PF14061 529-579, PHD PF00628 98-151, Pfam-B_31053 PB031053 1-59 Phf19 1921266 Q9CXG9 PHF19_MOUSE TDRD, PHF Tudor domain containing, Zinc fingers, PHD-type Chromatin remodelling, Histone modification write cofactor #, Histone acetylation 15563832 PRC2 histone # # # 15563832 Based on motifs identified within the hPCL3 =PHF19 open reading frames, hPCL3 proteins are likely to be nuclear proteins that regulate transcription and/or chromatin structure.
PHF2
(details)
# 8920 PHD finger protein 2 5253 O75151 PHF2_HUMAN JmjC PF02373 236-336, PHD PF00628 7-56, Pfam-B_3847 PB003847 851-988 Phf2 1338034 Q9WTU0 PHF2_MOUSE KDM, PHF Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type Histone modification erase Histone methylation 21532585 # histone H3K9me2 H3K9 # 21532585 The protein kinase A (PKA)-dependent histone lysine demethylase complex, PHF2-ARID5B. PHF2, a jmjC demethylase, is enzymatically inactive by itself, but becomes an active H3K9Me2 demethylase through PKA-mediated phosphorylation.
PHF20
(details)
# 16098 PHD finger protein 20 51230 Q9BVI0 PHF20_HUMAN DUF3776 PF12618 173-279, PHD PF00628 654-700, Pfam-B_21846 PB021846 511-589, Pfam-B_23453 PB023453 280-309 Phf20 2444148 Q8BLG0 PHF20_MOUSE TDRD, PHF Tudor domain containing, Zinc fingers, PHD-type Histone modification write Histone acetylation 22449972 NSL, CHD8, MLL2/3, MLL4/WBP7 histone H4 H4ac # 22449972 The second Tudor domain of PHF20 displays preference for dimethylated histones substrates.
PHF20L1
(details)
# 24280 PHD finger protein 20-like 1 51105 A8MW92 P20L1_HUMAN DUF3776 PF12618 210-317 415-518, PHD PF00628 683-729, Pfam-B_37699 PB037699 791-849 Phf20l1 2444412 Q8CCJ9 P20L1_MOUSE TDRD, PHF Tudor domain containing, Zinc fingers, PHD-type Histone modification read # 21423274 # histone H3K4me # # 21423274 Table 1 in the reference. Via its PWWP domain it specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair rea
PHF21A
(details)
# 24156 PHD finger protein 21A 51317 Q96BD5 PF21A_HUMAN AT_hook PF02178 425-436, PHD PF00628 490-535, Pfam-B_15568 PB015568 536-649, Pfam-B_7050 PB007050 1-349 Phf21a 2384756 Q6ZPK0 PF21A_MOUSE PHF Zinc fingers, PHD-type Histone modification erase cofactor Histone methylation 16140033 BHC, LSD-CoREST histone # # # 16140033 LSD1 is a recently identified human lysine (K)-specific histone demethylase. LSD1 is associated with HDAC1/2; CoREST, a SANT domain-containing corepressor; and BHC80=PHF21A, a PHD domain-containing protein, among others.
PHF8
(details)
# 20672 PHD finger protein 8 23133 Q9UPP1 PHF8_HUMAN JmjC PF02373 270-370, PHD PF00628 43-92, Pfam-B_22520 PB022520 499-557, Pfam-B_5629 PB005629 779-877 Phf8 2444341 Q80TJ7 PHF8_MOUSE KDM, PHF Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type Histone modification erase Histone methylation 21423274 # histone H3K9me1, H3K9me2, H3K27me2, H4K20me1, H3K36me2, H3K36me3, H3K4me3 H3K9, H3K27, H4K20, H3K36, H3K4 # 21423274 Table 1 in the reference. Via its PWWP domain it specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair rea
PHIP
(details)
# 15673 pleckstrin homology domain interacting protein 55023 Q8WWQ0 PHIP_HUMAN Bromodomain PF00439 1165-1251 1325-1409, Pfam-B_15784 PB015784 743-864, Pfam-B_60538 PB060538 1-77, WD40 PF00400 174-211 215-253 257-298 355-393 456-495 Phip 1932404 Q8VDD9 PHIP_MOUSE WDR, DCAF WD repeat domain containing, DDB1 and CUL4 associated factors Histone modification read # 22464331 # histone H3 # # 22464331 Fig. 5 in the reference.
PIWIL4
(details)
# 18444 piwi-like RNA-mediated gene silencing 4 143689 Q7Z3Z4 PIWL4_HUMAN PAZ PF02170 271-407, Pfam-B_2782 PB002782 101-219, Pfam-B_34294 PB034294 1-99, Piwi PF02171 546-838 Piwil4 3041167 Q8CGT6 PIWL4_MOUSE AGO Argonaute/PIWI family Chromatin remodelling, Histone modification erase cofactor #, Histone methylation 17544373 # histone H3K9 # # 17544373 Induced histone H3 lysine 9 methylation at the p16(Ink4a) (CDKN2A) locus. Suggests that PIWIL4 plays important roles in the chromatin-modifying pathway in human somatic cells.
PKM
(details)
# 9021 pyruvate kinase, muscle 5315 P14618 KPYM_HUMAN PK PF00224 42-395, PK_C PF02887 409-529 Pkm 97591 P52480 KPYM_MOUSE # # Histone modification write cofactor Histone phosphorylation 24706538 # histone H3S10, H3S28, H2BS32 H3S10ph, H3S28ph, H2BS32ph, H3T11ph # 24706538 Transcriptional activation by epidermal growth factor (EGF) is mediated via phosphorylation of H3S10, H3S28, and H2BS32 by Rsk-2 and PKM2.
PKN1
(details)
# 9405 protein kinase N1 5585 Q16512 PKN1_HUMAN HR1 PF02185 37-105 126-198 213-285, Pfam-B_33979 PB033979 8-36, Pkinase PF00069 615-874, Pkinase_C PF00433 894-940 Pkn1 108022 P70268 PKN1_MOUSE # # Histone modification write Histone phosphorylation 18066052 # histone H3T11 H3T11ph # 18066052 Protein-kinase-C-related kinase 1 (PRK1=PKN1) phosphorylates histone H3 at threonine 11 (H3T11) upon ligand-dependent recruitment to androgen receptor target genes.
POGZ
(details)
New 18801 pogo transposable element with ZNF domain 23126 Q7Z3K3 POGZ_HUMAN DDE_1 PF03184 1117-1304, HTH_Tnp_Tc5 PF03221 1024-1085, Pfam-B_10413 PB010413 693-771, Pfam-B_10981 PB010981 1-69, Pfam-B_5179 PB005179 796-843, Pfam-B_6754 PB006754 773-795 Pogz 2442117 Q8BZH4 POGZ_MOUSE # # Histone modification read Histone methylation 20562864, 20850016 # histone H3K9me3 # # # Part of a H3K9me3 reader complex; modulates dissociation of HP1alpha.
POLE3
(details)
# 13546 polymerase (DNA directed), epsilon 3, accessory subunit 54107 Q9NRF9 DPOE3_HUMAN CBFD_NFYB_HMF PF00808 8-73, Pfam-B_35841 PB035841 74-135 Pole3 1933378 Q9JKP7 DPOE3_MOUSE POL DNA polymerases Histone chaperone # 10880450 CHRAC histone # # # 10880450 The human homologues of two novel putative histone-fold proteins in Drosophila CHRAC are present in HuCHRAC. The two human histone-fold proteins form a stable complex that binds naked DNA but not nucleosomes.
PPARGC1A
(details)
New 9237 peroxisome proliferator-activated receptor gamma, coactivator 1 alpha 10891 Q9UBK2 PRGC1_HUMAN Pfam-B_19319 PB019319 241-286, RRM_1 PF00076 679-742 Ppargc1a 1342774 O70343 PRGC1_MOUSE RBM RNA binding motif (RRM) containing Histone modification cofactor # 10558993 # histone # # # # PPARgamma coactivator-1 (PGC-1) promotes transcription through the assembly of a complex that includes the histone acetyltransferases steroid receptor coactivator-1 (SRC-1). Promotes transcription through the assembly of a complex that includes HAT p300.
PPM1G
(details)
# 9278 protein phosphatase, Mg2+/Mn2+ dependent, 1G 5496 O15355 PPM1G_HUMAN PP2C PF00481 25-120 264-492 Ppm1g 106065 Q61074 PPM1G_MOUSE PPM Serine/threonine phosphatases / Protein phosphatases, Mg2+/Mn2+ dependent Chromatin remodelling # 23723158 # chromatin # # # 23723158 Together with CHRAC1, ACF1 and ISWI/SNF2H proteins, it forms the ISWI chromatin-remodeling complex, CHRAC (UniProt).
PPP2CA
(details)
# 9299 protein phosphatase 2, catalytic subunit, alpha isozyme 5515 P67775 PP2AA_HUMAN Metallophos PF00149 50-245 Ppp2ca 1321159 P63330 PP2AA_MOUSE PPP Serine/threonine phosphatases / Protein phosphatase, catalytic subunits Histone modification write Histone phosphorylation 18758438 # histone H2AX H2AXph # 18758438 PP2A =PPP2CA (rather than PP4) has been implicated as a mammalian γH2AX phosphatase.
PPP4C
(details)
# 9319 protein phosphatase 4, catalytic subunit 5531 P60510 PP4C_HUMAN Metallophos PF00149 47-242 Ppp4c 1891763 P97470 PP4C_MOUSE PPP Serine/threonine phosphatases / Protein phosphatase, catalytic subunits Histone modification erase Histone phosphorylation 18758438 PPP4C-PPP4R2-PPP4R3A histone H2AXS139ph H2AXS139 # 18758438 PP4 and PP2A counteract phosphorylation of H2AX.
PPP4R2
(details)
New 18296 protein phosphatase 4, regulatory subunit 2 151987 Q9NY27 PP4R2_HUMAN PPP4R2 PF09184 2-267 Ppp4r2 3027896 Q0VGB7 PP4R2_MOUSE PPP4R Serine/threonine phosphatases / Protein phosphatase 4, regulatory subunits Histone modification cofactor # 18614045 PPP4C-PPP4R2-PPP4R3A histone # # # # Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4) complex. PPARgamma coactivator-1 (PGC-1) promotes transcription through the assembly of a complex that includes the histone acetyltransferases steroid receptor coactivator-1
PRDM1
(details)
# 9346 PR domain containing 1, with ZNF domain 639 O75626 PRDM1_HUMAN SET PF00856 99-201, zf-H2C2_2 PF13465 589-614 617-642 645-670 Prdm1 99655 Q60636 PRDM1_MOUSE ZNF Zinc fingers, C2H2-type Histone modification write cofactor Histone methylation 23856557 # histone H3K9 H3K9me # 23856557 The Prdm family may possess HKMTase properties. Some Prdms show intrinsic HKMTase activity (Prdm2, Prdm3, Prdm8, Prdm9, and Prdm16). In addition, Prdm1, Prdm5, and Prdm6 lack intrinsic HKMTase activity, but instead recruit G9a/Ehmt2/KMT1C, a strong mammalian histone H3 lysine 9 (H3K9) methyltransferase, to mediate HKMTase activity (see Fog et al., 2012 for a review). Another structural feature is that the Prdm family has multiple kruppel-type zinc finger (ZF) domains in the C-terminus involved in sequence-specific DNA binding and protein-protein interactions.
PRDM11
(details)
# 13996 PR domain containing 11 56981 Q9NQV5 PRD11_HUMAN Pfam-B_3219 PB003219 1-353 Prdm11 2685553 A2AGX3 PRD11_MOUSE # # Histone modification write Histone methylation 23508829 # histone # # # 23508829 The PR (PRDI-BF1 and RIZ) domain is 20–30% identical to the SET module, which is directly responsible for the catalytic activity of several histone lysine-methyltransferases .
PRDM12
(details)
# 13997 PR domain containing 12 59335 Q9H4Q4 PRD12_HUMAN Pfam-B_39033 PB039033 1-49, zf-H2C2_2 PF13465 257-282 285-310 Prdm12 2685844 A2AJ77 PRD12_MOUSE ZNF Zinc fingers, C2H2-type Histone modification write cofactor Histone methylation 23856557 # histone H3K9 H3K9me # 23856557 Prdm12 recruits G9a to methylate histone H3 on lysine 9 through its zinc finger domains. 
PRDM13
(details)
New 13998 PR domain containing 13 59336 Q9H4Q3 PRD13_HUMAN zf-C2H2 PF00096 137-160, zf-H2C2_2 PF13465 587-611 615-641 Prdm13 2448528 E9PZZ1 PRD13_MOUSE # # Histone modification write Histone methylation 24370451 # histone # # # # PRDM13 identified as a histone methyltransferase.
PRDM14
(details)
New 14001 PR domain containing 14 63978 Q9GZV8 PRD14_HUMAN SET PF00856 265-367, zf-C2H2 PF00096 546-568, zf-C2H2_4 PF13894 400-421 432-455, zf-H2C2_2 PF13465 475-500 504-528 Prdm14 3588194 E9Q3T6 PRD14_MOUSE ZNF Zinc fingers, C2H2-type DNA modification DNA demethylation 24335252 # DNA mC # # 24335252 PRDM14 promotes active DNA demethylation.
PRDM16
(details)
# 14000 PR domain containing 16 63976 Q9HAZ2 PRD16_HUMAN Pfam-B_2662 PB002662 14-127, zf-C2H2 PF00096 337-360 366-388 394-416 423-445 979-1002 1008-1032, zf-C2H2_6 PF13912 229-255, zf-H2C2_2 PF13465 295-319 965-989 Prdm16 1917923 A2A935 PRD16_MOUSE ZNF Zinc fingers, C2H2-type Histone modification write cofactor, TF Histone methylation, TF repressor 12816872, 23856557 # histone, DNA H3K9, DNA motif H3K9me # 23856557 The Prdm family may possess HKMTase properties. Some Prdms show intrinsic HKMTase activity (Prdm2, Prdm3, Prdm8, Prdm9, and Prdm16). In addition, Prdm1, Prdm5, and Prdm6 lack intrinsic HKMTase activity, but instead recruit G9a/Ehmt2/KMT1C, a strong mammalian histone H3 lysine 9 (H3K9) methyltransferase, to mediate HKMTase activity (see Fog et al., 2012 for a review). Another structural feature is that the Prdm family has multiple kruppel-type zinc finger (ZF) domains in the C-terminus involved in sequence-specific DNA binding and protein-protein interactions.
PRDM2
(details)
# 9347 PR domain containing 2, with ZNF domain 7799 Q13029 PRDM2_HUMAN Pfam-B_29325 PB029325 1053-1085, SET PF00856 41-141, zf-C2H2 PF00096 390-412, zf-C2H2_4 PF13894 360-383 483-506 1134-1157 1191-1214 1455-1475 Prdm2 107628 # # KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation 20084102 # histone H3K9 H3K9me # 20084102 The structures of the catalytic domains of GLP, G9a, Suv39H2 and PRDM2, four of the eight known human H3K9 methyltransferases in their apo conformation or in complex with the methyl donating cofactor, and peptide substrates.
PRDM4
(details)
# 9348 PR domain containing 4 11108 Q9UKN5 PRDM4_HUMAN Pfam-B_13260 PB013260 461-509, zf-C2H2 PF00096 730-752, zf-H2C2_2 PF13465 632-657 660-683 688-713 Prdm4 1920093 Q80V63 PRDM4_MOUSE ZNF Zinc fingers, C2H2-type Histone modification write Histone methylation 23048031 # histone H4R3 H4R3me2s # 23048031 Transcription factor positive regulatory domain 4 (PRDM4) recruits protein arginine methyltransferase 5 (PRMT5) to mediate histone arginine methylation and control neural stem cell proliferation and differentiation.
PRDM5
(details)
# 9349 PR domain containing 5 11107 Q9NQX1 PRDM5_HUMAN zf-C2H2 PF00096 199-221 262-287 603-625, zf-C2H2_4 PF13894 167-190, zf-C2H2_jaz PF12171 375-399, zf-H2C2_2 PF13465 334-359 418-443 446-472 475-500 503-528 531-556 559-583, zf-met PF12874 234-254 295-317 Prdm5 1918029 Q9CXE0 PRDM5_MOUSE ZNF Zinc fingers, C2H2-type Histone modification write Histone methylation 23856557 # histone H3K9 H3K9me # 23856557 Some Prdms show intrinsic HKMTase activity (Prdm2, Prdm3, Prdm8, Prdm9, and Prdm16). In addition, Prdm1, Prdm5, and Prdm6 lack intrinsic HKMTase activity, but instead recruit G9a/Ehmt2/KMT1C, a strong mammalian histone H3 lysine 9 (H3K9) methyltransferase, to mediate HKMTase activity (see Fog et al., 2012 for a review). Another structural feature is that the Prdm family has multiple kruppel-type zinc finger (ZF) domains in the C-terminus involved in sequence-specific DNA binding and protein-protein interactions.
PRDM6
(details)
# 9350 PR domain containing 6 93166 Q9NQX0 PRDM6_HUMAN SET PF00856 259-365, zf-C2H2 PF00096 501-523, zf-C2H2_4 PF13894 473-495, zf-H2C2_2 PF13465 543-568 Prdm6 2684938 Q3UZD5 PRDM6_MOUSE ZNF Zinc fingers, C2H2-type Histone modification write Histone methylation 17898714, 16537907 # histone H3R2, H4K20 H3R2me1, H3R2me2, H4K20me1 # 17898714, 18057026 The arginine methyltransferase PRMT6 catalyses H3R2 di-methylation in vitro and controls global levels of H3R2me2a in vivo. H3R2 methylation by PRMT6 was prevented by the presence of H3K4me3 on the H3 tail. PRISM =PRDM6 acts as a transcriptional repressor by interacting with class I histone deacetylases and the G9a histone methyltransferase, thereby identifying PRISM as a novel SMC-restricted epigenetic regulator.
PRDM7
(details)
# 9351 PR domain containing 7 11105 Q9NQW5 PRDM7_HUMAN KRAB PF01352 27-65, SSXRD PF09514 170-202 # # # # ZNF, ZKRAB Zinc fingers, C2H2-type Histone modification write Histone methylation # # histone # # # # Probable histone methyltransferase (by similarity).
PRDM8
(details)
# 13993 PR domain containing 8 56978 Q9NQV8 PRDM8_HUMAN zf-C2H2 PF00096 627-648 666-688 Prdm8 1924880 Q8BZ97 PRDM8_MOUSE # # Histone modification write Histone methylation 23856557 # histone # # # 23856557 Some Prdms show intrinsic HKMTase activity (Prdm2, Prdm3, Prdm8, Prdm9, and Prdm16). In addition, Prdm1, Prdm5, and Prdm6 lack intrinsic HKMTase activity, but instead recruit G9a/Ehmt2/KMT1C, a strong mammalian histone H3 lysine 9 (H3K9) methyltransferase, to mediate HKMTase activity (see Fog et al., 2012 for a review). Another structural feature is that the Prdm family has multiple kruppel-type zinc finger (ZF) domains in the C-terminus involved in sequence-specific DNA binding and protein-protein interactions.
PRDM9
(details)
# 13994 PR domain containing 9 56979 Q9NQV7 PRDM9_HUMAN KRAB PF01352 27-65, SSXRD PF09514 170-202, zf-C2H2 PF00096 860-882, zf-H2C2_2 PF13465 540-562 566-590 594-619 622-647 650-674 678-702 706-731 734-758 762-786 790-815 818-843 846-871 Prdm9 2384854 Q96EQ9 PRDM9_MOUSE ZKRAB, ZNF Zinc fingers, C2H2-type Histone modification write Histone methylation 17916234 # histone H3K4 H3K4me3 # 17916234 Meisetz, the mouse ortholog of the long PRDM9 isoform, is able to activate the progression into meiosis through the trimethylation of the lysine 4 on histone H3.
PRKAA1
(details)
New 9376 protein kinase, AMP-activated, alpha 1 catalytic subunit 5562 Q13131 AAPK1_HUMAN Pfam-B_8588 PB008588 351-524, Pkinase PF00069 27-279 Prkaa1 2145955 Q5EG47 AAPK1_MOUSE # # Histone modification write Histone phosphorylation 20647423 # histone H2BS36 H2BS36ph # # In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Part of AMPK.
PRKAA2
(details)
New 9377 protein kinase, AMP-activated, alpha 2 catalytic subunit 5563 P54646 AAPK2_HUMAN Pkinase PF00069 16-268 Prkaa2 1336173 Q8BRK8 AAPK2_MOUSE # # Histone modification write Histone phosphorylation 20647423 # histone H2BS36 H2BS36ph # # In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph) as a part of AMPK.
PRKAB1
(details)
New 9378 protein kinase, AMP-activated, beta 1 non-catalytic subunit 5564 Q9Y478 AAKB1_HUMAN AMPKBI PF04739 149-270 Prkab1 1336167 Q9R078 AAKB1_MOUSE # # Histone modification write cofactor Histone phosphorylation 20647423 # histone # # # # Non-catalytic subunit of AMP-activated protein kinase (AMPK).
PRKAB2
(details)
New 9379 protein kinase, AMP-activated, beta 2 non-catalytic subunit 5565 O43741 AAKB2_HUMAN AMPKBI PF04739 155-272 Prkab2 1336185 Q6PAM0 AAKB2_MOUSE # # Histone modification write cofactor Histone phosphorylation 20647423 # histone # # # # Non-catalytic subunit of AMP-activated protein kinase (AMPK).
PRKAG1
(details)
New 9385 protein kinase, AMP-activated, gamma 1 non-catalytic subunit 5571 P54619 AAKG1_HUMAN CBS PF00571 39-97 118-178 187-252 263-324 Prkag1 108411 O54950 AAKG1_MOUSE # # Histone modification write cofactor Histone phosphorylation 20647423 # histone # # # # AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK).
PRKAG2
(details)
New 9386 protein kinase, AMP-activated, gamma 2 non-catalytic subunit 51422 Q9UGJ0 AAKG2_HUMAN CBS PF00571 350-410 428-484 494-556, Pfam-B_5182 PB005182 268-349 Prkag2 1336153 Q91WG5 AAKG2_MOUSE # # Histone modification write cofactor Histone phosphorylation 20647423 # histone # # # # AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK).
PRKAG3
(details)
New 9387 protein kinase, AMP-activated, gamma 3 non-catalytic subunit 53632 Q9UGI9 AAKG3_HUMAN CBS PF00571 273-333 350-406 414-479 Prkag3 1891343 Q8BGM7 AAKG3_MOUSE # # Histone modification write cofactor Histone phosphorylation 20647423 # histone # # # # AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK).
PRKCA
(details)
New 9393 protein kinase C, alpha 5578 P17252 KPCA_HUMAN C1_1 PF00130 37-89 102-154, C2 PF00168 173-260, Pkinase PF00069 339-597, Pkinase_C PF00433 622-662 Prkca 97595 P20444 KPCA_MOUSE # # Histone modification write cofactor Histone phosphorylation 22796964 # histone H3 # # # Modifies H3, but may be a quite general kinase.
PRKCB
(details)
# 9395 protein kinase C, beta 5579 P05771 KPCB_HUMAN C1_1 PF00130 37-89 102-154, C2 PF00168 173-260, Pkinase PF00069 342-600, Pkinase_C PF00433 620-666 Prkcb 97596 P68404 KPCB_MOUSE # # Histone modification write Histone methylation 20228790 # histone H3T6 H3T6ph # 20228790 Phosphorylation of histone H3 at threonine 6 (H3T6) by protein kinase C beta I (PKCbeta(I), also known as PRKCbeta) is the key event that prevents LSD1 from demethylating H3K4 during AR-dependent gene activation.
PRKCD
(details)
New 9399 protein kinase C, delta 5580 Q05655 KPCD_HUMAN C1_1 PF00130 159-211 231-283, Pkinase PF00069 349-603, Pkinase_C PF00433 623-669 Prkcd 97598 P28867 KPCD_MOUSE # # Histone modification # 17984964 # histone # # # # Cross-regulation of histone modifications
PRKDC
(details)
# 9413 protein kinase, DNA-activated, catalytic polypeptide 5591 P78527 PRKDC_HUMAN FAT PF02259 3023-3470, FATC PF02260 4096-4128, NUC194 PF08163 1813-2210, PI3_PI4_kinase PF00454 3747-4015, Pfam-B_14440 PB014440 411-472, Pfam-B_1565 PB001565 131-345, Pfam-B_9125 PB009125 2650-2694 Prkdc 104779 P97313 PRKDC_MOUSE # # Histone modification write Histone phosphorylation 14627815 # histone H2AXS139, H2AFXS139 H2AXS139ph, H2AFXS139ph # 14627815 Acetylation largely enhances the phosphorylation of H2AX by DNA-PK=PRKDC, and this acetylation effect is observed when H2AX exists in the context of nucleosomes but not in a free form.
PRMT1
(details)
# 5187 protein arginine methyltransferase 1 3276 Q99873 ANM1_HUMAN Methyltransf_31 PF13847 76-216 Prmt1 107846 Q9JIF0 ANM1_MOUSE PRMT Protein arginine methyltransferases Histone modification write Histone methylation 11387442 # histone H4R3 H4R3me1, H4R3me2a # 11387442 PRMT1 specifically methylates arginine 3 (Arg 3) of H4 in vitro and in vivo. Methylation of Arg 3 by PRMT1 facilitates subsequent acetylation of H4 tails by p300.
PRMT2
(details)
# 5186 protein arginine methyltransferase 2 3275 P55345 ANM2_HUMAN PRMT5 PF05185 114-415, SH3_9 PF14604 37-84 Prmt2 1316652 Q9R144 ANM2_MOUSE PRMT Protein arginine methyltransferases Histone modification write Histone methylation 19405910 # histone H4 H4me # 19405910 PRMT2 activity is substantially lower than PRMT1 in vitro, but both enzymes selectively methylate histone H4 and PRMT2, like PRMT1, may act as a transcription co-activator through this modification.
PRMT5
(details)
# 10894 protein arginine methyltransferase 5 10419 O14744 ANM5_HUMAN PRMT5 PF05185 181-619, Pfam-B_18578 PB018578 1-49 Prmt5 1351645 Q8CIG8 ANM5_MOUSE PRMT Protein arginine methyltransferases Histone modification write Histone methylation 18404153 methylosome histone H3R8, H4R3 H3R8me, H4R3me # 18404153 PRMT5 regulates gene transcription by methylating histones H3 (R8) and H4.
PRMT6
(details)
# 18241 protein arginine methyltransferase 6 55170 Q96LA8 ANM6_HUMAN Methyltransf_18 PF12847 82-189 Prmt6 2139971 Q6NZB1 ANM6_MOUSE PRMT Protein arginine methyltransferases Histone modification write Histone methylation 18079182 # histone H2AR3, H3R2, H4R4 H2AR3me, H4R3me, H3R2me2a # 18079182 PRMT6 methylates histone H3 at R2 and histones H4/H2A at R3 in vitro. Overexpression and knockdown analysis identify PRMT6 as the major H3 R2 methyltransferase in vivo.
PRMT7
(details)
# 25557 protein arginine methyltransferase 7 54496 Q9NVM4 ANM7_HUMAN Pfam-B_13426 PB013426 301-359, PrmA PF06325 54-149 Prmt7 2384879 Q922X9 ANM7_MOUSE PRMT Protein arginine methyltransferases Histone modification write Histone methylation 15494416 # histone H2A, H4R3 H2A, H4R3me2 # 15494416 PRMT7 contains methyltransferase activity, the methylated (labeled) histones are H2A and H4.
PRMT8
(details)
# 5188 protein arginine methyltransferase 8 56341 Q9NR22 ANM8_HUMAN PrmA PF06325 102-200 Prmt8 3043083 Q6PAK3 ANM8_MOUSE PRMT Protein arginine methyltransferases Histone modification write Histone methylation 16051612 # histone H4R H4Rme # 16051612 PRMT8 preferentially methylates histone H4 and the recombinant forms of GAR and Npl3, thus displaying PRMT1-like substrate specificity.
PRMT9
(details)
# 25099 protein arginine methyltransferase 9 90826 Q6P2P2 ANM9_HUMAN PrmA PF06325 167-257, TPR_11 PF13414 67-132 Prmt10 2142651 Q3U3W5 ANM9_MOUSE PRMT Protein arginine methyltransferases Histone modification write Histone methylation 18007657 # histone H4R3 H4R3me2 # 18007657 Arabidopsis thaliana protein arginine methyltransferase 10 (AtPRMT10)--the Arabidopsis homologue of PHRMT10 (=PRMT9)--has been shown to be a type I PRMT, which preferentially asymmetrically methylated histone H4R3 in vitro. Belongs to SAM-binding ethyltransferase superfamily.
PRPF31
(details)
# 15446 pre-mRNA processing factor 31 26121 Q8WWY3 PRP31_HUMAN NOSIC PF08060 92-144, Nop PF01798 186-334, Pfam-B_23523 PB023523 1-44, Prp31_C PF09785 336-465 Prpf31 1916238 Q8CCF0 PRP31_MOUSE # # Histone modification write cofactor, Histone modification write cofactor Histone methylation, Histone acetylation # CHD8, MLL2/3, MLL4/WBP7 histone # # # # Added because it is a complex partner
PRR14
(details)
New 28458 proline rich 14 78994 Q9BWN1 PRR14_HUMAN Tantalus PF15386 457-517 Prr14 2384565 Q7TPN9 PRR14_MOUSE # # Histone modification write Histone phosphorylation 24209742 # histone H3K9me2, H3K9me3 # # # Binds to H3K9me2/3 through interaction with HP1, and not by direct interaction. PRR14 is incorporated rapidly into chromatin through HP1 binding, tethering heterochromatin to nuclear lamina.
PSIP1
(details)
# 9527 PC4 and SFRS1 interacting protein 1 11168 O75475 PSIP1_HUMAN LEDGF PF11467 349-455, PWWP PF00855 5-87 Psip1 2142116 Q99JF8 PSIP1_MOUSE # # Chromatin remodelling # 217205545 # chromatin # # # 217205545 The PWWP domain in PSIP1 displays affinity for DNA and chromatin and its chromatin binding ability is crucial for the HIV-1 integration. PSIP1 has been found to promote association of the MLL complex with transcriptionally active chromatin through its PWWP domain.
RAD51
(details)
# 9817 RAD51 recombinase 5888 Q06609 RAD51_HUMAN HHH_5 PF14520 28-80, Rad51 PF08423 83-338 Rad51 97890 Q08297 RAD51_MOUSE # # Histone modification erase Histone ubiquitination 15665856 BRCC # histone # # 15665856 #
RAD54B
(details)
# 17228 RAD54 homolog B (S. cerevisiae) 25788 Q9Y620 RA54B_HUMAN Helicase_C PF00271 678-758, Pfam-B_10171 PB010171 772-829, SNF2_N PF00176 299-598 Rad54b 3605986 Q6PFE3 RA54B_MOUSE # # Chromatin remodelling # 21357745 # chromatin # # # 21357745 Rad54’s ATPase =RAD54B affects the chromatin association of the protein and Rad54 ATPase activity specifically influences its dissociation from foci.
RAD54L
(details)
# 9826 RAD54-like (S. cerevisiae) 8438 Q92698 RAD54_HUMAN Helicase_C PF00271 531-611, Pfam-B_14570 PB014570 674-743, Rad54_N PF08658 33-138, SNF2_N PF00176 156-463 Rad54l 894697 P70270 RAD54_MOUSE # # Chromatin remodelling # 8805304 # chromatin # # # 8805304 V(D)J recombination does not involve homologous recombination, but mHR54 =RAD54L could mediate a substrate preparation step that V(D)J and meiotic recombination have in common, such as changing the chromatin structure of the loci that will be rearranged.
RAD54L2
(details)
# 29123 RAD54-like 2 (S. cerevisiae) 23132 Q9Y4B4 ARIP4_HUMAN Helicase_C PF00271 774-854, Pfam-B_2830 PB002830 105-259, SNF2_N PF00176 274-625 Rad54l2 1933196 Q99NG0 ARIP4_MOUSE # # Chromatin remodelling # 19692572 # chromatin # # # 19692572 ARIP4 =RAD54L2 contains SNF2 domain that functions as a motor protein in chromatin remodeling complexes.
RAG1
(details)
# 9831 recombination activating gene 1 5896 P15918 RAG1_HUMAN Pfam-B_793 PB000793 1-89, RAG1 PF12940 513-953, zf-C3HC4 PF00097 293-331, zf-RAG1 PF10426 354-383 Rag1 97848 P15919 RAG1_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write Histone ubiquitination 21256161 # histone, DNA H3.3K, DNA motif H3.3Kub # 21256161 It has been suggested that RAG1 targets H3.3, the H3 variant known to be associated with recombining loci, and thus most likely to be encountered by RAG1 during V(D)J recombination. This reaction is absolutely dependent on an intact RAG1 RING domain, and requires regions of the far N-terminus of RAG1 where the H3.3 binding sight is likely to reside and regions within the H3 amino-terminal tail. Several H3.3 lysines are subject to ubiquitylation.
RAG2
(details)
# 9832 recombination activating gene 2 5897 P55895 RAG2_HUMAN RAG2 PF03089 51-389, RAG2_PHD PF13341 414-491 Rag2 97849 P21784 RAG2_MOUSE # # Histone modification read # 21423274 # histone H3K4me3 # # 21423274 Recombination-activating protein, RAG2, binds to H3K4me3 at transcribed genes while RAG1 recognizes the recombination signal sequence.
RAI1
(details)
New 9834 retinoic acid induced 1 10743 Q7Z5J4 RAI1_HUMAN Pfam-B_11259 PB011259 438-596, Pfam-B_27361 PB027361 388-436, Pfam-B_6090 PB006090 1665-1710, zf-HC5HC2H PF13771 1825-1903 Rai1 103291 Q61818 RAI1_MOUSE # # Chromatin remodelling # 22498752 # chromatin # # # # RAI1 regulates transcription through chromatin remodeling, according to UniProt.
RARA
(details)
# 9864 retinoic acid receptor, alpha 5914 P10276 RARA_HUMAN Hormone_recep PF00104 207-409, zf-C4 PF00105 86-155 Rara 97856 P11416 RARA_MOUSE NR Nuclear hormone receptors Histone modification write cofactor, TF, TF Histone methylation, TF activator, TF repressor 19377461 # histone H3K4 H3K4me, H3K4me2 # 19377461 MLL5 is biochemically identified in a GlcNAcylation-dependent multi-subunit complex associating with nuclear retinoic acid receptor RARalpha (also known as RARA), serving as a mono- and di-methyl transferase to H3K4.
RB1
(details)
# 9884 retinoblastoma 1 5925 P06400 RB_HUMAN DUF3452 PF11934 105-229, RB_A PF01858 373-573, RB_B PF01857 645-766, Rb_C PF08934 768-927 Rb1 97874 P13405 RB_MOUSE ENDOLIG Endogenous ligands Chromatin remodelling, Histone modification write #, Histone ubiquitination 19149898 CREST-BRG1, L3MBTL1 histone # # # 19149898 Hypophosphorylated pRb can repress gene transcription at least partly by remodelling chromatin structure through its interactions with proteins such as HDAC1, BRM and BRG1.
RBBP4
(details)
# 9887 retinoblastoma binding protein 4 5928 Q09028 RBBP4_HUMAN CAF1C_H4-bd PF12265 18-89, WD40 PF00400 167-206 218-256 263-302 307-346 364-403 Rbbp4 1194912 Q60972 RBBP4_MOUSE WDR WD repeat domain containing Histone chaperone # 8858152 NuRF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, NuRD, mSin3A, core HDAC, mSin3A-like complex, PRC2, CAF-1 histone H4 # # 8858152 RbAp46 and RbAp48 (pRB-associated proteins p46 and p48, also known as RBBP7 and RBBP4, respectively) are highly homologous histone chaperones that play key roles in establishing and maintaining chromatin structure. Human p48 =RBBP4 can bind to histone H4 in the absence of CAF-1 p150 and p60. p48, also a known subunit of a histone deacetylase, copurifies with a chromatin assembly complex (CAC), which contains the three subunits of CAF-1 (p150, p60, p48) and H3 and H4, and promotes DNA replication-dependent chromatin assembly.
RBBP5
(details)
# 9888 retinoblastoma binding protein 5 5929 Q15291 RBBP5_HUMAN Pfam-B_3428 PB003428 121-325, WD40 PF00400 23-52 58-94 Rbbp5 1918367 Q8BX09 RBBP5_MOUSE WDR WD repeat domain containing Histone modification write cofactor Histone methylation 19556245 COMPASS, Menin-associated_HMT, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7, COMPASS-like MLL3,4 histone H3K4 H3K4me1, H3K4me2, H3K4me3 # 19556245 A five-component 200-kDa MLL1 core complex containing human MLL1, WDR5, RbBP5, Ash2L, and DPY-30.
RBBP7
(details)
# 9890 retinoblastoma binding protein 7 5931 Q16576 RBBP7_HUMAN CAF1C_H4-bd PF12265 17-88, WD40 PF00400 166-205 217-255 262-301 306-345 363-402 Rbbp7 1194910 Q60973 RBBP7_MOUSE WDR WD repeat domain containing Histone chaperone # 18571423 NuRF, NuRD, mSin3A, core HDAC, mSin3A-like complex, PRC2 histone H4 # # 18571423 RbAp46 and RbAp48 (pRB-associated proteins p46 and p48, also known as RBBP7 and RBBP4, respectively) are highly homologous histone chaperones that play key roles in establishing and maintaining chromatin structure. When a histone H3/H4 dimer (or tetramer) binds to RbAp46 or RbAp48, helix 1 of histone H4 unfolds to interact with the histone chaperone.
RBX1
(details)
# 9928 ring-box 1, E3 ubiquitin protein ligase 9978 P62877 RBX1_HUMAN zf-rbx1 PF12678 21-98 Rbx1 1891829 P62878 RBX1_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write cofactor Histone ubiquitination 18593899 # histone H3, H4 H3ub, H4ub # 18593899 Histones H3 and H4 are targets of the CUL4-DDB-RBX1 E3 ligase ( 34). It has been proposed that both DDB1-CUL4DDB2 and Ring2 ligases are recruited to UV-induced lesions to modify histones.
RCC1
(details)
New 1913 regulator of chromosome condensation 1 1104 P18754 RCC1_HUMAN RCC1 PF00415 34-82 85-134 137-187 190-255 258-309 312-360 363-414 Rcc1 1913989 Q8VE37 RCC1_MOUSE # # Chromatin remodelling # 11375490 # histone H2A, H2B # # # Binds to histones H2A and H2B.
RCOR1
(details)
# 17441 REST corepressor 1 23186 Q9UKL0 RCOR1_HUMAN ELM2 PF01448 102-157, Myb_DNA-binding PF00249 381-425 Rcor1 106340 Q8CFE3 RCOR1_MOUSE # # Histone modification erase cofactor, Histone modification erase cofactor Histone acetylation, Histone methylation 10449787 BHC, SCL, LSD-CoREST histone # # # 10449787 CoREST=RCOR1 may function as a repressor by recruiting, either directly or indirectly, histone deacetylase activity.
RCOR3
(details)
New 25594 REST corepressor 3 55758 Q9P2K3 RCOR3_HUMAN ELM2 PF01448 1-54, Myb_DNA-binding PF00249 288-332 Rcor3 2441920 Q6PGA0 RCOR3_MOUSE # # Histone modification erase cofactor Histone acetylation 23752268 LSD-CoREST histone # # # 23752268 Part of the HDAC interactome.
REST
(details)
# 9966 RE1-silencing transcription factor 5978 Q13127 REST_HUMAN Pfam-B_2325 PB002325 821-909, Pfam-B_9727 PB009727 1001-1095, zf-C2H2_4 PF13894 216-238, zf-H2C2_2 PF13465 290-315 318-343 346-372 Rest 104897 Q8VIG1 REST_MOUSE # # Histone modification erase cofactor, TF, TF Histone acetylation, TF activator, TF repressor 12399542 # DNA DNA motif # # 12399542 REST/NRSF can mediate repression, in part, through the association of its NH2-terminal repression domain with the mSin3/histone deacethylase 1,2 (HDAC1,2) complex.
RING1
(details)
# 10018 ring finger protein 1 6015 Q06587 RING1_HUMAN Pfam-B_11743 PB011743 292-404, Pfam-B_13488 PB013488 241-291, Pfam-B_23468 PB023468 191-239, zf-C3HC4 PF00097 48-87 Ring1 1101770 O35730 RING1_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write, Polycomb group (PcG) protein Histone ubiquitination, # 15386022 PRC1, BCOR, RING2-L3MBTL2, RING2-FBRS histone H2AK119 H2AK119ub # 15386022 The complex hPRC1L (human Polycomb repressive complex 1-like) is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2. hPRC1L monoubiquitinates nucleosomal histone H2A at lysine 119.
RLIM
(details)
New 13429 ring finger protein, LIM domain interacting 51132 Q9NVW2 RNF12_HUMAN zf-RING_2 PF13639 568-611 Rlim 1342291 Q9WTV7 RNF12_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification erase cofactor Histone acetylation 10431247 # histone # # # # Recruits the Sin3A/histone deacetylase corepressor complex.
RMI1
(details)
# 25764 RecQ mediated genome instability 1 80010 Q9H9A7 RMI1_HUMAN DUF1767 PF08585 12-104, Pfam-B_227 PB000227 590-623 Rmi1 1921636 Q9D4G9 RMI1_MOUSE # # DNA modification # 16537486 # DNA # # # 16537486 #
RNF168
(details)
# 26661 ring finger protein 168, E3 ubiquitin protein ligase 165918 Q8IYW5 RN168_HUMAN Pfam-B_30754 PB030754 528-566, zf-C3HC4_2 PF13923 16-54 Rnf168 1917488 Q80XJ2 RN168_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write Histone ubiquitination 22980979 # histone H2AK13, H2AK15, H2AXK13, H2AXK15 H2AK13ub, H2AK15ub, H2AXK13ub, H2AXK15ub # 22980979 RNF8 and RNF168 targets histone H2A and H2AX. RNF8 is the first ligase recruited to the damage site, and RNF168 follows RNF8-dependent ubiquitination. This suggests that RNF8 initiates H2A/H2AX ubiquitination with K63-linked ubiquitin chains and RNF168 extends them. RNF8 is inactive toward nucleosomal H2A, whereas RNF168 catalyzes the monoubiquitination of the histones specifically on K13-15.
