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Q9JHD1

- KAT2B_MOUSE

UniProt

Q9JHD1 - KAT2B_MOUSE

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Protein
Histone acetyltransferase KAT2B
Gene
Kat2b, Pcaf
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers By similarity.

Catalytic activityi

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

GO - Molecular functioni

  1. cyclin-dependent protein serine/threonine kinase inhibitor activity Source: UniProtKB
  2. histone acetyltransferase activity Source: MGI
  3. lysine N-acetyltransferase activity Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein kinase binding Source: UniProtKB
  6. transcription coactivator activity Source: MGI

GO - Biological processi

  1. N-terminal peptidyl-lysine acetylation Source: Ensembl
  2. cell cycle Source: UniProtKB-KW
  3. cellular response to insulin stimulus Source: Ensembl
  4. chromatin remodeling Source: UniProtKB
  5. histone H3-K9 acetylation Source: MGI
  6. histone acetylation Source: MGI
  7. internal peptidyl-lysine acetylation Source: UniProtKB
  8. negative regulation of cell proliferation Source: Ensembl
  9. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  10. positive regulation of gluconeogenesis Source: MGI
  11. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  12. positive regulation of transcription, DNA-templated Source: MGI
  13. protein acetylation Source: MGI
  14. regulation of protein ADP-ribosylation Source: Ensembl
  15. regulation of transcription, DNA-templated Source: MGI
  16. rhythmic process Source: UniProtKB-KW
  17. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_196520. Pre-NOTCH Transcription and Translation.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_223683. Notch-HLH transcription pathway.
REACT_226917. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Kat2b
Synonyms:Pcaf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1343094. Kat2b.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. A band Source: MGI
  2. Ada2/Gcn5/Ada3 transcription activator complex Source: MGI
  3. I band Source: MGI
  4. actomyosin Source: MGI
  5. histone acetyltransferase complex Source: MGI
  6. kinetochore Source: MGI
  7. nucleoplasm Source: Reactome
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 813813Histone acetyltransferase KAT2B
PRO_0000322986Add
BLAST

Proteomic databases

PaxDbiQ9JHD1.
PRIDEiQ9JHD1.

Expressioni

Gene expression databases

ArrayExpressiQ9JHD1.
BgeeiQ9JHD1.
GenevestigatoriQ9JHD1.

Interactioni

Subunit structurei

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. Interacts with NPAS2, ARNTL/BMAL1 and CLOCK By similarity. Interacts (unsumoylated form) with NR2C1; the interaction promotes transactivation activity.2 Publications

Protein-protein interaction databases

BioGridi202042. 15 interactions.
DIPiDIP-29281N.
IntActiQ9JHD1. 2 interactions.
MINTiMINT-7984938.

Structurei

3D structure databases

ProteinModelPortaliQ9JHD1.
SMRiQ9JHD1. Positions 474-633, 706-812.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini484 – 632149N-acetyltransferase
Add
BLAST
Domaini721 – 79171Bromo
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi48 – 536Poly-Gly

Domaini

The bromodomain mediates binding to HIV-1 Tat.

Sequence similaritiesi

Contains 1 bromo domain.

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00740000115051.
HOGENOMiHOG000007151.
InParanoidiQ9JHD1.
KOiK06062.
OMAiKIMMWLV.
OrthoDBiEOG7ZKS9B.
PhylomeDBiQ9JHD1.
TreeFamiTF105399.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view]
PfamiPF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003048. Histone_acetylase_PCAF. 1 hit.
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JHD1-1 [UniParc]FASTAAdd to Basket

