HUMAN:EP300

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	EP300 (synonyms: P300)
Protein Name(s)	Histone acetyltransferase p300 p300 HAT E1A-associated protein p300
External Links
UniProt	Q09472
EMBL	U01877 AL080243 AL035658 AL096765 AL096765 AL035658 AL080243 AL035658 AL080243 AL096765 CH471095
CCDS	CCDS14010.1
PIR	A54277
RefSeq	NP_001420.2
UniGene	Hs.517517 Hs.655211
PDB	1L3E 1P4Q 2K8F 2MH0 3BIY 3I3J 3IO2 3P57 3T92 4BHW 4PZR 4PZS 4PZT
PDBsum	1L3E 1P4Q 2K8F 2MH0 3BIY 3I3J 3IO2 3P57 3T92 4BHW 4PZR 4PZS 4PZT
DisProt	DP00633
ProteinModelPortal	Q09472
SMR	Q09472
BioGrid	108347
DIP	DIP-257N
IntAct	Q09472
MINT	MINT-104535
STRING	9606.ENSP00000263253
BindingDB	Q09472
ChEMBL	CHEMBL3784
GuidetoPHARMACOLOGY	2735
PhosphoSite	Q09472
DMDM	223590203
MaxQB	Q09472
PaxDb	Q09472
PRIDE	Q09472
Ensembl	ENST00000263253
GeneID	2033
KEGG	hsa:2033
UCSC	uc003azl.4
CTD	2033
GeneCards	GC22P041487
GeneReviews	EP300
H-InvDB	HIX0203186
HGNC	HGNC:3373
HPA	CAB000146 HPA003128 HPA004112
MIM	602700 613684
neXtProt	NX_Q09472
Orphanet	353284
PharmGKB	PA27807
eggNOG	COG5076
GeneTree	ENSGT00760000119206
HOGENOM	HOG000111353
HOVERGEN	HBG000185
InParanoid	Q09472
KO	K04498
OMA	PTMIRGS
OrthoDB	EOG75B84F
PhylomeDB	Q09472
TreeFam	TF101097
Reactome	REACT_1006 REACT_111118 REACT_116145 REACT_118568 REACT_118659 REACT_118780 REACT_118789 REACT_121092 REACT_160243 REACT_160254 REACT_163743 REACT_163910 REACT_172610 REACT_200624 REACT_200753 REACT_24938 REACT_24941 REACT_24970 REACT_25026 REACT_27161
SignaLink	Q09472
ChiTaRS	EP300
EvolutionaryTrace	Q09472
GeneWiki	EP300
GenomeRNAi	2033
NextBio	8251
PRO	PR:Q09472
Proteomes	UP000005640
Bgee	Q09472
CleanEx	HS_EP300
ExpressionAtlas	Q09472
Genevestigator	Q09472
GO	GO:0000785 GO:0005737 GO:0000123 GO:0005654 GO:0005634 GO:0032993 GO:0005667 GO:0016407 GO:0033613 GO:0050681 GO:0003823 GO:0008013 GO:0003682 GO:0031490 GO:0001047 GO:0003677 GO:0004402 GO:0004468 GO:0035257 GO:0097157 GO:0001102 GO:0000978 GO:0000979 GO:0003700 GO:0003713 GO:0008134 GO:0016746 GO:0008270 GO:0006915 GO:0071320 GO:0071549 GO:0035690 GO:0071333 GO:0070301 GO:0071456 GO:0071389 GO:1990090 GO:0071300 GO:0035984 GO:0006325 GO:0007623 GO:0048565 GO:0000086 GO:0007507 GO:0043969 GO:0043966 GO:0043967 GO:0045087 GO:0018393 GO:0006475 GO:0042771 GO:0001889 GO:0030324 GO:0000278 GO:0018076 GO:0043154 GO:2000629 GO:0000122 GO:0007399 GO:0007219 GO:0009887 GO:0043923 GO:0045773 GO:0010942 GO:0045793 GO:0032967 GO:0043388 GO:0010560 GO:0014737 GO:1901985 GO:0032092 GO:0033160 GO:0001934 GO:0050714 GO:0045862 GO:0060298 GO:0051091 GO:0045944 GO:0045727 GO:0032481 GO:0043491 GO:0065004 GO:0060765 GO:0060177 GO:0051726 GO:0061418 GO:0006355 GO:0090043 GO:0051592 GO:0032025 GO:0043627 GO:0045471 GO:0070542 GO:0001666 GO:0034612 GO:0007519 GO:0001756 GO:0006351 GO:0016032
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	Extension	Notes	Status
	GO:0004402	histone acetyltransferase activity	PMID:25644304^[1]	ECO:0000314			F		This paper provides necessary information about the function and use of histone acetyltransferase 300 that is useful for the making of this annotation.	complete CACAO 10684
enables	GO:0001102	RNA polymerase II activating transcription factor binding	PMID:23811396^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q04206	F		Seeded From UniProt	complete
enables	GO:0001102	RNA polymerase II activating transcription factor binding	PMID:23811396^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19838:PRO_0000030311	F		Seeded From UniProt	complete
enables	GO:0000977	RNA polymerase II regulatory region sequence-specific DNA binding	PMID:23811396^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	part_of:(GO:0045944) has_input:(ENSEMBL:ENSG00000089250)	Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:23811396^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19838:PRO_0000030311	F	part_of:(GO:0045944) has_input:(ENSEMBL:ENSG00000089250)	Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:23811396^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q04206	F	part_of:(GO:0045944) has_input:(ENSEMBL:ENSG00000089250)	Seeded From UniProt	complete
enables	GO:0051059	NF-kappaB binding	PMID:23811396^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q04206	F	part_of:(GO:0018394) occurs_in:(GO:0005634)	Seeded From UniProt	complete
enables	GO:0051059	NF-kappaB binding	PMID:23811396^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19838:PRO_0000030311	F	part_of:(GO:0018394) occurs_in:(GO:0005634)	Seeded From UniProt	complete
involved_in	GO:0018394	peptidyl-lysine acetylation	PMID:23811396^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:1901224) has_input:(UniProtKB:P19838:PRO_0000030311)\|part_of(GO:1901224) has_input:(UniProtKB:Q04206)	Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:23811396^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	part_of:(GO:1901224) has_input:(UniProtKB:P19838:PRO_0000030311) part_of:(GO:0018394)\|part_of:(GO:1901224) has_input:(UniProtKB:Q04206) part_of:(GO:0018394)	Seeded From UniProt	complete
involved_in	GO:1905636	positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding	PMID:23811396^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:1901224) has_regulation_target:(UniProtKB:P19838:PRO_0000030311) regulates_expression_of:(ENSEMBL:ENSG00000089250)\|part_of(GO:1901224) has_regulation_target:(UniProtKB:Q04206) regulates_expression_of:(ENSEMBL:ENSG00000089250)	Seeded From UniProt	complete
involved_in	GO:1901224	positive regulation of NIK/NF-kappaB signaling	PMID:23811396^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:23811396^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	regulates_expression_of:(ENSEMBL:ENSG00000089250) positively_regulates:(GO:0000977) positively_regulates:(GO:0051059)	Seeded From UniProt	complete
involved_in	GO:0030511	positive regulation of transforming growth factor beta receptor signaling pathway	PMID:25514493^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032460	negative regulation of protein oligomerization	PMID:23962722^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P10636-6)	Seeded From UniProt	complete
involved_in	GO:0018394	peptidyl-lysine acetylation	PMID:23962722^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P10636-6) negatively_regulates:(GO:0051259)	Seeded From UniProt	complete
involved_in	GO:0045721	negative regulation of gluconeogenesis	PMID:30193097^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:10362258^[6]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:A0A0G2QC09	C	coincident_with:(ENSEMBL:ENSMUSG00000023067) coincident_with:(CHEBI:4705) coincident_with:(SO:0000167)	Seeded From UniProt	complete
enables	GO:0048156	tau protein binding	PMID:28386764^[7]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:11940591^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0010742	macrophage derived foam cell differentiation	PMID:26504087^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051091	positive regulation of DNA-binding transcription factor activity	PMID:25818647^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045815	positive regulation of gene expression, epigenetic	PMID:25818647^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016573	histone acetylation	PMID:25818647^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:25818647^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	PMID:25818647^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0140066	peptidyl-lysine crotonylation	PMID:25818647^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0140068	histone crotonyltransferase activity	PMID:25818647^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0061920	protein propionyltransferase activity	PMID:17267393^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0061921	peptidyl-lysine propionylation	PMID:17267393^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0140065	peptide butyryltransferase activity	PMID:17267393^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0140067	peptidyl-lysine butyrylation	PMID:17267393^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:26504087^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P40763 UniProtKB:P42224	F		Seeded From UniProt	complete
enables	GO:0097677	STAT family protein binding	PMID:26479788^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P42224	F		Seeded From UniProt	complete
involved_in	GO:0016573	histone acetylation	PMID:27256286^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010976	positive regulation of neuron projection development	PMID:27256286^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045444	fat cell differentiation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:B2RWS6	P		Seeded From UniProt	complete
involved_in	GO:0006473	protein acetylation	PMID:21030595^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034644	cellular response to UV	PMID:24939902^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:24939902^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:24939902^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:24939902^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006473	protein acetylation	PMID:24939902^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	PMID:24939902^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:B2RWS6	P		Seeded From UniProt	complete
involved_in	GO:0006990	positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:B2RWS6	P		Seeded From UniProt	complete
involved_in	GO:0060765	regulation of androgen receptor signaling pathway	PMID:18487222^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0050681	androgen receptor binding	PMID:18487222^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P10275	F		Seeded From UniProt	complete
involved_in	GO:0043923	positive regulation by host of viral transcription	PMID:16687403^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008013	beta-catenin binding	PMID:12408825^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q02248	F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:16687403^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:18487222^[16]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0001102	RNA polymerase II activating transcription factor binding	PMID:20018936^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P18146	F		Seeded From UniProt	complete
involved_in	GO:0090043	regulation of tubulin deacetylation	PMID:18722353^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051091	positive regulation of DNA-binding transcription factor activity	PMID:10518217^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:16325578^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:18722353^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:12586840^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043969	histone H2B acetylation	PMID:23415232^[24]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043967	histone H4 acetylation	PMID:16325578^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043627	response to estrogen	PMID:11581164^[25]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042771	intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator	PMID:17403783^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0035257	nuclear hormone receptor binding	PMID:9862959^[27]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35398	F		Seeded From UniProt	complete
