EP300
entrez
2033
canonical
uniprot
Q09472
canonical
ensembl
ENSG00000100393
resolver
ensp
ENSP00000263253
resolver
ensp
ENSP00000501078
resolver
ensp
ENSP00000520505
resolver
enst
ENST00000263253
resolver
enst
ENST00000674155
resolver
enst
ENST00000715703
resolver
genesymbol
EP300
resolver
genesymbol_syn
P300
resolver
hgnc
HGNC:3373
resolver
uniprot
A0A669KB12
resolver
uniprot
B1AKC2
resolver
uniprot
Q7Z6C1
resolver
uniprot_entry
A0A669KB12_HUMAN
resolver
uniprot_entry
EP300_HUMAN
resolver
uniprot_entry
Q7Z6C1_HUMAN
resolver
uniprot_sec
B1AKC2
resolver
amino_acid_sequence
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMPNMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQSTLDIH
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in EP300 may play a role in epithelial cancer.; DISEASE: Note=Chromosomal aberrations involving EP300 may be a cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13) with KAT6A.; DISEASE: Rubinstein-Taybi syndrome 2 (RSTS2) [MIM:613684]: A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, intellectual disability and a propensity for development of malignancies. Some individuals with RSTS2 have less severe mental impairment, more severe microcephaly, and a greater degree of changes in facial bone structure than RSTS1 patients. {ECO:0000269|PubMed:15706485}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Menke-Hennekam syndrome 2 (MKHK2) [MIM:618333]: A form of Menke-Hennekam syndrome, a congenital autosomal dominant disease characterized by developmental delay, growth retardation, and craniofacial dysmorphism. Patients have intellectual disability of variable severity, speech delay, autistic behavior, short stature and microcephaly. Main facial characteristics include short palpebral fissures, telecanthi, depressed nasal ridge, short nose, anteverted nares, short columella and long philtrum. {ECO:0000269|PubMed:29460469}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
function
FUNCTION: Functions as a histone acetyltransferase and regulates transcription via chromatin remodeling (PubMed:23415232, PubMed:23934153, PubMed:40240600, PubMed:8945521). Acetylates all four core histones in nucleosomes (PubMed:23415232, PubMed:23934153, PubMed:8945521). Histone acetylation gives an epigenetic tag for transcriptional activation (PubMed:23415232, PubMed:23934153, PubMed:8945521). Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (PubMed:23415232). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (PubMed:21131905, PubMed:23911289). Also able to acetylate histone lysine residues that are already monomethylated on the same side chain to form N6-acetyl-N6-methyllysine (Kacme), an epigenetic mark of active chromatin associated with increased transcriptional initiation (PubMed:37731000). Catalyzes formation of histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively) (PubMed:37731000). In response to DNA damage, catalyzes acetylation of histone H1 at 'Lys-75' (H1K75ac) following histone H1 deamidation by CTPS1, increasing chromatin accessibility to facilitate the recruitment of DNA repair proteins (PubMed:40240600). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRDM16, PRMT1, SIRT2, STAT3, ZNF76 or GLUL (PubMed:12929931, PubMed:15653507, PubMed:16285960, PubMed:16337145, PubMed:16762839, PubMed:18722353, PubMed:18782771, PubMed:26990986). Acetylates 'Lys-131' of ALX1 and acts as its coactivator (PubMed:12929931). Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of p53/TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (PubMed:18722353). Following DNA damage, forms a stress-responsive p53/TP53 coactivator complex with JMY which mediates p53/TP53 acetylation, thereby increasing p53/TP53-dependent transcription and apoptosis (PubMed:11511361, PubMed:15448695). Promotes chromatin acetylation in heat shock responsive HSP genes during the heat shock response (HSR), thereby stimulating HSR transcription (PubMed:18451878). Acetylates HDAC1 leading to its inactivation and modulation of transcription (PubMed:16762839). Acetylates 'Lys-247' of EGR2 (By similarity). Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2 (PubMed:12586840). Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement (PubMed:14752053). Can also mediate transcriptional repression. Acetylates FOXO1 and enhances its transcriptional activity (PubMed:15890677). Acetylates STAT3 at different sites, promoting both STAT3 dimerization and activation and recruitment to chromatin (PubMed:15653507, PubMed:16285960, PubMed:18782771). Acetylates BCL6 which disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity (PubMed:12402037). Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter (PubMed:14645221). Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:16617102). Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). Acetylates MEF2D (PubMed:21030595). Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degradation, this mechanism may be involved in CD4/CD8 lineage differentiation (PubMed:20810990). Acetylates GABPB1, impairing GABPB1 heterotetramerization and activity (By similarity). Acetylates PCK1 and promotes PCK1 anaplerotic activity (PubMed:30193097). Acetylates RXRA and RXRG (PubMed:17761950). Acetylates isoform M2 of PKM (PKM2), promoting its homodimerization and conversion into a protein kinase (PubMed:24120661). Acetylates RPTOR in response to leucine, leading to activation of the mTORC1 complex (PubMed:30197302, PubMed:32561715). Acetylates RICTOR, leading to activation of the mTORC2 complex (PubMed:22084251). Mediates cAMP-gene regulation by binding specifically to phosphorylated CREBBP (PubMed:8917528). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA), 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), lactoyl-CoA, propanoyl-CoA (propionyl-CoA) or isonicotinyl-CoA, and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation, lactylation, propionylation or isonicotinylation, respectively (PubMed:17267393, PubMed:25818647, PubMed:29775581, PubMed:31645732, PubMed:34545082). Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:25818647). Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (2E)-butenoyl-CoA (crotonyl-CoA) concentration is low (PubMed:25818647). Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:17267393). Catalyzes histone lactylation in macrophages by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription (PubMed:31645732). Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes (PubMed:29775581). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493). {ECO:0000250|UniProtKB:B2RWS6, ECO:0000269|PubMed:10733570, ECO:0000269|PubMed:11430825, ECO:0000269|PubMed:11511361, ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:12586840, ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:14752053, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:15653507, ECO:0000269|PubMed:15890677, ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:16337145, ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:16762839, ECO:0000269|PubMed:17267393, ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:18451878, ECO:0000269|PubMed:18722353, ECO:0000269|PubMed:18782771, ECO:0000269|PubMed:18995842, ECO:0000269|PubMed:20810990, ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:21131905, ECO:0000269|PubMed:22084251, ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:25818647, ECO:0000269|PubMed:26990986, ECO:0000269|PubMed:29775581, ECO:0000269|PubMed:30193097, ECO:0000269|PubMed:30197302, ECO:0000269|PubMed:31645732, ECO:0000269|PubMed:32561715, ECO:0000269|PubMed:34545082, ECO:0000269|PubMed:37731000, ECO:0000269|PubMed:40240600, ECO:0000269|PubMed:8917528, ECO:0000269|PubMed:8945521, ECO:0000305|PubMed:20955178}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. {ECO:0000269|PubMed:10545121, ECO:0000269|PubMed:11080476}.
uniprot
proteins
mass_dalton
264161
uniprot
proteins
mutagenesis
MUTAGEN 89; /note="S->A: Abolishes AMPK-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:11518699"; MUTAGEN 89; /note="S->D: Phosphomimetic mutant that leads to descreased interaction with nuclear receptors."; /evidence="ECO:0000269|PubMed:11518699"; MUTAGEN 344; /note="L->A: Inhibits interaction with HIF1A and transcription activation; when associated with A-345."; /evidence="ECO:0000269|PubMed:12778114"; MUTAGEN 345; /note="L->A: Inhibits interaction with HIF1A and transcription activation; when associated with A-344."; /evidence="ECO:0000269|PubMed:12778114"; MUTAGEN 371..376; /note="TMKNVL->NAAIRS: Inhibits interaction with HIF1A. Reduces interaction with CITED2."; /evidence="ECO:0000269|PubMed:9887100"; MUTAGEN 413..418; /note="VCLPLK->NAAIRS: Inhibits interaction with HIF1A. Does not inhibit interaction with CITED2."; /evidence="ECO:0000269|PubMed:9887100"; MUTAGEN 1020; /note="K->A: Abolishes sumoylation and transcriptional repression when associated with A-1024."; /evidence="ECO:0000269|PubMed:12718889, ECO:0000269|PubMed:15632193"; MUTAGEN 1020; /note="K->R: Abolishes sumoylation and transcriptional repression; when associated with R-1024."; /evidence="ECO:0000269|PubMed:12718889, ECO:0000269|PubMed:15632193"; MUTAGEN 1024; /note="K->A: Abolishes sumoylation and transcriptional repression; when associated with A-1020."; /evidence="ECO:0000269|PubMed:12718889, ECO:0000269|PubMed:15632193"; MUTAGEN 1024; /note="K->R: Abolishes sumoylation and transcriptional repression; when associated with R-1020."; /evidence="ECO:0000269|PubMed:12718889, ECO:0000269|PubMed:15632193"; MUTAGEN 1170; /note="F->E: Increased acetyltransferase activity."; /evidence="ECO:0000269|PubMed:23934153"; MUTAGEN 1204; /note="C->R: Increased acetyltransferase activity."; /evidence="ECO:0000269|PubMed:23934153"; MUTAGEN 1242; /note="E->K: Increased acetyltransferase activity."; /evidence="ECO:0000269|PubMed:23934153"; MUTAGEN 1357; /note="T->L: 40% decrease in activity."; /evidence="ECO:0000269|PubMed:18273021"; MUTAGEN 1357; /note="T->R: 40% decrease in activity. 90% decrease in activity; when associated with R-1505; R-1625 and R-1628."; /evidence="ECO:0000269|PubMed:18273021"; MUTAGEN 1396; /note="S->R: Loss of activity; when associated with R-1397."; /evidence="ECO:0000269|PubMed:18273021"; MUTAGEN 1396; /note="S->W: Loss of activity; when associated with W-1396."; /evidence="ECO:0000269|PubMed:18273021"; MUTAGEN 1397; /note="Y->R: Loss of activity; when associated with R-1396."; /evidence="ECO:0000269|PubMed:18273021"; MUTAGEN 1397; /note="Y->W: Loss of activity; when associated with W-1397."; /evidence="ECO:0000269|PubMed:18273021"; MUTAGEN 1399; /note="D->Y: Abolished acetyltransferase and acyltransferase activities. Abolishes autoacetylation. Does not interact with TFAP2A and inhibits transcriptional coactivation of TFAP2A by CITED2. Does not inhibit interaction with CITED2, DNA-binding of TFAP2A or nuclear localization of TFAP2A or CITED2. No enhancement of FOXO1-mediated transcriptional activity. No inhibition of insulin-mediated translocation to the cytoplasm. No acetylation of RXRA."; /evidence="ECO:0000269|PubMed:12586840, ECO:0000269|PubMed:15890677, ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:29775581, ECO:0000269|PubMed:40240600"; MUTAGEN 1467; /note="Y->F: Abolishes autoacetylation. Loss of acetyltransferase activity."; /evidence="ECO:0000269|PubMed:23934153"; MUTAGEN 1504; /note="F->A: Abolished acetyltransferase activity."; /evidence="ECO:0000269|PubMed:24835996"; MUTAGEN 1505; /note="E->R: 90% decrease in activity; when associated with R-1625 and R-1628. 90% decrease in activity; when associated with R-1357; R-1625 and R-1628."; /evidence="ECO:0000269|PubMed:18273021"; MUTAGEN 1625; /note="D->R: 70% decrease in activity; when associated with R-1628. 90% decrease in activity; when associated with R-1505 and R-1628. 90% decrease in activity; when associated with R-1357; R-1505 and R-1628."; /evidence="ECO:0000269|PubMed:18273021"; MUTAGEN 1628; /note="D->R: 70% decrease in activity; when associated with R-1625. 90% decrease in activity; when associated with E-1505 and R-1625. 90% decrease in activity; when associated with R-1357; R-1505 and R-1625."; /evidence="ECO:0000269|PubMed:18273021"; MUTAGEN 1645..1646; /note="RR->EE: Increased acetyltransferase activity."; /evidence="ECO:0000269|PubMed:23934153"; MUTAGEN 2056; /note="R->K: No effect on interaction with NCOA2."; /evidence="ECO:0000269|PubMed:15731352"; MUTAGEN 2088; /note="R->K: Abolishes interaction with NCOA2."; /evidence="ECO:0000269|PubMed:15731352"; MUTAGEN 2142; /note="R->K: Strongly reduces interaction with NCOA2."; /evidence="ECO:0000269|PubMed:15731352
uniprot
proteins
post_translational_modification
PTM: Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1020. Deacetylated by SIRT2, preferentially at Lys-418, Lys-423, Lys-1542, Lys-1546, Lys-1549, Lys-1699, Lys-1704 and Lys-1707. {ECO:0000269|PubMed:15004546, ECO:0000269|PubMed:15632193, ECO:0000269|PubMed:17065153, ECO:0000269|PubMed:18995842, ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:24177535}.; PTM: Citrullinated at Arg-2142 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1. {ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:15731352}.; PTM: Methylated at Arg-580 and Arg-604 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2142 by CARM1, which impairs interaction with NCOA2/GRIP1. {ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:15731352}.; PTM: Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3. {ECO:0000269|PubMed:12718889, ECO:0000269|PubMed:19680224}.; PTM: Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation.; PTM: Phosphorylated by HIPK2 in a RUNX1-dependent manner. This phosphorylation that activates EP300 happens when RUNX1 is associated with DNA and CBFB. Phosphorylated by ROCK2 and this enhances its activity. Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG. {ECO:0000269|PubMed:11518699, ECO:0000269|PubMed:12446687, ECO:0000269|PubMed:16574662, ECO:0000269|PubMed:18695000}.
uniprot
proteins
pubmed
10518217
uniprot
proteins
pubmed
10545121
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
10700188
uniprot
proteins
pubmed
10722728
uniprot
proteins
pubmed
10733570
uniprot
proteins
pubmed
10823961
uniprot
proteins
pubmed
10824998
uniprot
proteins
pubmed
11073989
uniprot
proteins
pubmed
11073990
uniprot
proteins
pubmed
11080476
uniprot
proteins
pubmed
11349124
uniprot
proteins
pubmed
11430825
uniprot
proteins
pubmed
11433299
uniprot
proteins
pubmed
11463834
uniprot
proteins
pubmed
11481323
uniprot
proteins
pubmed
11511361
uniprot
proteins
pubmed
11518699
uniprot
proteins
pubmed
11559821
uniprot
proteins
pubmed
11564735
uniprot
proteins
pubmed
11581164
uniprot
proteins
pubmed
11581372
uniprot
proteins
pubmed
11701890
uniprot
proteins
pubmed
11744733
uniprot
proteins
pubmed
11864910
uniprot
proteins
pubmed
11909954
uniprot
proteins
pubmed
11940591
uniprot
proteins
pubmed
11959990
uniprot
proteins
pubmed
11997499
uniprot
proteins
pubmed
12402037
uniprot
proteins
pubmed
12446687
uniprot
proteins
pubmed
12527917
uniprot
proteins
pubmed
12586840
uniprot
proteins
pubmed
12718889
uniprot
proteins
pubmed
12732631
uniprot
proteins
pubmed
12750254
uniprot
proteins
pubmed
12778114
uniprot
proteins
pubmed
12837748
uniprot
proteins
pubmed
12929931
uniprot
proteins
pubmed
14605447
uniprot
proteins
pubmed
14645221
uniprot
proteins
pubmed
14716005
uniprot
proteins
pubmed
14752053
uniprot
proteins
pubmed
15004546
uniprot
proteins
pubmed
15075319
uniprot
proteins
pubmed
15186775
uniprot
proteins
pubmed
15297880
uniprot
proteins
pubmed
15448695
uniprot
proteins
pubmed
15509808
uniprot
proteins
pubmed
15632193
uniprot
proteins
pubmed
15653507
uniprot
proteins
pubmed
15706485
uniprot
proteins
pubmed
15731352
uniprot
proteins
pubmed
15890677
uniprot
proteins
pubmed
16219772
uniprot
proteins
pubmed
16285960
uniprot
proteins
pubmed
16337145
uniprot
proteins
pubmed
16478997
uniprot
proteins
pubmed
16574662
uniprot
proteins
pubmed
16617102
uniprot
proteins
pubmed
16762839
uniprot
proteins
pubmed
16809611
uniprot
proteins
pubmed
16864582
uniprot
proteins
pubmed
17065153
uniprot
proteins
pubmed
17226766
uniprot
proteins
pubmed
17267393
uniprot
proteins
pubmed
17761950
uniprot
proteins
pubmed
17872950
uniprot
proteins
pubmed
18160048
uniprot
proteins
pubmed
18273021
uniprot
proteins
pubmed
18451878
uniprot
proteins
pubmed
18599479
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18695000
uniprot
proteins
pubmed
18722353
uniprot
proteins
pubmed
18782771
uniprot
proteins
pubmed
18809579
uniprot
proteins
pubmed
18995842
uniprot
proteins
pubmed
19217391
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19680224
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20081228
uniprot
proteins
pubmed
20810990
uniprot
proteins
pubmed
20940255
uniprot
proteins
pubmed
20955178
uniprot
proteins
pubmed
21030595
uniprot
proteins
pubmed
21131905
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22084251
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22464331
uniprot
proteins
pubmed
23145062
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23415232
uniprot
proteins
pubmed
23911289
uniprot
proteins
pubmed
23934153
uniprot
proteins
pubmed
23999430
uniprot
proteins
pubmed
24120661
uniprot
proteins
pubmed
24177535
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24324267
uniprot
proteins
pubmed
24382891
uniprot
proteins
pubmed
24413532
uniprot
proteins
pubmed
24476420
uniprot
proteins
pubmed
24819397
uniprot
proteins
pubmed
24835996
uniprot
proteins
pubmed
24939902
uniprot
proteins
pubmed
25219498
uniprot
proteins
pubmed
25245946
uniprot
proteins
pubmed
25514493
uniprot
proteins
pubmed
25593309
uniprot
proteins
pubmed
25818647
uniprot
proteins
pubmed
26479788
uniprot
proteins
pubmed
26951377
uniprot
proteins
pubmed
26990986
uniprot
proteins
pubmed
27189267
uniprot
proteins
pubmed
27959755
uniprot
proteins
pubmed
28128295
uniprot
proteins
pubmed
29053796
uniprot
proteins
pubmed
29460469
uniprot
proteins
pubmed
29775581
uniprot
proteins
pubmed
30193097
uniprot
proteins
pubmed
30197302
uniprot
proteins
pubmed
31645732
uniprot
proteins
pubmed
32561715
uniprot
proteins
pubmed
34545082
uniprot
proteins
pubmed
37731000
uniprot
proteins
pubmed
40240600
uniprot
proteins
pubmed
7523245
uniprot
proteins
pubmed
7870179
uniprot
proteins
pubmed
8684459
uniprot
proteins
pubmed
8917528
uniprot
proteins
pubmed
8945521
uniprot
proteins
pubmed
9528808
uniprot
proteins
pubmed
9590696
uniprot
proteins
pubmed
9862959
uniprot
proteins
pubmed
9887100
uniprot
proteins
sequence_length
2414
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:20940255}. Nucleus {ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:16219772, ECO:0000269|PubMed:16574662, ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:20940255, ECO:0000269|PubMed:25593309}. Chromosome {ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:25818647}. Note=Localizes to active chromatin: Colocalizes with histone H3 acetylated and/or crotonylated at 'Lys-18' (H3K18ac and H3K18cr, respectively) (PubMed:25818647). In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus (PubMed:12929931). Localizes to sites of DNA damage (PubMed:25593309). {ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:25818647}.
uniprot
proteins