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Q9JHD1 (KAT2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length813 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 By similarity.

Catalytic activity

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

Subunit structure

Interacts with SIRT1. Interacts with EP300, CREBBP and DDX17. Component of a large chromatin remodeling complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and KIF11/TRIP5. 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 NR2C2 (hypophosphorylated and unsumoylated form); the interaction promotes the transactivation activity of NR2C2 By similarity. Interacts with NFE4. Interacts with MECOM. Interacts with E2F1; the interaction acetylates E2F1 augmenting its DNA-binding and transcriptional activity By similarity. Interacts (unsumoylated form) with NR2C1; the interaction promotes transactivation activity. Ref.4 Ref.5

Subcellular location

Nucleus By similarity.

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
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainBromodomain
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal peptidyl-lysine acetylation

Inferred from electronic annotation. Source: Ensembl

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

chromatin remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3 acetylation

Inferred from electronic annotation. Source: Ensembl

histone acetylation

Inferred from direct assay PubMed 15992539. Source: MGI

internal peptidyl-lysine acetylation

Inferred from mutant phenotype PubMed 19773423. Source: UniProtKB

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

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

Inferred from direct assay PubMed 19773423. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15509593PubMed 15647252. Source: MGI

protein acetylation

Traceable author statement PubMed 10722926. Source: MGI

regulation of protein ADP-ribosylation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Traceable author statement PubMed 10722926. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentA band

Inferred from direct assay PubMed 18250163. Source: MGI

Ada2/Gcn5/Ada3 transcription activator complex

Inferred from direct assay PubMed 20508642. Source: MGI

I band

Inferred from direct assay PubMed 18250163. Source: MGI

actomyosin

Inferred from direct assay PubMed 18250163. Source: MGI

histone acetyltransferase complex

Inferred from direct assay Ref.1. Source: MGI

kinetochore

Inferred from direct assay PubMed 14519686. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 19773423. Source: UniProtKB

   Molecular_functioncyclin-dependent protein serine/threonine kinase inhibitor activity

Inferred from direct assay PubMed 19773423. Source: UniProtKB

histone acetyltransferase activity

Inferred from direct assay PubMed 15992539Ref.1. Source: MGI

lysine N-acetyltransferase activity

Inferred from direct assay PubMed 19773423. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 19773423. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay PubMed 15509593PubMed 15647252. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 813813Histone acetyltransferase KAT2B
PRO_0000322986

Regions

Domain484 – 632149N-acetyltransferase
Domain721 – 79171Bromo
Compositional bias48 – 536Poly-Gly

Experimental info

Sequence conflict293 – 2942LL → FV in AAF70498. Ref.1
Sequence conflict3191E → G in BAE33658. Ref.2
Sequence conflict4591H → L in AAF70498. Ref.1
Sequence conflict5481G → A in AAF70498. Ref.1
Sequence conflict5541F → L in AAF70498. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JHD1 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 38E52F326794F523

FASTA81391,769
        10         20         30         40         50         60 
MAEAGGAGSP ALPPAPPHGS PRTLATAAGS SASCGPATAV AAAGTAEGPG GGGSARIAVK 

        70         80         90        100        110        120 
KAQLRSAPRA KKLEKLGVYS ACKAEESCKC NGWKNPNPSP TPPRGDLQQI IVSLTESCRS 

       130        140        150        160        170        180 
CSHALAAHVS HLENVSEEEM DRLLGIVLDV EYLFTCVHKE EDADTKQVYF YLFKLLRKSI 

       190        200        210        220        230        240 
LQRGKPVVEG SLEKKPPFEK PSIEQGVNNF VQYKFSHLPS KERQTTIELA KMFLNRINYW 

       250        260        270        280        290        300 
HLEAPSQRRL RSPNDDISGY KENYTRWLCY CNVPQFCDSL PRYETTKVFG RTLLRSVFTI 

       310        320        330        340        350        360 
MRRQLLEQAR QEKDKLPLEK RTLILTHFPK FLSMLEEEVY SQNSPIWDQD FLSASSRTSP 

       370        380        390        400        410        420 
LGIQTVISPP VTGTALFSSN STSHEQINGG RTSPGCRGSS GLEANPGEKR KMNNSHAPEE 

       430        440        450        460        470        480 
AKRSRVMGDI PVELINEVMS TITDPAGMLG PETNFLSAHS ARDEAARLEE RRGVIEFHVV 

       490        500        510        520        530        540 
GNSLNQKPNK KILMWLVGLQ NVFSHQLPRM PKEYITRLVF DPKHKTLALI KDGRVIGGIC 

       550        560        570        580        590        600 
FRMFPSQGFT EIVFCAVTSN EQVKGYGTHL MNHLKEYHIK HEILNFLTYA DEYAIGYFKK 

       610        620        630        640        650        660 
QGFSKEIKIP KTKYVGYIKD YEGATLMGCE LNPQIPYTEF SVIIKKQKEI IKKLIERKQA 

       670        680        690        700        710        720 
QIRKVYPGLS CFKDGVRQIP IESIPGIRET GWKPSGKEKS KEPKDPEQLY STLKNILQQV 

       730        740        750        760        770        780 
KNHPNAWPFM EPVKRTEAPG YYEVIRFPMD LKTMSERLRN RYYVSKKLFM ADLQRVFTNC 

       790        800        810 
KEYNPPESEY YKCASILEKF FFSKIKEAGL IDK 

« Hide

References

« Hide 'large scale' references
[1]"Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates."
Xu W., Edmondson D.G., Roth S.Y.
Mol. Cell. Biol. 18:5659-5669(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: Spleen.
[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].
Strain: C57BL/6.
Tissue: Brain and Eye.
[4]"SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells."
Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.
Nat. Struct. Mol. Biol. 14:68-75(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2C1.
[5]"Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression."
Gupta P., Ho P.C., Huq M.M., Ha S.G., Park S.W., Khan A.A., Tsai N.P., Wei L.N.
Proc. Natl. Acad. Sci. U.S.A. 105:11424-11429(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2C1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF254442 mRNA. Translation: AAF70498.1.
AK156290 mRNA. Translation: BAE33658.1.
BC082581 mRNA. Translation: AAH82581.1.
BC145896 mRNA. Translation: AAI45897.1.
RefSeqNP_064389.2. NM_020005.4.
UniGeneMm.255025.

3D structure databases

ProteinModelPortalQ9JHD1.
SMRQ9JHD1. Positions 474-812.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202042. 15 interactions.
DIPDIP-29281N.
IntActQ9JHD1. 2 interactions.
MINTMINT-7984938.

Proteomic databases

PaxDbQ9JHD1.
PRIDEQ9JHD1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000724; ENSMUSP00000000724; ENSMUSG00000000708.
GeneID18519.
KEGGmmu:18519.
UCSCuc008czp.2. mouse.

Organism-specific databases

CTD8850.
MGIMGI:1343094. Kat2b.

Phylogenomic databases

eggNOGCOG5076.
GeneTreeENSGT00740000115051.
HOGENOMHOG000007151.
InParanoidQ9JHD1.
KOK06062.
OMAEKRKMTD.
OrthoDBEOG7ZKS9B.
PhylomeDBQ9JHD1.
TreeFamTF105399.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_189085. Disease.

Gene expression databases

ArrayExpressQ9JHD1.
BgeeQ9JHD1.
GenevestigatorQ9JHD1.

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. mouse.
NextBio294272.
PROQ9JHD1.
SOURCESearch...

Entry information

Entry nameKAT2B_MOUSE
AccessionPrimary (citable) accession number: Q9JHD1
Secondary accession number(s): Q3U142, Q640M9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: April 16, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot