HUMAN:KAT2B

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	KAT2B (synonyms: PCAF)
Protein Name(s)	Histone acetyltransferase KAT2B Histone acetyltransferase PCAF Histone acetylase PCAF Lysine acetyltransferase 2B P300/CBP-associated factor P/CAF
External Links
UniProt	Q92831
EMBL	U57317 BC060823 BC070075
CCDS	CCDS2634.1
PIR	S71788
RefSeq	NP_003875.3
UniGene	Hs.533055
PDB	1CM0 1JM4 1N72 1WUG 1WUM 1ZS5 2RNW 2RNX 3GG3 4NSQ
PDBsum	1CM0 1JM4 1N72 1WUG 1WUM 1ZS5 2RNW 2RNX 3GG3 4NSQ
ProteinModelPortal	Q92831
SMR	Q92831
BioGrid	114375
DIP	DIP-29778N
IntAct	Q92831
MINT	MINT-150079
STRING	9606.ENSP00000263754
BindingDB	Q92831
ChEMBL	CHEMBL5500
GuidetoPHARMACOLOGY	2737
PhosphoSite	Q92831
DMDM	83287776
REPRODUCTION-2DPAGE	Q92831
MaxQB	Q92831
PaxDb	Q92831
PRIDE	Q92831
GeneID	8850
KEGG	hsa:8850
UCSC	uc003cbq.3
CTD	8850
GeneCards	GC03P020081
HGNC	HGNC:8638
HPA	CAB004526
MIM	602303
neXtProt	NX_Q92831
PharmGKB	PA162392705
eggNOG	COG5076
GeneTree	ENSGT00760000119099
HOGENOM	HOG000007151
InParanoid	Q92831
KO	K06062
OMA	KIMMWLV
OrthoDB	EOG7ZKS9B
PhylomeDB	Q92831
TreeFam	TF105399
Reactome	REACT_118568 REACT_118713 REACT_118780 REACT_14835 REACT_160243 REACT_160254 REACT_172610 REACT_953
ChiTaRS	KAT2B
EvolutionaryTrace	Q92831
GeneWiki	PCAF
GenomeRNAi	8850
NextBio	33221
PRO	PR:Q92831
Proteomes	UP000005640
Bgee	Q92831
CleanEx	HS_KAT2B
Genevestigator	Q92831
GO	GO:0031672 GO:0042641 GO:0005671 GO:0031674 GO:0000776 GO:0005654 GO:0005634 GO:0000125 GO:0016407 GO:0004861 GO:0004402 GO:0042826 GO:0004468 GO:0032403 GO:0019901 GO:0003713 GO:0003712 GO:0008134 GO:0007050 GO:0032869 GO:0006325 GO:0006338 GO:0010467 GO:0043966 GO:0043970 GO:0018393 GO:0018076 GO:0008285 GO:0045736 GO:0007219 GO:0018394 GO:0045722 GO:0045944 GO:0006473 GO:0010835 GO:0048511 GO:0006360 GO:0006361 GO:0006367 GO:0016032
Gene3D	1.20.920.10 3.40.630.30
InterPro	IPR016181 IPR001487 IPR018359 IPR000182 IPR016376 IPR009464
Pfam	PF13508 PF00439 PF06466
PIRSF	PIRSF003048
PRINTS	PR00503
SMART	SM00297
SUPFAM	SSF47370 SSF55729
PROSITE	PS00633 PS50014 PS51186

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:16829519^[1]	ECO:0000315			F		Figure 4 demonstrates that PCAF-mediates acetylation of PTEN lysines 125 and 128.	complete CACAO 2102
involved_in	GO:0060173	limb development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q1LUC3	P		Seeded From UniProt	complete
involved_in	GO:0007507	heart development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q1LUC3	P		Seeded From UniProt	complete
involved_in	GO:0046600	negative regulation of centriole replication	PMID:27796307^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005813	centrosome	PMID:27796307^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:27796307^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0018393	internal peptidyl-lysine acetylation	PMID:27796307^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061733	peptide-lysine-N-acetyltransferase activity	PMID:27796307^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0018393	internal peptidyl-lysine acetylation	PMID:29174768^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061733	peptide-lysine-N-acetyltransferase activity	PMID:29174768^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:15273251^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:15273251^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006473	protein acetylation	PMID:15273251^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9JHD1	F		Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:17301242^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:17301242^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P28033	F		Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	PMID:16829519^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:17505058^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H6U6	F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:19470756^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043966	histone H3 acetylation	PMID:18838386^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032869	cellular response to insulin stimulus	PMID:19303849^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018394	peptidyl-lysine acetylation	PMID:19303849^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018394	peptidyl-lysine acetylation	PMID:19470756^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P09874)	Seeded From UniProt	complete
involved_in	GO:0010835	regulation of protein ADP-ribosylation	PMID:19470756^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005671	Ada2/Gcn5/Ada3 transcription activator complex	PMID:18838386^[8]	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:19303849^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004468	lysine N-acetyltransferase activity, acting on acetyl phosphate as donor	PMID:19470756^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	has_input:(UniProtKB:P09874)	Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	PMID:12887892^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8IXJ6	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:17707232^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P52732,UniProtKB:P98175,UniProtKB:Q5VVJ2	C		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9JHD1	F		Seeded From UniProt	complete
involved_in	GO:0018393	internal peptidyl-lysine acetylation	PMID:23932781^[12]	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^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016407	acetyltransferase activity	PMID:8684459^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	PMID:8684459^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:15509593^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35680-1	F		Seeded From UniProt	complete
involved_in	GO:0006338	chromatin remodeling	PMID:17707232^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006338	chromatin remodeling	PMID:10365964^[16]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9JHD1	C		Seeded From UniProt	complete
enables	GO:0004861	cyclin-dependent protein serine/threonine kinase inhibitor activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9JHD1	F		Seeded From UniProt	complete
enables	GO:0004468	lysine N-acetyltransferase activity, acting on acetyl phosphate as donor	PMID:23932781^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004468	lysine N-acetyltransferase activity, acting on acetyl phosphate as donor	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9JHD1	F		Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	PMID:14645221^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:14645221^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:12435739^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003712	transcription coregulator activity	PMID:8684459^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q92793	F		Seeded From UniProt	complete
enables	GO:0003712	transcription coregulator activity	PMID:8684459^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q09472	F		Seeded From UniProt	complete
part_of	GO:0000125	PCAF complex	PMID:17707232^[11]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	PMID:23555303^[18]	ECO:0000269	experimental evidence used in manual assertion		F		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:Q9JHD1 ensembl:ENSMUSP00000000724	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:Q9JHD1 ensembl:ENSMUSP00000000724	P		Seeded From UniProt	complete
involved_in	GO:0045736	negative regulation of cyclin-dependent protein serine/threonine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	P		Seeded From UniProt	complete
involved_in	GO:0043970	histone H3-K9 acetylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	P		Seeded From UniProt	complete
part_of	GO:0042641	actomyosin	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	C		Seeded From UniProt	complete
involved_in	GO:0035948	positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	P		Seeded From UniProt	complete
part_of	GO:0031674	I band	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	C		Seeded From UniProt	complete
part_of	GO:0031672	A band	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	C		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	F		Seeded From UniProt	complete
involved_in	GO:0018393	internal peptidyl-lysine acetylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	P		Seeded From UniProt	complete
involved_in	GO:0016573	histone acetylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	C		Seeded From UniProt	complete
enables	GO:0004861	cyclin-dependent protein serine/threonine kinase inhibitor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	F		Seeded From UniProt	complete
enables	GO:0004468	lysine N-acetyltransferase activity, acting on acetyl phosphate as donor	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	F		Seeded From UniProt	complete
enables	GO:0004402	histone acetyltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	F		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	F		Seeded From UniProt	complete
enables	GO:0000977	RNA polymerase II regulatory region sequence-specific DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	F		Seeded From UniProt	complete
part_of	GO:0000776	kinetochore	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	C		Seeded From UniProt	complete
part_of	GO:0000123	histone acetyltransferase complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9JHD1 ensembl:ENSMUSP00000000724	C		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:IPR009464 InterPro:IPR016376 InterPro:IPR037800	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:IPR009464 InterPro:IPR016376	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:IPR009464 InterPro:IPR016376	P		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:IPR016376	P		Seeded From UniProt	complete
enables	GO:0004145	diamine N-acetyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.57	F		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:0007050	cell cycle arrest	PMID:8684459^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006473	protein acetylation	PMID:8684459^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006338	chromatin remodeling	PMID:8684459^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10891508^[19]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		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: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:0006367	transcription initiation from RNA polymerase II promoter	Reactome:R-HSA-350054 Reactome:R-HSA-2032785	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-4396363 Reactome:R-NUL-2065178 Reactome:R-NUL-2064916 Reactome:R-HSA-9620515 Reactome:R-HSA-9023860 Reactome:R-HSA-9021451 Reactome:R-HSA-9017835 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-5691381 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-2220971 Reactome:R-HSA-2220964 Reactome:R-HSA-2220957 Reactome:R-HSA-212356 Reactome:R-HSA-2032794 Reactome:R-HSA-1912394	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		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
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
part_of	GO:0005856	cytoskeleton	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206	C		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
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:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		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
part_of	GO:0005815	microtubule organizing center	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0048	C		Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 Okumura, K et al. (2006) PCAF modulates PTEN activity. J. Biol. Chem. 281 26562-8 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Fournier, M et al. (2016) KAT2A/KAT2B-targeted acetylome reveals a role for PLK4 acetylation in preventing centrosome amplification. Nat Commun 7 13227 PubMed GONUTS page
↑ ^3.0 ^3.1 Ghosh, TK et al. (2018) Acetylation of TBX5 by KAT2B and KAT2A regulates heart and limb development. J. Mol. Cell. Cardiol. 114 185-198 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Zhao, Q et al. (2004) Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1. J. Biol. Chem. 279 41477-86 PubMed GONUTS page
↑ ^5.0 ^5.1 Wiper-Bergeron, N et al. (2007) Glucocorticoid-stimulated preadipocyte differentiation is mediated through acetylation of C/EBPbeta by GCN5. Proc. Natl. Acad. Sci. U.S.A. 104 2703-8 PubMed GONUTS page
↑ Gururaj, AE et al. (2007) Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1). Mol. Endocrinol. 21 1847-60 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Rajamohan, SB et al. (2009) SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1. Mol. Cell. Biol. 29 4116-29 PubMed GONUTS page
↑ ^8.0 ^8.1 Wang, YL et al. (2008) Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein. J. Biol. Chem. 283 33808-15 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Wong, RH et al. (2009) A role of DNA-PK for the metabolic gene regulation in response to insulin. Cell 136 1056-72 PubMed GONUTS page
↑ Fulco, M et al. (2003) Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol. Cell 12 51-62 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Zhu, P et al. (2007) A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation. Mol. Cell 27 609-21 PubMed GONUTS page
↑ ^12.0 ^12.1 Lin, R et al. (2013) Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth. Mol. Cell 51 506-18 PubMed GONUTS page
↑ ^13.0 ^13.1 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
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 ^14.6 Yang, XJ et al. (1996) A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382 319-24 PubMed GONUTS page
↑ 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
↑ Dhalluin, C et al. (1999) Structure and ligand of a histone acetyltransferase bromodomain. Nature 399 491-6 PubMed GONUTS page
↑ ^17.0 ^17.1 Curtis, AM et al. (2004) Histone acetyltransferase-dependent chromatin remodeling and the vascular clock. J. Biol. Chem. 279 7091-7 PubMed GONUTS page
↑ Sarshad, A et al. (2013) Nuclear myosin 1c facilitates the chromatin modifications required to activate rRNA gene transcription and cell cycle progression. PLoS Genet. 9 e1003397 PubMed GONUTS page
↑ Cotter, MA 2nd & Robertson, ES (2000) Modulation of histone acetyltransferase activity through interaction of epstein-barr nuclear antigen 3C with prothymosin alpha. Mol. Cell. Biol. 20 5722-35 PubMed GONUTS page

