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Q92830

- KAT2A_HUMAN

UniProt

Q92830 - KAT2A_HUMAN

Protein

Histone acetyltransferase KAT2A

Gene

KAT2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (14 Oct 2008)
      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. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.1 Publication

    Catalytic activityi

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

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. H3 histone acetyltransferase activity Source: BHF-UCL
    3. histone acetyltransferase activity Source: UniProtKB
    4. histone acetyltransferase activity (H4-K12 specific) Source: Ensembl
    5. histone deacetylase binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: Ensembl
    2. chromatin organization Source: Reactome
    3. chromatin remodeling Source: ProtInc
    4. histone deubiquitination Source: UniProtKB
    5. histone H3 acetylation Source: UniProtKB
    6. histone H3-K14 acetylation Source: Ensembl
    7. in utero embryonic development Source: Ensembl
    8. metencephalon development Source: Ensembl
    9. midbrain development Source: Ensembl
    10. multicellular organism growth Source: Ensembl
    11. neural tube closure Source: Ensembl
    12. regulation of protein stability Source: MGI
    13. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    14. somitogenesis Source: Ensembl
    15. telencephalon development Source: Ensembl
    16. transcription from RNA polymerase II promoter Source: ProtInc
    17. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Host-virus interaction, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_14835. Notch-HLH transcription pathway.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_172610. HATs acetylate histones.
    REACT_953. RNA Polymerase I Transcription Initiation.
    SignaLinkiQ92830.

    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:
    HsGCN5
    Lysine acetyltransferase 2A
    STAF97
    Gene namesi
    Name:KAT2A
    Synonyms:GCN5, GCN5L2, HGCN5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4201. KAT2A.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
    2. extracellular space Source: UniProt
    3. mitotic spindle Source: Ensembl
    4. nucleoplasm Source: Reactome
    5. STAGA complex Source: UniProtKB
    6. transcription factor TFTC complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162392664.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 837836Histone acetyltransferase KAT2APRO_0000211202Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ92830.
    PaxDbiQ92830.
    PRIDEiQ92830.

    PTM databases

    PhosphoSiteiQ92830.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested, with most abundant expression in ovary.

    Gene expression databases

    ArrayExpressiQ92830.
    BgeeiQ92830.
    CleanExiHS_KAT2A.
    GenevestigatoriQ92830.

    Organism-specific databases

    HPAiHPA048958.

    Interactioni

    Subunit structurei

    Interacts with EP300, CREBBP and ADA2. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TAF3, 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. Interacts with and acetylates HIV-1 Tat. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with CSRP2BP, MBIP and WDR5. Interacts with PML By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    WDHD1O757175EBI-477622,EBI-3951691
    ZZZ3Q8IYH52EBI-477622,EBI-2795524

    Protein-protein interaction databases

    BioGridi108918. 103 interactions.
    DIPiDIP-28146N.
    IntActiQ92830. 36 interactions.
    MINTiMINT-199927.
    STRINGi9606.ENSP00000225916.

    Structurei

    Secondary structure

    1
    837
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi498 – 5047
    Helixi514 – 53017
    Helixi536 – 5438
    Beta strandi549 – 5557
    Beta strandi558 – 56811
    Turni569 – 5724
    Beta strandi573 – 5819
    Helixi583 – 5853
    Beta strandi587 – 5893
    Helixi590 – 60415
    Beta strandi609 – 6146
    Helixi616 – 6183
    Helixi619 – 6246
    Beta strandi627 – 6293
    Helixi635 – 6384
    Turni639 – 6413
    Beta strandi649 – 6546
    Helixi730 – 74617
    Helixi748 – 7536
    Turni759 – 7613
    Helixi765 – 7684
    Helixi775 – 7839
    Helixi790 – 80718
    Helixi813 – 83119

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F68NMR-A730-832[»]
    1Z4RX-ray1.74A497-662[»]
    3D7CX-ray2.06A/B729-837[»]
    ProteinModelPortaliQ92830.
    SMRiQ92830. Positions 497-658, 730-835.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92830.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini503 – 656154N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST
    Domaini745 – 81571BromoPROSITE-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.
    HOGENOMiHOG000007151.
    InParanoidiQ92830.
    KOiK06062.
    OMAiNSPIWES.
    PhylomeDBiQ92830.
    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]
    PfamiPF00583. Acetyltransf_1. 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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92830-1) [UniParc]FASTAAdd to Basket

