Reviewed, UniProtKB/Swiss-Prot Q92831 (KAT2B_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase KAT2B
    EC=2.3.1.48
Alternative name(s):
    Lysine acetyltransferase 2B
    Histone acetyltransferase PCAF
      Short name=Histone acetylase PCAF
    P300/CBP-associated factor
      Short name=P/CAF

Gene names

Name:	KAT2B
Synonyms:	PCAF

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	832 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Ref.1 Ref.7
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Interacts with SIRT1 By similarity. Interacts with EP300 and CREBBP. Interacts with NCOA1 and NCOA3. Component of a large chromatin remodeling complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and KIF11/TRIP5. Binds to HTLV-1 Tax. Interacts with and acetylates HIV-1 Tat. Interacts with KLF1; the interaction does not acetylate KLF1 and there is no enhancement of its transactivational activity. Interacts with NFE4. Interacts with MECOM. Ref.1 Ref.7 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12
Subcellular location	Nucleus By similarity UniProtKB Q92830.
Tissue specificity	Ubiquitously expressed but most abundant in heart and skeletal muscle. Ref.1
Domain	The bromodomain mediates binding to HIV-1 Tat.
Sequence similarities	Belongs to the GCN5 family. Contains 1 bromo domain. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Biological process	Cell cycle Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Bromodomain
Molecular function	Acyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	N-terminal peptidyl-lysine acetylation Inferred from direct assay. Source: UniProtKB cell cycle arrest Ref.1 Traceable author statement. Source: ProtInc cellular response to insulin stimulus Inferred from direct assay. Source: UniProtKB chromatin remodeling Ref.1 Ref.15 Non-traceable author statement. Source: UniProtKB histone acetylation Inferred from electronic annotation. Source: InterPro interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell proliferation Ref.1 Inferred from direct assay. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	PCAF complex Non-traceable author statement. Source: UniProtKB chromatin remodeling complex Inferred from direct assay. Source: UniProtKB
Molecular function	cyclin-dependent protein kinase inhibitor activity Inferred from sequence or structural similarity. Source: UniProtKB histone acetyltransferase activity Inferred from electronic annotation. Source: EC histone deacetylase binding Inferred from physical interaction. Source: UniProtKB protein kinase binding Inferred from sequence or structural similarity. Source: UniProtKB transcription coactivator activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CREBBP	Q92793	2	EBI-477430,EBI-81215
EP300	Q09472	2	EBI-477430,EBI-447295
GATAD2A	Q86YP4	1	EBI-477430,EBI-726224
GATAD2B	Q8WXI9	1	EBI-477430,EBI-923440
HIF1A	Q16665	2	EBI-477430,EBI-447269
His3	P02299	1	EBI-477430,EBI-522090	From a different organism.
His4	P84040	1	EBI-477430,EBI-185028	From a different organism.
SIRT2	Q8IXJ6	2	EBI-477430,EBI-477232
TAF9	Q16594	1	EBI-477430,EBI-712521
Wwtr1	Q9EPK5	1	EBI-477430,EBI-1211920	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 832

832

Histone acetyltransferase KAT2B

PRO_0000211208

Regions

Domain

503 – 651

149

N-acetyltransferase UniProtKB Q92830

Domain

740 – 810

71

Bromo

Amino acid modifications

Modified residue

40

1

Phosphoserine By similarity

Modified residue

729

1

Phosphotyrosine Ref.13

Modified residue

733

1

N6-acetyllysine Ref.14

Natural variations

Natural variant

386

1

N → S: dbSNP rs17006625.

VAR_034372

Experimental info

Mutagenesis

752

1

V → A: Reduced acetyl-lysine binding. Ref.15

Mutagenesis

760

1

Y → A: Reduced acetyl-lysine binding. Ref.15

Mutagenesis

802

1

Y → A: Reduced acetyl-lysine binding. Ref.15

Mutagenesis

809

1

Y → A: Complete loss of acetyl-lysine binding. Ref.15

Sequence conflict

804 – 805

2

PP → AA in AAC50890. Ref.1

Secondary structure

1

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832

Helix Strand Turn

Details...

