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Q92831

- KAT2B_HUMAN

UniProt

Q92831 - KAT2B_HUMAN

Protein

Histone acetyltransferase KAT2B

Gene

KAT2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 3 (10 May 2005)
      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. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. 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. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers.5 Publications

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

    GO - Molecular functioni

    1. acetyltransferase activity Source: UniProtKB
    2. cyclin-dependent protein serine/threonine kinase inhibitor activity Source: UniProtKB
    3. histone acetyltransferase activity Source: UniProtKB
    4. histone deacetylase binding Source: UniProtKB
    5. lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein complex binding Source: UniProtKB
    8. protein kinase binding Source: UniProtKB
    9. transcription coactivator activity Source: UniProtKB
    10. transcription cofactor activity Source: UniProtKB
    11. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: ProtInc
    2. cellular response to insulin stimulus Source: BHF-UCL
    3. chromatin organization Source: Reactome
    4. chromatin remodeling Source: UniProtKB
    5. gene expression Source: Reactome
    6. histone H3 acetylation Source: BHF-UCL
    7. internal peptidyl-lysine acetylation Source: UniProtKB
    8. negative regulation of cell proliferation Source: UniProtKB
    9. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
    10. Notch signaling pathway Source: Reactome
    11. N-terminal peptidyl-lysine acetylation Source: UniProtKB
    12. peptidyl-lysine acetylation Source: BHF-UCL
    13. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    14. protein acetylation Source: ProtInc
    15. regulation of protein ADP-ribosylation Source: BHF-UCL
    16. rhythmic process Source: UniProtKB-KW
    17. transcription from RNA polymerase I promoter Source: Reactome
    18. transcription initiation from RNA polymerase II promoter Source: Reactome
    19. transcription initiation from RNA polymerase I promoter Source: Reactome
    20. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Acyltransferase, Transferase

    Keywords - Biological processi

    Biological rhythms, Cell cycle, Host-virus interaction, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    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.

    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
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:8638. KAT2B.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. A band Source: Ensembl
    2. actomyosin Source: Ensembl
    3. Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
    4. I band Source: Ensembl
    5. kinetochore Source: Ensembl
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProtKB
    8. PCAF complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi752 – 7521V → A: Reduced acetyl-lysine binding. 1 Publication
    Mutagenesisi760 – 7601Y → A: Reduced acetyl-lysine binding. 1 Publication
    Mutagenesisi802 – 8021Y → A: Reduced acetyl-lysine binding. 1 Publication
    Mutagenesisi809 – 8091Y → A: Complete loss of acetyl-lysine binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA162392705.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 832832Histone acetyltransferase KAT2BPRO_0000211208Add
    BLAST

    Proteomic databases

    MaxQBiQ92831.
    PaxDbiQ92831.
    PRIDEiQ92831.

    2D gel databases

    REPRODUCTION-2DPAGEQ92831.

    PTM databases

    PhosphoSiteiQ92831.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed but most abundant in heart and skeletal muscle.1 Publication

    Gene expression databases

    BgeeiQ92831.
    CleanExiHS_KAT2B.
    GenevestigatoriQ92831.

    Organism-specific databases

    HPAiCAB004526.

    Interactioni

    Subunit structurei

    Interacts with SIRT1. Interacts (unsumoylated form) with NR2C1; the interaction promotes transactivation activity By similarity. Interacts with EP300, CREBBP and DDX17. Interacts with NCOA1 and NCOA3. Component of a large chromatin remodeling complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and KIF11/TRIP5. Interacts with NR2C2 (hypophosphorylated and unsumoylated form); the interaction promotes the transactivation activity of NR2C2. Binds to HTLV-1 Tax. Interacts with and acetylates HIV-1 Tat. 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 E2F1; the interaction acetylates E2F1 augmenting its DNA-binding and transcriptional activity. Interacts with NPAS2, ARNTL/BMAL1 and CLOCK.By similarity15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P032553EBI-477430,EBI-2603114From a different organism.
    P03255-23EBI-477430,EBI-6859460From a different organism.
    BUB1BO6056613EBI-477430,EBI-1001438
    CREBBPQ927934EBI-477430,EBI-81215
    E7P031295EBI-477430,EBI-866453From a different organism.
    EHMT2Q96KQ73EBI-477430,EBI-744366
    EP300Q094722EBI-477430,EBI-447295
    HIF1AQ166652EBI-477430,EBI-447269
    His3:CG33854P022992EBI-477430,EBI-522090From a different organism.
    His4:CG33909P840402EBI-477430,EBI-185028From a different organism.
    SIRT1Q96EB63EBI-477430,EBI-1802965
    SIRT2Q8IXJ64EBI-477430,EBI-477232
    TAF9Q165943EBI-477430,EBI-712521
    Tp63O88898-23EBI-477430,EBI-2338228From a different organism.
    TWIST1Q156722EBI-477430,EBI-1797287
    USF1P224155EBI-477430,EBI-1054489

    Protein-protein interaction databases

    BioGridi114375. 136 interactions.
    DIPiDIP-29778N.
    IntActiQ92831. 35 interactions.
    MINTiMINT-150079.
    STRINGi9606.ENSP00000263754.

    Structurei

    Secondary structure

    1
    832
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi494 – 4996
    Beta strandi503 – 5053
    Helixi509 – 52517
    Helixi531 – 5388
    Beta strandi543 – 5508
    Beta strandi553 – 56311
    Turni564 – 5674
    Beta strandi568 – 5769
    Helixi578 – 5803
    Beta strandi582 – 5843
    Helixi585 – 59915
    Beta strandi604 – 6096
    Turni611 – 6133
    Helixi614 – 6185
    Turni619 – 6213
    Beta strandi623 – 6253
    Helixi630 – 6334
    Beta strandi644 – 6496
    Helixi727 – 74115
    Beta strandi742 – 7443
    Helixi746 – 7483
    Helixi754 – 7563
    Beta strandi757 – 7593
    Helixi760 – 7634
    Beta strandi764 – 7663
    Helixi770 – 7789
    Helixi785 – 80218
    Beta strandi805 – 8073
    Helixi808 – 82619
    Beta strandi828 – 8303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CM0X-ray2.30A/B493-658[»]
    1JM4NMR-B719-832[»]
    1N72NMR-A719-832[»]
    1WUGNMR-A719-832[»]
    1WUMNMR-A719-832[»]
    1ZS5NMR-A719-832[»]
    2RNWNMR-A719-832[»]
    2RNXNMR-A719-832[»]
    3GG3X-ray2.25A/B715-831[»]
    4NSQX-ray2.31A/B/C/D493-658[»]
    ProteinModelPortaliQ92831.
    SMRiQ92831. Positions 493-653, 719-832.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92831.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini503 – 651149N-acetyltransferaseBy similarityPROSITE-ProRule annotationAdd
    BLAST
    Domaini740 – 81071BromoCuratedPROSITE-ProRule annotationAdd
    BLAST

    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.
    HOGENOMiHOG000007151.
    InParanoidiQ92831.
    KOiK06062.
    OMAiKIMMWLV.
    OrthoDBiEOG7ZKS9B.
    PhylomeDBiQ92831.
    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.

    Q92831-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEAGGAGPG GCGAGAGAGA GPGALPPQPA ALPPAPPQGS PCAAAAGGSG    50
    ACGPATAVAA AGTAEGPGGG GSARIAVKKA QLRSAPRAKK LEKLGVYSAC 100
    KAEESCKCNG WKNPNPSPTP PRADLQQIIV SLTESCRSCS HALAAHVSHL 150
    ENVSEEEMNR LLGIVLDVEY LFTCVHKEED ADTKQVYFYL FKLLRKSILQ 200
    RGKPVVEGSL EKKPPFEKPS IEQGVNNFVQ YKFSHLPAKE RQTIVELAKM 250
    FLNRINYWHL EAPSQRRLRS PNDDISGYKE NYTRWLCYCN VPQFCDSLPR 300
    YETTQVFGRT LLRSVFTVMR RQLLEQARQE KDKLPLEKRT LILTHFPKFL 350
    SMLEEEVYSQ NSPIWDQDFL SASSRTSQLG IQTVINPPPV AGTISYNSTS 400
    SSLEQPNAGS SSPACKASSG LEANPGEKRK MTDSHVLEEA KKPRVMGDIP 450
    MELINEVMST ITDPAAMLGP ETNFLSAHSA RDEAARLEER RGVIEFHVVG 500
    NSLNQKPNKK ILMWLVGLQN VFSHQLPRMP KEYITRLVFD PKHKTLALIK 550
    DGRVIGGICF RMFPSQGFTE IVFCAVTSNE QVKGYGTHLM NHLKEYHIKH 600
    DILNFLTYAD EYAIGYFKKQ GFSKEIKIPK TKYVGYIKDY EGATLMGCEL 650
    NPRIPYTEFS VIIKKQKEII KKLIERKQAQ IRKVYPGLSC FKDGVRQIPI 700
    ESIPGIRETG WKPSGKEKSK EPRDPDQLYS TLKSILQQVK SHQSAWPFME 750
    PVKRTEAPGY YEVIRFPMDL KTMSERLKNR YYVSKKLFMA DLQRVFTNCK 800
    EYNPPESEYY KCANILEKFF FSKIKEAGLI DK 832
    Length:832
    Mass (Da):93,013
    Last modified:May 10, 2005 - v3
    Checksum:i72F516E8BC00CC0C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti804 – 8052PP → AA in AAC50890. (PubMed:8684459)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti386 – 3861N → S.
    Corresponds to variant rs17006625 [ dbSNP | Ensembl ].
    VAR_034372

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U57317 mRNA. Translation: AAC50890.2.
    BC060823 mRNA. Translation: AAH60823.1.
    BC070075 mRNA. Translation: AAH70075.1.
    CCDSiCCDS2634.1.
    PIRiS71788.
    RefSeqiNP_003875.3. NM_003884.4.
    UniGeneiHs.533055.

    Genome annotation databases

    EnsembliENST00000263754; ENSP00000263754; ENSG00000114166.
    GeneIDi8850.
    KEGGihsa:8850.
    UCSCiuc003cbq.3. human.

    Polymorphism databases

    DMDMi83287776.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U57317 mRNA. Translation: AAC50890.2 .
    BC060823 mRNA. Translation: AAH60823.1 .
    BC070075 mRNA. Translation: AAH70075.1 .
    CCDSi CCDS2634.1.
    PIRi S71788.
    RefSeqi NP_003875.3. NM_003884.4.
    UniGenei Hs.533055.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CM0 X-ray 2.30 A/B 493-658 [» ]
    1JM4 NMR - B 719-832 [» ]
    1N72 NMR - A 719-832 [» ]
    1WUG NMR - A 719-832 [» ]
    1WUM NMR - A 719-832 [» ]
    1ZS5 NMR - A 719-832 [» ]
    2RNW NMR - A 719-832 [» ]
    2RNX NMR - A 719-832 [» ]
    3GG3 X-ray 2.25 A/B 715-831 [» ]
    4NSQ X-ray 2.31 A/B/C/D 493-658 [» ]
    ProteinModelPortali Q92831.
    SMRi Q92831. Positions 493-653, 719-832.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114375. 136 interactions.
    DIPi DIP-29778N.
    IntActi Q92831. 35 interactions.
    MINTi MINT-150079.
    STRINGi 9606.ENSP00000263754.

    Chemistry

    BindingDBi Q92831.
    ChEMBLi CHEMBL5500.
    GuidetoPHARMACOLOGYi 2737.

    PTM databases

    PhosphoSitei Q92831.

    Polymorphism databases

    DMDMi 83287776.

    2D gel databases

    REPRODUCTION-2DPAGE Q92831.

    Proteomic databases

    MaxQBi Q92831.
    PaxDbi Q92831.
    PRIDEi Q92831.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263754 ; ENSP00000263754 ; ENSG00000114166 .
    GeneIDi 8850.
    KEGGi hsa:8850.
    UCSCi uc003cbq.3. human.

