HUMAN:KAT2B

From GONUTS

Jump to: navigation, search

Species (Taxon ID)	Homo sapiens (Human). ([1])
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
EMBL	U57317 BC060823 BC070075
IPI	IPI00022055
PIR	S71788
RefSeq	NP_003875.3
UniGene	Hs.533055
PDB	1CM0 1JM4 1N72 1WUG 1WUM 1ZS5 2RNW 2RNX 3GG3
PDBsum	1CM0 1JM4 1N72 1WUG 1WUM 1ZS5 2RNW 2RNX 3GG3
ProteinModelPortal	Q92831
SMR	Q92831
DIP	DIP-29778N
IntAct	Q92831
MINT	MINT-150079
STRING	Q92831
PhosphoSite	Q92831
REPRODUCTION-2DPAGE	Q92831
PRIDE	Q92831
Ensembl	ENST00000263754
GeneID	8850
KEGG	hsa:8850
UCSC	uc003cbq.1
CTD	8850
GeneCards	GC03P020021
H-InvDB	HIX0003121
HGNC	HGNC:8638
HPA	CAB004526
MIM	602303
neXtProt	NX_Q92831
PharmGKB	PA162392705
eggNOG	prNOG11279
GeneTree	ENSGT00430000030976
InParanoid	Q92831
OMA	YSACKAE
OrthoDB	EOG4F1X2G
PhylomeDB	Q92831
Pathway_Interaction_DB	foxopathway ar_tf_pathway smad2_3nuclearpathway retinoic_acid_pathway hdac_classi_pathway hdac_classiii_pathway
Reactome	REACT_1788 REACT_71
NextBio	33221
ArrayExpress	Q92831
Bgee	Q92831
CleanEx	HS_KAT2B
Genevestigator	Q92831
GermOnline	ENSG00000114166
GO	GO:0005671 GO:0016585 GO:0000125 GO:0004861 GO:0004402 GO:0042826 GO:0019901 GO:0003713 GO:0008134 GO:0007050 GO:0032869 GO:0006338 GO:0043966 GO:0044419 GO:0018076 GO:0008285 GO:0006361
InterPro	IPR000182 IPR016181 IPR001487 IPR018359 IPR016376 IPR009464
Gene3D	G3DSA:3.40.630.30 G3DSA:1.20.920.10
Pfam	PF00583 PF00439 PF06466
PIRSF	PIRSF003048
PRINTS	PR00503
SMART	SM00297
SUPFAM	SSF55729 SSF47370
PROSITE	PS00633 PS50014 PS51186

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0000123	histone acetyltransferase complex	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	C	Seeded From UniProt
	GO:0000125	PCAF complex	PMID:18669648^[1]	NAS: Non-traceable Author Statement		C	Seeded From UniProt
	GO:0000776	kinetochore	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	C	Seeded From UniProt
	GO:0003712	transcription cofactor activity	PMID:8684459^[2]	IPI: Inferred from Physical Interaction	UniProtKB:Q09472	F	Seeded From UniProt
	GO:0003712	transcription cofactor activity	PMID:8684459^[2]	IPI: Inferred from Physical Interaction	UniProtKB:Q92793	F	Seeded From UniProt
	GO:0003713	transcription coactivator activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	F	Seeded From UniProt
	GO:0003713	transcription coactivator activity	PMID:12435739^[3]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0004402	histone acetyltransferase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR009464	F	Seeded From UniProt
	GO:0004402	histone acetyltransferase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016376	F	Seeded From UniProt
	GO:0004402	histone acetyltransferase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:2.3.1.48	F	Seeded From UniProt
	GO:0004402	histone acetyltransferase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	F	Seeded From UniProt
	GO:0004468	lysine N-acetyltransferase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	F	Seeded From UniProt
	GO:0004468	lysine N-acetyltransferase activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q9JHD1	F	Seeded From UniProt
	GO:0004468	lysine N-acetyltransferase activity	PMID:19303849^[4]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0004861	cyclin-dependent protein kinase inhibitor activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	F	Seeded From UniProt
	GO:0004861	cyclin-dependent protein kinase inhibitor activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q9JHD1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11568182^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q03112	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:12435739^[3]	IPI: Inferred from Physical Interaction	UniProtKB:P15923-2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:12887892^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q8IXJ6	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16332960^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q9EPK5	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16543236^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q16665	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18504427^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q15672	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19303849^[4]	IPI: Inferred from Physical Interaction	UniProtKB:P22415	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:8684459^[2]	IPI: Inferred from Physical Interaction	UniProtKB:Q09472	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:8684459^[2]	IPI: Inferred from Physical Interaction	UniProtKB:Q92793	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9674425^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q16594	F	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR009464	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016376	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000058599	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q9JHD1	C	Seeded From UniProt
	GO:0005634	nucleus	PMID:10891508^[11]	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005654	nucleoplasm	Reactome:REACT_14814	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005654	nucleoplasm	Reactome:REACT_2113	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005671	Ada2/Gcn5/Ada3 transcription activator complex	PMID:18838386^[12]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0006338	chromatin remodeling	PMID:10365964^[13]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0006338	chromatin remodeling	PMID:8684459^[2]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0006351	transcription, DNA-dependent	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0804	P	Seeded From UniProt
	GO:0006355	regulation of transcription, DNA-dependent	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR009464	P	Seeded From UniProt
	GO:0006355	regulation of transcription, DNA-dependent	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016376	P	Seeded From UniProt
	GO:0006355	regulation of transcription, DNA-dependent	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0805	P	Seeded From UniProt
	GO:0006360	transcription from RNA polymerase I promoter	Reactome:REACT_1309	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0006361	transcription initiation from RNA polymerase I promoter	Reactome:REACT_1974	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0006361	transcription initiation from RNA polymerase I promoter	Reactome:REACT_953	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0006473	protein acetylation	PMID:8684459^[2]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007049	cell cycle	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0131	P	Seeded From UniProt
	GO:0007050	cell cycle arrest	PMID:8684459^[2]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0008080	N-acetyltransferase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000182	F	Seeded From UniProt
	GO:0008134	transcription factor binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000058599	F	Seeded From UniProt
	GO:0008134	transcription factor binding	PMID:15509593^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P35680-1	F	Seeded From UniProt
	GO:0008152	metabolic process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000182	P	Seeded From UniProt
	GO:0008285	negative regulation of cell proliferation	PMID:8684459^[2]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0010467	gene expression	Reactome:REACT_71	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0016407	acetyltransferase activity	PMID:8684459^[2]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0016573	histone acetylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016376	P	Seeded From UniProt
	GO:0016573	histone acetylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	P	Seeded From UniProt
	GO:0016585	chromatin remodeling complex	PMID:18669648^[1]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0016740	transferase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0808	F	Seeded From UniProt
	GO:0016746	transferase activity, transferring acyl groups	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0012	F	Seeded From UniProt
	GO:0018076	N-terminal peptidyl-lysine acetylation	PMID:12435739^[3]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0018393	internal peptidyl-lysine acetylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	P	Seeded From UniProt
	GO:0018394	peptidyl-lysine acetylation	PMID:19303849^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0019901	protein kinase binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	F	Seeded From UniProt
	GO:0019901	protein kinase binding	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q9JHD1	F	Seeded From UniProt
	GO:0031672	A band	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	C	Seeded From UniProt
	GO:0031674	I band	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	C	Seeded From UniProt
	GO:0032869	cellular response to insulin stimulus	PMID:19303849^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0042641	actomyosin	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	C	Seeded From UniProt
	GO:0042826	histone deacetylase binding	PMID:12887892^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q8IXJ6	F	Seeded From UniProt
	GO:0043966	histone H3 acetylation	PMID:18838386^[12]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0044419	interspecies interaction between organisms	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0945	P	Seeded From UniProt
	GO:0045736	negative regulation of cyclin-dependent protein kinase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	P	Seeded From UniProt
	GO:0045893	positive regulation of transcription, DNA-dependent	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	P	Seeded From UniProt
	GO:0045944	positive regulation of transcription from RNA polymerase II promoter	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000000724	P	Seeded From UniProt
	GO:0004402	histone acetyltransferase activity	PMID:16829519^[15]	IMP: Inferred from Mutant Phenotype		F	Figure 4 demonstrates that PCAF-mediates acetylation of PTEN lysines 125 and 128.	complete