RNF2
(details)
# 10061 ring finger protein 2 6045 Q99496 RING2_HUMAN zf-C3HC4 PF00097 51-90 Rnf2 1101759 Q9CQJ4 RING2_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write Histone ubiquitination 16943429 PRC1, BCOR, RING2-L3MBTL2, RING2-FBRS, CHD8, MLL2/3, MLL4/WBP7 histone H2AK119 H2AK119ub # 16943429 RNF2 is the only BCOR complex PcG protein with a known enzymatic activity: an E3 ligase for the histone protein H2A (12, 78). Ub-H2A is thought to be involved in maintaining a repressed chromatin state.
RNF20
(details)
# 10062 ring finger protein 20, E3 ubiquitin protein ligase 56254 Q5VTR2 BRE1A_HUMAN Pfam-B_13436 PB013436 97-179, Pfam-B_14933 PB014933 35-95, Pfam-B_6844 PB006844 735-892, zf-C3HC4 PF00097 922-960 Rnf20 1925927 Q5DTM8 BRE1A_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write Histone ubiquitination 16307923 # histone H2BK120 H2BK120ub1 # 16307923 Two copies each of the E3 ligases RNF20 and RNF40 are present in the same complex catalyzing histone H2B-K120 monoubiquitination. The complex that catalyzes histone H2A-K119 monoubiquitination also contains two E3 ligases, Ring1 and Ring2.
RNF40
(details)
# 16867 ring finger protein 40, E3 ubiquitin protein ligase 9810 O75150 BRE1B_HUMAN Pfam-B_21314 PB021314 191-299, Pfam-B_9159 PB009159 1-189, zf-C3HC4 PF00097 948-986 Rnf40 2142048 Q3U319 BRE1B_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write cofactor Histone ubiquitination 16307923 # histone H2BK121 H2BK120ub2 # 16307923 Two copies each of the E3 ligases RNF20 and RNF40 are present in the same complex catalyzing histone H2B-K120 monoubiquitination. The complex that catalyzes histone H2A-K119 monoubiquitination also contains two E3 ligases, Ring1 and Ring2.
RNF8
(details)
# 10071 ring finger protein 8, E3 ubiquitin protein ligase 9025 O76064 RNF8_HUMAN FHA PF00498 38-109, zf-RING_2 PF13639 401-441 Rnf8 1929069 Q8VC56 RNF8_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write Histone ubiquitination 22980979 # histone H2AK63, H2AXK63, H2AK48, H2AXK48 H2AK63ub, H2AXK63ub, H2AK48ub, H2AXK48ub # 22980979 Ubiquitin-dependent signaling during the DNA damage response (DDR) to double-strand breaks (DSBs) is initiated by two E3 ligases, RNF8 and RNF168, targeting histone H2A and H2AX. RNF8 is the first ligase recruited to the damage site, and RNF168 follows RNF8-dependent ubiquitination. This suggests that RNF8 initiates H2A/H2AX ubiquitination with K63-linked ubiquitin chains and RNF168 extends them.
RPS6KA3
(details)
# 10432 ribosomal protein S6 kinase, 90kDa, polypeptide 3 6197 P51812 KS6A3_HUMAN Pkinase PF00069 68-327 422-679, Pkinase_C PF00433 349-389 Rps6ka3 104557 P18654 KS6A3_MOUSE # # Histone modification write cofactor Histone phosphorylation 10436156 # histone H3S10 H3S10ph # 10436156 Is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes.
RPS6KA4
(details)
# 10433 ribosomal protein S6 kinase, 90kDa, polypeptide 4 8986 O75676 KS6A4_HUMAN Pkinase PF00069 33-301 413-674, Pkinase_C PF00433 321-365 Rps6ka4 1930076 Q9Z2B9 KS6A4_MOUSE # # Histone modification write Histone phosphorylation 12773393 # histone H3S10, H3S28 H3S10ph, H3S28ph # 12773393 The MSKs, particularly MSK2=RPS6KA4, but not RSK2, are the major histone H3 and HMG-14 kinases.
RPS6KA5
(details)
# 10434 ribosomal protein S6 kinase, 90kDa, polypeptide 5 9252 O75582 KS6A5_HUMAN Pkinase PF00069 49-318 427-687, Pkinase_C PF00433 338-381 Rps6ka5 1920336 Q8C050 KS6A5_MOUSE # # Histone modification write Histone phosphorylation 12773393 # histone H2AS1, H3S10, H3S28 H2AS1ph, H3S10ph, H3S28ph # 12773393 The MSKs=(RPS6KA4, RPS6KA5), particularly MSK2, but not RSK2, are the major histone H3 and HMG-14 kinases.
RRP8
(details)
New 29030 ribosomal RNA processing 8, methyltransferase, homolog (yeast) 23378 O43159 RRP8_HUMAN Methyltransf_8 PF05148 237-456 Rrp8 1914251 Q9DB85 RRP8_MOUSE # # Histone modification cofactor # 18485871 eNoSc histone H3ac H3K9me2 # # A component of the eNoSC complex, that mediates silencing of rDNA by recruiting histone-modifying enzymes, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus.
RSF1
(details)
# 18118 remodeling and spacing factor 1 51773 Q96T23 RSF1_HUMAN PHD PF00628 893-941, WHIM1 PF15612 98-148, WHIM2 PF15613 150-182, WHIM3 PF15614 188-409 Rsf1 2682305 # # PHF Zinc fingers, PHD-type Histone modification read # 12972596 RSF histone # # # 12972596 Recombinant RSF complex coimmunoprecipitates with core histones, and Rsf-1 alone also interacts with core histones.
RUVBL1
(details)
# 10474 RuvB-like AAA ATPase 1 8607 Q9Y265 RUVB1_HUMAN TIP49 PF06068 14-416 Ruvbl1 1928760 P60122 RUVB1_MOUSE INO80, AATP INO80 complex subunits, ATPases / AAA-type Chromatin remodelling, Histone modification write #, Histone phosphorylation 14695187 Ino80, SWR, NuA4, NuA4-related complex, CHD8, MLL2/3, MLL4/WBP7, SRCAP chromatin # # # 14695187 The ability of TIP49=RUVBL1 to inhibit ITF-2 gene expression has been linked to decreased acetylation of histones in the vicinity of the TCF-binding sites in the ITF-2 promoter region. It has been suggested that TIP49 is an important cofactor in beta-catenin/TCF gene regulation in normal and neoplastic cells, likely functioning in chromatin remodeling.
RUVBL2
(details)
# 10475 RuvB-like AAA ATPase 2 10856 Q9Y230 RUVB2_HUMAN TIP49 PF06068 21-412 Ruvbl2 1342299 Q9WTM5 RUVB2_MOUSE INO80, AATP INO80 complex subunits, ATPases / AAA-type Chromatin remodelling cofactor # 18026119 Ino80, SWR, NuA4, NuA4-related complex, CHD8, MLL2/3, MLL4/WBP7, SRCAP chromatin # # # 18026119 The seven human INO80 complex components include TIP49A and TIP49B (previously identified as ‘RuvB-like’ proteins, and labeled RUVBL1 and RUVBL2).
RYBP
(details)
# 10480 RING1 and YY1 binding protein 23429 Q8N488 RYBP_HUMAN Pfam-B_18067 PB018067 49-226, zf-RanBP PF00641 22-48 Rybp 1929059 Q8CCI5 RYBP_MOUSE # # Polycomb group (PcG) protein # 19098711 BCOR, RING2-L3MBTL2, RING2-FBRS # # # # 19098711 RYBP (RING1- and YY1-binding protein), a member of the polycomb group (PcG), interacts with MDM2 and decreases MDM2-mediated p53 ubiquitination, leading to stabilization of p53 and an increase in p53 activity.
SAFB
(details)
New 10520 scaffold attachment factor B 6294 Q15424 SAFB1_HUMAN Pfam-B_12198 PB012198 66-89, RRM_6 PF14259 409-478, SAP PF02037 31-65 Safb 2146974 D3YXK2 SAFB1_MOUSE RBM RNA binding motif (RRM) containing Chromatin remodelling # 24055346 # chromatin # # # # The chromatine scaffold protein, a component of the DNA damage response cooperating with histone acetylation to allow for efficient γH2AX spreading.
SAP130
(details)
# 29813 Sin3A-associated protein, 130kDa 79595 Q9H0E3 SP130_HUMAN Pfam-B_10398 PB010398 431-719, Pfam-B_13351 PB013351 101-249, Pfam-B_17122 PB017122 781-837, Pfam-B_18714 PB018714 721-779, Pfam-B_237 PB000237 949-984 Sap130 1919782 Q8BIH0 SP130_MOUSE # # Histone modification erase cofactor Histone acetylation 12724404 # histone # # # 12724404 SAP130 has a repression domain at its C terminus that interacts with the mSin3A-HDAC complex and an N-terminal domain that probably mediates an interaction with a transcriptional activator.
SAP18
(details)
# 10530 Sin3A-associated protein, 18kDa 10284 O00422 SAP18_HUMAN SAP18 PF06487 16-137 Sap18 1277978 O55128 SAP18_MOUSE # # Histone modification erase cofactor Histone acetylation 9150135 mSin3A histone # # # 9150135 SAP18 Interacts with mSin3 and enhances the ability of mSin3-mediated repression of transcription.
SAP25
(details)
# 41908 Sin3A-associated protein, 25kDa 100316904 Q8TEE9 SAP25_HUMAN SAP25 PF15476 1-199 Sap25 3802945 Q1EHW4 SAP25_MOUSE # # Histone modification erase cofactor Histone acetylation 16449650 # histone # # # 16449650 SAP25 binds to the PAH1 domain of mSin3A, associates with the mSin3A-HDAC complex in vivo, and represses transcription when tethered to DNA. SAP25 is required for mSin3A-mediated, but not N-CoR-mediated, repression.
SAP30
(details)
# 10532 Sin3A-associated protein, 30kDa 8819 O75446 SAP30_HUMAN SAP30_Sin3_bdg PF13867 153-205, zf-SAP30 PF13866 56-134 Sap30 1929129 O88574 SAP30_MOUSE # # Histone modification erase cofactor Histone acetylation 9651585 mSin3A, mSin3A-like complex histone # # # 9651585 The human SAP30 complex is active in deacetylating core histone octamers.
SAP30L
(details)
# 25663 SAP30-like 79685 Q9HAJ7 SP30L_HUMAN SAP30_Sin3_bdg PF13867 114-166, zf-SAP30 PF13866 18-95 Sap30l 1354709 Q5SQF8 SP30L_MOUSE # # Histone modification erase cofactor Histone acetylation 16820529 # histone # # # 16820529 SAP30L induces transcriptional repression, possibly via recruitment of Sin3A and histone deacetylases. A functional nucleolar localization signal in SAP30L means that SAP30L and SAP30 are able to target Sin3A to the nucleolus.
SATB1
(details)
New 10541 SATB homeobox 1 6304 Q01826 SATB1_HUMAN CUT PF02376 362-448 485-571, Homeobox PF00046 645-702, Pfam-B_9146 PB009146 141-299 Satb1 105084 Q60611 SATB1_MOUSE CUT Homeoboxes / CUT class Chromatin remodelling cofactor # 15713622, 24055346, 12374985, 12374985, 24055346 # chromatin # # # # Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Forms chromatin loops. SATB1 also targets ACF1 and ISWI, subunits of CHRAC and ACF nucleosome mobilizing complexes. SAFB1 is a component of the DNA damage response and shows that SAFB1 cooperates with histone acetylation to allow for efficient γH2AX spreading.
SATB2
(details)
New 21637 SATB homeobox 2 23314 Q9UPW6 SATB2_HUMAN CUT PF02376 352-437 474-560, Homeobox PF00046 615-672, Pfam-B_8103 PB008103 1-268 Satb2 2679336 Q8VI24 SATB2_MOUSE CUT Homeoboxes / CUT class Chromatin remodelling cofactor # 18255031 # chromatin # # # # Cromatin remodelling in mouse. UniProt: Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers.
SCMH1
(details)
# 19003 sex comb on midleg homolog 1 (Drosophila) 22955 Q96GD3 SCMH1_HUMAN DUF3588 PF12140 355-469, MBT PF02820 62-134 171-239, SAM_1 PF00536 591-656 Scmh1 1352762 Q8K214 SCMH1_MOUSE SAMD Sterile alpha motif (SAM) domain containing Polycomb group (PcG) protein # 23356856 PRC1 # # # # 23356856 SCMH1 is part of a polycomb group complex 1 (PcG1) involved in transcriptional silencing and proteosomal degradation for the Geminin protein, important for regulation of replication and maintenance of undifferentiated states.
SCML2
(details)
# 10581 sex comb on midleg-like 2 (Drosophila) 10389 Q9UQR0 SCML2_HUMAN DUF3588 PF12140 353-468, MBT PF02820 67-139 176-244, SAM_1 PF00536 629-695 # # # # SAMD Sterile alpha motif (SAM) domain containing Polycomb group (PcG) protein # 24727478 PRC1 # # # # 24727478 Scml2 is a member of the Polycomb group of proteins involved in epigenetic gene silencing. Human Scml2 is a part of a multisubunit protein complex, PRC1 (Polycomb repressive complex 1), which is responsible for maintenance of gene repression, prevention of chromatin remodeling, preservation of the "stemness" of the cell, and cell differentiation.
SCML4
(details)
# 21397 sex comb on midleg-like 4 (Drosophila) 256380 Q8N228 SCML4_HUMAN DUF3588 PF12140 92-208, SAM_1 PF00536 344-410 Scml4 2446140 Q80VG1 SCML4_MOUSE SAMD Sterile alpha motif (SAM) domain containing Polycomb group (PcG) protein # # # # # # # # Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. (Annotated by similarity.)
SENP1
(details)
# 17927 SUMO1/sentrin specific peptidase 1 29843 Q9P0U3 SENP1_HUMAN Peptidase_C48 PF02902 464-642, Pfam-B_2161 PB002161 1-189, Pfam-B_34931 PB034931 191-249 Senp1 2445054 P59110 SENP1_MOUSE # # Histone modification erase cofactor Histone sumoylation 15199155 # histone H4 # # 15199155 SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1.
SENP3
(details)
# 17862 SUMO1/sentrin/SMT3 specific peptidase 3 26168 Q9H4L4 SENP3_HUMAN Peptidase_C48 PF02902 400-572, Pfam-B_2161 PB002161 1-349 Senp3 2158736 Q9EP97 SENP3_MOUSE # # Histone modification erase, Histone modification write cofactor Histone sumoylation, Histone acetylation # CHD8, MLL2/3, MLL4/WBP7 histone H3 H3ac # 18850004 Facultative member of the MLL1/MLL complex (UniProt).
SET
(details)
New 10760 SET nuclear proto-oncogene 6418 Q01105 SET_HUMAN NAP PF00956 42-237 Set 1860267 Q9EQU5 SET_MOUSE # # Histone modification # 17320507 # histone # # # # Classified as histone-modifying enzymes in paper.
SETD1A
(details)
# 29010 SET domain containing 1A 9739 O15047 SET1A_HUMAN N-SET PF11764 1418-1558, Pfam-B_24657 PB024657 752-1010, Pfam-B_24930 PB024930 331-410, Pfam-B_41492 PB041492 622-680, RRM_1 PF00076 99-166, SET PF00856 1579-1685 Setd1a 2446244 # # KMT, RBM Chromatin-modifying enzymes / K-methyltransferases, RNA binding motif (RRM) containing Histone modification write Histone methylation 17355966 COMPASS histone H3K4 H3K4me # 17355966 The CFP1 complex contains human homologues of the COMPASS complex, including Set1A=SETD1A, Wdr5, Ash2, Rbbp5, and Wdr82 (previously denoted hSwd2). The human Set1A-CFP1 complex exhibits histone H3-Lys4 methyltransferase activity in vitro.
SETD1B
(details)
# 29187 SET domain containing 1B 23067 Q9UPS6 SET1B_HUMAN N-SET PF11764 1629-1774, Pfam-B_1367 PB001367 1017-1148, Pfam-B_14013 PB014013 887-1015, RRM_1 PF00076 108-175, SET PF00856 1795-1901 Setd1b 2652820 Q8CFT2 SET1B_MOUSE KMT, RBM Chromatin-modifying enzymes / K-methyltransferases, RNA binding motif (RRM) containing Histone modification write Histone methylation 17355966 COMPASS histone H3K4 H3K4me # 17355966 The extensive homology between Set1A and Set1B=SETD1B, particularly throughout the SET domain, suggests that Set1B functions as a histone methyltransferase.
SETD2
(details)
# 18420 SET domain containing 2 29072 Q9BYW2 SETD2_HUMAN Pfam-B_18604 PB018604 305-521, Pfam-B_22486 PB022486 541-599, Pfam-B_2796 PB002796 2146-2339, Pfam-B_3607 PB003607 1826-2144, Pfam-B_67824 PB067824 31-77, SET PF00856 1561-1667, SRI PF08236 2465-2559, WW PF00397 2391-2420 Setd2 1918177 E9Q5F9 SETD2_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation 16118227 # histone H3K36me2 H3K36me3 # 16118227 HYPB HMTase=SETD2 may coordinate histone methylation and transcriptional regulation in mammals.
SETD3
(details)
# 20493 SET domain containing 3 84193 Q86TU7 SETD3_HUMAN Rubis-subs-bind PF09273 343-475, SET PF00856 105-314 Setd3 1289184 Q91WC0 SETD3_MOUSE # # Histone modification write Histone methylation # # histone H3K36 H3K36me # # Histone methyltransferase that methylates 'Lys-36' of histone H3 (H3K36me). H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation. (Annotated by similarity.)
SETD5
(details)
# 25566 SET domain containing 5 55209 Q9C0A6 SETD5_HUMAN Pfam-B_7713 PB007713 700-789, SET PF00856 285-390 Setd5 1920145 Q5XJV7 SETD5_MOUSE # # Histone modification write Histone methylation 24680889 # histone # # # 24680889 Encoding methyltransferases regulating histone modification.
SETD6
(details)
# 26116 SET domain containing 6 79918 Q8TBK2 SETD6_HUMAN Pfam-B_25912 PB025912 1-69, Rubis-subs-bind PF09273 329-465, SET PF00856 74-286 Setd6 1913333 Q9CWY3 SETD6_MOUSE # # Chromatin remodelling, Histone modification write #, Histone methylation 21131967 # histone # # # 21131967 SETD6 monomethylation of nuclear RelA at K310 attenuates NF-κB signaling by docking GLP (via its ankyrin repeats) at target genes to generate a silent chromatin state, effectively rendering chromatin-bound RelA inert. As deregulation of NF-κB is linked to pathologic inflammatory processes and cancer8 and SETD6 inhibits NF-κB signaling in diverse cell types, including primary human cells, SETD6 may provide a new link by which protein lysine methylation and chromatin regulation influence tumor suppression and anti-inflammatory respons.
SETD7
(details)
# 30412 SET domain containing (lysine methyltransferase) 7 80854 Q8WTS6 SETD7_HUMAN MORN PF02493 13-35 36-58 60-81 106-128, SET PF00856 227-336 Setd7 1920501 Q8VHL1 SETD7_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation 11779497 # histone H3K4 H3K4me1 # 11779497 SET7 methylates H3-K4 in vitro and in vivo. In addition, methylation of H3-K4 and H3-K9 inhibit each other. Furthermore, H3-K4 and H3-K9 methylation by SET7 and SUV39H1, respectively, have differential effects on subsequent histone acetylation by p300. May explain differential effects of H3-K4 and H3-K9 methylation on transcription.
SETD8
(details)
# 29489 SET domain containing (lysine methyltransferase) 8 387893 Q9NQR1 SETD8_HUMAN SET PF00856 268-378 Setd8 1915206 Q2YDW7 SETD8_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation 12086618 # histone H4K20 H4K20me1 # 12086618 The encoding gene PR/SET07 =SETD8 of a human histone H4 lysine 20 methyltransferase.
SETDB1
(details)
# 10761 SET domain, bifurcated 1 9869 Q15047 SETB1_HUMAN MBD PF01429 594-668, Pfam-B_23747 PB023747 365-520, Pfam-B_27578 PB027578 341-364, Pre-SET PF05033 681-795, SET PF00856 814-1266 Setdb1 1934229 O88974 SETB1_MOUSE KMT, TDRD Chromatin-modifying enzymes / K-methyltransferases, Tudor domain containing Histone modification write Histone methylation 11959841 # histone H3K9 H3K9me3 # 11959841 In vitro methylation of the N-terminal tail of histone H3 by SETDB1 is sufficient to enhance the binding of HP1 proteins, which requires both an intact chromodomain and chromoshadow domain.
SETDB2
(details)
# 20263 SET domain, bifurcated 2 83852 Q96T68 SETB2_HUMAN MBD PF01429 160-232, Pre-SET PF05033 245-359, SET PF00856 378-694 Setdb2 2685139 Q8C267 SETB2_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation 20404330 # histone H3K9 H3K9me3 # 20404330 A member of the histone H3K9 methyltransferase family named CLLD8 (or SETDB2 or KMT1F).
SETMAR
(details)
# 10762 SET domain and mariner transposase fusion gene 6419 Q53H47 SETMR_HUMAN HTH_Tnp_Tc3_2 PF01498 401-466, Pre-SET PF05033 16-118, SET PF00856 137-250, Transposase_1 PF01359 488-568 Setmar 1921979 Q80UJ9 SETMR_MOUSE # # Histone modification write Histone methylation 16332963 # histone H3K4, H3K36 H3K4me, H3K36me # 16332963 Metnase =SETMAR that has a SET domain and a transposase/nuclease domain. Metnase methylates histone H3 lysines 4 and 36, which are associated with open chromatin. Metnase increases resistance to ionizing radiation and increases nonhomologous end-joining repair of DNA doublestrand breaks.
SF3B1
(details)
# 10768 splicing factor 3b, subunit 1, 155kDa 23451 O75533 SF3B1_HUMAN Pfam-B_1720 PB001720 1099-1147, SF3b1 PF08920 282-457 Sf3b1 1932339 Q99NB9 SF3B1_MOUSE # # RNA modification # 23568491 B-WICH RNA # # # 23568491 Although the causative link between SF3B1 mutation and CLL pathogenesis remains unclear, several lines of evidence suggest SF3B1 mutation might be linked to genomic stability and epigenetic modification.
SF3B3
(details)
# 10770 splicing factor 3b, subunit 3, 130kDa 23450 Q15393 SF3B3_HUMAN CPSF_A PF03178 863-1184, MMS1_N PF10433 76-597 Sf3b3 1289341 Q921M3 SF3B3_MOUSE # # RNA modification # 17643112 # RNA # # # 17643112 #
SFMBT1
(details)
# 20255 Scm-like with four mbt domains 1 51460 Q9UHJ3 SMBT1_HUMAN DUF3588 PF12140 501-620, MBT PF02820 54-128 167-240 279-356 388-461, Pfam-B_19576 PB019576 672-751, SAM_1 PF00536 794-857 Sfmbt1 1859609 Q9JMD1 SMBT1_MOUSE # # Polycomb group (PcG) protein # 21423274 SCL histone H4K20 # # 21423274 Table 1 in the reference.
SFMBT2
(details)
# 20256 Scm-like with four mbt domains 2 57713 Q5VUG0 SMBT2_HUMAN DUF3588 PF12140 527-646, MBT PF02820 78-152 191-263 304-380 412-485, SAM_1 PF00536 822-885 Sfmbt2 2447794 Q5DTW2 SMBT2_MOUSE SAMD Sterile alpha motif (SAM) domain containing Histone modification read, Polycomb group (PcG) protein, TF #, #, TF repressor 23385818 # histone, DNA H3K9me2, H3K9me3, H3K27me3, H4K20me2, H4K20me3 H3, H4 # 23385818 SFMBT2 binds preferentially to methylated histone H3 and H4 that are associated with transcriptional repression. Occupancy of SFMBT2 coincide with enrichment of diand tri-methylated H3K9 and H4K20 as well as tri-methylated H3K27 at the HOXB13 gene promoter.
SFPQ
(details)
# 10774 splicing factor proline/glutamine-rich 6421 P23246 SFPQ_HUMAN NOPS PF08075 444-495, RRM_1 PF00076 299-363 373-440 Sfpq 1918764 Q8VIJ6 SFPQ_MOUSE RBM RNA binding motif (RRM) containing Chromatin remodelling cofactor, RNA modification, TF #, #, TF repressor 22783022, 10858305, 8449401 # DNA, RNA # # # 22783022, 10858305, 8449401 Four components of the Sin3a transcriptional repressor complex: SAP130, SUDS3, SFPQ, and TGIF2. Since the RNA splicing factors do not have an endogenous DNA relaxation activity, topoisomerase I (Chromatin remodeller) gets stimulated by the interaction with the PSF= SFPQ/p54nrb heterodimer. PSF=SFPQ is an essential pre-mRNA splicing factor required early in spliceosome formation.
SHPRH
(details)
# 19336 SNF2 histone linker PHD RING helicase, E3 ubiquitin protein ligase 257218 Q149N8 SHPRH_HUMAN Helicase_C PF00271 1545-1622, Linker_histone PF00538 438-512, Pfam-B_11163 PB011163 1-248, SNF2_N PF00176 307-987, zf-C3HC4_2 PF13923 1432-1478 Shprh 1917581 Q7TPQ3 SHPRH_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification write cofactor Histone ubiquitination 17130289 # histone # # # 17130289 SHPRH associates with PCNA, RAD18, and the ubiquitin-conjugating enzyme UBC13 (E2) and promotes methyl methanesulfonate (MMS)-induced PCNA polyubiquitination.
SIN3A
(details)
# 19353 SIN3 transcription regulator family member A 25942 Q96ST3 SIN3A_HUMAN PAH PF02671 141-187 322-381 477-523, Pfam-B_10250 PB010250 1-99, Pfam-B_10714 PB010714 1098-1128, Pfam-B_8471 PB008471 1055-1090, Sin3_corepress PF08295 550-650 Sin3a 107157 Q60520 SIN3A_MOUSE # # Histone modification erase cofactor, TF, TF Histone acetylation, TF activator, TF repressor 12670868 SWI/SNF_Brg1(I), SWI/SNF_Brm, mSin3A, mSin3A-like complex histone, DNA DNA motif # # 12670868 Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1.
SIN3B
(details)
# 19354 SIN3 transcription regulator family member B 23309 O75182 SIN3B_HUMAN PAH PF02671 59-105 180-236 321-367, Sin3_corepress PF08295 393-448 450-525 Sin3b 107158 Q62141 SIN3B_MOUSE # # Histone modification erase cofactor, TF Histone acetylation, TF repressor 12670868 mSin3A histone, DNA DNA motif # # 12670868 Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1.
SIRT1
(details)
# 14929 sirtuin 1 23411 Q96EB6 SIR1_HUMAN Pfam-B_28511 PB028511 1-109, Pfam-B_5913 PB005913 111-189, Pfam-B_8042 PB008042 611-745, SIR2 PF02146 261-447 Sirt1 2135607 Q923E4 SIR1_MOUSE # # Histone modification erase, Histone modification write cofactor Histone acetylation, Histone methylation 15469825 eNoSc histone H1K26ac, H3K9ac, H4K16ac H1K26, H3K9, H4K16 # 15469825 SirT1 deacetylates histone polypeptides with a preference for histone H4 lysine 16 (H4-K16Ac) and H3 lysine 9 (H3-K9Ac) in vitro.
SIRT2
(details)
# 10886 sirtuin 2 22933 Q8IXJ6 SIR2_HUMAN SIR2 PF02146 84-268 Sirt2 1927664 Q8VDQ8 SIR2_MOUSE # # Histone modification erase, Histone modification write cofactor Histone acetylation, Histone methylation 11427894 # histone H3K18ac, H3K56ac, H4K16ac, H4K20me1 H3K18, H3K56, H4K16, H4K20me2, H4K20me3 # 11427894 Sir2 =SIRT2 is an NAD-dependent histone deacetylase that mediates transcriptional silencing at mating-type loci, telomeres and ribosomal gene clusters.
SIRT6
(details)
# 14934 sirtuin 6 51548 Q8N6T7 SIR6_HUMAN SIR2 PF02146 52-89 80-221 Sirt6 1354161 P59941 SIR6_MOUSE # # Histone modification erase Histone acetylation 18337721 # histone H3K9ac, H3K56ac H3K9, H3K56 # 18337721 The human SIRT6 protein is an NAD+-dependent, histone H3 lysine 9 (H3K9) deacetylase that modulates telomeric chromatin. SIRT6 associates specifically with telomeres, and SIRT6 depletion leads to telomere dysfunction with end-to-end chromosomal fusions and premature cellular senescence.
SIRT7
(details)
# 14935 sirtuin 7 51547 Q9NRC8 SIR7_HUMAN SIR2 PF02146 133-275 Sirt7 2385849 Q8BKJ9 SIR7_MOUSE # # Histone modification erase Histone acetylation 22722849 B-WICH histone H3K18ac H3K18 # 22722849 Genome-wide binding studies reveal that SIRT7 binds to promoters of a specific set of gene targets, where it deacetylates H3K18Ac and promotes transcriptional repression.
SKP1
(details)
# 10899 S-phase kinase-associated protein 1 6500 P63208 SKP1_HUMAN Skp1 PF01466 85-162, Skp1_POZ PF03931 2-67 Akp1a 103575 Q9WTX5 SKP1_MOUSE # # Histone modification write cofactor Histone ubiquitination 16943429 BCOR histone # # # 16943429 The proteins in the BCOR complex include the PcG and PcG-associated proteins NSPC1, RING1, RNF2, and RYBP as well as components of an SCF ubiquitin ligase, SKP1, and FBXL10. BCOR recruits a unique combination of enzymatic activities to chromatin targets: a PcG E3 ubiquitin ligase for histone H2A, a demethylase for histone H3 K36, and an SCF E3 ubiquitin ligase.
SMARCA1
(details)
# 11097 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 6594 P28370 SMCA1_HUMAN DBINO PF13892 42-119, HAND PF09110 758-856, Helicase_C PF00271 520-612, SLIDE PF09111 912-1028, SNF2_N PF00176 186-466 Smarca1 1935127 Q6PGB8 SMCA1_MOUSE # # Chromatin remodelling, Histone modification erase #, Histone acetylation 15310751 NuRF, CERF, CERF chromatin # # # 15310751 Mammalian genomes encode two imitation switch family chromatin remodeling proteins, SNF2H and SNF2L =SMARCA1.
SMARCA2
(details)
# 11098 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 6595 P51531 SMCA2_HUMAN BRK PF07533 588-633, Bromodomain PF00439 1411-1493, HSA PF07529 436-508, Helicase_C PF00271 1084-1164, Pfam-B_17897 PB017897 1369-1398, Pfam-B_2366 PB002366 333-414, QLQ PF08880 172-208, SNF2_N PF00176 727-1022, SnAC PF14619 1257-1326 Smarca2 99603 Q6DIC0 SMCA2_MOUSE # # Histone modification read, TF #, TF activator 22464331 BAF, nBAF, npBAF, WINAC, bBAF, SWI/SNF BRM-BRG1 histone, DNA H3, DNA motif # # 22464331 Fig. 5 in the reference.
SMARCA4
(details)
# 11100 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 6597 P51532 SMCA4_HUMAN BRK PF07533 610-655, Bromodomain PF00439 1462-1551, HSA PF07529 460-532, Helicase_C PF00271 1114-1194, QLQ PF08880 170-206, SNF2_N PF00176 757-1052, SnAC PF14619 1321-1389 Smarca4 88192 Q3TKT4 SMCA4_MOUSE # # Histone modification read, TF #, TF activator 17582821 BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1, CREST-BRG1 histone H3, H4 # # 17582821 The BRG1 =SMARCA4 bromodomain exhibits binding, albeit weak, to acetylated peptides that are derived from histones H3 and H4.
SMARCA5
(details)
# 11101 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 8467 O60264 SMCA5_HUMAN DBINO PF13892 58-116, HAND PF09110 743-841, Helicase_C PF00271 517-597, Pfam-B_36230 PB036230 1-39, SLIDE PF09111 897-1013, SNF2_N PF00176 183-463 Smarca5 1935129 Q91ZW3 SMCA5_MOUSE # # Chromatin remodelling # 10880450 ACF, B-WICH, RSF, CHRAC, NoRC chromatin # # # 10880450 The DNA-binding properties of the p15–p17 complex are possibly relevant for incorporation of p15–p17 into chromatin, aided by the nucleosome remodelling activity of hSNF2H =SMARCA5 plus hACF1.
SMARCAD1
(details)
# 18398 SWI/SNF-related, matrix-associated actin-dependent regulator of chromatin, subfamily a, containing DEAD/H box 1 56916 Q9H4L7 SMRCD_HUMAN Helicase_C PF00271 888-967, Pfam-B_295 PB000295 41-308, SNF2_N PF00176 500-788 Smarcad1 95453 Q04692 SMRCD_MOUSE # # Chromatin remodelling # 22960744 # chromatin # # # 22960744 The yeast Saccharomyces cerevisiae Fun30 protein and its human counterpart SMARCAD1, two ATP-dependent chromatin remodellers of the Snf2 ATPase family, are directly involved in the DSB response.
SMARCAL1
(details)
# 11102 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a-like 1 50485 Q9NZC9 SMAL1_HUMAN HARP PF07443 248-302 343-397, Helicase_C PF00271 743-822, Pfam-B_7889 PB007889 1-159, SNF2_N PF00176 434-716 Smarcal1 1859183 Q8BJL0 SMAL1_MOUSE # # Chromatin remodelling # 11799392 # chromatin # # # 11799392 The unique constellation of findings constituting SIOD indicates that SMARCAL1 regulates the transcriptional activity of a particular subset of genes through chromatin remodeling during both development and later life.
SMARCB1
(details)
# 11103 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1 6598 Q12824 SNF5_HUMAN Pfam-B_9879 PB009879 2-146, SNF5 PF04855 178-373 Smarcb1 1328366 Q9Z0H3 SNF5_MOUSE # # Histone modification read # 21423274 BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1 histone H3K56 # # 21423274 Table 1 in the reference (SMARCB1 =Snf5)
SMARCC1
(details)
# 11104 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1 6599 Q92922 SMRC1_HUMAN Myb_DNA-binding PF00249 620-665, SWIRM PF04433 449-537 Smarcc1 1203524 P97496 SMRC1_MOUSE # # Chromatin remodelling cofactor # 10078207 BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1 chromatin # # # 10078207 The addition of INI1, BAF155 =SMARCC1, and BAF170 to BRG1 increases remodeling activity to a level comparable to that of the whole hSWI/SNF complex.
SMARCC2
(details)
# 11105 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2 6601 Q8TAQ2 SMRC2_HUMAN Myb_DNA-binding PF00249 598-643, Pfam-B_1849 PB001849 1-168, SWIRM PF04433 424-512 Smarcc2 1915344 Q6PDG5 SMRC2_MOUSE # # Chromatin remodelling cofactor # 10078207 BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1 chromatin # # # 10078207 The addition of INI1, BAF155, and BAF170 =SMARCC2 to BRG1 increases remodeling activity to a level comparable to that of the whole hSWI/SNF complex.
SMARCD1
(details)
# 11106 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1 6602 Q96GM5 SMRD1_HUMAN Pfam-B_13759 PB013759 1-79, Pfam-B_3130 PB003130 378-473, SWIB PF02201 291-366 Smarcd1 1933623 Q61466 SMRD1_MOUSE # # Chromatin remodelling # 12917342 BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, SWI/SNF BRM-BRG1 chromatin # # # 12917342 BAF60a =SMARCD1 possesses at least two interaction surfaces, one for GR and BRG1 and a second for BAF155 and BAF170. A GR mutant, GR(R488Q), that fails to interact with BAF60a=SMARCD1 in vitro has reduced chromatin-remodeling activity and reduced transcriptional activity from the promoter assembled as chromatin in vivo.
SMARCD2
(details)
# 11107 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 2 6603 Q92925 SMRD2_HUMAN Pfam-B_13705 PB013705 420-516, Pfam-B_7929 PB007929 141-287, SWIB PF02201 307-382 Smarcd2 1933621 Q99JR8 SMRD2_MOUSE # # Chromatin remodelling cofactor # 20148946 BAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brm, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1 chromatin # # # 20148946 The SWI/SNF chromatin remodelling complexes are important regulators of transcription; they consist of large multisubunit assemblies containing either Brm or Brg1 as the catalytic ATPase subunit and a variable subset of approximately 10 Brg/Brm-associated factors (BAF). Among these factors, BAF60 proteins (BAF60a, BAF60b=SMARCD2 or BAF60c), which are found in most complexes, are thought to bridge interactions between transcription factors and SWI/SNF complexes.
SMARCD3
(details)
# 11108 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 3 6604 Q6STE5 SMRD3_HUMAN Pfam-B_18257 PB018257 7-73, Pfam-B_3130 PB003130 346-441, SWIB PF02201 259-334 Smarcd3 1914243 Q6P9Z1 SMRD3_MOUSE # # Chromatin remodelling cofactor # 20148946 BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brm, SWI/SNF BRM-BRG1 chromatin # # # 20148946 The SWI/SNF chromatin remodelling complexes are important regulators of transcription; they consist of large multisubunit assemblies containing either Brm or Brg1 as the catalytic ATPase subunit and a variable subset of approximately 10 Brg/Brm-associated factors (BAF). Among these factors, BAF60 proteins (BAF60a, BAF60b or BAF60c=SMARCD3), which are found in most complexes, are thought to bridge interactions between transcription factors and SWI/SNF complexes.
SMARCE1
(details)
# 11109 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 6605 Q969G3 SMCE1_HUMAN HMG_box PF00505 66-134, Pfam-B_14199 PB014199 371-409 Smarce1 1927347 O54941 SMCE1_MOUSE # # Chromatin remodelling cofactor # 12672490 BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, bBAF chromatin # # # 12672490 In addition to Swi2/Snf2 proteins, there is evidence that other core components are required for chromatin-remodeling activity. More recently, two additional human Swi/Snf members, BAF57 =SMARCE1 and BAF60a, have been shown to interact directly with regulatory proteins.
SMEK1
(details)
New 20219 SMEK homolog 1, suppressor of mek1 (Dictyostelium) 55671 Q6IN85 P4R3A_HUMAN Pfam-B_1700 PB001700 381-501, Pfam-B_334 PB000334 506-611, SMK-1 PF04802 164-357 Smek1 1915984 Q6P2K6 P4R3A_MOUSE # # Histone modification erase cofactor Histone phosphorylation 18614045 PPP4C-PPP4R2-PPP4R3A histone H2AFX # # # Member of PPP4C-PPP4R2-PPP4R3A PP4 complex which specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX).
SMEK2
(details)
New 29267 SMEK homolog 2, suppressor of mek1 (Dictyostelium) 57223 Q5MIZ7 P4R3B_HUMAN Pfam-B_2986 PB002986 536-638, SMK-1 PF04802 166-359 Smek2 2144474 Q922R5 P4R3B_MOUSE # # Histone modification erase cofactor Histone phosphorylation 18614045 # histone H2AFX # # # Member of PPP4C-PPP4R2-PPP4R3B complex which dephosphorylates H2AFX.
SMYD1
(details)
New 20986 SET and MYND domain containing 1 150572 Q8NB12 SMYD1_HUMAN SET PF00856 18-253, zf-MYND PF01753 52-90 Smyd1 104790 P97443 SMYD1_MOUSE ZMYND, KMT Zinc fingers, MYND-type, "Chromatin-modifying enzymes / K-methyltransferases" Histone modification write Histone methylation 22498752 # histone H3K4 H3K4me # # SMYD1 methylates histone H3 at Lys-4 (H3K4me), according to UniProt.
SMYD2
(details)
# 20982 SET and MYND domain containing 2 56950 Q9NRG4 SMYD2_HUMAN SET PF00856 18-241, zf-MYND PF01753 52-90 Smyd2 1915889 Q8R5A0 SMYD2_MOUSE ZMYND, KMT Zinc fingers, MYND-type, Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation 18065756 # histone H3K4, H3K36 H3K4me, H3K36me2 # 18065756 Some reports indicate that SMYD2 methylates p53 and histone H3.
SMYD3
(details)
# 15513 SET and MYND domain containing 3 64754 Q9H7B4 SMYD3_HUMAN Pfam-B_27974 PB027974 391-422, SET PF00856 15-240, zf-MYND PF01753 47-87 Smyd3 1916976 Q9CWR2 SMYD3_MOUSE ZMYND, KMT Zinc fingers, MYND-type, Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation 15235609 # histone H3K4, H3K5 H3K4me2, H3K4me3, H3K5me2, H3K5me3 # 15235609 The SET domain of SMYD3 shows histone H3-lysine 4 (H3-K4)-specific methyltransferase activity, which is enhanced in the presence of the heat-shock protein HSP90A.
SMYD4
(details)
New 21067 SET and MYND domain containing 4 114826 Q8IYR2 SMYD4_HUMAN Pfam-B_24699 PB024699 740-795, Pfam-B_50317 PB050317 1-65, SET PF00856 244-574, TPR_11 PF13414 66-135, zf-MYND PF01753 296-335 Smyd4 2442796 Q8BTK5 SMYD4_MOUSE ZMYND Zinc fingers, MYND-type Histone modification erase cofactor Histone acetylation 18714374 # # # # # # SMYD4 interacts with HDAC1 and HDAC3.
SNAI2
(details)
New 11094 snail family zinc finger 2 6591 O43623 SNAI2_HUMAN zf-C2H2 PF00096 159-181, zf-C2H2_6 PF13912 127-153, zf-H2C2_2 PF13465 199-224 227-252 Snai2 1096393 P97469 SNAI2_MOUSE SNAI, ZNF Snail homologs, Zinc fingers, C2H2-type Histone modification erase cofactor # 15734731, 22986495 # histone # # # # May recruit HDAC1. PHD12 interacts directly with Sin3A/HDAC, which in turn interacts with Snail2.
SP1
(details)
# 11205 Sp1 transcription factor # P08047 SP1_HUMAN Pfam-B_20467 PB020467 61-148, Pfam-B_7620 PB007620 371-482, zf-C2H2 PF00096 626-650 686-708, zf-H2C2_2 PF13465 672-695 Sp1 98372 O89090 SP1_MOUSE SP, ZNF Specificity protein transcription factors, Zinc fingers, C2H2-type Chromatin remodelling, TF, TF #, TF activator, TF repressor 17827154, 18850004 CREST-BRG1 DNA DNA motif # # 17049555 #
SP100
(details)
# 11206 SP100 nuclear antigen 6672 P23497 SP100_HUMAN HMG_box PF00505 769-837, HMG_box_2 PF09011 684-753, Pfam-B_182547 PB182547 845-873, Pfam-B_41802 PB041802 151-337, SAND PF01342 595-676, Sp100 PF03172 47-150 Sp100 109561 O35892 SP100_MOUSE PHF Zinc fingers, PHD-type Chromatin remodelling cofactor # 9636146 # chromatin # # # 9636146 There is an association between the PML/SP100 NBs and the chromatin nuclear compartment. This supports a model in which the NBs may play a role in certain aspects of chromatin dynamics.
SP140
(details)
# 17133 SP140 nuclear body protein 11262 Q13342 SP140_HUMAN Bromodomain PF00439 775-842, PHD PF00628 692-736, SAND PF01342 580-661, Sp100 PF03172 36-139 Sp140 3702467 # # PHF Zinc fingers, PHD-type Histone modification read, TF #, # 22464331 # histone H3 # # 22464331 Fig. 5 in the reference.
SPEN
(details)
# 17575 spen family transcriptional repressor 23013 Q96T58 MINT_HUMAN Pfam-B_1253 PB001253 981-1331, Pfam-B_17673 PB017673 621-899, Pfam-B_17985 PB017985 901-979, Pfam-B_2825 PB002825 1826-1859, RRM_1 PF00076 8-74 337-407 440-507, RRM_5 PF13893 533-587, SPOC PF07744 3509-3630 Spen 1891706 Q62504 MINT_MOUSE RBM RNA binding motif (RRM) containing Histone modification erase cofactor, TF, TF Histone acetylation, TF activator, TF repressor 11331609 # histone # # # 11331609 SHARP =SPEN recruits histone deacetylase activity. SHARP is a potent transcriptional repressor whose repression domain (RD) interacts directly with SMRT and at least five members of the NuRD complex including HDAC1 and HDAC2.
SPOP
(details)
# 11254 speckle-type POZ protein 8405 O43791 SPOP_HUMAN BTB PF00651 190-297, MATH PF00917 38-163 Spop 1343085 Q6ZWS8 SPOP_MOUSE BTBD BTB/POZ domain containing Histone modification write Histone ubiquitination 15897469 # histone MacroH2A1 MacroH2A1ub # 15897469 The E3 ubiquitin ligase consisting of SPOP and CULLIN3 is able to ubiquitinate the Polycomb group protein BMI1 and the variant histone MACROH2A.
SRCAP
(details)
# 16974 Snf2-related CREBBP activator protein 10847 Q6ZRS2 SRCAP_HUMAN HSA PF07529 125-196, Helicase_C PF00271 2077-2156, SNF2_N PF00176 621-907 Srcap 2444036 # # # # Chromatin remodelling, Histone modification erase #, Histone acetylation 17617668 NuA4-related complex, SRCAP histone H2A.Z # # 17617668 The chromatin remodeling protein, SRCAP, is critical for deposition of the histone variant H2A.Z at promoters.
SRSF1
(details)
# 10780 serine/arginine-rich splicing factor 1 6426 Q07955 SRSF1_HUMAN Pfam-B_5206 PB005206 192-246, RRM_1 PF00076 18-85 123-186 Srsf1 98283 Q6PDM2 SRSF1_MOUSE SRSF, RBM Serine/arginine-rich splicing factors, RNA binding motif (RRM) containing RNA modification # 24706538 # RNA # # # 24706538 H3S10 phosphorylation has been shown to promote the recruitment of per-mRNA-splicing factor SRp20 and alternative-splicing factor (ASF)/per-mRNAsplicing factor 2 (SF2) modular proteins to the chromosomes.
SRSF3
(details)
# 10785 serine/arginine-rich splicing factor 3 6428 P84103 SRSF3_HUMAN Pfam-B_13909 PB013909 131-162, RRM_1 PF00076 12-77 Srsf3 98285 P84104 SRSF3_MOUSE SRSF, RBM Serine/arginine-rich splicing factors, RNA binding motif (RRM) containing RNA modification # 24706538 # RNA # # # 24706538 H3S10 phosphorylation has been shown to promote the recruitment of per-mRNA-splicing factor SRp20 and alternative-splicing factor (ASF)/per-mRNAsplicing factor 2 (SF2) modular proteins to the chromosomes.
SS18L1
(details)
# 15592 synovial sarcoma translocation gene on chromosome 18-like 1 26039 O75177 CREST_HUMAN Pfam-B_16193 PB016193 365-394, Pfam-B_22298 PB022298 315-363, SSXT PF05030 11-76 Ss18l1 2444061 Q8BW22 CREST_MOUSE # # Chromatin remodelling # 23799466 CREST-BRG1 chromatin # # # 23799466 -
SS18L2
(details)
# 15593 synovial sarcoma translocation gene on chromosome 18-like 2 51188 Q9UHA2 S18L2_HUMAN SSXT PF05030 11-76 Deb1 1349474 Q9D174 S18L2_MOUSE # # Chromatin remodelling # 19163965, 8666667 # chromatin # # # 15986999.4285714 #
SSRP1
(details)
# 11327 structure specific recognition protein 1 6749 Q08945 SSRP1_HUMAN HMG_box PF00505 547-615, Pfam-B_9245 PB009245 1-73, Rtt106 PF08512 338-428, SSrecog PF03531 74-285 Ssrp1 107912 Q08943 SSRP1_MOUSE # # Chromatin remodelling # 12934006 FACT histone H3, H4 # # 12934006 Both FACT and Spt16 can bind to nucleosomes and H2A-H2B dimers, whereas SSRP1 can only bind to H3-H4 tetramers but not to intact nucleosomes. Possibly, upon FACT binding to the nucleosome in the transcribed region, Spt16 facilitates the H2A-H2B displacement, which promotes the interaction between SSRP1 and the “altered” nucleosome.
STK4
(details)
# 11408 serine/threonine kinase 4 6789 Q13043 STK4_HUMAN Mst1_SARAH PF11629 432-480, Pfam-B_12195 PB012195 341-431, Pkinase PF00069 30-281 Stk4 1929004 Q9JI11 STK4_MOUSE # # Histone modification write Histone phosphorylation 12757711 # histone H2AS14 H2BS14ph # 12757711 Mst1 =STK4 can phosphorylate H2B at S14 in vitro and in vivo, and the onset of H2B S14 phosphorylation is dependent upon cleavage of Mst1 by caspase-3.
SUDS3
(details)
# 29545 suppressor of defective silencing 3 homolog (S. cerevisiae) 64426 Q9H7L9 SDS3_HUMAN Sds3 PF08598 53-223 Suds3 1919204 Q8BR65 SDS3_MOUSE # # Histone modification erase cofactor Histone acetylation 21239494 mSin3A histone # # # 21239494 SDS3 is a key component of the histone deacetylase (HDAC)-dependent Sin3A co-repressor complex, serving to maintain its HDAC activity.
SUPT16H
(details)
# 11465 suppressor of Ty 16 homolog (S. cerevisiae) 11198 Q9Y5B9 SP16H_HUMAN FACT-Spt16_Nlob PF14826 5-168, Peptidase_M24 PF00557 181-411, Pfam-B_18241 PB018241 958-1024, Rtt106 PF08512 806-896, SPT16 PF08644 529-689 Supt16 1890948 Q920B9 SP16H_MOUSE # # Histone modification read # 12934006 WINAC, FACT histone H2A, H2B # # 12934006 Both FACT and Spt16=SUPT16H can bind to nucleosomes and H2A-H2B dimers, whereas SSRP1 can only bind to H3-H4 tetramers but not to intact nucleosomes. Possibly, upon FACT binding to the nucleosome in the transcribed region, Spt16 facilitates the H2A-H2B displacement, which promotes the interaction between SSRP1 and the “altered” nucleosome.
SUPT3H
(details)
# 11466 suppressor of Ty 3 homolog (S. cerevisiae) 8464 O75486 SUPT3_HUMAN TFIID-18kDa PF02269 106-198 # # # # # # Histone modification write cofactor Histone acetylation 11564863 PCAF, SAGA, STAGA histone # # # 11564863 GCN5 is a histone acetyltransferase (HAT) originally identified in Saccharomyces cerevisiae and required for transcription of specific genes within chromatin as part of the SAGA (SPT-ADA-GCN5 acetylase) coactivator complex. Mammalian cells have two distinct GCN5 homologs (PCAF and GCN5L) that have been found in three different SAGA-like complexes (PCAF complex, TFTC [TATA-binding-protein-free TAFII-containing complex], and STAGA [SPT3-TAFII31-GCN5L acetylase]).
SUPT6H
(details)
New 11470 suppressor of Ty 6 homolog (S. cerevisiae) 6830 Q7KZ85 SPT6H_HUMAN DLD PF14878 1050-1160, HHH_7 PF14635 935-1038, HTH_44 PF14641 300-437, Pfam-B_17741 PB017741 172-225, Pfam-B_27919 PB027919 129-149, S1 PF00575 1226-1282, SH2_2 PF14633 1295-1515, SPT6_acidic PF14632 35-128, YqgF PF14639 775-931 Supt6 107726 Q62383 SPT6H_MOUSE SH2D SH2 domain containing Histone modification erase cofactor Histone methylation 23503590 # histone # # # # Coordinates H3K27 demethylation.
SUPT7L
(details)
# 30632 suppressor of Ty 7 (S. cerevisiae)-like 9913 O94864 ST65G_HUMAN Bromo_TP PF07524 151-230, Pfam-B_18361 PB018361 301-379, Pfam-B_18885 PB018885 1-69 Supt7l 1919445 Q9CZV5 ST65G_MOUSE # # Histone chaperone # 11564863 TFTC-HAT, STAGA histone # # # 11564863 STAGA contains homologs of most yeast SAGA components, including two novel human proteins with histone-like folds and sequence relationships to yeast SPT7 and ADA1. STAGA preferentially acetylates histone H3 within nucleosomes.
SUV39H1
(details)
# 11479 suppressor of variegation 3-9 homolog 1 (Drosophila) 6839 O43463 SUV91_HUMAN Chromo PF00385 43-92, Pre-SET PF05033 135-235, SET PF00856 255-366 Suv39h1 1099440 O54864 SUV91_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write, Histone modification write Histone methylation, Histone phosphorylation 10949293 eNoSc histone H3S10, H3K9me1, H4 H3K9me3 # 10949293 In vivo, deregulated SUV39H1 or disrupted Suv39h activity modulate H3 serine 10 phosphorylation in native chromatin and induce aberrant mitotic divisions.
SUV39H2
(details)
# 17287 suppressor of variegation 3-9 homolog 2 (Drosophila) 79723 Q9H5I1 SUV92_HUMAN Chromo PF00385 47-96, Pre-SET PF05033 144-242, SET PF00856 262-373 Suv39h2 1890396 Q9EQQ0 SUV92_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation 15107829 # histone H3K9me1 H3K9me3 # 15107829 Suv39h proteins are histone methyltransferases that methylate histone H3 on lysine 9, resulting in transcriptional repression or silencing of target genes.
SUV420H1
(details)
# 24283 suppressor of variegation 4-20 homolog 1 (Drosophila) 51111 Q4FZB7 SV421_HUMAN Pfam-B_23340 PB023340 771-839, Pfam-B_24134 PB024134 711-769, Pfam-B_32221 PB032221 551-609, Pfam-B_49669 PB049669 841-883, SET PF00856 99-308 Suv420h1 2444557 Q3U8K7 SV421_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation # # histone H4K20 H4K20me3 # # Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. (Annotated by similarity.)
SUV420H2
(details)
# 28405 suppressor of variegation 4-20 homolog 2 (Drosophila) 84787 Q86Y97 SV422_HUMAN Pfam-B_18005 PB018005 261-379, Pfam-B_59617 PB059617 1-39, Pfam-B_6511 PB006511 381-460, SET PF00856 121-218 Suv420h2 2385262 Q6Q783 SV422_MOUSE KMT Chromatin-modifying enzymes / K-methyltransferases Histone modification write Histone methylation # # histone H4K20 H4K20me3 # # Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. (Annotated by similarity.)
SUZ12
(details)
# 17101 SUZ12 polycomb repressive complex 2 subunit 23512 Q15022 SUZ12_HUMAN VEFS-Box PF09733 544-681 Suz12 1261758 Q80U70 SUZ12_MOUSE ZNF Zinc fingers, C2H2-type Histone modification write cofactor, Histone modification write cofactor, Polycomb group (PcG) protein, TF Histone methylation, Histone ubiquitination, #, TF repressor 15385962 PRC2 DNA DNA motif # # 15385962 SUZ12 is a recently identified Polycomb group (PcG) protein, which together with EZH2 and EED forms different Polycomb repressive complexes (PRC2/3).
SYNCRIP
(details)
# 16918 synaptotagmin binding, cytoplasmic RNA interacting protein 10492 O60506 HNRPQ_HUMAN RRM_1 PF00076 164-232 245-312 340-402 Syncrip 1891690 Q7TMK9 HNRPQ_MOUSE RBM RNA binding motif (RRM) containing RNA modification mRNA editing 11134005, 11352648 APOB_mRNA_editosome RNA mRNA # # 11134005, 11352648 GRY-RBP =HNRPQ has been shown to bind to apobec-1, the catalytic component of apoB mRNA editosome, in vivo and in vitro.
TADA1
(details)
# 30631 transcriptional adaptor 1 117143 Q96BN2 TADA1_HUMAN SAGA-Tad1 PF12767 3-195 Tada1 1196415 Q99LM9 TADA1_MOUSE # # Histone chaperone # 11564863 STAGA histone H2A # # 11564863 Within STAGA are two novel histone fold-containing protein subunits: STAF65γ, which is encoded by the KIAA0764 gene of previously unknown function, and STAF42=TADA1, a novel histone H2A-like protein.
TADA2A
(details)
# 11531 transcriptional adaptor 2A 6871 O75478 TAD2A_HUMAN Myb_DNA-binding PF00249 72-118, SWIRM PF04433 362-442 Tada2a 2144471 Q8CHV6 TAD2A_MOUSE # # Histone modification read, TF #, TF activator 19103755 PCAF, ATAC histone H3 # # 19103755 The SANT domain of c-Myb has been shown to bind histone H3 tails and position them for acetylation. The SANT domains in ADA2a=TADA2A and ZZZ3/ATAC1 might enable the complex to associate with nucleosome tails in order to potentiate the catalytic activities of GCN5 and ATAC2, similar to what has been shown for the SANT domains in yeast Ada2 and Swi3.
TADA2B
(details)
# 30781 transcriptional adaptor 2B 93624 Q86TJ2 TAD2B_HUMAN Myb_DNA-binding PF00249 67-113, ZZ PF00569 6-47 Tada2b 3035274 # # # # Histone modification write cofactor Histone acetylation 17694077 TFTC-HAT histone # # # 17694077 ADA2b =TADA2B is present in human STAGA/TFTC-type complexes.
TADA3
(details)
# 19422 transcriptional adaptor 3 10474 O75528 TADA3_HUMAN Ada3 PF10198 308-432 Tada3 1915724 Q8R0L9 TADA3_MOUSE # # Histone modification write cofactor Histone acetylation 11773077 PCAF, TFTC-HAT, ATAC, STAGA histone # # # 11773077 Ada2 potentiates the Gcn5 catalytic activity and Ada3 =TADA3 facilitates nucleosomal acetylation and an expanded lysine specificity.
TAF1
(details)
# 11535 TAF1 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 250kDa 6872 P21675 TAF1_HUMAN Bromodomain PF00439 1389-1472 1509-1595, DUF3591 PF12157 565-1028, Pfam-B_10720 PB010720 311-366, TBP-binding PF09247 22-87, zf-CCHC_6 PF15288 1261-1300 Taf1 1336878 Q80UV9 TAF1_MOUSE KAT Chromatin-modifying enzymes / K-acetyltransferases Histone modification write Histone acetylation 11295558 CHD8, MLL2/3, MLL4/WBP7 histone H3, H4 H3ac, H4ac # 11295558 TAFII250 has histone acetyltransferase (HAT) activity and can acetylate the tails of the core histones H3 and H4 in vitro. Both the N- and C-terminal kinase domains of TAFII250 are required for efficient transphosphorylation of RAP74 on serine residues. This suggests that the targeted phosphorylation of RAP74 by TAFII250 may provide a mechanism for signaling between components within the initiation complex to regulate transcription.
TAF10
(details)
# 11543 TAF10 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 30kDa 6881 Q12962 TAF10_HUMAN TFIID_30kDa PF03540 128-178 Taf10 1346320 Q8K0H5 TAF10_MOUSE # # Histone chaperone, Histone modification write #, Histone acetylation 15099517 PCAF, TFTC-HAT, SAGA, STAGA histone H3, H4 # # 15099517 SET9 can monomethylate the TBP-associated factor TAF10 at a single lysine residue located at the loop 2 region within the putative histone-fold domain of the protein.
TAF12
(details)
# 11545 TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa 6883 Q16514 TAF12_HUMAN Pfam-B_25018 PB025018 1-58, TFIID_20kDa PF03847 59-126 Taf12 1913714 Q8VE65 TAF12_MOUSE # # Histone chaperone, Histone modification write #, Histone acetylation 10594036 PCAF, STAGA histone # # # 10594036 Heterodimerization requires the alpha2 and alpha3 helices of the hTAF(II)20 histone fold and is abolished by mutations in the hydrophobic face of the hTAF(II)20 alpha2 helix. Interaction with hTAF(II)20 requires a domain of hTAF(II)135 which shows sequence homology to H2A.
TAF1L
(details)
# 18056 TAF1 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 210kDa-like 138474 Q8IZX4 TAF1L_HUMAN Bromodomain PF00439 1408-1491 1528-1614, DUF3591 PF12157 584-1047, Pfam-B_10720 PB010720 330-385, TBP-binding PF09247 21-86, zf-CCHC_6 PF15288 1280-1319 # # # # # # Histone modification read # 22464331 # histone H1.4ac, H2Aac, H2Bac, H3ac, H4ac # # 22464331 Interacts (via bromo domains) with acetylated lysine residues on the N-terminus of histone H1.4, H2A, H2B, H3 and H4 (in vitro).
TAF2
(details)
# 11536 TAF2 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 150kDa 6873 Q6P1X5 TAF2_HUMAN Peptidase_M1 PF01433 21-406, Pfam-B_2101 PB002101 661-979, Pfam-B_21717 PB021717 1111-1159, Pfam-B_6210 PB006210 1161-1197, Pfam-B_8840 PB008840 981-1109 Taf2 2443028 Q8C176 TAF2_MOUSE # # TF # # TFTC-HAT DNA DNA motif # # # Added because it is a complex partner
TAF3
(details)
# 17303 TAF3 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 140kDa 83860 Q5VWG9 TAF3_HUMAN Bromo_TP PF07524 3-79, PHD PF00628 867-915 Taf3 2388097 Q5HZG4 TAF3_MOUSE PHF Zinc fingers, PHD-type Histone modification read # 21423274 # histone H3K4me # # 21423274 Table 1 in the reference.
TAF4
(details)
# 11537 TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa 6874 O00268 TAF4_HUMAN Pfam-B_41790 PB041790 141-219, Pfam-B_7817 PB007817 411-499, Pfam-B_906 PB000906 1-139, TAF4 PF05236 834-1084, TAFH PF07531 590-688 # # # # # # Histone chaperone # 10594036 TFTC-HAT, CHD8, MLL2/3, MLL4/WBP7 histone # # # 10594036 The histone fold region of hTAFII135 is required for coactivator activity in mammalian cells.
TAF5
(details)
# 11539 TAF5 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 100kDa 6877 Q15542 TAF5_HUMAN Pfam-B_22190 PB022190 61-159, Pfam-B_34937 PB034937 1-59, TFIID_90kDa PF04494 199-338, WD40 PF00400 461-498 533-571 575-613 617-655 659-697 701-739 Taf5 2442144 Q8C092 TAF5_MOUSE WDR WD repeat domain containing Histone modification write cofactor Histone acetylation 10373431 TFTC-HAT histone # # # 10373431 TFTC, similar to other TBP-free TAFII complexes (yeast SAGA, hSTAGA, and hPCAF) contains the acetyltransferase hGCN5 and is able to acetylate histones in both a free and a nucleosomal context. A monoclonal antibody raised against hTAFII100 recognized hTAFII100=TAF5 not only in TFTC, but detected also a weak band in the PCAF complex.
TAF5L
(details)
# 17304 TAF5-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa 27097 O75529 TAF5L_HUMAN TFIID_90kDa PF04494 55-196, WD40 PF00400 259-296 332-370 375-412 416-454 458-496 500-538 Taf5l 1919039 Q91WQ5 TAF5L_MOUSE WDR WD repeat domain containing Histone modification write cofactor Histone acetylation 10373431 PCAF, TFTC-HAT, STAGA histone # # # 10373431 The PCAF complex contains hPAF65β=TAF5L, a WD40 repeat-containing factor having similarity to Htafii100(row=423) (5). Antibodies raised against hPAF65β revealed a band around 65 kDa in both the PCAF and the TFTC complexes.
TAF6
(details)
# 11540 TAF6 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 80kDa 6878 P49848 TAF6_HUMAN DUF1546 PF07571 308-399, Pfam-B_25920 PB025920 618-675, TAF PF02969 11-76 Taf6 109129 Q62311 TAF6_MOUSE # # Histone chaperone # 9611234 TFTC-HAT, CHD8, MLL2/3, MLL4/WBP7 DNA # # # 9611234 The N-CoR/Sin3/HDAc complexes have a key role in the regulation of cellular proliferation and differentiation. N-CoR interacts directly with each of the basal factors, TFIIB and TAFII70 (=TAF6).
TAF6L
(details)
# 17305 TAF6-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa 10629 Q9Y6J9 TAF6L_HUMAN DUF1546 PF07571 242-333, Pfam-B_32143 PB032143 200-239, Pfam-B_32396 PB032396 161-199, TAF PF02969 9-73 Taf6l 2444957 Q8R2K4 TAF6L_MOUSE # # Histone chaperone # 12601814 PCAF, TFTC-HAT, STAGA histone # # # 12601814 Human PAF65-alpha shows a strong sequence homology to TAFII80 and also contains a putative HFD. Thus, PAF65-alpha may also interact with TAFII32 in the TFTC complex.
TAF7
(details)
# 11541 TAF7 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 55kDa 6879 Q15545 TAF7_HUMAN TAFII55_N PF04658 12-178 Taf7 1346348 Q9R1C0 TAF7_MOUSE # # Histone modification write cofactor, Histone modification write cofactor Histone methylation, Histone acetylation 22711989 CHD8, MLL2/3, MLL4/WBP7 histone # # # 22711989 The largest transcription factor IID (TFIID) subunit, TBP-associated factor 1 (TAF1), possesses protein kinase and histone acetyltransferase (HAT) activities.
TAF8
(details)
# 17300 TAF8 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 43kDa 129685 Q7Z7C8 TAF8_HUMAN Bromo_TP PF07524 29-106, TAF8_C PF10406 144-194 Taf8 1926879 Q9EQH4 TAF8_MOUSE # # Histone chaperone # 17375202 # histone # # # 17375202 Present in a small TAF complex (SMAT), containing TAF8, TAF10 and SPT7L.
TAF9
(details)
# 11542 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa 6880 Q16594 TAF9_HUMAN TFIID-31kDa PF02291 2-130 Taf9 1888697 Q8VI33 TAF9_MOUSE # # Histone chaperone # 9674425 PCAF, STAGA, CHD8, MLL2/3, MLL4/WBP7 DNA # # # 9674425 Histone-like TAFs, including TAFII31 =TAF9, are found within the PCAF histone acetylase complex.
TAF9B
(details)
# 17306 TAF9B RNA polymerase II, TATA box binding protein (TBP)-associated factor, 31kDa 51616 Q9HBM6 TAF9B_HUMAN TFIID-31kDa PF02291 2-130 Taf9b 3039562 Q6NZA9 TAF9B_MOUSE # # Histone chaperone # 15899866 TFTC-HAT histone # # # 15899866 TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping roles with TAF9.
TBL1XR1
(details)
New 29529 transducin (beta)-like 1 X-linked receptor 1 79718 Q9BZK7 TBL1R_HUMAN LisH PF08513 6-32, Pfam-B_2526 PB002526 471-510, WD40 PF00400 160-197 224-253 256-294 298-335 339-377 381-428 432-470 Tbl1xr1 2441730 Q8BHJ5 TBL1R_MOUSE WDR WD repeat domain containing # # 15601853 # histone # # # # Targets Ncor repressive complex to deacethylated histones.
TDG
(details)
# 11700 thymine-DNA glycosylase 6996 Q13569 TDG_HUMAN UDG PF03167 125-293 Tdg 108247 P56581 TDG_MOUSE # # DNA modification DNA hydroxymethylation 22962365 # DNA G:U, G:T, G:hmU C, 5mC, 5hmC # 22962365 The mammalian thymine DNA glycosylase (TDG) is implicated in active DNA demethylation via the base excision repair pathway.
TDRD3
(details)
# 20612 tudor domain containing 3 81550 Q9H7E2 TDRD3_HUMAN TUDOR PF00567 542-615, UBA PF00627 194-230 Tdrd3 2444023 Q91W18 TDRD3_MOUSE TDRD Tudor domain containing Histone modification read # 21172665 # histone H3R17me2a, H4R3me2a # # 21172665 TDRD3 is an effector molecule for arginine-methylated histone marks.
TDRD7
(details)
# 30831 tudor domain containing 7 23424 Q8NHU6 TDRD7_HUMAN OST-HTH PF12872 5-73, Pfam-B_27056 PB027056 101-149, TUDOR PF00567 459-581 648-775 908-1026 Tdrd7 2140279 Q8K1H1 TDRD7_MOUSE TDRD Tudor domain containing Histone modification read # 21423274 # histone H3K9 # # 21423274 Table 1 in the reference.
TDRKH
(details)
# 11713 tudor and KH domain containing 11022 Q9Y2W6 TDRKH_HUMAN KH_1 PF00013 54-115 126-190, Pfam-B_19308 PB019308 201-301, TUDOR PF00567 302-423 Tdrkh 1919884 Q80VL1 TDRKH_MOUSE TDRD Tudor domain containing RNA modification # 23714778 # RNA piRNA # # 23714778 Piwi proteins and Piwi-interacting RNAs (piRNAs) repress transposition, regulate translation, and guide epigenetic programming in the germline. The evolutionarily conserved Tudor and KH domain-containing protein, Tdrkh (a.k.a. Tdrd2), is required for spermatogenesis and involved in piRNA biogenesis, the primary piRNA biogenesis pathway involves 3'→5' processing of 31-37 nt intermediates and that Tdrkh promotes this final step of piRNA biogenesis but not the ping-pong cycle.
TET1
(details)
# 29484 tet methylcytosine dioxygenase 1 80312 Q8NFU7 TET1_HUMAN Pfam-B_12165 PB012165 2056-2134, Pfam-B_35074 PB035074 1-139, Pfam-B_6123 PB006123 782-815, Tet_JBP PF12851 1580-2052, zf-CXXC PF02008 583-624 Tet1 1098693 Q3URK3 TET1_MOUSE # # DNA modification DNA hydroxymethylation 23222540 # DNA mC hmC # 23222540 Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription.
TET2
(details)
# 25941 tet methylcytosine dioxygenase 2 54790 Q6N021 TET2_HUMAN Pfam-B_32546 PB032546 930-1046, Pfam-B_34477 PB034477 1927-1975, Tet_JBP PF12851 1290-1905 Tet2 2443298 Q4JK59 TET2_MOUSE # # DNA modification DNA hydroxymethylation 23222540 # DNA mC hmC # 23222540 Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription. Downregulation of TET2 reduces the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation.
TET3
(details)
# 28313 tet methylcytosine dioxygenase 3 200424 O43151 TET3_HUMAN Pfam-B_188 PB000188 1613-1658, Pfam-B_19260 PB019260 1-109, Tet_JBP PF12851 850-1562 Tet3 2446229 Q8BG87 TET3_MOUSE # # DNA modification DNA hydroxymethylation 23222540 # DNA mC hmC # 23222540 Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription. There is a direct interaction of TET2 and TET3 with O-GlcNAc transferase (OGT).
TEX10
(details)
# 25988 testis expressed 10 54881 Q9NXF1 TEX10_HUMAN Ipi1_N PF12333 130-235, Pfam-B_18291 PB018291 611-869 Tex10 1344413 Q3URQ0 TEX10_MOUSE # # Histone modification write cofactor, Histone modification write cofactor Histone methylation, Histone acetylation # CHD8, MLL2/3, MLL4/WBP7 histone # # # 22872859 -
TFDP1
(details)
New 11749 transcription factor Dp-1 7027 Q14186 TFDP1_HUMAN DP PF08781 200-344, E2F_TDP PF02319 111-193 Tfdp1 101934 Q08639 TFDP1_MOUSE # # Histone modification # 24217316, 22325352 RING2-L3MBTL2 histone # # # 24217316, 22325352 Part of a RING2 complex.
TFPT
(details)
# 13630 TCF3 (E2A) fusion partner (in childhood Leukemia) 29844 P0C1Z6 TFPT_HUMAN Pfam-B_10240 PB010240 10-162, Pfam-B_26015 PB026015 181-212 Tfpt 1916964 Q3U1J1 TFPT_MOUSE INO80 INO80 complex subunits Chromatin remodelling cofactor, DNA modification #, DNA hydroxymethylation 16230350 Ino80 chromatin # # # 16230350 Subunit Composition of the hINO80 Complex: These proteins included the “Pim-1 kinase-associated protein-associated protein 1” (PAPA-1, GI 13775202), Amida (also known as TCF3 =TFPT).
TLE1
(details)
# 11837 transducin-like enhancer of split 1 (E(sp1) homolog, Drosophila) 7088 Q04724 TLE1_HUMAN TLE_N PF03920 1-136, WD40 PF00400 477-511 523-558 565-602 606-644 689-726 736-767 Tle1 104636 Q62440 TLE1_MOUSE WDR WD repeat domain containing Chromatin remodelling, Histone modification cofactor #, # 9334241, 17041588 # histone H3 # # 9334241, 17041588 Native Groucho/TLE proteins interact specifically with histone H3 and not with other core histones.
TLE2
(details)
# 11838 transducin-like enhancer of split 2 7089 Q04725 TLE2_HUMAN TLE_N PF03920 1-132, WD40 PF00400 450-484 538-575 579-617 661-699 709-740 Tle2 104635 Q9WVB2 TLE2_MOUSE WDR WD repeat domain containing Histone modification cofactor # 17041588 # histone H3 H3K4, H3K9, H3K27me # 17041588 CUL4-DDB1 complexes interact with multiple WD40-repeat proteins (WDRs) including TLE1-3, WDR5, L2DTL (also known as CDT2) and the Polycomb-group protein EED (also known as ESC). WDR5 and EED are core components of histone methylation complexes that are essential for histone H3 methylation and epigenetic control at K4 or K9 and K27, respectively.
TLE4
(details)
# 11840 transducin-like enhancer of split 4 7091 Q04727 TLE4_HUMAN TLE_N PF03920 8-141, WD40 PF00400 480-514 526-561 568-605 609-647 692-729 739-770 Tle4 104633 Q62441 TLE4_MOUSE WDR WD repeat domain containing Histone modification erase cofactor, TF #, # 24190972 # histone H3ac, H4ac # # 24190972 Tle4 is the transcriptional repressor responsible for the establishment of the epigenetic repressive marks at the Ifng locus that result in silencing of Ifng gene expression. Tle proteins have been shown to oligomerize, to associate with amino-terminal domains of histone-modifying proteins, and to form higher-order structures as parts of repressive complexes.
TLK1
(details)
# 11841 tousled-like kinase 1 9874 Q9UKI8 TLK1_HUMAN Pfam-B_2740 PB002740 1-109, Pfam-B_9699 PB009699 111-179, Pkinase PF00069 456-734 Tlk1 2441683 Q8C0V0 TLK1_MOUSE # # Histone modification write Histone phosphorylation 11314006 # histone H3S10 H3S10ph # 11314006 Purified TLK1B phosphorylates histone H3 at S(10) with high specificity both in a mix of core histones and in isolated chromatin, suggesting that histone H3 is a physiological substrate for TLK1B.
TLK2
(details)
# 11842 tousled-like kinase 2 11011 Q86UE8 TLK2_HUMAN Pfam-B_24604 PB024604 91-129, Pfam-B_3701 PB003701 1-89, Pkinase PF00069 462-741 Tlk2 1346023 O55047 TLK2_MOUSE # # Histone modification write Histone phosphorylation 12660173 # chromatin # # # 12660173 There is a functional co-operation between ATM and Chk1 in propagation of a checkpoint response during S phase, suggesting that, through transient inhibition of Tlk kinases, the ATM-Chk1-Tlk pathway may regulate processes involved in chromatin assembly.
TNP1
(details)
# 11951 transition protein 1 (during histone to protamine replacement) 7141 P09430 STP1_HUMAN TP1 PF02079 2-55 Tnp1 98784 P10856 STP1_MOUSE # # Chromatin remodelling # 12743712 # chromatin # # # 12743712 Distinct roles for the two major transition nuclear proteins, TP1 = STP1 and TP2 = STP2, in histone displacement, sperm nuclear shaping, chromatin condensation, and maintenance of DNA integrity have been proposed.
TNP2
(details)
# 11952 transition protein 2 (during histone to protamine replacement) 7142 Q05952 STP2_HUMAN TP2 PF01254 1-138 Tnp2 98785 P11378 STP2_MOUSE # # Chromatin remodelling # 12743712 # chromatin # # # 12743712 Distinct roles for the two major transition nuclear proteins, TP1 = STP1 and TP2 = STP2, in histone displacement, sperm nuclear shaping, chromatin condensation, and maintenance of DNA integrity have been proposed.
TONSL
(details)
# 7801 tonsoku-like, DNA repair protein 4796 Q96HA7 TONSL_HUMAN Ank PF00023 528-560 561-591 597-629, LRR_6 PF13516 1097-1121, Pfam-B_27656 PB027656 642-670, Pfam-B_51992 PB051992 204-263, TPR_11 PF13414 350-422 Tonsl 1919999 Q6NZL6 TONSL_MOUSE ANKRD Ankyrin repeat domain containing Chromatin remodelling # 21113133 # histone # # # 21113133 Mms22L associates with Nfkbil2 =TONSL, which may function as a scaffolding unit to bridge chromatin to multiple protein complexes.
TOP2A
(details)
# 11989 topoisomerase (DNA) II alpha 170kDa 7153 P11388 TOP2A_HUMAN DNA_gyraseB PF00204 266-430, DNA_topoisoIV PF00521 713-1172, DTHCT PF08070 1435-1523, HATPase_c PF02518 77-224, Toprim PF01751 456-572 Top2a 98790 Q01320 TOP2A_MOUSE # # Chromatin remodelling # 11062478 # DNA DNA # # 11062478 Histone deacetylase interacts directly with DNA topoisomerase II.
TOP2B
(details)
# 11990 topoisomerase (DNA) II beta 180kDa 7155 Q02880 TOP2B_HUMAN DNA_gyraseB PF00204 287-450, DNA_topoisoIV PF00521 734-1190, DTHCT PF08070 1508-1611, HATPase_c PF02518 98-245, Toprim PF01751 477-593 Top2b 98791 Q64511 TOP2B_MOUSE # # Chromatin remodelling # 11062478 WINAC chromatin # # # 11062478 Histone deacetylase interacts directly with DNA topoisomerase II.
TP53
(details)
# 11998 tumor protein p53 7157 P04637 P53_HUMAN P53 PF00870 95-289, P53_TAD PF08563 5-29, P53_tetramer PF07710 318-359 Trp53 98834 P02340 P53_MOUSE # # Histone modification write cofactor, TF, TF Histone acetylation, TF activator, TF repressor 23870121 # histone H3 # # 23870121 SET1 complex (SET1C)-mediated H3K4 trimethylation is dependent upon p53- and p300-mediated H3 acetylation. Complementary cell-based assays demonstrate a DNA-damage-induced p53-SET1C interaction, a corresponding enrichment of SET1C and H3K4me3 on a p53 target gene (p21/WAF1), and a corresponding codependency of H3K4 trimethylation and transcription upon p300 and SET1C.
TP53BP1
(details)
# 11999 tumor protein p53 binding protein 1 7158 Q12888 TP53B_HUMAN 53-BP1_Tudor PF09038 1483-1604, Pfam-B_14288 PB014288 1213-1356, Pfam-B_21507 PB021507 1-59, Pfam-B_24656 PB024656 1358-1386, Pfam-B_24892 PB024892 970-1000, Pfam-B_44 PB000044 528-565, Pfam-B_689 PB000689 567-698, Pfam-B_9132 PB009132 902-939, Pfam-B_9249 PB009249 1611-1967 Trp53bp1 1351320 P70399 TP53B_MOUSE # # Histone modification read # 15525939 # histone H4K79me2, H4K20me2 # # 15525939 In vitro, the 53BP1 =TP53BP1 tandem tudor domain binds histone H3 methylated on Lys 79 using residues that form the walls of the pocket; these residues are also required for recruitment of 53BP1 to DSBs.
TRIM16
(details)
New 17241 tripartite motif containing 16 10626 O95361 TRI16_HUMAN PRY PF13765 375-424, Pfam-B_10855 PB010855 281-339, SPRY PF00622 426-551, zf-B_box PF00643 126-165 Trim16 2137356 Q99PP9 TRI16_MOUSE TRIM Tripartite motif containing / Tripartite motif containing Histone modification write Histone acetylation 19147277, 20729920 # histone, DNA # # # # Overexpression of this gene increases histone acetylation. TRIM16 has been identified as a DNA-binding protein with histone acetylase activity.
TRIM24
(details)
# 11812 tripartite motif containing 24 8805 O15164 TIF1A_HUMAN Bromodomain PF00439 908-992, PHD PF00628 828-873, Pfam-B_14213 PB014213 595-656, Pfam-B_4946 PB004946 372-591, zf-B_box PF00643 158-205 218-259 Trim24 109275 Q64127 TIF1A_MOUSE TRIM, RNF, PHF Tripartite motif containing / Tripartite motif containing, RING-type (C3HC4) zinc fingers, Zinc fingers, PHD-type Histone modification read # 22464331 # histone H3K4, H3K23ac # # 21164480 Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac) (UniProt).
TRIM27
(details)
New 9975 tripartite motif containing 27 5987 P14373 TRI27_HUMAN PRY PF13765 318-366, SPRY PF00622 368-493, zf-B_box PF00643 91-132, zf-C3HC4 PF00097 16-56 Trim27 97904 Q62158 TRI27_MOUSE TRIM, RNF Tripartite motif containing / Tripartite motif containing, RING-type (C3HC4) zinc fingers Histone modification erase cofactor Histone acetylation 19351825 # # # # # # The recruitment of HDAC1 to the TBP-2 promoter is mediated by a protein complex consisting of RET finger protein (RFP; also called TRIM27) and the trimeric transcription factor NF-Y.
TRIM28
(details)
# 16384 tripartite motif containing 28 10155 Q13263 TIF1B_HUMAN PHD PF00628 627-672, zf-B_box PF00643 148-195 204-245, zf-RING_5 PF14634 64-122 Trim28 109274 Q62318 TIF1B_MOUSE TRIM, RNF, PHF Tripartite motif containing / Tripartite motif containing, RING-type (C3HC4) zinc fingers, Zinc fingers, PHD-type Histone modification read # 22464331 # histone H3 # # 22464331 Fig. 5 in the reference.
TRIM33
(details)
# 16290 tripartite motif containing 33 51592 Q9UPN9 TRI33_HUMAN Bromodomain PF00439 966-1051, PHD PF00628 889-933, Pfam-B_10963 PB010963 664-696, Pfam-B_11449 PB011449 608-663, Pfam-B_11628 PB011628 535-606, zf-B_box PF00643 212-258 271-312, zf-RING_2 PF13639 123-185 Trim33 2137357 Q99PP7 TRI33_MOUSE TRIM, PHF, RNF Tripartite motif containing / Tripartite motif containing, Zinc fingers, PHD-type, RING-type (C3HC4) zinc fingers Histone modification read # 23926104 # histone H3K9me3, H3K18ac # # 23926104 TRIM33 helps recruit SMAD2/3 to chromatin via interaction of its PHD and Bromo domains with histone H3 trimethylated at lysine 9 (H3K9me3) and histone H3 acetylated at lysine 18 (H3K18ac), respectively.
TRRAP
(details)
# 12347 transformation/transcription domain-associated protein 8295 Q9Y4A5 TRRAP_HUMAN FAT PF02259 2849-3204, PI3_PI4_kinase PF00454 3526-3783, Pfam-B_11387 PB011387 1471-1587, Pfam-B_12811 PB012811 141-238, Pfam-B_15427 PB015427 1-139, Pfam-B_3253 PB003253 1858-1890 1946-2001, Pfam-B_6491 PB006491 1589-1667, Pfam-B_6680 PB006680 2445-2544 Trrap 2153272 Q80YV3 TRRAP_MOUSE # # Histone modification write cofactor Histone acetylation 14966270 SWR, PCAF, TFTC-HAT, NuA4, SAGA, NuA4-related complex, STAGA histone # # # 14966270 The complex(es) contain(s) other subunits shared with NuA4, including TRRAP, p400/hDomino, Brd8.
TSSK6
(details)
New 30410 testis-specific serine kinase 6 83983 Q9BXA6 TSSK6_HUMAN Pkinase PF00069 12-267 Tssk6 2148775 Q925K9 TSSK6_MOUSE # # Histone modification write Histone phosphorylation 15870294 # histone H1, H2A, H2AX, H3 # # # Phosphorylates histones H1, H2A, H2AX, and H3 but not H2B or H4 in vitro.
TTK
(details)
# 12401 TTK protein kinase 7272 P33981 TTK_HUMAN Pfam-B_2743 PB002743 1-291, Pkinase PF00069 525-791 Ttk 1194921 P35761 TTK_MOUSE # # Histone modification write cofactor Histone phosphorylation 22732840 # histone H2AT120 H2AT120ph # 22732840 Mps1 = TTK activity enhances H2A‐T120ph and is critical for Sgo1 recruitment to centromeres, thereby promoting Aurora B centromere recruitment in early mitosis.
TYW5
(details)
# 26754 tRNA-yW synthesizing protein 5 129450 A2RUC4 TYW5_HUMAN Cupin_8 PF13621 16-256 Tyw5 1915986 A2RSX7 TYW5_MOUSE # # RNA modification # 20972222 # RNA # # # 20972222 Functional analyses of structure-based mutants have revealed the essential Arg residues participating in tRNA recognition by TYW5. These findings extend the repertoire of the tRNA modification enzyme into the Fe(II)/2-OG oxygenase superfamily.
UBE2A
(details)
# 12472 ubiquitin-conjugating enzyme E2A 7319 P49459 UBE2A_HUMAN UQ_con PF00179 8-145 Ube2a 102959 Q9Z255 UBE2A_MOUSE UBE2 Ubiquitin-conjugating enzymes E2 Histone modification write Histone ubiquitination 8797826 # histone H2A, H2BK120 H2BK120ub1 # 8797826 RAD6 (=UBE2) has been identified as the first ubiquitin-conjugating enzyme, able to mono- and polyubiquitinate histones 2A and 2B in vitro.
UBE2B
(details)
# 12473 ubiquitin-conjugating enzyme E2B 7320 P63146 UBE2B_HUMAN UQ_con PF00179 8-145 Ube2b 102944 P63147 UBE2B_MOUSE UBE2 Ubiquitin-conjugating enzymes E2 Histone modification write Histone ubiquitination 8797826 # histone H2A, H2BK121 H2BK120ub2 # 8797826 RAD6 (=UBE2) has been identified as the first ubiquitin-conjugating enzyme, able to mono- and polyubiquitinate histones 2A and 2B in vitro.
UBE2D1
(details)
# 12474 ubiquitin-conjugating enzyme E2D 1 7321 P51668 UB2D1_HUMAN UQ_con PF00179 5-142 Ube2d1 2384911 P61080 UB2D1_MOUSE UBE2 Ubiquitin-conjugating enzymes E2 Histone modification write Histone ubiquitination 22438555 # histone H2BK48 H2BK48ub # 22438555 Ubiquitination of TP53.
UBE2D3
(details)
# 12476 ubiquitin-conjugating enzyme E2D 3 7323 P61077 UB2D3_HUMAN UQ_con PF00179 5-142 Ube2d3 1913355 P61079 UB2D3_MOUSE UBE2 Ubiquitin-conjugating enzymes E2 Histone modification write Histone ubiquitination 21772249 # histone H2AK119 H2AK119ub # 21772249 Figure 7 in the reference (UBE2D3 =UbcH5c).
UBE2E1
(details)
# 12477 ubiquitin-conjugating enzyme E2E 1 7324 P51965 UB2E1_HUMAN UQ_con PF00179 51-188 Ube2e1 107411 P52482 UB2E1_MOUSE UBE2 Ubiquitin-conjugating enzymes E2 Histone modification write Histone ubiquitination 16307923 # histone H2BK120 H2BK120ub # 16307923 The human RNF20/40 complex functions as the E3 ligase and UbcH6 (=UBE2E1) as the ubiquitin E2-conjugating enzyme for histone H2B-K120 monoubiquitination.
UBE2H
(details)
# 12484 ubiquitin-conjugating enzyme E2H 7328 P62256 UBE2H_HUMAN UQ_con PF00179 9-145 Ube2h 104632 P62257 UBE2H_MOUSE UBE2 Ubiquitin-conjugating enzymes E2 Histone modification write Histone ubiquitination 8132613 # histone H2A, H2B H2Aub, H2Bub # 8132613 The capacity of the UBC8I UbcH2 enzymes to ubiquitinate histones in vitro raises makes it possible that these enzymes may be involved in this process in vivo.
UBE2N
(details)
# 12492 ubiquitin-conjugating enzyme E2N 7334 P61088 UBE2N_HUMAN UQ_con PF00179 7-144 Ube2n 1934835 P61089 UBE2N_MOUSE UBE2 Ubiquitin-conjugating enzymes E2 Histone modification write Histone ubiquitination 17709392 # histone H2AX H2AXub # 17709392 TIP60 regulates the ubiquitination of H2AX via the ubiquitin-conjugating enzyme UBC13 (=UBE2N), which is induced by DNA damage.
UBE2T
(details)
# 25009 ubiquitin-conjugating enzyme E2T (putative) 29089 Q9NPD8 UBE2T_HUMAN UQ_con PF00179 6-147 Ube2t 1914446 Q9CQ37 UBE2T_MOUSE UBE2 Ubiquitin-conjugating enzymes E2 Histone modification write Histone ubiquitination 17938197 # histone # # # 17938197 histone
UBN1
(details)
New 12506 ubinuclein 1 29855 Q9NPG3 UBN1_HUMAN HUN PF08729 115-169, UBN_AB PF14075 353-575 Ubn1 1891307 Q4G0F8 UBN1_MOUSE # # Histone modification write cofactor Histone methylation 19029251, 21807893 # histone # # # # Binds to proliferation-promoting genes and associates with histone methyltransferase activity that methylates lysine 9 of histone H3. Human CABIN1 is a functional member of the human HIRA/UBN1/ASF1a histone H3.3 chaperone complex.
UBR2
(details)
# 21289 ubiquitin protein ligase E3 component n-recognin 2 23304 Q8IWV8 UBR2_HUMAN ClpS PF02617 221-302, Pfam-B_10464 PB010464 668-730, Pfam-B_14814 PB014814 1413-1491, Pfam-B_15951 PB015951 1298-1365, Pfam-B_2665 PB002665 1020-1065, zf-UBR PF02207 97-167 Ubr2 1861099 Q6WKZ8 UBR2_MOUSE UBR Ubiquitin protein ligase E3 component n-recognins Histone modification write Histone ubiquitination # # histone H2A # # # Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. (Annotated by similarity.)
UBR5
(details)
# 16806 ubiquitin protein ligase E3 component n-recognin 5 51366 O95071 UBR5_HUMAN E3_UbLigase_EDD PF11547 178-230, HECT PF00632 2497-2799, PABP PF00658 2376-2449, Pfam-B_10556 PB010556 1381-1499, Pfam-B_14783 PB014783 601-649, Pfam-B_18259 PB018259 22-174, Pfam-B_5733 PB005733 1011-1149, Pfam-B_664 PB000664 651-1009, Pfam-B_8293 PB008293 1591-1748, Pfam-B_8878 PB008878 1249-1379, zf-UBR PF02207 1177-1248 Ubr5 1918040 Q80TP3 UBR5_MOUSE UBR Ubiquitin protein ligase E3 component n-recognins Chromatin remodelling, Histone modification write cofactor #, Histone ubiquitination 22884692 # histone H2A, H2AX H2Aub, H2AXub # 22884692 Excessive spreading of a DNA-damage-associated chromatin modification can occur. TRIP12 and UBR5 are two suppressors of such spreading.
UBR7
(details)
New 20344 ubiquitin protein ligase E3 component n-recognin 7 (putative) 55148 Q8N806 UBR7_HUMAN Pfam-B_38998 PB038998 361-423, zf-UBR PF02207 44-115 Ubr7 1913872 Q8BU04 UBR7_MOUSE UBR Ubiquitin protein ligase E3 component n-recognins DNA modification cofactor DNA methylation 21745816 # DNA # # # 21745816 Part of the DNMT1/USP7/UHRF1 complex which increases DNA methylation efficiency.
UCHL5
(details)
# 19678 ubiquitin carboxyl-terminal hydrolase L5 51377 Q9Y5K5 UCHL5_HUMAN Peptidase_C12 PF01088 7-211 Uchl5 1914848 Q9WUP7 UCHL5_MOUSE INO80 INO80 complex subunits Histone modification erase cofactor Histone ubiquitination 18922472 Ino80 histone # # # 18922472 Deubiquitination by Uch37 is activated by proteasomal binding, which enables Uch37 to process polyubiquitin chains. In the nucleus Uch37 is also associated with the human Ino80 chromatin-remodeling complex (hINO80). In hINO80, Uch37 is held in an inactive state; however, it can be activated by transient interaction of the Ino80 complex with the proteasome.
UHRF1
(details)
# 12556 ubiquitin-like with PHD and ring finger domains 1 29128 Q96T88 UHRF1_HUMAN DUF3590 PF12148 140-236, PHD PF00628 317-366, SAD_SRA PF02182 415-586, ubiquitin PF00240 6-76 Uhrf1 1338889 Q8VDF2 UHRF1_MOUSE RNF RING-type (C3HC4) zinc fingers Histone modification read, Histone modification write cofactor Histone ubiquitination, # 17967883 # histone, DNA H3K9me3, H3R2, H3, mCG H3ub # 17967883 ICBP90 =UHRF1and its murine homologue Np95 are enriched in pericentric heterochromatin of interphase nuclei, and this localization is dependent on H3K9 methylation.
UHRF2
(details)
# 12557 ubiquitin-like with PHD and ring finger domains 2, E3 ubiquitin protein ligase 115426 Q96PU4 UHRF2_HUMAN DUF3590 PF12148 177-261, PHD PF00628 346-395, SAD_SRA PF02182 444-616, ubiquitin PF00240 6-76 Uhrf2 1923718 Q7TMI3 UHRF2_MOUSE RNF, PHF RING-type (C3HC4) zinc fingers, Zinc fingers, PHD-type Histone modification read # 15361834 # histone, DNA H3K9me3, mCG # # 15361834 The SRA domain of the murine homologue of ICBP90=UHRF2, Np95, has histone H3-binding activity (Citterio et al., 2004). Methylated DNA twisted around histone H3 might be the primary target for Np95 and ICBP90 in vivo.
UIMC1
(details)
# 30298 ubiquitin interaction motif containing 1 51720 Q96RL1 UIMC1_HUMAN Pfam-B_20901 PB020901 471-524 Uimc1 103185 Q5U5Q9 UIMC1_MOUSE # # Histone modification read # 19015238 BRCA1-A histone H2AK63ub, H2AXK63ub, H2BK63ub # # 19015238 The interaction between RAP80 =UIMC1 and ubiquitinated histones H2A and H2B is increased following DNA damage.
USP11
(details)
# 12609 ubiquitin specific peptidase 11 8237 P51784 UBP11_HUMAN DUSP PF06337 99-185, Pfam-B_176820 PB176820 1-47, UCH PF00443 308-927, Ubiquitin_3 PF14836 198-285 Usp11 2384312 Q99K46 UBP11_MOUSE USP Ubiquitin-specific peptidases Histone modification erase cofactor Histone ubiquitination 20233726 # histone # # # 20233726 USP11 is a chromatin-associated protein and its catalytic activity is required for its genome maintenance activities. USP11 may be a DUB that functions in the DNA damage response to double-strand breaks.
USP12
(details)
New 20485 ubiquitin specific peptidase 12 219333 O75317 UBP12_HUMAN UCH PF00443 38-366 Usp12 1270128 Q9D9M2 UBP12_MOUSE USP Ubiquitin-specific peptidases Histone modification erase Histone ubiquitination 22033037 # histone H2Aub H2A # 22033037 Involved in H2A deubiquitination.
USP15
(details)
# 12613 ubiquitin specific peptidase 15 9958 Q9Y4E8 UBP15_HUMAN DUSP PF06337 27-119, UCH PF00443 288-930, USP7_C2 PF14533 459-614, Ubiquitin_3 PF14836 135-222 Usp15 101857 Q8R5H1 UBP15_MOUSE USP Ubiquitin-specific peptidases Histone modification erase Histone ubiquitination 24526689 # histone H2BK120ub H2BK120 # 24526689 Enhanced Usp15 binding to ubH2B facilitates deubiquitination of ubH2B in free histones but not in nucleosomes.
USP16
(details)
# 12614 ubiquitin specific peptidase 16 10600 Q9Y5T5 UBP16_HUMAN UCH PF00443 195-819, zf-UBP PF02148 48-128 Usp16 1921362 Q99LG0 UBP16_MOUSE USP Ubiquitin-specific peptidases Histone modification erase Histone ubiquitination 10077596 # histone H2Aub H2A # 10077596 Recombinant Ubp-M=USP16 is able to deubiquitinate histone H2A in vitro, and the phosphorylated form is also enzymatically active.
USP17L2
(details)
# 34434 ubiquitin specific peptidase 17-like family member 2 377630 Q6R6M4 U17L2_HUMAN HABP4_PAI-RBP1 PF04774 374-458, Pfam-B_24444 PB024444 1-39, UCH PF00443 79-372 Usp17le 3643640 Q7M764 U17PE_MOUSE # # Histone modification erase cofactor Histone ubiquitination 21239494 # histone # # # 21239494 SDS3 is a key component of the histone deacetylase (HDAC)-dependent Sin3A co-repressor complex, serving to maintain its HDAC activity. Both exogenous and endogenous functional interaction between deubiquitinating enzyme USP17 = USP17L2 and human SDS3 has been reported.
USP21
(details)
# 12620 ubiquitin specific peptidase 21 27005 Q9UK80 UBP21_HUMAN UCH PF00443 211-555 Usp21 1353665 Q9QZL6 UBP21_MOUSE USP Ubiquitin-specific peptidases Histone modification erase Histone ubiquitination # # histone H2Aub H2A # # Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination. (Annotated by similarity.)
USP22
(details)
# 12621 ubiquitin specific peptidase 22 23326 Q9UPT9 UBP22_HUMAN UCH PF00443 175-517, zf-UBP PF02148 63-124 Usp22 2144157 Q5DU02 UBP22_MOUSE USP Ubiquitin-specific peptidases Histone modification write cofactor Histone ubiquitination 18469533 SAGA histone H2Aub, H2Bub H2A, H2B # 18469533 USP22 deubiquitylates histone H2A in addition to H2B. This supports a model in which the H2A ubiquitin hydrolase USP22 is coordinately expressed with Polycomb H2A ubiquitin ligases in order that the transcription of certain critical transforming genes be maintained in the face of the global repression mediated by Polycomb.
USP3
(details)
# 12626 ubiquitin specific peptidase 3 9960 Q9Y6I4 UBP3_HUMAN UCH PF00443 158-508, zf-UBP PF02148 29-107 Usp3 2152450 Q91W36 UBP3_MOUSE USP Ubiquitin-specific peptidases Histone modification write Histone ubiquitination 17980597 # histone H2Aub, H2Bub H2A, H2B # 17980597 The ubiquitin-specific protease 3 USP3 is a deubiquitinating enzyme for uH2A and uH2B. USP3 dynamically associates with chromatin and deubiquitinates H2A/H2B in vivo.
USP36
(details)
# 20062 ubiquitin specific peptidase 36 57602 Q9P275 UBP36_HUMAN Pfam-B_17191 PB017191 1088-1118, Pfam-B_20267 PB020267 1065-1087, UCH PF00443 121-420 Usp36 1919594 B1AQJ2 UBP36_MOUSE USP Ubiquitin-specific peptidases Histone modification write cofactor Histone ubiquitination 22622177 # histone H2Bub H2B # 22622177 Deubiquitination of histone H2B at the promoters of genes critical for cellular differentiation, thereby preventing histone H3 'Lys-4' trimethylation (H3K4).
USP44
(details)
# 20064 ubiquitin specific peptidase 44 84101 Q9H0E7 UBP44_HUMAN UCH PF00443 272-675, zf-UBP PF02148 29-91 Usp44 3045318 Q8C2S0 UBP44_MOUSE USP Ubiquitin-specific peptidases Histone modification erase Histone ubiquitination 22681888 # histone H2Bub1 H2B # 22681888 USP44 is most likely an H2Bub1-specific DUB, whose downregulation during ESC differentiation contributes to increased H2Bub1 levels.
USP46
(details)
New 20075 ubiquitin specific peptidase 46 64854 P62068 UBP46_HUMAN UCH PF00443 34-362 Usp46 1916977 P62069 UBP46_MOUSE USP Ubiquitin-specific peptidases Histone modification erase Histone ubiquitination 22033037 # histone H2Aub H2A # 22033037 Involved in H2A deubiquitination.
USP49
(details)
# 20078 ubiquitin specific peptidase 49 25862 Q70CQ1 UBP49_HUMAN UCH PF00443 252-654, zf-UBP PF02148 20-88 Usp49 2685391 Q6P9L4 UBP49_MOUSE USP Ubiquitin-specific peptidases Histone modification erase Histone ubiquitination 23824326 # histone H2Bub H2B # 23824326 Ubiquitin-specific peptidase 49 (USP49) is a histone H2B-specific deubiquitinase and shows that H2B deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons.
USP7
(details)
New 12630 ubiquitin specific peptidase 7 (herpes virus-associated) 7874 Q93009 UBP7_HUMAN MATH PF00917 56-197, Pfam-B_12182 PB012182 591-618, Pfam-B_45828 PB045828 1-39, UCH PF00443 213-518, USP7_C2 PF14533 874-1088, USP7_ICP0_bdg PF12436 619-865 Usp7 2182061 Q6A4J8 UBP7_MOUSE USP Ubiquitin-specific peptidases Histone modification erase, DNA modification cofactor Histone ubiquitination, DNA methylation 15749019 BCOR histone, DNA H2Bub H2B # 15749019 GMP synthetase stimulates histone H2B deubiquitylation by the epigenetic silencer USP7
UTY
(details)
# 12638 ubiquitously transcribed tetratricopeptide repeat containing, Y-linked 7404 O14607 UTY_HUMAN JmjC PF02373 1080-1188, Pfam-B_2066 PB002066 1-49, Pfam-B_604 PB000604 580-716, Pfam-B_972 PB000972 718-1056, TPR_1 PF00515 127-160 315-348 349-377, TPR_17 PF13431 269-301, TPR_8 PF13181 202-233 Uty 894810 P79457 UTY_MOUSE TTC Tetratricopeptide (TTC) repeat domain containing Histone modification erase Histone ubiquitination 24798337 # histone H3K27me # # 24798337 The Jumonji C lysine demethylases (KDMs) are 2-oxoglutarate- and Fe(II)-dependent oxygenases. KDM6A (UTX) and KDM6B (JMJD3) are KDM6 subfamily members that catalyze demethylation of Nϵ-methylated histone 3 lysine 27 (H3K27), a mark important for transcriptional repression. Despite reports stating that UTY (KDM6C) is inactive as a KDM, we demonstrate by biochemical studies, employing MS and NMR, that UTY (KDM6C) is an active KDM. Crystallographic analyses reveal that the UTY(KDM6C) active site is highly conserved with those of KDM6B and KDM6A.
VDR
(details)
# 12679 vitamin D (1,25- dihydroxyvitamin D3) receptor 7421 P11473 VDR_HUMAN Hormone_recep PF00104 209-418, zf-C4 PF00105 22-91 Vdr 103076 P48281 VDR_MOUSE NR Nuclear hormone receptors Chromatin remodelling cofactor, TF #, # 16252006 # histone H2BK12ac, H3K14ac, H4K16ac # # 16252006 WINAC associates with chromatin through a physical interaction between the WSTF bromodomain and acetylated histones, which appears to be indispensable for VDR/promoter association for ligand-induced transrepression of 1α(OH)ase gene expression.
VPS72
(details)
# 11644 vacuolar protein sorting 72 homolog (S. cerevisiae) 6944 Q15906 VPS72_HUMAN YL1 PF05764 4-218, YL1_C PF08265 290-319 Vps72 1202305 Q62481 VPS72_MOUSE # # Histone modification write cofactor Histone acetylation 14966270 NuA4, NuA4-related complex chromatin # # # 14966270 The YL1 =VPS72 protein is a subunit of the TRRAP/TIP60 HAT complex. The YL1 protein is also present in cells as a subunit of the previously uncharacterized mammalian SRCAP complex, which bears a striking similarity to the S. cerevisiae SWR1 chromatin remodeling complex.
VRK1
(details)
New 12718 vaccinia related kinase 1 7443 Q99986 VRK1_HUMAN Pkinase PF00069 37-325 Vrk1 1261847 Q80X41 VRK1_MOUSE # # Histone modification write Histone phosphorylation 22194607 # histone H3S10, H3T3 H3S10ph, H3T3ph # # Phosphorylates histones H3-S10, H3-T3.
WAC
(details)
New 17327 WW domain containing adaptor with coiled-coil 51322 Q9BTA9 WAC_HUMAN WW PF00397 131-160 Wac 2387357 Q924H7 WAC_MOUSE # # Histone modification write cofactor Histone ubiquitination 21329877 # histone # # # # Regulates H2B ubiquitinations.
WDR5
(details)
# 12757 WD repeat domain 5 11091 P61964 WDR5_HUMAN WD40 PF00400 36-73 77-115 119-157 161-199 203-242 246-287 291-331 Wdr5 2155884 P61965 WDR5_MOUSE WDR WD repeat domain containing Histone modification read # 16946699 ATAC, NSL, RING2-L3MBTL2, COMPASS, Menin-associated_HMT, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7, COMPASS-like MLL3,4 histone H3K4, H3K4me1, H3K4me2, H3K4me3 # # 16946699 The WD40 domain of WDR5 represents a new class of histone methyl-lysine recognition domains that is important for recruiting H3K4 methyltransferases to K4-dimethylated histone H3 tail as well as for global and gene-specific K4 trimethylation. Here is given the crystal structures of full-length WDR5, WDR5Delta23 and its complexes with unmodified, mono-, di- and trimethylated histone H3K4 peptides.
WDR77
(details)
New 29652 WD repeat domain 77 79084 Q9BQA1 MEP50_HUMAN Pfam-B_26289 PB026289 1-49, WD40 PF00400 117-153 157-196 245-284 Wdr77 1917715 Q99J09 MEP50_MOUSE WDR WD repeat domain containing Histone modification write Histone methylation 22009756 methylosome histone H2A, H4 H2Ame, H4me # # Methylates histones H2A and H4 in Xenopus.
WDR82
(details)
# 28826 WD repeat domain 82 80335 Q6UXN9 WDR82_HUMAN WD40 PF00400 12-49 97-135 245-267 273-304 Wdr82 1924555 Q8BFQ4 WDR82_MOUSE WDR WD repeat domain containing Histone modification write cofactor Histone methylation 17355966 COMPASS histone # # # 17355966 A mammalian Set1A complex analogous to the yeast Set1/COMPASS histone H3-Lys4 methyltransferase complex has previously been identified. WDR82 is a regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes.
WHSC1
(details)
# 12766 Wolf-Hirschhorn syndrome candidate 1 7468 O96028 NSD2_HUMAN HMG_box PF00505 455-508, PHD PF00628 833-875, PWWP PF00855 220-332 878-968, SET PF00856 1074-1180 Whsc1 1276574 Q8BVE8 NSD2_MOUSE PHF Zinc fingers, PHD-type Histone modification write Histone methylation 18172012 # histone H3K27 H3K27me # 18172012 Multiple-myeloma-related WHSC1/MMSET isoform RE-IIBP is a histone methyltransferase with transcriptional repression activity.
WHSC1L1
(details)
# 12767 Wolf-Hirschhorn syndrome candidate 1-like 1 54904 Q9BZ95 NSD3_HUMAN PWWP PF00855 268-378 958-1047, Pfam-B_7848 PB007848 619-671, SET PF00856 1156-1262 Whsc1l1 2142581 Q6P2L6 NSD3_MOUSE # # Chromatin remodelling cofactor, TF #, # 16682010 # histone H3K4, H3K27 # # 16682010 WHISTLE =WHSC1L1 di-methylates H3K4 and di-, and tri-methylates H3K27 of histones.
WSB2
(details)
# 19222 WD repeat and SOCS box containing 2 55884 Q9NYS7 WSB2_HUMAN Pfam-B_17306 PB017306 1-52, SOCS_box PF07525 366-402, WD40 PF00400 83-139 143-182 187-225 229-267 288-321 337-361 Wsb2 2144041 O54929 WSB2_MOUSE WDR WD repeat domain containing Histone modification write Histone ubiquitination 21070969 # histone # # # # May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, including histones. (Annotated by similarity).
YAF2
(details)
# 17363 YY1 associated factor 2 10138 Q8IY57 YAF2_HUMAN zf-RanBP PF00641 20-46 Yaf2 1914307 Q99LW6 YAF2_MOUSE # # Chromatin remodelling cofactor # 11593398 BCOR, RING2-L3MBTL2, RING2-FBRS chromatin # # # 11593398 Both Myc and Yaf2 could play a role in chromatin remodeling complexes.
YEATS2
(details)
# 25489 YEATS domain containing 2 55689 Q9ULM3 YETS2_HUMAN Pfam-B_10841 PB010841 976-1072, Pfam-B_13347 PB013347 678-756, Pfam-B_19332 PB019332 758-854, YEATS PF03366 231-314 Yeats2 2447762 Q3TUF7 YETS2_MOUSE # # Histone chaperone # 18838386 ATAC histone # # # 18838386 A YEATS2-NC2beta histone fold module that interacts with the TATA-binding protein (TBP) and negatively regulates transcription when recruited to a promoter. The p38 kinase-interacting protein (p38IP/FAM48A) is a novel component of STAGA with distant similarity to yeast Spt20.
YEATS4
(details)
# 24859 YEATS domain containing 4 8089 O95619 YETS4_HUMAN YEATS PF03366 44-126 Yeats4 1927224 Q9CR11 YETS4_MOUSE # # Histone modification write cofactor Histone acetylation 14966270 NuA4, NuA4-related complex, SRCAP histone # # # 14966270 The essential GAS41 =YEATS4 protein is a member of the AF9/ENL-related (YEATS) family, and associated to transcription/chromatin-modifying complexes, including yeast NuA4, NuA3, Sas2, SWI/SNF, TFIID/mediator/TFIIF, and human SWI/SNF complexes.
YWHAB
(details)
# 12849 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta 7529 P31946 1433B_HUMAN 14-3-3 PF00244 5-238 Ywhab 1891917 Q9CQV8 1433B_MOUSE # # Histone modification erase cofactor Histone acetylation 10869435 # histone # # # 10869435 Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent (=YWHAB) cellular localization.
YWHAE
(details)
# 12851 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, epsilon 7531 P62258 1433E_HUMAN 14-3-3 PF00244 4-239 Ywhae 894689 P62259 1433E_MOUSE # # Histone modification erase cofactor Histone acetylation 10869435 # histone # # # 10869435 Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent (=YWHAE) cellular localization.
YWHAZ
(details)
# 12855 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, zeta 7534 P63104 1433Z_HUMAN 14-3-3 PF00244 3-236 Ywhaz 109484 P63101 1433Z_MOUSE # # Histone modification read # 16246723 # histone H3 # # 16246723 14-3-3 =YWHAZ isoforms are proteins that bind modified H3 tail peptide tails in a strictly phosphorylation-dependent manner.
YY1
(details)
# 12856 YY1 transcription factor 7528 P25490 TYY1_HUMAN zf-C2H2 PF00096 383-407, zf-H2C2_2 PF13465 339-365 Yy1 99150 Q00899 TYY1_MOUSE INO80, ZNF INO80 complex subunits, Zinc fingers, C2H2-type Chromatin remodelling cofactor, TF #, TF repressor 11445535.1895069 Ino80 DNA DNA motif # # 11445535.1895069 YY1 is complex comprising components of the evolutionarily conserved INO80 chromatin-remodeling complex.
ZBTB16
(details)
New 12930 zinc finger and BTB domain containing 16 7704 Q05516 ZBT16_HUMAN BTB PF00651 24-126, zf-C2H2 PF00096 491-512 630-652, zf-C2H2_4 PF13894 432-455, zf-C2H2_6 PF13912 460-486, zf-H2C2_2 PF13465 532-556 560-584 588-612 Zbtb16 103222 # # ZBTB, ZNF, BTBD #, Zinc fingers, C2H2-type, BTB/POZ domain containing Histone modification erase cofactor Histone acetylation 9627120, 15467736 # histone # # # # Recruites SMRT-mSin3-HDAC co-repressor complex. The repressive domains of PLZF function by recruiting N-CoR/Sin3A co-repressor complexes which in turn recruit histone deacetylases (HDACs).
ZBTB33
(details)
# 16682 zinc finger and BTB domain containing 33 10009 Q86T24 KAISO_HUMAN BTB PF00651 22-118, zf-H2C2_2 PF13465 508-532 537-561 Zbtb33 1927290 Q8BN78 KAISO_MOUSE ZBTB, BTBD, ZNF BTB/POZ domain containing, Zinc fingers, C2H2-type Histone modification write cofactor, Histone modification erase cofactor, TF Histone acetylation, Histone methylation, TF repressor 14527417 # DNA CG, mCG, DNA motif # # 14527417 Kaiso, a methyl CpG binding protein belonging to the BTB/POZ family of transcription factors, is a component of the human N-CoR complex. In vitro, the Kaiso/N-CoR complex binds specific CpG-rich sequences in a methylation-dependent manner. In vivo, Kaiso targets the N-CoR complex to the MTA2 gene promoter in a methylation-dependent manner. This repression also requires a functional N-CoR deacetylase complex, which brings about histone hypoacetylation and methylation of H3 lysine 9 to the MTA2 locus.
ZBTB7C
(details)
# 31700 zinc finger and BTB domain containing 7C 201501 A1YPR0 ZBT7C_HUMAN BTB PF00651 24-130, zf-H2C2_2 PF13465 379-403 406-431 434-459 Zbtb7c 2443302 Q8VCZ7 ZBT7C_MOUSE ZBTB, ZNF, BTBD Zinc fingers, C2H2-type, BTB/POZ domain containing Histone modification cofactor # 21804610 # histone # # # 21804610 Kr-pok =ZBTB7C competes with MIZ-1 in binding to these elements and represses transcription by inhibiting MIZ-1/p300 recruitment, which decreases the acetylation of histones H3 and H4.
ZCWPW1
(details)
# 23486 zinc finger, CW type with PWWP domain 1 55063 Q9H0M4 ZCPW1_HUMAN PWWP PF00855 315-411, Pfam-B_36867 PB036867 512-557, zf-CW PF07496 254-303 Zcwpw1 2685899 Q6IR42 ZCPW1_MOUSE # # Histone modification read # 21423274 # histone H3K4me # # 21423274 Table 1 in the reference.
ZFP57
(details)
# 18791 ZFP57 zinc finger protein 346171 Q9NU63 ZFP57_HUMAN KRAB PF01352 16-56, zf-C2H2 PF00096 91-113 175-197, zf-C2H2_4 PF13894 300-323 329-351 356-377, zf-H2C2_2 PF13465 133-156 Zfp57 99204 Q8C6P8 ZFP57_MOUSE # # TF TF repressor # # DNA mC, DNA motif # # # Acts by controlling DNA methylation during the earliest multicellular stages of development at multiple imprinting control regions. (UniProt)
ZGPAT
(details)
New 15948 zinc finger, CCCH-type with G patch domain 84619 Q8N5A5 ZGPAT_HUMAN G-patch PF01585 333-376 Zgpat 2449939 Q8VDM1 ZGPAT_MOUSE ZC3H, GPATCH Zinc fingers, CCCH-type domain containing, "G patch domain containing" TF TF repressor 22498752 # DNA DNA motif # # # Recruits the chromatin multiprotein complex NuRD to target promoters.
ZHX1
(details)
# 12871 zinc fingers and homeoboxes 1 11244 Q9UKY1 ZHX1_HUMAN Homeobox PF00046 297-339 467-521 573-623 665-717, Homez PF11569 776-827, Pfam-B_22595 PB022595 1-37 Zhx1 109271 P70121 ZHX1_MOUSE ZNF, ZFHX Zinc fingers, C2H2-type, Homeoboxes / ZF class Chromatin remodelling, Histone modification write cofactor, Histone modification write cofactor #, Histone acetylation, Histone methylation 17303076 # histone # # # 17303076 Presence of a PWWP domain is required for interaction of ZHX1. This domain may function as a site of protein–protein interaction and influence chromatin remodeling, and thereby facilitate the fine tuning of transcriptional processes.
ZMYM2
(details)
# 12989 zinc finger, MYM-type 2 7750 Q9UBW7 ZMYM2_HUMAN DUF3504 PF12012 1190-1361, Pfam-B_10252 PB010252 941-1179, Pfam-B_2297 PB002297 1-159, zf-FCS PF06467 323-363 365-409 417-456 459-502 528-570 576-616 631-671 719-758 760-799 Zmym2 1923257 Q9CU65 ZMYM2_MOUSE ZMYM Zinc fingers, MYM type Histone modification erase cofactor, TF Histone acetylation, # 12493763 BHC, LSD-CoREST DNA DNA motif # # 12493763 A family of HDAC1,2-associated complexes includes proteins with a putative role in DNA binding such as ZNF261/XFIM (=ZMYM3), ZNF198/FIM (=ZMYM2), and ZNF217.
ZMYM3
(details)
# 13054 zinc finger, MYM-type 3 9203 Q14202 ZMYM3_HUMAN DUF3504 PF12012 1183-1354, Pfam-B_2297 PB002297 1-189, Pfam-B_24258 PB024258 191-229, Pfam-B_5192 PB005192 1100-1142, zf-FCS PF06467 304-343 345-389 402-440 443-488 490-532 538-578 583-623 626-664 671-710 712-751 Zmym3 1927231 Q9JLM4 ZMYM3_MOUSE ZMYM Zinc fingers, MYM type Histone modification erase cofactor Histone acetylation 12493763 BHC DNA # # # 12493763 A family of HDAC1,2-associated complexes includes proteins with a putative role in DNA binding such as ZNF261/XFIM (=ZMYM3), ZNF198/FIM (=ZMYM2), and ZNF217.
ZMYND11
(details)
New 16966 zinc finger, MYND-type containing 11 10771 Q15326 ZMY11_HUMAN Bromodomain PF00439 122-203, PWWP PF00855 238-313, Pfam-B_7883 PB007883 342-530, Pfam-B_8532 PB008532 532-560 Zmynd11 1913755 Q8R5C8 ZMY11_MOUSE ZMYND Zinc fingers, MYND-type Histone modification read Histone methylation 22498752 # histone H3.3K36me3 # # # ZMYND11 recognizes and binds histone H3.3 trimethylated at Lys-36 (H3.3K36me3), according to UniProt.
ZMYND8
(details)
New 9397 zinc finger, MYND-type containing 8 23613 Q9ULU4 PKCB1_HUMAN Bromodomain PF00439 157-240, DUF3544 PF12064 412-622, PHD PF00628 90-133, PWWP PF00855 275-349, zf-MYND PF01753 1028-1062 Zmynd8 1918025 # # ZMYND, PHF Zinc fingers, MYND-type, "Zinc fingers, PHD-type" Histone modification erase cofactor Histone acetylation 25123934 # histone # # # # ZMYND8 is part of the NuRD complex.
ZNF217
(details)
# 13009 zinc finger protein 217 7764 O75362 ZN217_HUMAN Pfam-B_30131 PB030131 913-979, zf-C2H2 PF00096 128-150 156-178, zf-C2H2_4 PF13894 65-88 216-239 375-398, zf-H2C2_2 PF13465 485-510 # # # # ZNF Zinc fingers, C2H2-type Histone modification erase cofactor, TF Histone acetylation, TF repressor 12493763 BHC, LSD-CoREST DNA # # # 12493763 A family of HDAC1,2-associated complexes includes proteins with a putative role in DNA binding such as ZNF261/XFIM (=ZMYM3), ZNF198/FIM (=ZMYM2), and ZNF217.
ZNF516
(details)
New 28990 zinc finger protein 516 9658 Q92618 ZN516_HUMAN zf-C2H2 PF00096 248-270 276-298 1098-1120, zf-C2H2_4 PF13894 174-197, zf-H2C2_2 PF13465 48-73 Zfp516 2443957 Q7TSH3 ZN516_MOUSE ZNF Zinc fingers, C2H2-type Histone modification erase cofactor, TF Histone acetylation, TF repressor 23752268 LSD-CoREST histone, DNA # # # 23752268 Part of the HDAC interactome, TF annotation from Uniprot.
ZNF532
(details)
New 30940 zinc finger protein 532 55205 Q9HCE3 ZN532_HUMAN Pfam-B_17557 PB017557 601-719, Pfam-B_19362 PB019362 831-959, zf-C2H2 PF00096 1265-1286 Zfp532 3036282 Q6NXK2 ZN532_MOUSE ZNF Zinc fingers, C2H2-type Histone modification erase cofactor Histone acetylation 25123934 # histone # # # # A member of NuRD complex.
ZNF541
(details)
New 25294 zinc finger protein 541 84215 Q9H0D2 ZN541_HUMAN ELM2 PF01448 1074-1131, Pfam-B_17081 PB017081 567-665, Pfam-B_27795 PB027795 956-1034, Pfam-B_3685 PB003685 772-954, Pfam-B_40457 PB040457 1171-1225, zf-C2H2 PF00096 168-190, zf-C2H2_4 PF13894 140-163 196-221 Zfp541 3647699 Q0GGX2 ZN541_MOUSE ZNF Zinc fingers, C2H2-type Chromatin remodelling # 18849567 # chromatin # # # # Forms a complex with chromatin remodeling activity during spermatogenesis. UniProt: Component of some chromatin remodeling multiprotein complex that plays a role during spermatogenesis (by similarity).
ZNF592
(details)
New 28986 zinc finger protein 592 9640 Q92610 ZN592_HUMAN Pfam-B_21220 PB021220 499-547, Pfam-B_27046 PB027046 771-913, Pfam-B_379 PB000379 1-97, zf-C2H2 PF00096 1013-1036 1043-1069 Zfp592 2443541 Q8BHZ4 ZN592_MOUSE ZNF Zinc fingers, C2H2-type Histone modification erase cofactor Histone acetylation 25123934 # histone # # # # A member of NuRD complex.
ZNF687
(details)
New 29277 zinc finger protein 687 57592 Q8N1G0 ZN687_HUMAN zf-C2H2 PF00096 1200-1222, zf-C2H2_4 PF13894 858-881 963-986 993-1016 Zfp687 1925516 Q9D2D7 ZN687_MOUSE # # Histone modification erase cofactor Histone acetylation 25123934 # histone # # # # A member of NuRD complex.
ZNF711
(details)
# 13128 zinc finger protein 711 7552 Q9Y462 ZN711_HUMAN Pfam-B_16491 PB016491 1-63, Zfx_Zfy_act PF04704 64-368, zf-C2H2 PF00096 383-405, zf-C2H2_4 PF13894 562-583 733-756, zf-H2C2_2 PF13465 490-516 519-543 604-630 690-715, zf-H2C2_5 PF13909 414-437 647-671 Zfp711 3045342 A2ANX9 ZN711_MOUSE ZNF Zinc fingers, C2H2-type Histone modification erase cofactor Histone acetylation 20346720 # histone # # # 20346720 The PHD domain of PHF8 binds to H3K4me3 and colocalizes with H3K4me3 at transcription initiation sites. Furthermore, PHF8 interacts with another XMLR protein, ZNF711, which binds to a subset of PHF8 target genes, including the XLMR gene JARID1C.
ZNHIT1
(details)
# 21688 zinc finger, HIT-type containing 1 10467 O43257 ZNHI1_HUMAN zf-HIT PF04438 113-142 Znhit1 1917353 Q8R331 ZNHI1_MOUSE ZNHIT Zinc fingers, HIT-type Chromatin remodelling cofactor, Histone modification erase cofactor #, Histone acetylation 15647280 SRCAP histone # # # 15647280 YL1 protein is also present in cells as a subunit of the previously uncharacterized mammalian SRCAP complex, which bears a striking similarity to the recently described S. cerevisiae SWR1 chromatin remodeling complex and is composed of the SNF2-related SRCAP helicase, ARP6, ZnF/HIT1.
ZRANB3
(details)
# 25249 zinc finger, RAN-binding domain containing 3 84083 Q5FWF4 ZRAB3_HUMAN HNH PF01844 1009-1051, Helicase_C PF00271 357-435, Pfam-B_14328 PB014328 729-854, SNF2_N PF00176 40-326, zf-RanBP PF00641 621-650 Zranb3 1918362 Q6NZP1 ZRAB3_MOUSE ZRANB Zinc fingers, RAN-binding domain containing Chromatin remodelling, Histone modification read cofactor #, Histone methylation 22705370 # histone # # # 22705370 All four proteins (HARP, HARP-like domain (HPL), SMARCA1, RAD54L) belong to the SNF2 =ZRANB3 family, whose members participate in a variety of processes including chromatin remodeling, transcription, DNA repair, and recombination.
ZZZ3
(details)
# 24523 zinc finger, ZZ-type containing 3 26009 Q8IYH5 ZZZ3_HUMAN Myb_DNA-binding PF00249 652-703, Pfam-B_19065 PB019065 361-439, Pfam-B_22505 PB022505 211-359, ZZ PF00569 817-865 Zzz3 1920453 Q6KAQ7 ZZZ3_MOUSE ZZZ Zinc fingers, ZZ-type Histone modification read # 19103755 ATAC histone # # # 19103755 The SANT domain of c-Myb has been shown to bind histone H3 tails and position them for acetylation (35). Moreover, the SANT domains in ADA2a and ZZZ3/ATAC1 might enable the complex to associate with nucleosome tails in order to potentiate the catalytic activities of GCN5 and ATAC2, similar to what has been shown for the SANT domains in yeast Ada2 and Swi3.