MOUSE:CBP

Species (Taxon ID)	Mus musculus (Mouse). (10090)
Gene Name(s)	Crebbp (synonyms: Cbp)
Protein Name(s)	CREB-binding protein
External Links
UniProt	P45481
EMBL	S66385 AC132380
CCDS	CCDS27915.1
PIR	S39161
UniGene	Mm.132238 Mm.392384
PDB	1F81 1JJS 1KBH 1KDX 1L8C 1R8U 1SB0 1TOT 1U2N 2AGH 2C52 2KA4 2KA6 2KKJ 2L14 2LQH 2LQI 2LWW 4I9O
PDBsum	1F81 1JJS 1KBH 1KDX 1L8C 1R8U 1SB0 1TOT 1U2N 2AGH 2C52 2KA4 2KA6 2KKJ 2L14 2LQH 2LQI 2LWW 4I9O
DisProt	DP00348
ProteinModelPortal	P45481
SMR	P45481
DIP	DIP-5974N
IntAct	P45481
MINT	MINT-203452
PhosphoSite	P45481
MaxQB	P45481
PaxDb	P45481
PRIDE	P45481
MGI	MGI:1098280
eggNOG	COG5076
HOGENOM	HOG000111353
HOVERGEN	HBG000185
InParanoid	P45481
Reactome	REACT_226917 REACT_252217 REACT_268602 REACT_27166
ChiTaRS	Crebbp
EvolutionaryTrace	P45481
PRO	PR:P45481
Proteomes	UP000000589
CleanEx	MM_CREBBP
Genevestigator	P45481
GO	GO:0000940 GO:0005737 GO:0000123 GO:0000790 GO:0005654 GO:0005634 GO:0016605 GO:0005667 GO:0016407 GO:0003682 GO:0003677 GO:0004402 GO:0043426 GO:0000977 GO:0001228 GO:0003713 GO:0008134 GO:0008270 GO:0030718 GO:0016573 GO:0018076 GO:0051091 GO:0045944 GO:0045893 GO:0006355 GO:0048511
Gene3D	1.10.1630.10 1.10.246.20 1.20.1020.10 1.20.920.10
InterPro	IPR001487 IPR018359 IPR010303 IPR013178 IPR003101 IPR009110 IPR014744 IPR000197 IPR000433
Pfam	PF00439 PF09030 PF06001 PF08214 PF02172 PF02135 PF00569
PRINTS	PR00503
SMART	SM00297 SM00551 SM00291
SUPFAM	SSF47040 SSF47370 SSF57933 SSF69125
PROSITE	PS00633 PS50014 PS51727 PS50952 PS50134 PS01357 PS50135

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0060235	lens induction in camera-type eye	PMID:24038357^[1]	ECO:0000316		UniProtKB:B2RWS6	P	Figure 3 details lens induction and the morphogenic differences observed in mutant mice.	complete CACAO 8912
involved_in	GO:0060325	face morphogenesis	PMID:19822209^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:14594809^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:14594809^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q16665	F	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:14594809^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:14594809^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q99967	F	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:11823864^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:11823864^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:11823864^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9Y6Q9	F	Seeded From UniProt	complete
involved_in	GO:0048525	negative regulation of viral process	PMID:11583620^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045358	negative regulation of interferon-beta biosynthetic process	PMID:11583620^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	PMID:11583620^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0098586	cellular response to virus	PMID:11583620^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:11583620^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:F5HF68	F	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:11583620^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q15596	F	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:11583620^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14653	F	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:11583620^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15036	F	Seeded From UniProt	complete
enables	GO:0008140	cAMP response element binding protein binding	PMID:9413984^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15337	F	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
involved_in	GO:0034644	cellular response to UV	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	PMID:16427017^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	PMID:15187136^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:10733899^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
enables	GO:0043426	MRF binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
involved_in	GO:0018076	N-terminal peptidyl-lysine acetylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
involved_in	GO:0016573	histone acetylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:10075717^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P10071	F	Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:1901224	positive regulation of NIK/NF-kappaB signaling	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:1900087	positive regulation of G1/S transition of mitotic cell cycle	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	P	Seeded From UniProt	complete
part_of	GO:0090575	RNA polymerase II transcription factor complex	PMID:7913207^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0090575	RNA polymerase II transcription factor complex	PMID:22977234^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0060355	positive regulation of cell adhesion molecule production	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	P	Seeded From UniProt	complete
enables	GO:0046332	SMAD binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	F	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:16012757^[13]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:1933126	P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0045944	positive regulation of transcription by RNA polymerase II	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0045893	positive regulation of transcription, DNA-templated	PMID:16145670^[14]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0045893	positive regulation of transcription, DNA-templated	PMID:15509593^[15]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0045893	positive regulation of transcription, DNA-templated	PMID:15464984^[16]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0045893	positive regulation of transcription, DNA-templated	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
enables	GO:0043426	MRF binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0042975	peroxisome proliferator activated receptor binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	F	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0035729	cellular response to hepatocyte growth factor stimulus	PMID:21072211^[17]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0034644	cellular response to UV	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
enables	GO:0033613	activating transcription factor binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	F	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	C	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0032793	positive regulation of CREB transcription factor activity	PMID:7913207^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0031648	protein destabilization	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0030718	germ-line stem cell population maintenance	PMID:17936260^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:2177588,MGI:MGI:3618462	P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0030511	positive regulation of transforming growth factor beta receptor signaling pathway	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0018076	N-terminal peptidyl-lysine acetylation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:17332504^[19]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:O60424	C	Seeded From UniProt	complete
part_of	GO:0016604	nuclear body	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	C	Seeded From UniProt	complete
part_of	GO:0016604	nuclear body	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	C	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0016573	histone acetylation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0016573	histone acetylation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	P	Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:12496368^[20]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0010628	positive regulation of gene expression	PMID:22523253^[21]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:1276116	P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0008283	cell population proliferation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	P	Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006473	protein acetylation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006355	regulation of transcription, DNA-templated	PMID:12464179^[22]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	C	Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	PMID:16606840^[23]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	PMID:12464179^[22]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	C	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15509593^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12496368^[20]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:11963968^[24]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	C	Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	PMID:11867645^[25]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	PMID:11115394^[26]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	F	Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:7913207^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
contributes_to	GO:0003700	DNA-binding transcription factor activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2401	F	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:15832170^[27]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:15681609^[28]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0002039	p53 binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	PMID:22780989^[29]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0001093	TFIIB-class transcription factor binding	PMID:7913207^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P62915	F	Seeded From UniProt	complete
enables	GO:0001085	RNA polymerase II transcription factor binding	PMID:7913207^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q01147	F	Seeded From UniProt	complete
enables	GO:0001085	RNA polymerase II transcription factor binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0000987	proximal promoter sequence-specific DNA binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	F	Seeded From UniProt	complete
enables	GO:0000977	RNA polymerase II regulatory region sequence-specific DNA binding	PMID:21402781^[30]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0000940	condensed chromosome outer kinetochore	PMID:14519686^[31]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	C	Seeded From UniProt	complete
part_of	GO:0000123	histone acetyltransferase complex	PMID:9742083^[32]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0000122	negative regulation of transcription by RNA polymerase II	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92793	P	Seeded From UniProt	complete
part_of	GO:0000123	histone acetyltransferase complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014744	C	Seeded From UniProt	complete
enables	GO:0003712	transcription coregulator activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000197 InterPro:IPR003101 InterPro:IPR036529	F	Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014744	F	Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000197 InterPro:IPR013178 InterPro:IPR014744	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000197 InterPro:IPR014744	C	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000197 InterPro:IPR003101 InterPro:IPR013178 InterPro:IPR014744 InterPro:IPR036529	P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000197 InterPro:IPR000433	F	Seeded From UniProt	complete
involved_in	GO:0016573	histone acetylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013178 InterPro:IPR014744	P	Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.48	F	Seeded From UniProt	complete
involved_in	GO:0051091	positive regulation of DNA-binding transcription factor activity	PMID:10733899^[9]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:10733899^[9]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0061733	peptide-lysine-N-acetyltransferase activity	Reactome:R-MMU-9617755	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-NUL-9626944 Reactome:R-MMU-9617755 Reactome:R-MMU-9617711 Reactome:R-MMU-5619441 Reactome:R-MMU-556760 Reactome:R-MMU-4568768 Reactome:R-MMU-4395232 Reactome:R-MMU-3927825	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	Reactome:R-NUL-9626944 Reactome:R-MMU-4568768	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016746	transferase activity, transferring acyl groups	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0012	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
involved_in	GO:0048511	rhythmic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0090	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Wolf, L et al. (2013) Histone posttranslational modifications and cell fate determination: lens induction requires the lysine acetyltransferases CBP and p300. Nucleic Acids Res. 41 10199-214 PubMed GONUTS page
↑ Viosca, J et al. (2010) Syndromic features and mild cognitive impairment in mice with genetic reduction on p300 activity: Differential contribution of p300 and CBP to Rubinstein-Taybi syndrome etiology. Neurobiol. Dis. 37 186-94 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 De Guzman, RN et al. (2004) Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. J. Biol. Chem. 279 3042-9 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Demarest, SJ et al. (2002) Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. Nature 415 549-53 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Lin, CH et al. (2001) A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies. Mol. Cell 8 581-90 PubMed GONUTS page
↑ Radhakrishnan, I et al. (1997) Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 91 741-52 PubMed GONUTS page
↑ Riccio, A et al. (2006) A nitric oxide signaling pathway controls CREB-mediated gene expression in neurons. Mol. Cell 21 283-94 PubMed GONUTS page
↑ Pauleau, AL et al. (2004) Enhancer-mediated control of macrophage-specific arginase I expression. J. Immunol. 172 7565-73 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Seo, T et al. (2000) Viral interferon regulatory factor 1 of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) binds to, and inhibits transactivation of, CREB-binding protein. Biochem. Biophys. Res. Commun. 270 23-7 PubMed GONUTS page
↑ Dai, P et al. (1999) Sonic Hedgehog-induced activation of the Gli1 promoter is mediated by GLI3. J. Biol. Chem. 274 8143-52 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 Kwok, RP et al. (1994) Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature 370 223-6 PubMed GONUTS page
↑ Wu, Z et al. (2012) Role of nuclear receptor coactivator 3 (Ncoa3) in pluripotency maintenance. J. Biol. Chem. 287 38295-304 PubMed GONUTS page
↑ Yin, X et al. (2005) Novel interaction between nuclear co-activator CBP and the CDK5 activator binding protein - C53. Int. J. Mol. Med. 16 251-6 PubMed GONUTS page
↑ Morikawa, Y et al. (2005) The basic helix-loop-helix factor Hand 2 regulates autonomic nervous system development. Dev. Dyn. 234 613-21 PubMed GONUTS page
↑ ^15.0 ^15.1 Barbacci, E et al. (2004) HNF1beta/TCF2 mutations impair transactivation potential through altered co-regulator recruitment. Hum. Mol. Genet. 13 3139-49 PubMed GONUTS page
↑ Warner, DR et al. (2004) Functional interaction between Smad, CREB binding protein, and p68 RNA helicase. Biochem. Biophys. Res. Commun. 324 70-6 PubMed GONUTS page
↑ Coudriet, GM et al. (2010) Hepatocyte growth factor modulates interleukin-6 production in bone marrow derived macrophages: implications for inflammatory mediated diseases. PLoS ONE 5 e15384 PubMed GONUTS page
↑ Elliott, AM et al. (2007) Identifying genes differentially expressed between PGCs and ES cells reveals a role for CREB-binding protein in germ cell survival. Dev. Biol. 311 347-58 PubMed GONUTS page
↑ Takahashi, K et al. (2007) Dynamic regulation of p53 subnuclear localization and senescence by MORC3. Mol. Biol. Cell 18 1701-9 PubMed GONUTS page
↑ ^20.0 ^20.1 Hong, W et al. (2002) Physical and functional interaction between the transcriptional cofactor CBP and the KH domain protein Sam68. Mol. Cancer Res. 1 48-55 PubMed GONUTS page
↑ Pentz, ES et al. (2012) Histone acetyl transferases CBP and p300 are necessary for maintenance of renin cell identity and transformation of smooth muscle cells to the renin phenotype. Am. J. Physiol. Heart Circ. Physiol. 302 H2545-52 PubMed GONUTS page
↑ ^22.0 ^22.1 Kioussi, C et al. (2002) Identification of a Wnt/Dvl/beta-Catenin --> Pitx2 pathway mediating cell-type-specific proliferation during development. Cell 111 673-85 PubMed GONUTS page
↑ Yujnovsky, I et al. (2006) Signaling mediated by the dopamine D2 receptor potentiates circadian regulation by CLOCK:BMAL1. Proc. Natl. Acad. Sci. U.S.A. 103 6386-91 PubMed GONUTS page
↑ Warner, DR et al. (2002) Expression of the nuclear coactivators CBP and p300 in developing craniofacial tissue. In Vitro Cell. Dev. Biol. Anim. 38 48-53 PubMed GONUTS page
↑ Li, Q et al. (2002) Histone acetyltransferase activities of cAMP-regulated enhancer-binding protein and p300 in tissues of fetal, young, and old mice. J. Gerontol. A Biol. Sci. Med. Sci. 57 B93-8 PubMed GONUTS page
↑ Mehra-Chaudhary, R et al. (2001) Msx3 protein recruits histone deacetylase to down-regulate the Msx1 promoter. Biochem. J. 353 13-22 PubMed GONUTS page
↑ Hartman, HB et al. (2005) The histone-binding code of nuclear receptor co-repressors matches the substrate specificity of histone deacetylase 3. EMBO Rep. 6 445-51 PubMed GONUTS page
↑ Guan, HP et al. (2005) Corepressors selectively control the transcriptional activity of PPARgamma in adipocytes. Genes Dev. 19 453-61 PubMed GONUTS page
↑ Faure, AJ et al. (2012) Cohesin regulates tissue-specific expression by stabilizing highly occupied cis-regulatory modules. Genome Res. 22 2163-75 PubMed GONUTS page
↑ Benlhabib, H & Mendelson, CR (2011) Epigenetic regulation of surfactant protein A gene (SP-A) expression in fetal lung reveals a critical role for Suv39h methyltransferases during development and hypoxia. Mol. Cell. Biol. 31 1949-58 PubMed GONUTS page
↑ Craig, JM et al. (2003) Analysis of mammalian proteins involved in chromatin modification reveals new metaphase centromeric proteins and distinct chromosomal distribution patterns. Hum. Mol. Genet. 12 3109-21 PubMed GONUTS page
↑ Xu, W et al. (1998) Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates. Mol. Cell. Biol. 18 5659-69 PubMed GONUTS page

[PMID:24038357-1] Wolf, L et al. (2013) Histone posttranslational modifications and cell fate determination: lens induction requires the lysine acetyltransferases CBP and p300. Nucleic Acids Res. 41 10199-214 PubMed GONUTS page

[PMID:19822209-2] Viosca, J et al. (2010) Syndromic features and mild cognitive impairment in mice with genetic reduction on p300 activity: Differential contribution of p300 and CBP to Rubinstein-Taybi syndrome etiology. Neurobiol. Dis. 37 186-94 PubMed GONUTS page

[PMID:14594809-3] 3.0 ^3.1 ^3.2 ^3.3 De Guzman, RN et al. (2004) Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. J. Biol. Chem. 279 3042-9 PubMed GONUTS page

[PMID:11823864-4] 4.0 ^4.1 ^4.2 Demarest, SJ et al. (2002) Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. Nature 415 549-53 PubMed GONUTS page

[PMID:11583620-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Lin, CH et al. (2001) A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies. Mol. Cell 8 581-90 PubMed GONUTS page

[PMID:9413984-6] Radhakrishnan, I et al. (1997) Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 91 741-52 PubMed GONUTS page

[PMID:16427017-7] Riccio, A et al. (2006) A nitric oxide signaling pathway controls CREB-mediated gene expression in neurons. Mol. Cell 21 283-94 PubMed GONUTS page

[PMID:15187136-8] Pauleau, AL et al. (2004) Enhancer-mediated control of macrophage-specific arginase I expression. J. Immunol. 172 7565-73 PubMed GONUTS page

[PMID:10733899-9] 9.0 ^9.1 ^9.2 Seo, T et al. (2000) Viral interferon regulatory factor 1 of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) binds to, and inhibits transactivation of, CREB-binding protein. Biochem. Biophys. Res. Commun. 270 23-7 PubMed GONUTS page

[PMID:10075717-10] Dai, P et al. (1999) Sonic Hedgehog-induced activation of the Gli1 promoter is mediated by GLI3. J. Biol. Chem. 274 8143-52 PubMed GONUTS page

[PMID:7913207-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 Kwok, RP et al. (1994) Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature 370 223-6 PubMed GONUTS page

[PMID:22977234-12] Wu, Z et al. (2012) Role of nuclear receptor coactivator 3 (Ncoa3) in pluripotency maintenance. J. Biol. Chem. 287 38295-304 PubMed GONUTS page

[PMID:16012757-13] Yin, X et al. (2005) Novel interaction between nuclear co-activator CBP and the CDK5 activator binding protein - C53. Int. J. Mol. Med. 16 251-6 PubMed GONUTS page

[PMID:16145670-14] Morikawa, Y et al. (2005) The basic helix-loop-helix factor Hand 2 regulates autonomic nervous system development. Dev. Dyn. 234 613-21 PubMed GONUTS page

[PMID:15509593-15] 15.0 ^15.1 Barbacci, E et al. (2004) HNF1beta/TCF2 mutations impair transactivation potential through altered co-regulator recruitment. Hum. Mol. Genet. 13 3139-49 PubMed GONUTS page

[PMID:15464984-16] Warner, DR et al. (2004) Functional interaction between Smad, CREB binding protein, and p68 RNA helicase. Biochem. Biophys. Res. Commun. 324 70-6 PubMed GONUTS page

[PMID:21072211-17] Coudriet, GM et al. (2010) Hepatocyte growth factor modulates interleukin-6 production in bone marrow derived macrophages: implications for inflammatory mediated diseases. PLoS ONE 5 e15384 PubMed GONUTS page

[PMID:17936260-18] Elliott, AM et al. (2007) Identifying genes differentially expressed between PGCs and ES cells reveals a role for CREB-binding protein in germ cell survival. Dev. Biol. 311 347-58 PubMed GONUTS page

[PMID:17332504-19] Takahashi, K et al. (2007) Dynamic regulation of p53 subnuclear localization and senescence by MORC3. Mol. Biol. Cell 18 1701-9 PubMed GONUTS page

[PMID:12496368-20] 20.0 ^20.1 Hong, W et al. (2002) Physical and functional interaction between the transcriptional cofactor CBP and the KH domain protein Sam68. Mol. Cancer Res. 1 48-55 PubMed GONUTS page

[PMID:22523253-21] Pentz, ES et al. (2012) Histone acetyl transferases CBP and p300 are necessary for maintenance of renin cell identity and transformation of smooth muscle cells to the renin phenotype. Am. J. Physiol. Heart Circ. Physiol. 302 H2545-52 PubMed GONUTS page

[PMID:12464179-22] 22.0 ^22.1 Kioussi, C et al. (2002) Identification of a Wnt/Dvl/beta-Catenin --> Pitx2 pathway mediating cell-type-specific proliferation during development. Cell 111 673-85 PubMed GONUTS page

[PMID:16606840-23] Yujnovsky, I et al. (2006) Signaling mediated by the dopamine D2 receptor potentiates circadian regulation by CLOCK:BMAL1. Proc. Natl. Acad. Sci. U.S.A. 103 6386-91 PubMed GONUTS page

[PMID:11963968-24] Warner, DR et al. (2002) Expression of the nuclear coactivators CBP and p300 in developing craniofacial tissue. In Vitro Cell. Dev. Biol. Anim. 38 48-53 PubMed GONUTS page

[PMID:11867645-25] Li, Q et al. (2002) Histone acetyltransferase activities of cAMP-regulated enhancer-binding protein and p300 in tissues of fetal, young, and old mice. J. Gerontol. A Biol. Sci. Med. Sci. 57 B93-8 PubMed GONUTS page

[PMID:11115394-26] Mehra-Chaudhary, R et al. (2001) Msx3 protein recruits histone deacetylase to down-regulate the Msx1 promoter. Biochem. J. 353 13-22 PubMed GONUTS page

[PMID:15832170-27] Hartman, HB et al. (2005) The histone-binding code of nuclear receptor co-repressors matches the substrate specificity of histone deacetylase 3. EMBO Rep. 6 445-51 PubMed GONUTS page

[PMID:15681609-28] Guan, HP et al. (2005) Corepressors selectively control the transcriptional activity of PPARgamma in adipocytes. Genes Dev. 19 453-61 PubMed GONUTS page

[PMID:22780989-29] Faure, AJ et al. (2012) Cohesin regulates tissue-specific expression by stabilizing highly occupied cis-regulatory modules. Genome Res. 22 2163-75 PubMed GONUTS page

[PMID:21402781-30] Benlhabib, H & Mendelson, CR (2011) Epigenetic regulation of surfactant protein A gene (SP-A) expression in fetal lung reveals a critical role for Suv39h methyltransferases during development and hypoxia. Mol. Cell. Biol. 31 1949-58 PubMed GONUTS page

[PMID:14519686-31] Craig, JM et al. (2003) Analysis of mammalian proteins involved in chromatin modification reveals new metaphase centromeric proteins and distinct chromosomal distribution patterns. Hum. Mol. Genet. 12 3109-21 PubMed GONUTS page

[PMID:9742083-32] Xu, W et al. (1998) Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates. Mol. Cell. Biol. 18 5659-69 PubMed GONUTS page

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