edit table

Notes

References

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

↑ ^1.0 ^1.1 Dephoure N et al. (2008) A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A 105: 10762-7 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 ^2.8 Yang XJ et al. (1996) A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382: 319-24 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 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
↑ ^4.0 ^4.1 ^4.2 ^4.3 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
↑ Chakraborty S et al. (2001) Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles. J Biol Chem 276: 44936-43 PubMed GONUTS page
↑ ^6.0 ^6.1 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
↑ Murakami M et al. (2005) A WW domain protein TAZ is a critical coactivator for TBX5, a transcription factor implicated in Holt-Oram syndrome. Proc Natl Acad Sci U S A 102: 18034-9 PubMed GONUTS page
↑ Fath DM et al. (2006) Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha. J Biol Chem 281: 13612-9 PubMed GONUTS page
↑ Shiota M et al. (2008) Twist and p53 reciprocally regulate target genes via direct interaction. Oncogene 27: 5543-53 PubMed GONUTS page
↑ Ogryzko VV et al. (1998) Histone-like TAFs within the PCAF histone acetylase complex. Cell 94: 35-44 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
↑ ^12.0 ^12.1 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
↑ Dhalluin C et al. (1999) Structure and ligand of a histone acetyltransferase bromodomain. Nature 399: 491-6 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
↑ Okumura K et al. (2006) PCAF modulates PTEN activity. J Biol Chem 281: 26562-8 PubMed GONUTS page

[PMID:18669648-0] 1.0 ^1.1 Dephoure N et al. (2008) A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A 105: 10762-7 PubMed GONUTS page

[PMID:8684459-1] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 ^2.8 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:12435739-2] 3.0 ^3.1 ^3.2 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:19303849-3] 4.0 ^4.1 ^4.2 ^4.3 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:11568182-4] Chakraborty S et al. (2001) Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles. J Biol Chem 276: 44936-43 PubMed GONUTS page

[PMID:12887892-5] 6.0 ^6.1 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:16332960-6] Murakami M et al. (2005) A WW domain protein TAZ is a critical coactivator for TBX5, a transcription factor implicated in Holt-Oram syndrome. Proc Natl Acad Sci U S A 102: 18034-9 PubMed GONUTS page

[PMID:16543236-7] Fath DM et al. (2006) Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha. J Biol Chem 281: 13612-9 PubMed GONUTS page

[PMID:18504427-8] Shiota M et al. (2008) Twist and p53 reciprocally regulate target genes via direct interaction. Oncogene 27: 5543-53 PubMed GONUTS page

[PMID:9674425-9] Ogryzko VV et al. (1998) Histone-like TAFs within the PCAF histone acetylase complex. Cell 94: 35-44 PubMed GONUTS page

[PMID:10891508-10] 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:18838386-11] 12.0 ^12.1 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:10365964-12] Dhalluin C et al. (1999) Structure and ligand of a histone acetyltransferase bromodomain. Nature 399: 491-6 PubMed GONUTS page

[PMID:15509593-13] 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:16829519-14] Okumura K et al. (2006) PCAF modulates PTEN activity. J Biol Chem 281: 26562-8 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

HUMAN:KAT2B

Contents

Annotations

Notes

References

a

c

g

h

h cont.

i

k

l

m

n

p

p cont.

r

t

Personal tools

Namespaces

Variants

Views

Actions

Search

Navigation

Cacao

Journal Clubs

page contributors

Toolbox