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Q9JHD2

- KAT2A_MOUSE

UniProt

Q9JHD2 - KAT2A_MOUSE

Protein

Histone acetyltransferase KAT2A

Gene

Kat2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles By similarity. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 By similarity.By similarity

    Catalytic activityi

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

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. H3 histone acetyltransferase activity Source: MGI
    3. histone acetyltransferase activity Source: MGI
    4. histone acetyltransferase activity (H4-K12 specific) Source: MGI
    5. N-acetyltransferase activity Source: MGI
    6. protein binding Source: IntAct
    7. transcription coactivator activity Source: Ensembl

    GO - Biological processi

    1. cell proliferation Source: MGI
    2. histone deubiquitination Source: Ensembl
    3. histone H3-K14 acetylation Source: MGI
    4. histone H4-K12 acetylation Source: MGI
    5. in utero embryonic development Source: MGI
    6. metencephalon development Source: MGI
    7. midbrain development Source: MGI
    8. multicellular organism growth Source: MGI
    9. nervous system development Source: MGI
    10. neural tube closure Source: MGI
    11. positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter Source: MGI
    12. regulation of protein stability Source: Ensembl
    13. somitogenesis Source: MGI
    14. telencephalon development Source: MGI
    15. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_226917. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase KAT2A (EC:2.3.1.48)
    Alternative name(s):
    General control of amino acid synthesis protein 5-like 2
    Histone acetyltransferase GCN5
    Short name:
    MmGCN5
    Lysine acetyltransferase 2A
    Gene namesi
    Name:Kat2a
    Synonyms:Gcn5l2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1343101. Kat2a.

    Subcellular locationi

    GO - Cellular componenti

    1. Ada2/Gcn5/Ada3 transcription activator complex Source: MGI
    2. histone acetyltransferase complex Source: MGI
    3. mitotic spindle Source: MGI
    4. nucleus Source: MGI
    5. STAGA complex Source: MGI
    6. transcription factor TFTC complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 830829Histone acetyltransferase KAT2APRO_0000211203Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9JHD2.
    PRIDEiQ9JHD2.

    PTM databases

    PhosphoSiteiQ9JHD2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9JHD2.
    BgeeiQ9JHD2.
    GenevestigatoriQ9JHD2.

    Interactioni

    Subunit structurei

    Interacts with EP300, CREBBP and ADA2. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, KAT2A/GCN5L2, TAF10 and TRRAP. Interacts with TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, KAT2A, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22 By similarity. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 By similarity. In the complex, it probably interacts directly with CSRP2BP, MBIP and WDR5 By similarity. Interacts with PML.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TrrapQ80YV33EBI-2943116,EBI-2942477

    Protein-protein interaction databases

    BioGridi199867. 10 interactions.
    DIPiDIP-29180N.
    IntActiQ9JHD2. 54 interactions.
    MINTiMINT-4617449.
    STRINGi10090.ENSMUSP00000099407.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JHD2.
    SMRiQ9JHD2. Positions 490-651, 723-828.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini496 – 649154N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST
    Domaini738 – 80871BromoPROSITE-ProRule annotationAdd
    BLAST