    Also known as: GCN5-L

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAEPSQAPTP APAAQPRPLQ SPAPAPTPTP APSPASAPIP TPTPAPAPAP    50
    AAAPAGSTGT GGPGVGSGGA GSGGDPARPG LSQQQRASQR KAQVRGLPRA 100
    KKLEKLGVFS ACKANETCKC NGWKNPKPPT APRMDLQQPA ANLSELCRSC 150
    EHPLADHVSH LENVSEDEIN RLLGMVVDVE NLFMSVHKEE DTDTKQVYFY 200
    LFKLLRKCIL QMTRPVVEGS LGSPPFEKPN IEQGVLNFVQ YKFSHLAPRE 250
    RQTMFELSKM FLLCLNYWKL ETPAQFRQRS QAEDVATYKV NYTRWLCYCH 300
    VPQSCDSLPR YETTHVFGRS LLRSIFTVTR RQLLEKFRVE KDKLVPEKRT 350
    LILTHFPKFL SMLEEEIYGA NSPIWESGFT MPPSEGTQLV PRPASVSAAV 400
    VPSTPIFSPS MGGGSNSSLS LDSAGAEPMP GEKRTLPENL TLEDAKRLRV 450
    MGDIPMELVN EVMLTITDPA AMLGPETSLL SANAARDETA RLEERRGIIE 500
    FHVIGNSLTP KANRRVLLWL VGLQNVFSHQ LPRMPKEYIA RLVFDPKHKT 550
    LALIKDGRVI GGICFRMFPT QGFTEIVFCA VTSNEQVKGY GTHLMNHLKE 600
    YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG YIKDYEGATL 650
    MECELNPRIP YTELSHIIKK QKEIIKKLIE RKQAQIRKVY PGLSCFKEGV 700
    RQIPVESVPG IRETGWKPLG KEKGKELKDP DQLYTTLKNL LAQIKSHPSA 750
    WPFMEPVKKS EAPDYYEVIR FPIDLKTMTE RLRSRYYVTR KLFVADLQRV 800
    IANCREYNPP DSEYCRCASA LEKFFYFKLK EGGLIDK 837
    Length:837
    Mass (Da):93,926
    Last modified:October 14, 2008 - v3
    Checksum:i728CC8ACF08600EA
    GO
    Isoform 2 (identifier: Q92830-2) [UniParc]FASTAAdd to Basket

    Also known as: GCN5-S

    The sequence of this isoform differs from the canonical sequence as follows:
         1-410: Missing.

    Show »
    Length:427
    Mass (Da):48,921
    Checksum:iA6EAE20DB0B49ADC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti116 – 1161E → G in AAC39769. (PubMed:8552087)Curated
    Sequence conflicti134 – 1341M → I in AAC39769. (PubMed:8552087)Curated
    Sequence conflicti269 – 2691K → E in AAC39769. (PubMed:8552087)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 410410Missing in isoform 2. CuratedVSP_000556Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF029777 mRNA. Translation: AAC39769.1.
    CH471152 Genomic DNA. Translation: EAW60803.1.
    BC032743 mRNA. Translation: AAH32743.1.
    BC039907 mRNA. Translation: AAH39907.1.
    BC105977 mRNA. Translation: AAI05978.1.
    U57316 Genomic DNA. Translation: AAC50641.1.
    CCDSiCCDS11417.1. [Q92830-1]
    PIRiS71789.
    RefSeqiNP_066564.2. NM_021078.2. [Q92830-1]
    UniGeneiHs.463045.

    Genome annotation databases

    EnsembliENST00000225916; ENSP00000225916; ENSG00000108773. [Q92830-1]
    GeneIDi2648.
    KEGGihsa:2648.
    UCSCiuc002hyx.2. human. [Q92830-1]

    Polymorphism databases

    DMDMi209572743.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF029777 mRNA. Translation: AAC39769.1 .
    CH471152 Genomic DNA. Translation: EAW60803.1 .
    BC032743 mRNA. Translation: AAH32743.1 .
    BC039907 mRNA. Translation: AAH39907.1 .
    BC105977 mRNA. Translation: AAI05978.1 .
    U57316 Genomic DNA. Translation: AAC50641.1 .
    CCDSi CCDS11417.1. [Q92830-1 ]
    PIRi S71789.
    RefSeqi NP_066564.2. NM_021078.2. [Q92830-1 ]
    UniGenei Hs.463045.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F68 NMR - A 730-832 [» ]
    1Z4R X-ray 1.74 A 497-662 [» ]
    3D7C X-ray 2.06 A/B 729-837 [» ]
    ProteinModelPortali Q92830.
    SMRi Q92830. Positions 497-658, 730-835.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108918. 103 interactions.
    DIPi DIP-28146N.
    IntActi Q92830. 36 interactions.
    MINTi MINT-199927.
    STRINGi 9606.ENSP00000225916.

