Skip Header

 
Contribute Send feedback
Read comments (?) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9JHD1 (KAT2B_MOUSE)

Last modified November 3, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length813 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 By similarity.

Catalytic activity

Acetyl-CoA + histone = CoA + acetylhistone.

Subunit structure

Interacts with SIRT1. Interacts with EP300 and CREBBP. 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 By similarity.

Subcellular location

Nucleus By similarity.

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.

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

Amino acid modifications

Modified residue201Phosphoserine Ref.4
Modified residue7101Phosphotyrosine By similarity
Modified residue7141N6-acetyllysine By similarity

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
Q9JHD1-1 [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: 9742083] [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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain and Eye.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF254442 mRNA. Translation: AAF70498.1.
AK156290 mRNA. Translation: BAE33658.1.
BC082581 mRNA. Translation: AAH82581.1.
BC145896 mRNA. Translation: AAI45897.1.
IPIIPI00471164.
RefSeqNP_064389.2.
UniGeneMm.255025

3D structure databases

HSSPHSSP built from PDB template 1CM0 based on UniProtKB Q92831.
SMRQ9JHD1. Positions 474-634, 696-813.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JHD1.

Proteomic databases

PRIDEQ9JHD1.

Genome annotation databases

EnsemblENSMUST00000000724; ENSMUSP00000000724; ENSMUSG00000000708; Mus musculus. [Genome view]
GeneID18519.
KEGGmmu:18519.
UCSCuc008czp.1. mouse.

Organism-specific databases

CTD18519.
MGIMGI:1343094. Kat2b.

Phylogenomic databases

HOVERGENQ9JHD1.
OMAYKENYTR.

Enzyme and pathway databases

BRENDA2.3.1.48. 244.

Gene expression databases

ArrayExpressQ9JHD1.
BgeeQ9JHD1.
GenevestigatorQ9JHD1.

Family and domain databases

InterProIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GCN5-rel_AcTrfase.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
G3DSA:1.20.920.10. Bromodomain. 1 hit.
PfamPF00583. Acetyltransf_1. 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]
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio294272.
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: November 3, 2009
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents