Names & Taxonomy
- Uniprot ID:
- Q92793
- Entry Name:
- CBP_HUMAN
- Status:
- reviewed
- Protein Names:
- CREB-binding protein (EC 2.3.1.48)
- Gene Names:
- CREBBP CBP
- Gene Names Primary:
- CREBBP
- Organism:
- Homo sapiens (Human)
Structure
- Length:
- 2442
- Sequence:
- MAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELGLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANMASLSAMGKSPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQGASSSVLAETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATGVNPQLASKQSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGTGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEMMEEDLQGASQVKEETDIAEQKSEPMEVDEKKPEVKVEVKEEEESSSNGTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIIHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETTEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVINTLPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVSMSPAGFPSVARTQPPTTVSTGKPTSQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRVNINNSMPPGRTGMGTPGSQMAPVSLNVPRPNQVSGPVMPSMPPGQWQQAPLPQQQPMPGLPRPVISMQAQAAVAGPRMPSVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQAMGGLNPQGQALNIMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQHLPLQGSSMGQMAAQMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSIDQGHLGNPEQSAMLPQLNTPSRSALSSELSLVGDTTGDTLEKFVEGL
- Proteomes:
- UP000005640
Subcellular location
- Subcellular Location:
- Cytoplasm. Nucleus. Note=Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus.
Function
- Function:
- Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 and FOXO1. 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-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902).
- Catalytic Activity:
- Acetyl-CoA + = CoA + acetyl-.
- Gene Ontology Go:
- cytoplasm
histone acetyltransferase complex
nuclear body
nuclear chromatin
nucleoplasm
nucleus
transcription factor complex
acetyltransferase activity
chromatin binding
core promoter proximal region sequence-specific DNA binding
damaged DNA binding
histone acetyltransferase activity
MRF binding
p53 binding
RNA polymerase II activating transcription factor binding
RNA polymerase II transcription coactivator activity
RNA polymerase II transcription factor binding
signal transducer activity
transcription coactivator activity
transcription factor activity, sequence-specific DNA binding
transcription factor binding
transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding
transcriptional repressor activity, RNA polymerase II transcription factor binding
zinc ion binding
cell proliferation
cell-cell adhesion
cellular lipid metabolic process
cellular response to heat
cellular response to hypoxia
cellular response to UV
chromatin organization
embryonic digit morphogenesis
gene expression
histone acetylation
homeostatic process
innate immune response
N-terminal peptidyl-lysine acetylation
negative regulation of transcription from RNA polymerase II promoter
Notch signaling pathway
positive regulation of cell adhesion molecule production
positive regulation of G1/S transition of mitotic cell cycle
positive regulation of NIK/NF-kappaB signaling
positive regulation of transcription, DNA-templated
positive regulation of type I interferon production
protein acetylation
protein complex assembly
regulation of cellular response to heat
regulation of smoothened signaling pathway
regulation of transcription from RNA polymerase II promoter in response to hypoxia
regulation of transcription, DNA-templated
response to hypoxia
response to interleukin-1
rhythmic process
signal transduction
small molecule metabolic process
stimulatory C-type lectin receptor signaling pathway
transcription initiation from RNA polymerase II promoter
viral process - Gene Ontology Biological Process:
- cell-cell adhesion
cell proliferation
cellular lipid metabolic process
cellular response to heat
cellular response to hypoxia
cellular response to UV
chromatin organization
embryonic digit morphogenesis
gene expression
histone acetylation
homeostatic process
innate immune response
negative regulation of transcription from RNA polymerase II promoter
Notch signaling pathway
N-terminal peptidyl-lysine acetylation
positive regulation of cell adhesion molecule production
positive regulation of G1/S transition of mitotic cell cycle
positive regulation of NIK/NF-kappaB signaling
positive regulation of transcription, DNA-templated
positive regulation of type I interferon production
protein acetylation
protein complex assembly
regulation of cellular response to heat
regulation of smoothened signaling pathway
regulation of transcription, DNA-templated
regulation of transcription from RNA polymerase II promoter in response to hypoxia
response to hypoxia
response to interleukin-1
rhythmic process
signal transduction
small molecule metabolic process
stimulatory C-type lectin receptor signaling pathway
transcription initiation from RNA polymerase II promoter
viral process - Gene Ontology Molecular Function:
- acetyltransferase activity
chromatin binding
core promoter proximal region sequence-specific DNA binding
damaged DNA binding
histone acetyltransferase activity
MRF binding
p53 binding
RNA polymerase II activating transcription factor binding
RNA polymerase II transcription coactivator activity
RNA polymerase II transcription factor binding
signal transducer activity
transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding
transcriptional repressor activity, RNA polymerase II transcription factor binding
transcription coactivator activity
transcription factor activity, sequence-specific DNA binding
transcription factor binding
zinc ion binding - Gene Ontology Cellular Component:
- cytoplasm
histone acetyltransferase complex
nuclear body
nuclear chromatin
nucleoplasm
nucleus
transcription factor complex - Keywords:
- 3D-structure
Acetylation
Activator
Acyltransferase
Alternative splicing
Biological rhythms
Bromodomain
Chromosomal rearrangement
Complete proteome
Cytoplasm
Disease mutation
Host-virus interaction
Isopeptide bond
Metal-binding
Methylation
Nucleus
Phosphoprotein
Polymorphism
Reference proteome
Repeat
Transcription
Transcription regulation
Transferase
Ubl conjugation
Zinc
Zinc-finger - Interacts With:
- P03070; P03255; P03259; P03259-2; P31749; P10275; P61201; P16220; P35222; Q9UER7; Q12778; O43524; Q16665; P42858; P48551; O14920; Q14653; Q92831; Q86UE4; P55209; Q14686; Q04206; O95863; P04608; P04637
Publication
- PubMed ID:
- 9238046 9177780 8782817 11157802 8684459 8917528 9528808 9707565 10347196 10077561 10490106 10722728 10866662 11154691 11514544 11568182 11463834 11559821 11349124 11481323 11314014 11864910 11744733 11971985 12738767 12730195 12929931 14645221 15075319 15126506 15488321 15220471 14716005 17434128 17525332 18316612 18669648 19413330 19690332 19608861 20068231 21269460 22814378 24275569 24939902 11959977 11742995 14744133 22464331 24616510 24361270 11331617 12114483 12566391 15706485 20684013 25388907