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Q92831 (KAT2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase KAT2B

EC=2.3.1.48
Alternative name(s):
Histone acetyltransferase PCAF
Short name=Histone acetylase PCAF
Lysine acetyltransferase 2B
P300/CBP-associated factor
Short name=P/CAF
Gene names
Name:KAT2B
Synonyms:PCAF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length832 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Also acetylates non-histone proteins, such as ACLY. 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 Ref.8 Ref.16

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.4

Subunit structure

Interacts with SIRT1. Interacts (unsumoylated form) with NR2C1; the interaction promotes transactivation activity By similarity. Interacts with EP300, CREBBP and DDX17. Interacts with NCOA1 and NCOA3. Component of a large chromatin remodeling complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and KIF11/TRIP5. Interacts with NR2C2 (hypophosphorylated and unsumoylated form); the interaction promotes the transactivation activity of NR2C2. 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. Interacts with E2F1; the interaction acetylates E2F1 augmenting its DNA-binding and transcriptional activity. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.19

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 acetyltransferase family. GCN5 subfamily.

Contains 1 bromo domain.

Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
   Biological processCell cycle
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainBromodomain
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal peptidyl-lysine acetylation

Inferred from direct assay PubMed 12435739. Source: UniProtKB

Notch signaling pathway

Traceable author statement. Source: Reactome

cell cycle arrest

Traceable author statement Ref.1. Source: ProtInc

cellular response to insulin stimulus

Inferred from direct assay PubMed 19303849. Source: BHF-UCL

chromatin organization

Traceable author statement. Source: Reactome

chromatin remodeling

Inferred from direct assay Ref.19. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

histone H3 acetylation

Inferred from direct assay PubMed 18838386. Source: BHF-UCL

internal peptidyl-lysine acetylation

Inferred from direct assay Ref.16. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

peptidyl-lysine acetylation

Inferred from direct assay PubMed 19303849PubMed 19470756. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19470756. Source: BHF-UCL

protein acetylation

Traceable author statement Ref.1. Source: ProtInc

regulation of protein ADP-ribosylation

Inferred from direct assay PubMed 19470756. Source: BHF-UCL

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentA band

Inferred from electronic annotation. Source: Ensembl

Ada2/Gcn5/Ada3 transcription activator complex

Inferred from direct assay PubMed 18838386. Source: BHF-UCL

I band

Inferred from electronic annotation. Source: Ensembl

PCAF complex

Non-traceable author statement Ref.19. Source: UniProtKB

actomyosin

Inferred from electronic annotation. Source: Ensembl

kinetochore

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionacetyltransferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

cyclin-dependent protein serine/threonine kinase inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

histone deacetylase binding

Inferred from physical interaction PubMed 12887892. Source: UniProtKB

lysine N-acetyltransferase activity

Inferred from direct assay Ref.16. Source: UniProtKB

protein complex binding

Inferred from direct assay Ref.19. Source: UniProtKB

protein kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay PubMed 12435739. Source: UniProtKB

transcription cofactor activity

Inferred from physical interaction Ref.1. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 15509593. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 832832Histone acetyltransferase KAT2B
PRO_0000211208

Regions

Domain503 – 651149N-acetyltransferase UniProtKB Q92830
Domain740 – 81071Bromo

Natural variations

Natural variant3861N → S.
Corresponds to variant rs17006625 [ dbSNP | Ensembl ].
VAR_034372

Experimental info

Mutagenesis7521V → A: Reduced acetyl-lysine binding. Ref.17
Mutagenesis7601Y → A: Reduced acetyl-lysine binding. Ref.17
Mutagenesis8021Y → A: Reduced acetyl-lysine binding. Ref.17
Mutagenesis8091Y → A: Complete loss of acetyl-lysine binding. Ref.17
Sequence conflict804 – 8052PP → AA in AAC50890. Ref.1

Secondary structure

................................................... 832
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92831 [UniParc].

Last modified May 10, 2005. Version 3.
Checksum: 72F516E8BC00CC0C

FASTA83293,013
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLF1, FUNCTION.
[8]"Regulation of E2F1 activity by acetylation."
Martinez-Balbas M.A., Bauer U.M., Nielsen S.J., Brehm A., Kouzarides T.
EMBO J. 19:662-671(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E2F1, FUNCTION.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTLV-1 TAX.
[10]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MECOM.
[11]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[12]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFE4.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TACC1; TACC2 AND TACC3.
[14]"Modulation of testicular receptor 4 activity by mitogen-activated protein kinase-mediated phosphorylation."
Huq M.D., Gupta P., Tsai N.P., Wei L.N.
Mol. Cell. Proteomics 5:2072-2082(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2C2.
[15]"Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF."
Shin S., Janknecht R.
J. Cell. Biochem. 101:1252-1265(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX17.
[16]"Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth."
Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.
Mol. Cell 51:506-518(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 715-832, MUTAGENESIS OF VAL-752; TYR-760; TYR-802 AND TYR-809.
Tissue: Liver.
[18]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 719-832 IN COMPLEX WITH HIV-1 TAT.
[19]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
[20]"Histone recognition and large-scale structural analysis of the human bromodomain family."
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., Gingras A.C., Arrowsmith C.H., Knapp S.
Cell 149:214-231(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 715-831.
+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.
PIRS71788.
RefSeqNP_003875.3. NM_003884.4.
UniGeneHs.533055.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CM0X-ray2.30A/B493-658[»]
1JM4NMR-B719-832[»]
1N72NMR-A719-832[»]
1WUGNMR-A719-832[»]
1WUMNMR-A719-832[»]
1ZS5NMR-A719-832[»]
2RNWNMR-A719-832[»]
2RNXNMR-A719-832[»]
3GG3X-ray2.25A/B715-831[»]
4NSQX-ray2.31A/B/C/D493-658[»]
ProteinModelPortalQ92831.
SMRQ92831. Positions 493-832.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114375. 136 interactions.
DIPDIP-29778N.
IntActQ92831. 35 interactions.
MINTMINT-150079.
STRING9606.ENSP00000263754.

Chemistry

BindingDBQ92831.
ChEMBLCHEMBL5500.

PTM databases

PhosphoSiteQ92831.

Polymorphism databases

DMDM83287776.

2D gel databases

REPRODUCTION-2DPAGEQ92831.

Proteomic databases

PaxDbQ92831.
PRIDEQ92831.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263754; ENSP00000263754; ENSG00000114166.
GeneID8850.
KEGGhsa:8850.
UCSCuc003cbq.3. human.

Organism-specific databases

CTD8850.
GeneCardsGC03P020081.
HGNCHGNC:8638. KAT2B.
HPACAB004526.
MIM602303. gene.
neXtProtNX_Q92831.
PharmGKBPA162392705.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000007151.
InParanoidQ92831.
KOK06062.
OMAEKRKMTD.
OrthoDBEOG7ZKS9B.
PhylomeDBQ92831.
TreeFamTF105399.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_172623. Chromatin organization.
REACT_1788. Transcription.
REACT_2155. NICD traffics to nucleus.
REACT_71. Gene Expression.

Gene expression databases

BgeeQ92831.
CleanExHS_KAT2B.
GenevestigatorQ92831.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view]
PfamPF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
[Graphical view]
PIRSFPIRSF003048. Histone_acetylase_PCAF. 1 hit.
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKAT2B. human.
EvolutionaryTraceQ92831.
GeneWikiPCAF.
GenomeRNAi8850.
NextBio33221.
PROQ92831.
SOURCESearch...

Entry information

Entry nameKAT2B_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM