P45481
uniprot
P45481
canonical
amino_acid_sequence
MAENLLDGPPNPKRAKLSSPGFSANDNTDFGSLFDLENDLPDELIPNGELSLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSTNMASLGAMGKSPLNQGDSSTPNLPKQAASTSGPTPPASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPYPAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTGTTSPFGQPFSQTGGQQMGATGVNPQLASKQSMVNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGAGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPMSIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRSEMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPEVKVEAKEEEENSSNDTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQNTALIAPHQIQGRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIINDYKDIFKQANEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETPEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVISTQPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVNMSPAGFPNVARTQPPTIVSAGKPTNQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRANINNGMPPGRAGMGTPGSQMTPVGLNVPRPNQVSGPVMSSMPPGQWQQAPIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPGHNPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNSASLAGGMAGHSQFQQPQGPGGYAPAMQQQRMQQHLPIQGSSMGQMAAPMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSMDQGHLGNPEQSAMLPQLNTPNRSALSSELSLVGDTTGDTLEKFVEGL
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
function
FUNCTION: Acetylates histones, giving a specific tag for transcriptional activation (PubMed:11115394). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (By similarity). Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (PubMed:10207073, PubMed:11701890, PubMed:15220471, PubMed:16287980). Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes (By similarity). Acts as a coactivator of ALX1 (By similarity). Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-BMAL1 and CLOCK-BMAL1 heterodimers (By similarity). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24737000). Acetylates POLR1E/PAF53, leading to decreased association of RNA polymerase I with the rDNA promoter region and coding region (By similarity). Acetylates DDX21, thereby inhibiting DDX21 helicase activity (By similarity). Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me) (By similarity). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as lactoyl-CoA, and is able to mediate protein lactylation (By similarity). Catalyzes lactylation of MRE11 in response to DNA damage, thereby promoting DNA double-strand breaks (DSBs) via homologous recombination (HR) (By similarity). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q92793, ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:11115394, ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:16287980, ECO:0000269|PubMed:24737000}.
uniprot
proteins
mass_dalton
265494
uniprot
proteins
mutagenesis
MUTAGEN 600; /note="R->N: Abolishes binding to CREB."; /evidence="ECO:0000269|PubMed:8552098"; MUTAGEN 999; /note="K->R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-1034 and R-1057."; /evidence="ECO:0000269|PubMed:16287980"; MUTAGEN 1015; /note="K->R: No change in sumoylation."; /evidence="ECO:0000269|PubMed:16287980"; MUTAGEN 1034; /note="K->R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-999 and R-1057."; /evidence="ECO:0000269|PubMed:16287980"; MUTAGEN 1043; /note="K->R: No change in sumoylation."; /evidence="ECO:0000269|PubMed:16287980"; MUTAGEN 1053; /note="K->R: No change in sumoylation."; /evidence="ECO:0000269|PubMed:16287980"; MUTAGEN 1057; /note="K->R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-999 and R-1034."; /evidence="ECO:0000269|PubMed:16287980"; MUTAGEN 1061; /note="K->R: No change in sumoylation."; /evidence="ECO:0000269|PubMed:16287980"; MUTAGEN 1087; /note="K->R: No change in sumoylation."; /evidence="ECO:0000269|PubMed:16287980"; MUTAGEN 1690..1691; /note="LC->KL: Abolishes histone acetyltransferase activity."; /evidence="ECO:0000269|PubMed:10207073
uniprot
proteins
post_translational_modification
PTM: Methylation of the KIX domain by CARM1 blocks association with CREB. This results in the blockade of CREB signaling, and in activation of apoptotic response. {ECO:0000269|PubMed:11701890}.; PTM: Phosphorylated by CHUK/IKKA at Ser-1383 and Ser-1387; these phosphorylations promote cell growth by switching the binding preference of CREBBP from TP53 to NF-kappa-B. {ECO:0000250|UniProtKB:Q92793}.; PTM: Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX. {ECO:0000269|PubMed:16287980}.; PTM: Autoacetylation is required for binding to protein substrates, such as acetylated histones and acetylated TP53/p53. Autoacetylation is induced by glucose and fatty acids. {ECO:0000250|UniProtKB:Q92793}.
uniprot
proteins
pubmed
10207073
uniprot
proteins
pubmed
10215616
uniprot
proteins
pubmed
10722728
uniprot
proteins
pubmed
11115394
uniprot
proteins
pubmed
11701890
uniprot
proteins
pubmed
11943779
uniprot
proteins
pubmed
12504852
uniprot
proteins
pubmed
12527917
uniprot
proteins
pubmed
14594809
uniprot
proteins
pubmed
15220471
uniprot
proteins
pubmed
16287980
uniprot
proteins
pubmed
17226766
uniprot
proteins
pubmed
18160706
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24737000
uniprot
proteins
pubmed
28552616
uniprot
proteins
pubmed
8413673
uniprot
proteins
pubmed
8552098
uniprot
proteins
pubmed
8616895
uniprot
proteins
pubmed
9192892
uniprot
proteins
sequence_length
2441
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92793}. Nucleus {ECO:0000250|UniProtKB:Q92793}. Note=Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Relocalizes from the nucleus to the cytoplasm following UV cell damage (By similarity). {ECO:0000250|UniProtKB:Q92793}.
uniprot
proteins