Beta strand

494 – 499

6

Beta strand

503 – 505

3

Helix

509 – 525

17

Helix

531 – 538

8

Beta strand

544 – 550

7

Beta strand

553 – 563

11

Turn

564 – 567

4

Beta strand

568 – 576

9

Helix

578 – 580

3

Beta strand

582 – 584

3

Helix

585 – 599

15

Beta strand

604 – 609

6

Turn

611 – 613

3

Helix

614 – 619

6

Beta strand

623 – 625

3

Helix

630 – 633

4

Beta strand

643 – 649

7

Helix

725 – 741

17

Helix

746 – 748

3

Beta strand

754 – 759

6

Helix

760 – 763

4

Helix

772 – 777

6

Turn

778 – 780

3

Helix

786 – 801

16

Helix

809 – 827

19

Beta strand

828 – 830

3

Sequences

	Sequence		Length	Mass (Da)
	Q92831-1 [UniParc]. Last modified May 10, 2005. Version 3. Checksum: 72F516E8BC00CC0C	FASTA	832	93,013
	10 20 30 40 50 60 MSEAGGAGPG GCGAGAGAGA GPGALPPQPA ALPPAPPQGS PCAAAAGGSG ACGPATAVAA 70 80 90 100 110 120 AGTAEGPGGG GSARIAVKKA QLRSAPRAKK LEKLGVYSAC KAEESCKCNG WKNPNPSPTP 130 140 150 160 170 180 PRADLQQIIV SLTESCRSCS HALAAHVSHL ENVSEEEMNR LLGIVLDVEY LFTCVHKEED 190 200 210 220 230 240 ADTKQVYFYL FKLLRKSILQ RGKPVVEGSL EKKPPFEKPS IEQGVNNFVQ YKFSHLPAKE 250 260 270 280 290 300 RQTIVELAKM FLNRINYWHL EAPSQRRLRS PNDDISGYKE NYTRWLCYCN VPQFCDSLPR 310 320 330 340 350 360 YETTQVFGRT LLRSVFTVMR RQLLEQARQE KDKLPLEKRT LILTHFPKFL SMLEEEVYSQ 370 380 390 400 410 420 NSPIWDQDFL SASSRTSQLG IQTVINPPPV AGTISYNSTS SSLEQPNAGS SSPACKASSG 430 440 450 460 470 480 LEANPGEKRK MTDSHVLEEA KKPRVMGDIP MELINEVMST ITDPAAMLGP ETNFLSAHSA 490 500 510 520 530 540 RDEAARLEER RGVIEFHVVG NSLNQKPNKK ILMWLVGLQN VFSHQLPRMP KEYITRLVFD 550 560 570 580 590 600 PKHKTLALIK DGRVIGGICF RMFPSQGFTE IVFCAVTSNE QVKGYGTHLM NHLKEYHIKH 610 620 630 640 650 660 DILNFLTYAD EYAIGYFKKQ GFSKEIKIPK TKYVGYIKDY EGATLMGCEL NPRIPYTEFS 670 680 690 700 710 720 VIIKKQKEII KKLIERKQAQ IRKVYPGLSC FKDGVRQIPI ESIPGIRETG WKPSGKEKSK 730 740 750 760 770 780 EPRDPDQLYS TLKSILQQVK SHQSAWPFME PVKRTEAPGY YEVIRFPMDL KTMSERLKNR 790 800 810 820 830 YYVSKKLFMA DLQRVFTNCK EYNPPESEYY KCANILEKFF FSKIKEAGLI DK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A." Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y. Nature 382:319-324(1996) [PubMed: 8684459] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH EP300 AND CREBBP. Tissue: Liver.
[2]	Nakatani Y. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Tissue: Liver.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The transcriptional coactivators p300 and CBP are histone acetyltransferases." Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y. Cell 87:953-959(1996) [PubMed: 8945521] [Abstract] Cited for: ENZYME ACTIVITY.
[5]	"TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1." Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W. J. Biol. Chem. 272:27629-27634(1997) [PubMed: 9346901] [Abstract] Cited for: INTERACTION WITH NCOA3.
[6]	"Steroid receptor coactivator-1 is a histone acetyltransferase." Spencer T.E., Jenster G., Burcin M.M., Allis C.D., Zhou J., Mizzen C.A., McKenna N.J., Onate S.A., Tsai S.Y., Tsai M.-J., O'Malley B.W. Nature 389:194-198(1997) [PubMed: 9296499] [Abstract] Cited for: INTERACTION WITH NCOA1.
[7]	"Acetylation and modulation of erythroid Krueppel-like factor (EKLF) activity by interaction with histone acetyltransferases." Zhang W., Bieker J.J. Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998) [PubMed: 9707565] [Abstract] Cited for: INTERACTION WITH KLF1, FUNCTION.
[8]	"p300 and p300/cAMP-responsive element-binding protein associated factor interact with human T-cell lymphotropic virus type-1 Tax in a multi-histone acetyltransferase/activator-enhancer complex." Harrod R., Kuo Y.-L., Tang Y., Yao Y., Vassilev A., Nakatani Y., Giam C.-Z. J. Biol. Chem. 275:11852-11857(2000) [PubMed: 10766811] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX.
[9]	"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." Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G. J. Biol. Chem. 276:44936-44943(2001) [PubMed: 11568182] [Abstract] Cited for: INTERACTION WITH MECOM.
[10]	"Differential acetylation of Tat coordinates its interaction with the co-activators cyclin T1 and PCAF." Bres V., Tagami H., Peloponese J.-M., Loret E., Jeang K.-T., Nakatani Y., Emiliani S., Benkirane M., Kiernan R.E. EMBO J. 21:6811-6819(2002) [PubMed: 12486002] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[11]	"Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1." Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M. J. Biol. Chem. 279:41477-41486(2004) [PubMed: 15273251] [Abstract] Cited for: INTERACTION WITH NFE4.
[12]	"The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases." Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H. Oncogene 23:2559-2563(2004) [PubMed: 14767476] [Abstract] Cited for: INTERACTION WITH TACC1; TACC2 AND TACC3.
[13]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-729, MASS SPECTROMETRY.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-733, MASS SPECTROMETRY.
[15]	"Structure and ligand of a histone acetyltransferase bromodomain." Dhalluin C., Carlson J.E., Zeng L., He C., Aggarwal A.K., Zhou M.-M. Nature 399:491-496(1999) [PubMed: 10365964] [Abstract] Cited for: STRUCTURE BY NMR OF 715-832, MUTAGENESIS OF VAL-752; TYR-760; TYR-802 AND TYR-809. Tissue: Liver.
[16]	"Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain." Mujtaba S., He Y., Zeng L., Farooq A., Carlson J.E., Ott M., Verdin E., Zhou M.-M. Mol. Cell 9:575-586(2002) [PubMed: 11931765] [Abstract] Cited for: STRUCTURE BY NMR OF 719-832 IN COMPLEX WITH HIV-1 TAT.
[17]	"A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation." Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G. Mol. Cell 27:609-621(2007) [PubMed: 17707232] [Abstract] Cited for: IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U57317 mRNA. Translation: AAC50890.2.
BC060823 mRNA. Translation: AAH60823.1.
BC070075 mRNA. Translation: AAH70075.1.