enables	GO:0033613	activating transcription factor binding	PMID:20590529^[28]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q02078	F		Seeded From UniProt	complete
involved_in	GO:0018393	internal peptidyl-lysine acetylation	PMID:17403783^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018076	N-terminal peptidyl-lysine acetylation	PMID:12435739^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016746	transferase activity, transferring acyl groups	PMID:17403783^[26]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:12435739^[29]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:18722353^[20]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:15261140^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q16665	F		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:11349124^[31]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q96PN7	F		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:8684459^[32]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q92831	F		Seeded From UniProt	complete
involved_in	GO:0007623	circadian rhythm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:B2RWS6	P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:9194565^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006475	internal protein amino acid acetylation	PMID:18722353^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	PMID:15261140^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:14645221^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12929931^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9194565^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004468	lysine N-acetyltransferase activity, acting on acetyl phosphate as donor	PMID:20019387^[36]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	PMID:14645221^[34]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	PMID:23415232^[24]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	PMID:12040021^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:12929931^[35]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:12586840^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:12435739^[29]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:17641689^[38]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:9194565^[33]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001666	response to hypoxia	PMID:9887100^[39]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001666	response to hypoxia	PMID:15261140^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	PMID:17641689^[38]	ECO:0000314	direct assay evidence used in manual assertion		F	has_participant:(UniProtKB:P10826)	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:10733570^[40]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:20228809^[41]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:16135789^[42]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:12456660^[43]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:17150957^[44]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0140069	histone butyryltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
involved_in	GO:0140067	peptidyl-lysine butyrylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
enables	GO:0097157	pre-mRNA intronic binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
involved_in	GO:0060325	face morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0051091	positive regulation of DNA-binding transcription factor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0045444	fat cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0036268	swimming	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0035855	megakaryocyte development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0035264	multicellular organism growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	C		Seeded From UniProt	complete
involved_in	GO:0032092	positive regulation of protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
enables	GO:0031490	chromatin DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
involved_in	GO:0030324	lung development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0030220	platelet formation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0030183	B cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0016573	histone acetylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0009887	animal organ morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
involved_in	GO:0007623	circadian rhythm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0007611	learning or memory	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0007519	skeletal muscle tissue development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0007507	heart development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0006990	positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0006473	protein acetylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	C		Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
involved_in	GO:0002209	behavioral defense response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
involved_in	GO:0001966	thigmotaxis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
involved_in	GO:0001756	somitogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	P		Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
enables	GO:0001102	RNA polymerase II activating transcription factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
enables	GO:0001085	RNA polymerase II transcription factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	F		Seeded From UniProt	complete