    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.
    HOVERGENiHBG051710.
    KOiK06062.
    OMAiNSPIWES.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9JHD2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEPSQAPNP VPAAQPRPLH SPAPAPTSTP APSPASASTP APTPAPAPAP    50
    AAAPAGSTGS GGAGVGSGGD PARPGLSQQQ RASQRKAQVR GLPRAKKLEK 100
    LGVFSACKAN ETCKCNGWKN PKPPTAPRMD LQQPAANLSE LCRSCEHPLA 150
    DHVSHLENVS EDEINRLLGM VVDVENLFMS VHKEEDTDTK QVYFYLFKLL 200
    RKCILQMTRP VVEGSLGSPP FEKPNIEQGV LNFVQYKFSH LAPRERQTMF 250
    ELSKMFLLCL NYWKLETPAQ FRQRSQSEDV ATYKVNYTRW LCYCHVPQSC 300
    DSLPRYETTH VFGRSLLRSI FTVTRRQLLE KFRVEKDKLV PEKRTLILTH 350
    FPKFLSMLEE EIYGANSPIW ESGFTMPPSE GTQLVPRPAT VSATVVPSFS 400
    PSMGGGSNSS LSLDSAGTEP MPAGEKRKLP ENLTLEDAKR LRVMGDIPME 450
    LVNEVMLTIT DPAAMLGPET SLLSANAARD ETARLEERRG IIEFHVIGNS 500
    LTPKANRRVL LWLVGLQNVF SHQLPRMPKE YIARLVFDPK HKTLALIKDG 550
    RVIGGICFRM FPTQGFTEIV FCAVTSNEQV KGYGTHLMNH LKEYHIKHSI 600
    LYFLTYADEY AIGYFKKQGF SKDIKVPKSR YLGYIKDYEG ATLMECELNP 650
    RIPYTELSHI IKKQKEIIKK LIERKQAQIR KVYPGLSCFK EGVRQIPVES 700
    VPGIRETGWK PLGKEKGKEL KDPDQLYTTL KNLLAQIKSH PSAWPFMEPV 750
    KKSEAPDYYE VIRFPIDLKT MTERLRSRYY VTRKLFVADL QRVIANCREY 800
    NPPDSEYCRC ASALEKFFYF KLKEGGLIDK 830
    Length:830
    Mass (Da):93,394
    Last modified:July 27, 2011 - v2
    Checksum:i7993CFFEA4734174
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti804 – 8041D → N in AAF70497. (PubMed:9742083)Curated
    Sequence conflicti815 – 8151E → K in AAF70497. (PubMed:9742083)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF254441 mRNA. Translation: AAF70497.1.
    AK158079 mRNA. Translation: BAE34351.1.
    AL591469 Genomic DNA. Translation: CAM22909.1.
    CH466662 Genomic DNA. Translation: EDL02541.1.
    CCDSiCCDS25433.1.
    RefSeqiNP_064388.2. NM_020004.5.
    UniGeneiMm.218837.

    Genome annotation databases

    EnsembliENSMUST00000103118; ENSMUSP00000099407; ENSMUSG00000020918.
    GeneIDi14534.
    KEGGimmu:14534.
    UCSCiuc007lma.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF254441 mRNA. Translation: AAF70497.1 .
    AK158079 mRNA. Translation: BAE34351.1 .
    AL591469 Genomic DNA. Translation: CAM22909.1 .
    CH466662 Genomic DNA. Translation: EDL02541.1 .
    CCDSi CCDS25433.1.
    RefSeqi NP_064388.2. NM_020004.5.
    UniGenei Mm.218837.

    3D structure databases

    ProteinModelPortali Q9JHD2.
    SMRi Q9JHD2. Positions 490-651, 723-828.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199867. 10 interactions.
    DIPi DIP-29180N.
    IntActi Q9JHD2. 54 interactions.
    MINTi MINT-4617449.
    STRINGi 10090.ENSMUSP00000099407.

    PTM databases

    PhosphoSitei Q9JHD2.

    Proteomic databases

    PaxDbi Q9JHD2.
    PRIDEi Q9JHD2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000103118 ; ENSMUSP00000099407 ; ENSMUSG00000020918 .
    GeneIDi 14534.
    KEGGi mmu:14534.
    UCSCi uc007lma.2. mouse.

    Organism-specific databases

    CTDi 2648.
    MGIi MGI:1343101. Kat2a.

    Phylogenomic databases

    eggNOGi COG5076.
    GeneTreei ENSGT00740000115051.
    HOGENOMi HOG000007151.
    HOVERGENi HBG051710.
    KOi K06062.
    OMAi NSPIWES.
    TreeFami TF105399.

    Enzyme and pathway databases

    Reactomei REACT_226917. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi KAT2A. mouse.
    NextBioi 286188.
    PROi Q9JHD2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JHD2.
    Bgeei Q9JHD2.
    Genevestigatori Q9JHD2.

    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: C57BL/6J.
      Tissue: Inner ear.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: INTERACTION WITH PML.

    Entry informationi

    Entry nameiKAT2A_MOUSE
    AccessioniPrimary (citable) accession number: Q9JHD2
    Secondary accession number(s): Q3TZ59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 120 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