IPI

IPI00022055.

PIR

S71788.

RefSeq

NP_003875.3.

UniGene

Hs.533055

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CM0	X-ray	2.30	A/B	493-658	[»]
1JM4	NMR	-	B	719-832	[»]
1N72	NMR	-	A	719-832	[»]
1WUG	NMR	-	A	719-832	[»]
1WUM	NMR	-	A	719-832	[»]
1ZS5	NMR	-	A	719-832	[»]
2RNW	NMR	-	A	719-832	[»]
2RNX	NMR	-	A	719-832	[»]
3GG3	X-ray	2.25	A/B	715-831	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29778N.

IntAct

Q92831. 24 interactions.

STRING

Q92831.

PTM databases

PhosphoSite

Q92831.

2-D gel databases

REPRODUCTION-2DPAGE

Q92831.

Proteomic databases

PRIDE

Q92831.

Genome annotation databases

Ensembl

ENST00000263754; ENSP00000263754; ENSG00000114166; Homo sapiens. [Genome view]

GeneID

8850.

KEGG

hsa:8850.

UCSC

uc003cbq.1. human.

Organism-specific databases

CTD

8850.

GeneCards

GC03P020057.

H-InvDB

HIX0003121.

HGNC

HGNC:8638. KAT2B.

HPA

CAB004526.

MIM

602303. gene.

PharmGKB

PA32977.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11279.

HOVERGEN

Q92831.

InParanoid

Q92831.

OMA

NSPIWDQ.

OrthoDB

EOG9642Z3.

PhylomeDB

Q92831.

Enzyme and pathway databases

BRENDA

2.3.1.48. 247.

Pathway_Interaction_DB

foxopathway. FoxO family signaling.
ar_tf_pathway. Regulation of Androgen receptor activity.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.

Reactome

REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q92831.

Bgee

Q92831.

CleanEx

HS_KAT2B.

Genevestigator

Q92831.

GermOnline

ENSG00000114166. Homo sapiens.

Family and domain databases

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GCN5-rel_AcTrfase.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
G3DSA:1.20.920.10. Bromodomain. 1 hit.

Pfam

PF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
[Graphical view]

PIRSF

PIRSF003048. Histone_acetylase_PCAF. 1 hit.

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
[Graphical view]

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

33221.

SOURCE

Search...

Entry information

Entry name

KAT2B_HUMAN

Accession

Primary (citable) accession number: Q92831
Secondary accession number(s): Q6NSK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	May 10, 2005
Last modified:	February 9, 2010
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.