part_of	GO:0000123	histone acetyltransferase complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B2RWS6 ensembl:ENSMUSP00000066789	C		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
enables	GO:0004402	histone acetyltransferase activity	PMID:10362258^[6] Reactome:R-HSA-3662335	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:10362258^[6]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	has_input:(ENSEMBL:ENSG00000124762) occurs_at:(SO:0000167)	Seeded From UniProt	complete
involved_in	GO:0010506	regulation of autophagy	PMID:24852146^[45]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:27256286^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	positively_regulates:(GO:0021954)	Seeded From UniProt	complete
involved_in	GO:0007399	nervous system development	PMID:27256286^[13] PMID:10205054^[46]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006473	protein acetylation	PMID:22013210^[47]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_direct_input:(UniProtKB:P17861-2)	Seeded From UniProt	complete
involved_in	GO:1904837	beta-catenin-TCF complex assembly	Reactome:R-HSA-201722	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901796	regulation of signal transduction by p53 class mediator	Reactome:R-HSA-5633007	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900034	regulation of cellular response to heat	Reactome:R-HSA-3371571	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061733	peptide-lysine-N-acetyltransferase activity	Reactome:R-NUL-9617757 Reactome:R-HSA-6811508	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0061418	regulation of transcription from RNA polymerase II promoter in response to hypoxia	Reactome:R-HSA-1234174	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051726	regulation of cell cycle	Reactome:R-HSA-156711	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	Reactome:R-HSA-8866907	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045815	positive regulation of gene expression, epigenetic	Reactome:R-HSA-5250924	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045747	positive regulation of Notch signaling pathway	Reactome:R-HSA-9017835	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045652	regulation of megakaryocyte differentiation	Reactome:R-HSA-8936459	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032481	positive regulation of type I interferon production	Reactome:R-HSA-1834949	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016579	protein deubiquitination	Reactome:R-HSA-5688426	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007221	positive regulation of transcription of Notch receptor target	Reactome:R-HSA-9021451	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007219	Notch signaling pathway	Reactome:R-HSA-1980143	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006977	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest	Reactome:R-HSA-6791312	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006283	transcription-coupled nucleotide-excision repair	Reactome:R-HSA-6781827	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-NUL-9617757 Reactome:R-NUL-9617742 Reactome:R-NUL-9617710 Reactome:R-NUL-4396363 Reactome:R-NUL-2065178 Reactome:R-NUL-2064916 Reactome:R-HSA-933536 Reactome:R-HSA-9038163 Reactome:R-HSA-9038052 Reactome:R-HSA-9023884 Reactome:R-HSA-9023860 Reactome:R-HSA-9023840 Reactome:R-HSA-9021451 Reactome:R-HSA-9018499 Reactome:R-HSA-9017835 Reactome:R-HSA-9011981 Reactome:R-HSA-9009371 Reactome:R-HSA-9008285 Reactome:R-HSA-9008271 Reactome:R-HSA-8952058 Reactome:R-HSA-8951977 Reactome:R-HSA-8951966 Reactome:R-HSA-8951951 Reactome:R-HSA-8937050 Reactome:R-HSA-8937037 Reactome:R-HSA-8937016 Reactome:R-HSA-8936979 Reactome:R-HSA-8936621 Reactome:R-HSA-8936616 Reactome:R-HSA-8936481 Reactome:R-HSA-8935740 Reactome:R-HSA-8878237 Reactome:R-HSA-8878220 Reactome:R-HSA-8878056 Reactome:R-HSA-8878050 Reactome:R-HSA-8864307 Reactome:R-HSA-6811508 Reactome:R-HSA-6811479 Reactome:R-HSA-6804383 Reactome:R-HSA-6804379 Reactome:R-HSA-6804242 Reactome:R-HSA-6804229 Reactome:R-HSA-6782234 Reactome:R-HSA-6782227 Reactome:R-HSA-6782224 Reactome:R-HSA-6782211 Reactome:R-HSA-6782208 Reactome:R-HSA-6782204 Reactome:R-HSA-6782141 Reactome:R-HSA-6782138 Reactome:R-HSA-6782131 Reactome:R-HSA-6782069 Reactome:R-HSA-6782004 Reactome:R-HSA-5691381 Reactome:R-HSA-5660666 Reactome:R-HSA-5660660 Reactome:R-HSA-5628871 Reactome:R-HSA-5250938 Reactome:R-HSA-5250930 Reactome:R-HSA-4396402 Reactome:R-HSA-4396401 Reactome:R-HSA-4396393 Reactome:R-HSA-4396392 Reactome:R-HSA-4396379 Reactome:R-HSA-4396371 Reactome:R-HSA-4088162 Reactome:R-HSA-3899291 Reactome:R-HSA-3662335 Reactome:R-HSA-3371554 Reactome:R-HSA-3322427 Reactome:R-HSA-3222093 Reactome:R-HSA-3215152 Reactome:R-HSA-3134883 Reactome:R-HSA-2220971 Reactome:R-HSA-2220964 Reactome:R-HSA-2220957 Reactome:R-HSA-1912394 Reactome:R-HSA-1234167 Reactome:R-HSA-1028820 Reactome:R-HSA-1028819 Reactome:R-HSA-1028817 Reactome:R-HSA-1028815	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002223	stimulatory C-type lectin receptor signaling pathway	Reactome:R-HSA-5621481	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		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
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		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: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: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
part_of	GO:0005694	chromosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0158 UniProtKB-SubCell:SL-0468	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
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P		Seeded From UniProt	complete
edit table

