CREBBP
entrez
1387
canonical
uniprot
Q92793
canonical
ensembl
ENSG00000005339
resolver
ensp
ENSP00000262367
resolver
ensp
ENSP00000371502
resolver
genesymbol
CREBBP
resolver
genesymbol_syn
CBP
resolver
hgnc
HGNC:2348
resolver
uniprot
D3DUC9
resolver
uniprot
O00147
resolver
uniprot
Q16376
resolver
uniprot
Q4LE28
resolver
uniprot_entry
CBP_HUMAN
resolver
uniprot_sec
D3DUC9
resolver
uniprot_sec
O00147
resolver
uniprot_sec
Q16376
resolver
uniprot_sec
Q4LE28
resolver
amino_acid_sequence
MAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELGLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANMASLSAMGKSPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQGASSSVLAETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATGVNPQLASKQSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGTGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEMMEEDLQGASQVKEETDIAEQKSEPMEVDEKKPEVKVEVKEEEESSSNGTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIIHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETTEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVINTLPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVSMSPAGFPSVARTQPPTTVSTGKPTSQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRVNINNSMPPGRTGMGTPGSQMAPVSLNVPRPNQVSGPVMPSMPPGQWQQAPLPQQQPMPGLPRPVISMQAQAAVAGPRMPSVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQAMGGLNPQGQALNIMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQHLPLQGSSMGQMAAQMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSIDQGHLGNPEQSAMLPQLNTPSRSALSSELSLVGDTTGDTLEKFVEGL
uniprot
proteins
disease_involvement
DISEASE: Note=Chromosomal aberrations involving CREBBP may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with KAT6A; translocation t(11;16)(q23;p13.3) with KMT2A/MLL1; translocation t(10;16)(q22;p13) with KAT6B. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription.; DISEASE: Rubinstein-Taybi syndrome 1 (RSTS1) [MIM:180849]: A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, intellectual disability and a propensity for development of malignancies. {ECO:0000269|PubMed:11331617, ECO:0000269|PubMed:12114483, ECO:0000269|PubMed:12566391, ECO:0000269|PubMed:15706485, ECO:0000269|PubMed:20684013, ECO:0000269|PubMed:24616510, ECO:0000269|PubMed:25388907}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Menke-Hennekam syndrome 1 (MKHK1) [MIM:618332]: 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:27311832, ECO:0000269|PubMed:29460469, ECO:0000269|PubMed:30737887}. 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: Acetylates histones, giving a specific tag for transcriptional activation (PubMed:21131905, PubMed:24616510). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (PubMed:21131905). Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (PubMed:10490106, PubMed:11154691, PubMed:12738767, PubMed:12929931, PubMed:24207024, PubMed:28790157, PubMed:30540930, PubMed:35675826, PubMed:9707565). Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-BMAL1 and CLOCK-BMAL1 heterodimers (PubMed:14645221). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). Acetylates POLR1E/PAF53, leading to decreased association of RNA polymerase I with the rDNA promoter region and coding region (PubMed:24207024). Acetylates DDX21, thereby inhibiting DDX21 helicase activity (PubMed:28790157). Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me) (PubMed:30540930). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as lactoyl-CoA, and is able to mediate protein lactylation (PubMed:38128537). Catalyzes lactylation of MRE11 in response to DNA damage, thereby promoting DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed:38128537). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493). {ECO:0000269|PubMed:10490106, ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:12738767, ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:21131905, ECO:0000269|PubMed:24207024, ECO:0000269|PubMed:24616510, ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:30540930, ECO:0000269|PubMed:35675826, ECO:0000269|PubMed:38128537, ECO:0000269|PubMed:9707565}.
