{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P45481","secondaryAccessions":["E9QPH4"],"uniProtkbId":"CBP_MOUSE","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-07-27","entryVersion":245,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Histone lysine acetyltransferase CREBBP"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11115394"}],"value":"2.3.1.48"}]},"alternativeNames":[{"fullName":{"value":"Protein lactyltransferas CREBBP"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q92793"}],"value":"2.3.1.-"}]},{"fullName":{"value":"Protein-lysine acetyltransferase CREBBP"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15220471"}],"value":"2.3.1.-"}]}]},"genes":[{"geneName":{"value":"Crebbp"},"synonyms":[{"value":"Cbp"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q92793"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10207073"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11115394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11701890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15220471"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16287980"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24737000"}],"value":"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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21992"},{"database":"Rhea","id":"RHEA-COMP:9845"},{"database":"Rhea","id":"RHEA-COMP:11338"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11115394"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15220471"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-lactoyl-CoA + L-lysyl-[protein] = N(6)-[(S)-lactoyl]-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:61996"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:19466"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:231527"},{"database":"ChEBI","id":"CHEBI:231528"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q92793"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:61997"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q92793"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q92793"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10207073"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10215616"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10722728"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11115394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11701890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11943779"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12504852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12527917"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14594809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16287980"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17226766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18160706"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24737000"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28552616"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8552098"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8616895"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9192892"}],"value":"Part of a complex composed of MSX3, CREBBP/CBP AND EP300/p300; the interaction with MSX3 decreases histone acetylation activity (PubMed:11115394). Interacts with DHX9 (via N-terminus); this interaction mediates association with RNA polymerase II holoenzyme and stimulates CREB-dependent transcriptional activation (By similarity). Interacts (via transactivation domain and C-terminus) with PCNA; the interaction occurs on chromatin in UV-irradiated damaged cells (By similarity). Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. The TAZ-type 1 domain interacts with HIF1A. Interacts with SRCAP, ELF3, MLLT7/FOXO4, N4BP2, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. Interacts with KLF1; the interaction results in acetylation and enhancement of transcriptional activity of KLF1. Interacts with MAFG; the interaction acetylates MAFG in the basic region and stimulates NFE2 transcriptional activity through increasing its DNA-binding activity. Interacts with IRF2; the interaction acetylates IRF2 and regulates its activity on the H4 promoter. Interacts with IRF3 (when phosphorylated); forming the dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I interferon genes (By similarity). Interacts (via N-terminus) with SS18L1/CREST (via C-terminus). Interacts with FOXO1; the interaction acetylates FOXO1 and inhibits its transcriptional activity. Interacts with MECOM and MTDH. Interacts with ASF1A and ASF1B; this promotes histone acetylation. Interacts with acetylated TP53/p53 and with the acetylated histones H3 and H4 (By similarity). Interacts with CITED1 (via C-terminus). Interacts with GATA1; the interaction results in acetylation and enhancement of transcriptional activity of GATA1. Interacts with MAF, CARM1. NCOA3, ZCCHC12, DDX17, DDX5 and CITED4 (C-terminal region). Interacts with phosphorylated CREB1. Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activity via recruitment of HDAC2 to DAXX. Interacts with NPAS2, CLOCK and BMAL1. Interacts with SMAD4; negatively regulated by ZBTB7A (By similarity). Forms a complex with KMT2A and CREB1 (By similarity). Interacts with DDX3X; this interaction may facilitate HNF4A acetylation (By similarity). Interacts with MSX1; the interaction may inhibit MSX1 autoinactivation (PubMed:10215616). Interacts with MSX3 (PubMed:10215616). Interacts with ACSS2 (PubMed:28552616)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"Q9WTL8-4","geneName":"Bmal1","intActId":"EBI-644568"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"Q02248","geneName":"Ctnnb1","intActId":"EBI-397872"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"P27577","geneName":"Ets1","intActId":"EBI-4289053"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"Q60749","geneName":"Khdrbs1","intActId":"EBI-519077"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"Q04207","geneName":"Rela","intActId":"EBI-644400"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"Q62318-1","geneName":"Trim28","intActId":"EBI-6876996"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"P41182","geneName":"BCL6","intActId":"EBI-765407"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"O60566","geneName":"BUB1B","intActId":"EBI-1001438"},"numberOfExperiments":3,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"P61201","geneName":"COPS2","intActId":"EBI-1050386"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"P17844","geneName":"DDX5","intActId":"EBI-351962"},"numberOfExperiments":3,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"P35637","geneName":"FUS","intActId":"EBI-400434"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"P62805","geneName":"H4C9","intActId":"EBI-302023"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"Q03164","geneName":"KMT2A","intActId":"EBI-591370"},"numberOfExperiments":7,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"O95863","geneName":"SNAI1","intActId":"EBI-1045459"},"numberOfExperiments":7,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"P04637","geneName":"TP53","intActId":"EBI-366083"},"numberOfExperiments":10,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"P03254","intActId":"EBI-8599077"},"numberOfExperiments":3,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"P03255","intActId":"EBI-2603114"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P45481","intActId":"EBI-296306"},"interactantTwo":{"uniProtKBAccession":"P88946","intActId":"EBI-936023"},"numberOfExperiments":6,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q92793"}],"value":"Recruited to nuclear bodies by SS18L1/CREST. 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