Notes

References

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

↑ Kikuchi, H et al. (2015) Histone acetyltransferase p300/CBP-associated factor is an effective suppressor of secretory immunoglobulin synthesis in immature B cells. Microbiol. Immunol. 59 243-7 PubMed GONUTS page
↑ ^2.00 ^2.01 ^2.02 ^2.03 ^2.04 ^2.05 ^2.06 ^2.07 ^2.08 ^2.09 ^2.10 ^2.11 Li, Y et al. (2013) Role of p300 in regulating neuronal nitric oxide synthase gene expression through nuclear factor-κB-mediated way in neuronal cells. Neuroscience 248 681-9 PubMed GONUTS page
↑ Yang, Y et al. (2015) Pokemon (FBI-1) interacts with Smad4 to repress TGF-β-induced transcriptional responses. Biochim. Biophys. Acta 1849 270-81 PubMed GONUTS page
↑ ^4.0 ^4.1 Cook, C et al. (2014) Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance. Hum. Mol. Genet. 23 104-16 PubMed GONUTS page
↑ Latorre-Muro, P et al. (2018) Dynamic Acetylation of Phosphoenolpyruvate Carboxykinase Toggles Enzyme Activity between Gluconeogenic and Anaplerotic Reactions. Mol. Cell 71 718-732.e9 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Billon, N et al. (1999) Cooperation of Sp1 and p300 in the induction of the CDK inhibitor p21WAF1/CIP1 during NGF-mediated neuronal differentiation. Oncogene 18 2872-82 PubMed GONUTS page
↑ Guo, T et al. (2017) Roles of tau protein in health and disease. Acta Neuropathol. 133 665-704 PubMed GONUTS page
↑ Hoffmeister, A et al. (2002) The HMG-I/Y-related protein p8 binds to p300 and Pax2 trans-activation domain-interacting protein to regulate the trans-activation activity of the Pax2A and Pax2B transcription factors on the glucagon gene promoter. J. Biol. Chem. 277 22314-9 PubMed GONUTS page
↑ ^9.0 ^9.1 Kotla, S & Rao, GN (2015) Reactive Oxygen Species (ROS) Mediate p300-dependent STAT1 Protein Interaction with Peroxisome Proliferator-activated Receptor (PPAR)-γ in CD36 Protein Expression and Foam Cell Formation. J. Biol. Chem. 290 30306-20 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 Sabari, BR et al. (2015) Intracellular crotonyl-CoA stimulates transcription through p300-catalyzed histone crotonylation. Mol. Cell 58 203-15 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Chen, Y et al. (2007) Lysine propionylation and butyrylation are novel post-translational modifications in histones. Mol. Cell Proteomics 6 812-9 PubMed GONUTS page
↑ Zhang, Y et al. (2015) PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection. Nat. Immunol. 16 1215-27 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Hegarty, SV et al. (2016) A Small Molecule Activator of p300/CBP Histone Acetyltransferase Promotes Survival and Neurite Growth in a Cellular Model of Parkinson's Disease. Neurotox Res 30 510-20 PubMed GONUTS page
↑ Chini, CC et al. (2010) HDAC3 is negatively regulated by the nuclear protein DBC1. J. Biol. Chem. 285 40830-7 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 Cazzalini, O et al. (2014) CBP and p300 acetylate PCNA to link its degradation with nucleotide excision repair synthesis. Nucleic Acids Res. 42 8433-48 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Dai, Y et al. (2008) Prohibitin and the SWI/SNF ATPase subunit BRG1 are required for effective androgen antagonist-mediated transcriptional repression of androgen receptor-regulated genes. Carcinogenesis 29 1725-33 PubMed GONUTS page
↑ ^17.0 ^17.1 Mahmoudi, T et al. (2006) The SWI/SNF chromatin-remodeling complex is a cofactor for Tat transactivation of the HIV promoter. J. Biol. Chem. 281 19960-8 PubMed GONUTS page
↑ Daniels, DL & Weis, WI (2002) ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules. Mol. Cell 10 573-84 PubMed GONUTS page
↑ Wang, B et al. (2010) Phosphorylation and acetylation of histone H3 and autoregulation by early growth response 1 mediate interleukin 1beta induction of early growth response 1 transcription. Arterioscler. Thromb. Vasc. Biol. 30 536-45 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 Han, Y et al. (2008) Acetylation of Sirt2 by p300 attenuates its deacetylase activity. Biochem. Biophys. Res. Commun. 375 576-80 PubMed GONUTS page
↑ Shikama, N et al. (1999) A novel cofactor for p300 that regulates the p53 response. Mol. Cell 4 365-76 PubMed GONUTS page
↑ ^22.0 ^22.1 Kang, J et al. (2005) A nuclear function of beta-arrestin1 in GPCR signaling: regulation of histone acetylation and gene transcription. Cell 123 833-47 PubMed GONUTS page
↑ ^23.0 ^23.1 Bragança, J et al. (2003) Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2. J. Biol. Chem. 278 16021-9 PubMed GONUTS page
↑ ^24.0 ^24.1 Tropberger, P et al. (2013) Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer. Cell 152 859-72 PubMed GONUTS page
↑ Yahata, T et al. (2001) Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein. Genes Dev. 15 2598-612 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 Sasaki, T et al. (2007) HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53. Genes Dev. 21 848-61 PubMed GONUTS page
↑ Lau, P et al. (1999) Exogenous expression of a dominant negative RORalpha1 vector in muscle cells impairs differentiation: RORalpha1 directly interacts with p300 and myoD. Nucleic Acids Res. 27 411-20 PubMed GONUTS page
↑ Aude-Garcia, C et al. (2010) Dual roles for MEF2A and MEF2D during human macrophage terminal differentiation and c-Jun expression. Biochem. J. 430 237-44 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 Bradney, C et al. (2003) Regulation of E2A activities by histone acetyltransferases in B lymphocyte development. J. Biol. Chem. 278 2370-6 PubMed GONUTS page
↑ ^30.0 ^30.1 ^30.2 Kung, AL et al. (2004) Small molecule blockade of transcriptional coactivation of the hypoxia-inducible factor pathway. Cancer Cell 6 33-43 PubMed GONUTS page
↑ Gizard, F et al. (2001) A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. J. Biol. Chem. 276 33881-92 PubMed GONUTS page
↑ Yang, XJ et al. (1996) A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382 319-24 PubMed GONUTS page
↑ ^33.0 ^33.1 ^33.2 Lill, NL et al. (1997) Binding and modulation of p53 by p300/CBP coactivators. Nature 387 823-7 PubMed GONUTS page
↑ ^34.0 ^34.1 Curtis, AM et al. (2004) Histone acetyltransferase-dependent chromatin remodeling and the vascular clock. J. Biol. Chem. 279 7091-7 PubMed GONUTS page
↑ ^35.0 ^35.1 Iioka, T et al. (2003) P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain. J. Bone Miner. Res. 18 1419-29 PubMed GONUTS page
↑ Balakrishnan, L et al. (2010) Acetylation of Dna2 endonuclease/helicase and flap endonuclease 1 by p300 promotes DNA stability by creating long flap intermediates. J. Biol. Chem. 285 4398-404 PubMed GONUTS page
↑ Brendel, C et al. (2002) Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism. Mol. Endocrinol. 16 1367-77 PubMed GONUTS page
↑ ^38.0 ^38.1 Lee, HK et al. (2007) MED25 is distinct from TRAP220/MED1 in cooperating with CBP for retinoid receptor activation. EMBO J. 26 3545-57 PubMed GONUTS page
↑ Bhattacharya, S et al. (1999) Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1. Genes Dev. 13 64-75 PubMed GONUTS page
↑ Snowden, AW et al. (2000) A novel transcriptional repression domain mediates p21(WAF1/CIP1) induction of p300 transactivation. Mol. Cell. Biol. 20 2676-86 PubMed GONUTS page
↑ Drost, J et al. (2010) BRD7 is a candidate tumour suppressor gene required for p53 function. Nat. Cell Biol. 12 380-9 PubMed GONUTS page
↑ Chen, LF et al. (2005) NF-kappaB RelA phosphorylation regulates RelA acetylation. Mol. Cell. Biol. 25 7966-75 PubMed GONUTS page
↑ Chen, LF et al. (2002) Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J. 21 6539-48 PubMed GONUTS page
↑ Shen, Y et al. (2007) Functional architecture of atrophins. J. Biol. Chem. 282 5037-44 PubMed GONUTS page
↑ Sebti, S et al. (2014) BAG6/BAT3 modulates autophagy by affecting EP300/p300 intracellular localization. Autophagy 10 1341-2 PubMed GONUTS page
↑ Nakashima, K et al. (1999) Synergistic signaling in fetal brain by STAT3-Smad1 complex bridged by p300. Science 284 479-82 PubMed GONUTS page
↑ Hetz, C et al. (2011) The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91 1219-43 PubMed GONUTS page

[PMID:25644304-1] Kikuchi, H et al. (2015) Histone acetyltransferase p300/CBP-associated factor is an effective suppressor of secretory immunoglobulin synthesis in immature B cells. Microbiol. Immunol. 59 243-7 PubMed GONUTS page

[PMID:23811396-2] 2.00 ^2.01 ^2.02 ^2.03 ^2.04 ^2.05 ^2.06 ^2.07 ^2.08 ^2.09 ^2.10 ^2.11 Li, Y et al. (2013) Role of p300 in regulating neuronal nitric oxide synthase gene expression through nuclear factor-κB-mediated way in neuronal cells. Neuroscience 248 681-9 PubMed GONUTS page

[PMID:25514493-3] Yang, Y et al. (2015) Pokemon (FBI-1) interacts with Smad4 to repress TGF-β-induced transcriptional responses. Biochim. Biophys. Acta 1849 270-81 PubMed GONUTS page

[PMID:23962722-4] 4.0 ^4.1 Cook, C et al. (2014) Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance. Hum. Mol. Genet. 23 104-16 PubMed GONUTS page

[PMID:30193097-5] Latorre-Muro, P et al. (2018) Dynamic Acetylation of Phosphoenolpyruvate Carboxykinase Toggles Enzyme Activity between Gluconeogenic and Anaplerotic Reactions. Mol. Cell 71 718-732.e9 PubMed GONUTS page

[PMID:10362258-6] 6.0 ^6.1 ^6.2 Billon, N et al. (1999) Cooperation of Sp1 and p300 in the induction of the CDK inhibitor p21WAF1/CIP1 during NGF-mediated neuronal differentiation. Oncogene 18 2872-82 PubMed GONUTS page

[PMID:28386764-7] Guo, T et al. (2017) Roles of tau protein in health and disease. Acta Neuropathol. 133 665-704 PubMed GONUTS page

[PMID:11940591-8] Hoffmeister, A et al. (2002) The HMG-I/Y-related protein p8 binds to p300 and Pax2 trans-activation domain-interacting protein to regulate the trans-activation activity of the Pax2A and Pax2B transcription factors on the glucagon gene promoter. J. Biol. Chem. 277 22314-9 PubMed GONUTS page

[PMID:26504087-9] 9.0 ^9.1 Kotla, S & Rao, GN (2015) Reactive Oxygen Species (ROS) Mediate p300-dependent STAT1 Protein Interaction with Peroxisome Proliferator-activated Receptor (PPAR)-γ in CD36 Protein Expression and Foam Cell Formation. J. Biol. Chem. 290 30306-20 PubMed GONUTS page

[PMID:25818647-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 Sabari, BR et al. (2015) Intracellular crotonyl-CoA stimulates transcription through p300-catalyzed histone crotonylation. Mol. Cell 58 203-15 PubMed GONUTS page

[PMID:17267393-11] 11.0 ^11.1 ^11.2 ^11.3 Chen, Y et al. (2007) Lysine propionylation and butyrylation are novel post-translational modifications in histones. Mol. Cell Proteomics 6 812-9 PubMed GONUTS page

[PMID:26479788-12] Zhang, Y et al. (2015) PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection. Nat. Immunol. 16 1215-27 PubMed GONUTS page

[PMID:27256286-13] 13.0 ^13.1 ^13.2 ^13.3 Hegarty, SV et al. (2016) A Small Molecule Activator of p300/CBP Histone Acetyltransferase Promotes Survival and Neurite Growth in a Cellular Model of Parkinson's Disease. Neurotox Res 30 510-20 PubMed GONUTS page

[PMID:21030595-14] Chini, CC et al. (2010) HDAC3 is negatively regulated by the nuclear protein DBC1. J. Biol. Chem. 285 40830-7 PubMed GONUTS page

[PMID:24939902-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 Cazzalini, O et al. (2014) CBP and p300 acetylate PCNA to link its degradation with nucleotide excision repair synthesis. Nucleic Acids Res. 42 8433-48 PubMed GONUTS page

[PMID:18487222-16] 16.0 ^16.1 ^16.2 Dai, Y et al. (2008) Prohibitin and the SWI/SNF ATPase subunit BRG1 are required for effective androgen antagonist-mediated transcriptional repression of androgen receptor-regulated genes. Carcinogenesis 29 1725-33 PubMed GONUTS page

[PMID:16687403-17] 17.0 ^17.1 Mahmoudi, T et al. (2006) The SWI/SNF chromatin-remodeling complex is a cofactor for Tat transactivation of the HIV promoter. J. Biol. Chem. 281 19960-8 PubMed GONUTS page

[PMID:12408825-18] Daniels, DL & Weis, WI (2002) ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules. Mol. Cell 10 573-84 PubMed GONUTS page

[PMID:20018936-19] Wang, B et al. (2010) Phosphorylation and acetylation of histone H3 and autoregulation by early growth response 1 mediate interleukin 1beta induction of early growth response 1 transcription. Arterioscler. Thromb. Vasc. Biol. 30 536-45 PubMed GONUTS page

[PMID:18722353-20] 20.0 ^20.1 ^20.2 ^20.3 Han, Y et al. (2008) Acetylation of Sirt2 by p300 attenuates its deacetylase activity. Biochem. Biophys. Res. Commun. 375 576-80 PubMed GONUTS page

[PMID:10518217-21] Shikama, N et al. (1999) A novel cofactor for p300 that regulates the p53 response. Mol. Cell 4 365-76 PubMed GONUTS page

[PMID:16325578-22] 22.0 ^22.1 Kang, J et al. (2005) A nuclear function of beta-arrestin1 in GPCR signaling: regulation of histone acetylation and gene transcription. Cell 123 833-47 PubMed GONUTS page