uniprot
proteins
mass_dalton
265351
uniprot
proteins
mutagenesis
MUTAGEN 124; /note="S->A: Decreased phosphorylation and lactylation of MRE11."; /evidence="ECO:0000269|PubMed:38128537"; MUTAGEN 1116; /note="D->R: Impairs binding to acetylated histones."; /evidence="ECO:0000269|PubMed:24616510"; MUTAGEN 1126; /note="F->A: Impairs binding to acetylated histones."; /evidence="ECO:0000269|PubMed:24616510"; MUTAGEN 1162; /note="N->E,R: Abolishes interaction with ASF1A."; /evidence="ECO:0000269|PubMed:24616510"; MUTAGEN 1165; /note="W->A: Abolishes interaction with ASF1A."; /evidence="ECO:0000269|PubMed:24616510"; MUTAGEN 1170; /note="K->E: Impairs binding to acetylated histones."; /evidence="ECO:0000269|PubMed:24616510"; MUTAGEN 1179; /note="S->I: Impairs interaction with ASF1A."; /evidence="ECO:0000269|PubMed:24616510"; MUTAGEN 1180; /note="K->E: Abolishes interaction with ASF1A."; /evidence="ECO:0000269|PubMed:24616510"; MUTAGEN 1183; /note="E->R: Abolishes interaction with ASF1A."; /evidence="ECO:0000269|PubMed:24616510
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 (By similarity). {ECO:0000250|UniProtKB:P45481}.; PTM: Phosphorylated by CHUK/IKKA at Ser-1382 and Ser-1386; these phosphorylations promote cell growth by switching the binding preference of CREBBP from TP53 to NF-kappa-B (PubMed:17434128). Phosphorylated by _ at Ser-124 in response to DNA damage, promoting interaction with MRE11 and lactylation of MRE11 (PubMed:38128537). {ECO:0000269|PubMed:17434128, ECO:0000269|PubMed:38128537}.; PTM: Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX. {ECO:0000250|UniProtKB:P45481}.; PTM: Autoacetylation is required for binding to protein substrates, such as acetylated histones and acetylated TP53/p53 (PubMed:24616510). Autoacetylation is induced by glucose and fatty acids (PubMed:35675826). {ECO:0000269|PubMed:24616510, ECO:0000269|PubMed:35675826}.
uniprot
proteins
pubmed
10077561
uniprot
proteins
pubmed
10347196
uniprot
proteins
pubmed
10490106
uniprot
proteins
pubmed
10722728
uniprot
proteins
pubmed
10866662
uniprot
proteins
pubmed
11154691
uniprot
proteins
pubmed
11157802
uniprot
proteins
pubmed
11314014
uniprot
proteins
pubmed
11331617
uniprot
proteins
pubmed
11349124
uniprot
proteins
pubmed
11463834
uniprot
proteins
pubmed
11481323
uniprot
proteins
pubmed
11514544
uniprot
proteins
pubmed
11559821
uniprot
proteins
pubmed
11568182
uniprot
proteins
pubmed
11742995
uniprot
proteins
pubmed
11744733
uniprot
proteins
pubmed
11864910
uniprot
proteins
pubmed
11959977
uniprot
proteins
pubmed
11971985
uniprot
proteins
pubmed
12114483
uniprot
proteins
pubmed
12566391
uniprot
proteins
pubmed
12730195
uniprot
proteins
pubmed
12738767
uniprot
proteins
pubmed
12929931
uniprot
proteins
pubmed
14645221
uniprot
proteins
pubmed
14716005
uniprot
proteins
pubmed
14744133
uniprot
proteins
pubmed
15023334
uniprot
proteins
pubmed
15075319
uniprot
proteins
pubmed
15126506
uniprot
proteins
pubmed
15220471
uniprot
proteins
pubmed
15488321
uniprot
proteins
pubmed
15706485
uniprot
proteins
pubmed
17434128
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18316612
uniprot
proteins
pubmed
18599479
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20684013
uniprot
proteins
pubmed
21131905
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22464331
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23651431
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24207024
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24361270
uniprot
proteins
pubmed
24616510
uniprot
proteins
pubmed
24939902
uniprot
proteins
pubmed
25388907
uniprot
proteins
pubmed
25514493
uniprot
proteins
pubmed
25593309
uniprot
proteins
pubmed
26951377
uniprot
proteins
pubmed
27302953
uniprot
proteins
pubmed
27311832
uniprot
proteins
pubmed
28128295
uniprot
proteins
pubmed
28790157
uniprot
proteins
pubmed
29460469
uniprot
proteins
pubmed
30540930
uniprot
proteins
pubmed
30737887
uniprot
proteins
pubmed
35675826
uniprot
proteins
pubmed
38128537
uniprot
proteins
pubmed
8684459
uniprot
proteins
pubmed
8782817
uniprot
proteins
pubmed
8917528
uniprot
proteins
pubmed
9177780
uniprot
proteins
pubmed
9238046
uniprot
proteins
pubmed
9323138
uniprot
proteins
pubmed
9528808
uniprot
proteins
pubmed
9707565
uniprot
proteins
sequence_length
2442
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:15023334}. Nucleus {ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:15023334, ECO:0000269|PubMed:15488321, ECO:0000269|PubMed:25593309}. Note=Recruited to nuclear bodies by SS18L1/CREST (PubMed:15488321). In the presence of ALX1 relocalizes from the cytoplasm to the nucleus (PubMed:12929931). Relocalizes from the nucleus to the cytoplasm following UV cell damage (PubMed:15023334). {ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:15023334, ECO:0000269|PubMed:15488321}.
uniprot
proteins