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Q9JHD1

- KAT2B_MOUSE

UniProt

Q9JHD1 - KAT2B_MOUSE

Protein

Histone acetyltransferase KAT2B

Gene

Kat2b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (18 Mar 2008)
      Previous versions | rss
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    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.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, acting on acetyl phosphate as donor Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase binding Source: UniProtKB
    6. transcription coactivator activity Source: MGI

    GO - Biological processi

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

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

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 813813Histone acetyltransferase KAT2BPRO_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.By similarity2 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini484 – 632149N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST
    Domaini721 – 79171BromoPROSITE-ProRule annotationAdd
    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.PROSITE-ProRule annotation
    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti293 – 2942LL → FV in AAF70498. (PubMed:9742083)Curated
    Sequence conflicti319 – 3191E → G in BAE33658. (PubMed:16141072)Curated
    Sequence conflicti459 – 4591H → L in AAF70498. (PubMed:9742083)Curated
    Sequence conflicti548 – 5481G → A in AAF70498. (PubMed:9742083)Curated
    Sequence conflicti554 – 5541F → L in AAF70498. (PubMed:9742083)Curated

    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

    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: October 1, 2014
    This is version 101 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