« Hide

MAEAGGAGSP ALPPAPPHGS PRTLATAAGS SASCGPATAV AAAGTAEGPG    50
GGGSARIAVK KAQLRSAPRA KKLEKLGVYS ACKAEESCKC NGWKNPNPSP 100
TPPRGDLQQI IVSLTESCRS CSHALAAHVS HLENVSEEEM DRLLGIVLDV 150
EYLFTCVHKE EDADTKQVYF YLFKLLRKSI LQRGKPVVEG SLEKKPPFEK 200
PSIEQGVNNF VQYKFSHLPS KERQTTIELA KMFLNRINYW HLEAPSQRRL 250
RSPNDDISGY KENYTRWLCY CNVPQFCDSL PRYETTKVFG RTLLRSVFTI 300
MRRQLLEQAR QEKDKLPLEK RTLILTHFPK FLSMLEEEVY SQNSPIWDQD 350
FLSASSRTSP LGIQTVISPP VTGTALFSSN STSHEQINGG RTSPGCRGSS 400
GLEANPGEKR KMNNSHAPEE AKRSRVMGDI PVELINEVMS TITDPAGMLG 450
PETNFLSAHS ARDEAARLEE RRGVIEFHVV GNSLNQKPNK KILMWLVGLQ 500
NVFSHQLPRM PKEYITRLVF DPKHKTLALI KDGRVIGGIC FRMFPSQGFT 550
EIVFCAVTSN EQVKGYGTHL MNHLKEYHIK HEILNFLTYA DEYAIGYFKK 600
QGFSKEIKIP KTKYVGYIKD YEGATLMGCE LNPQIPYTEF SVIIKKQKEI 650
IKKLIERKQA QIRKVYPGLS CFKDGVRQIP IESIPGIRET GWKPSGKEKS 700
KEPKDPEQLY STLKNILQQV KNHPNAWPFM EPVKRTEAPG YYEVIRFPMD 750
LKTMSERLRN RYYVSKKLFM ADLQRVFTNC KEYNPPESEY YKCASILEKF 800
FFSKIKEAGL IDK 813
Length:813
Mass (Da):91,769
Last modified:March 18, 2008 - v2
Checksum:i38E52F326794F523
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti293 – 2942LL → FV in AAF70498. 1 Publication
Sequence conflicti319 – 3191E → G in BAE33658. 1 Publication
Sequence conflicti459 – 4591H → L in AAF70498. 1 Publication
Sequence conflicti548 – 5481G → A in AAF70498. 1 Publication
Sequence conflicti554 – 5541F → L in AAF70498. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF254442 mRNA. Translation: AAF70498.1.
AK156290 mRNA. Translation: BAE33658.1.
BC082581 mRNA. Translation: AAH82581.1.
BC145896 mRNA. Translation: AAI45897.1.
CCDSiCCDS28880.1.
RefSeqiNP_064389.2. NM_020005.4.
UniGeneiMm.255025.

Genome annotation databases

EnsembliENSMUST00000000724; ENSMUSP00000000724; ENSMUSG00000000708.
GeneIDi18519.
KEGGimmu:18519.
UCSCiuc008czp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF254442 mRNA. Translation: AAF70498.1 .
AK156290 mRNA. Translation: BAE33658.1 .
BC082581 mRNA. Translation: AAH82581.1 .
BC145896 mRNA. Translation: AAI45897.1 .
CCDSi CCDS28880.1.
RefSeqi NP_064389.2. NM_020005.4.
UniGenei Mm.255025.

3D structure databases

ProteinModelPortali Q9JHD1.
SMRi Q9JHD1. Positions 474-633, 706-812.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202042. 15 interactions.
DIPi DIP-29281N.
IntActi Q9JHD1. 2 interactions.
MINTi MINT-7984938.

Proteomic databases

PaxDbi Q9JHD1.
PRIDEi Q9JHD1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000724 ; ENSMUSP00000000724 ; ENSMUSG00000000708 .
GeneIDi 18519.
KEGGi mmu:18519.
UCSCi uc008czp.2. mouse.

Organism-specific databases

CTDi 8850.
MGIi MGI:1343094. Kat2b.

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00740000115051.
HOGENOMi HOG000007151.
InParanoidi Q9JHD1.
KOi K06062.
OMAi KIMMWLV.
OrthoDBi EOG7ZKS9B.
PhylomeDBi Q9JHD1.
TreeFami TF105399.

Enzyme and pathway databases

Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_196520. Pre-NOTCH Transcription and Translation.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_223683. Notch-HLH transcription pathway.
REACT_226917. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi KAT2B. mouse.
NextBioi 294272.
PROi Q9JHD1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9JHD1.
Bgeei Q9JHD1.
Genevestigatori Q9JHD1.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view ]
Pfami PF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF003048. Histone_acetylase_PCAF. 1 hit.
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiKAT2B_MOUSE
AccessioniPrimary (citable) accession number: Q9JHD1
Secondary accession number(s): Q3U142, Q640M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: September 3, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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