[PMID:12586840-23] 23.0 ^23.1 Bragança, J et al. (2003) Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2. J. Biol. Chem. 278 16021-9 PubMed GONUTS page

[PMID:23415232-24] 24.0 ^24.1 Tropberger, P et al. (2013) Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer. Cell 152 859-72 PubMed GONUTS page

[PMID:11581164-25] Yahata, T et al. (2001) Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein. Genes Dev. 15 2598-612 PubMed GONUTS page

[PMID:17403783-26] 26.0 ^26.1 ^26.2 Sasaki, T et al. (2007) HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53. Genes Dev. 21 848-61 PubMed GONUTS page

[PMID:9862959-27] Lau, P et al. (1999) Exogenous expression of a dominant negative RORalpha1 vector in muscle cells impairs differentiation: RORalpha1 directly interacts with p300 and myoD. Nucleic Acids Res. 27 411-20 PubMed GONUTS page

[PMID:20590529-28] Aude-Garcia, C et al. (2010) Dual roles for MEF2A and MEF2D during human macrophage terminal differentiation and c-Jun expression. Biochem. J. 430 237-44 PubMed GONUTS page

[PMID:12435739-29] 29.0 ^29.1 ^29.2 Bradney, C et al. (2003) Regulation of E2A activities by histone acetyltransferases in B lymphocyte development. J. Biol. Chem. 278 2370-6 PubMed GONUTS page

[PMID:15261140-30] 30.0 ^30.1 ^30.2 Kung, AL et al. (2004) Small molecule blockade of transcriptional coactivation of the hypoxia-inducible factor pathway. Cancer Cell 6 33-43 PubMed GONUTS page

[PMID:11349124-31] Gizard, F et al. (2001) A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. J. Biol. Chem. 276 33881-92 PubMed GONUTS page

[PMID:8684459-32] Yang, XJ et al. (1996) A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382 319-24 PubMed GONUTS page

[PMID:9194565-33] 33.0 ^33.1 ^33.2 Lill, NL et al. (1997) Binding and modulation of p53 by p300/CBP coactivators. Nature 387 823-7 PubMed GONUTS page

[PMID:14645221-34] 34.0 ^34.1 Curtis, AM et al. (2004) Histone acetyltransferase-dependent chromatin remodeling and the vascular clock. J. Biol. Chem. 279 7091-7 PubMed GONUTS page

[PMID:12929931-35] 35.0 ^35.1 Iioka, T et al. (2003) P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain. J. Bone Miner. Res. 18 1419-29 PubMed GONUTS page

[PMID:20019387-36] Balakrishnan, L et al. (2010) Acetylation of Dna2 endonuclease/helicase and flap endonuclease 1 by p300 promotes DNA stability by creating long flap intermediates. J. Biol. Chem. 285 4398-404 PubMed GONUTS page

[PMID:12040021-37] Brendel, C et al. (2002) Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism. Mol. Endocrinol. 16 1367-77 PubMed GONUTS page

[PMID:17641689-38] 38.0 ^38.1 Lee, HK et al. (2007) MED25 is distinct from TRAP220/MED1 in cooperating with CBP for retinoid receptor activation. EMBO J. 26 3545-57 PubMed GONUTS page

[PMID:9887100-39] Bhattacharya, S et al. (1999) Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1. Genes Dev. 13 64-75 PubMed GONUTS page

[PMID:10733570-40] Snowden, AW et al. (2000) A novel transcriptional repression domain mediates p21(WAF1/CIP1) induction of p300 transactivation. Mol. Cell. Biol. 20 2676-86 PubMed GONUTS page

[PMID:20228809-41] Drost, J et al. (2010) BRD7 is a candidate tumour suppressor gene required for p53 function. Nat. Cell Biol. 12 380-9 PubMed GONUTS page

[PMID:16135789-42] Chen, LF et al. (2005) NF-kappaB RelA phosphorylation regulates RelA acetylation. Mol. Cell. Biol. 25 7966-75 PubMed GONUTS page

[PMID:12456660-43] Chen, LF et al. (2002) Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J. 21 6539-48 PubMed GONUTS page

[PMID:17150957-44] Shen, Y et al. (2007) Functional architecture of atrophins. J. Biol. Chem. 282 5037-44 PubMed GONUTS page

[PMID:24852146-45] Sebti, S et al. (2014) BAG6/BAT3 modulates autophagy by affecting EP300/p300 intracellular localization. Autophagy 10 1341-2 PubMed GONUTS page

[PMID:10205054-46] Nakashima, K et al. (1999) Synergistic signaling in fetal brain by STAT3-Smad1 complex bridged by p300. Science 284 479-82 PubMed GONUTS page

[PMID:22013210-47] Hetz, C et al. (2011) The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91 1219-43 PubMed GONUTS page

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HUMAN:EP300

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