[PMID:16829519-1] 1.0 ^1.1 Okumura, K et al. (2006) PCAF modulates PTEN activity. J. Biol. Chem. 281 26562-8 PubMed GONUTS page

[PMID:27796307-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Fournier, M et al. (2016) KAT2A/KAT2B-targeted acetylome reveals a role for PLK4 acetylation in preventing centrosome amplification. Nat Commun 7 13227 PubMed GONUTS page

[PMID:29174768-3] 3.0 ^3.1 Ghosh, TK et al. (2018) Acetylation of TBX5 by KAT2B and KAT2A regulates heart and limb development. J. Mol. Cell. Cardiol. 114 185-198 PubMed GONUTS page

[PMID:15273251-4] 4.0 ^4.1 ^4.2 Zhao, Q et al. (2004) Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1. J. Biol. Chem. 279 41477-86 PubMed GONUTS page

[PMID:17301242-5] 5.0 ^5.1 Wiper-Bergeron, N et al. (2007) Glucocorticoid-stimulated preadipocyte differentiation is mediated through acetylation of C/EBPbeta by GCN5. Proc. Natl. Acad. Sci. U.S.A. 104 2703-8 PubMed GONUTS page

[PMID:17505058-6] Gururaj, AE et al. (2007) Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1). Mol. Endocrinol. 21 1847-60 PubMed GONUTS page

[PMID:19470756-7] 7.0 ^7.1 ^7.2 ^7.3 Rajamohan, SB et al. (2009) SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1. Mol. Cell. Biol. 29 4116-29 PubMed GONUTS page

[PMID:18838386-8] 8.0 ^8.1 Wang, YL et al. (2008) Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein. J. Biol. Chem. 283 33808-15 PubMed GONUTS page

[PMID:19303849-9] 9.0 ^9.1 ^9.2 Wong, RH et al. (2009) A role of DNA-PK for the metabolic gene regulation in response to insulin. Cell 136 1056-72 PubMed GONUTS page

[PMID:12887892-10] Fulco, M et al. (2003) Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol. Cell 12 51-62 PubMed GONUTS page

[PMID:17707232-11] 11.0 ^11.1 ^11.2 Zhu, P et al. (2007) A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation. Mol. Cell 27 609-21 PubMed GONUTS page

[PMID:23932781-12] 12.0 ^12.1 Lin, R et al. (2013) Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth. Mol. Cell 51 506-18 PubMed GONUTS page

[PMID:12435739-13] 13.0 ^13.1 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:8684459-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 ^14.6 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:15509593-15] 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:10365964-16] Dhalluin, C et al. (1999) Structure and ligand of a histone acetyltransferase bromodomain. Nature 399 491-6 PubMed GONUTS page

[PMID:14645221-17] 17.0 ^17.1 Curtis, AM et al. (2004) Histone acetyltransferase-dependent chromatin remodeling and the vascular clock. J. Biol. Chem. 279 7091-7 PubMed GONUTS page

[PMID:23555303-18] Sarshad, A et al. (2013) Nuclear myosin 1c facilitates the chromatin modifications required to activate rRNA gene transcription and cell cycle progression. PLoS Genet. 9 e1003397 PubMed GONUTS page

[PMID:10891508-19] Cotter, MA 2nd & Robertson, ES (2000) Modulation of histone acetyltransferase activity through interaction of epstein-barr nuclear antigen 3C with prothymosin alpha. Mol. Cell. Biol. 20 5722-35 PubMed GONUTS page

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HUMAN:KAT2B

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