    Chemistry

    ChEMBLi CHEMBL5501.

    PTM databases

    PhosphoSitei Q92830.

    Polymorphism databases

    DMDMi 209572743.

    Proteomic databases

    MaxQBi Q92830.
    PaxDbi Q92830.
    PRIDEi Q92830.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225916 ; ENSP00000225916 ; ENSG00000108773 . [Q92830-1 ]
    GeneIDi 2648.
    KEGGi hsa:2648.
    UCSCi uc002hyx.2. human. [Q92830-1 ]

    Organism-specific databases

    CTDi 2648.
    GeneCardsi GC17M040265.
    HGNCi HGNC:4201. KAT2A.
    HPAi HPA048958.
    MIMi 602301. gene.
    neXtProti NX_Q92830.
    PharmGKBi PA162392664.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000007151.
    InParanoidi Q92830.
    KOi K06062.
    OMAi NSPIWES.
    PhylomeDBi Q92830.
    TreeFami TF105399.

    Enzyme and pathway databases

    Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_14835. Notch-HLH transcription pathway.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_172610. HATs acetylate histones.
    REACT_953. RNA Polymerase I Transcription Initiation.
    SignaLinki Q92830.

    Miscellaneous databases

    ChiTaRSi KAT2A. human.
    EvolutionaryTracei Q92830.
    GeneWikii GCN5L2.
    GenomeRNAii 2648.
    NextBioi 10450.
    PROi Q92830.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92830.
    Bgeei Q92830.
    CleanExi HS_KAT2A.
    Genevestigatori Q92830.

    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 PF00583. Acetyltransf_1. 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. "Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5."
      Candau R., Moore P.A., Wang L., Barlev N., Ying C.Y., Rosen C.A., Berger S.L.
      Mol. Cell. Biol. 16:593-602(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), CHARACTERIZATION.
      Tissue: Testis.
    2. "Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members."
      Smith E.R., Belote J.M., Schlitz R.L., Yang X.-J., Moore P.A., Berger S.L., Nakatani Y., Allis C.D.
      Nucleic Acids Res. 26:2948-2954(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
      Tissue: Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Eye, Skin and Testis.
    5. "A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A."
      Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.
      Nature 382:319-324(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-837 (ISOFORM 1).
      Tissue: Brain.
    6. "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo."
      Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., Kundu T.K., Chait B.T., Roeder R.G.
      Mol. Cell. Biol. 21:6782-6795(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10; TAF12 AND TAF9, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction."
      Brand M., Yamamoto K., Staub A., Tora L.
      J. Biol. Chem. 274:18285-18289(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H; TAF2; TAF4; TAF5; TRRAP AND TAF10.
    8. "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc."
      McMahon S.B., Wood M.A., Cole M.D.
      Mol. Cell. Biol. 20:556-562(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRRAP.
    9. "The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat."
      Col E., Caron C., Seigneurin-Berny D., Gracia J., Favier A., Khochbin S.
      J. Biol. Chem. 276:28179-28184(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    10. "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger."
      Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C., Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.
      Mol. Cell. Biol. 21:5109-5121(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAF3.
    11. "The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases."
      Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.
      Oncogene 23:2559-2563(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TACC1; TACC2 AND TACC3.
    12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
      Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
      Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN STAGA COMPLEX.
    14. "The double-histone-acetyltransferase complex ATAC is essential for mammalian development."
      Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., Lill J.R., Zha J.
      Mol. Cell. Biol. 29:1176-1188(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN ATAC COMPLEX.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain."
      Hudson B.P., Martinez-Yamout M.A., Dyson H.J., Wright P.E.
      J. Mol. Biol. 304:355-370(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 730-832.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 729-837.

    Entry informationi

    Entry nameiKAT2A_HUMAN
    AccessioniPrimary (citable) accession number: Q92830
    Secondary accession number(s): Q8N1A2, Q9UCW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 161 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3