    Organism-specific databases

    CTDi 8850.
    GeneCardsi GC03P020081.
    HGNCi HGNC:8638. KAT2B.
    HPAi CAB004526.
    MIMi 602303. gene.
    neXtProti NX_Q92831.
    PharmGKBi PA162392705.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000007151.
    InParanoidi Q92831.
    KOi K06062.
    OMAi KIMMWLV.
    OrthoDBi EOG7ZKS9B.
    PhylomeDBi Q92831.
    TreeFami TF105399.

    Enzyme and pathway databases

    Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    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.

    Miscellaneous databases

    ChiTaRSi KAT2B. human.
    EvolutionaryTracei Q92831.
    GeneWikii PCAF.
    GenomeRNAii 8850.
    NextBioi 33221.
    PROi Q92831.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q92831.
    CleanExi HS_KAT2B.
    Genevestigatori Q92831.

    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. "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 [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH EP300 AND CREBBP.
      Tissue: Liver.
    2. Nakatani Y.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
      Tissue: Liver.
    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].
    4. "The transcriptional coactivators p300 and CBP are histone acetyltransferases."
      Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y.
      Cell 87:953-959(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY.
    5. "TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1."
      Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W.
      J. Biol. Chem. 272:27629-27634(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA3.
    6. Cited for: INTERACTION WITH NCOA1.
    7. "Acetylation and modulation of erythroid Krueppel-like factor (EKLF) activity by interaction with histone acetyltransferases."
      Zhang W., Bieker J.J.
      Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KLF1, FUNCTION.
    8. Cited for: INTERACTION WITH E2F1, FUNCTION.
    9. "p300 and p300/cAMP-responsive element-binding protein associated factor interact with human T-cell lymphotropic virus type-1 Tax in a multi-histone acetyltransferase/activator-enhancer complex."
      Harrod R., Kuo Y.-L., Tang Y., Yao Y., Vassilev A., Nakatani Y., Giam C.-Z.
      J. Biol. Chem. 275:11852-11857(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 TAX.
    10. "Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles."
      Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.
      J. Biol. Chem. 276:44936-44943(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MECOM.
    11. "Differential acetylation of Tat coordinates its interaction with the co-activators cyclin T1 and PCAF."
      Bres V., Tagami H., Peloponese J.-M., Loret E., Jeang K.-T., Nakatani Y., Emiliani S., Benkirane M., Kiernan R.E.
      EMBO J. 21:6811-6819(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    12. "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock."
      Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., Chakravarti D., FitzGerald G.A., McNamara P.
      J. Biol. Chem. 279:7091-7097(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NPAS2; ARNTL/BMAL1 AND CLOCK.
    13. "Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1."
      Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.
      J. Biol. Chem. 279:41477-41486(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFE4.
    14. "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.
    15. "Modulation of testicular receptor 4 activity by mitogen-activated protein kinase-mediated phosphorylation."
      Huq M.D., Gupta P., Tsai N.P., Wei L.N.
      Mol. Cell. Proteomics 5:2072-2082(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR2C2.
    16. "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF."
      Shin S., Janknecht R.
      J. Cell. Biochem. 101:1252-1265(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX17.
    17. "Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth."
      Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.
      Mol. Cell 51:506-518(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Structure and ligand of a histone acetyltransferase bromodomain."
      Dhalluin C., Carlson J.E., Zeng L., He C., Aggarwal A.K., Zhou M.-M.
      Nature 399:491-496(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 715-832, MUTAGENESIS OF VAL-752; TYR-760; TYR-802 AND TYR-809.
      Tissue: Liver.
    19. "Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain."
      Mujtaba S., He Y., Zeng L., Farooq A., Carlson J.E., Ott M., Verdin E., Zhou M.-M.
      Mol. Cell 9:575-586(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 719-832 IN COMPLEX WITH HIV-1 TAT.
    20. "A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation."
      Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G.
      Mol. Cell 27:609-621(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 715-831.

    Entry informationi

    Entry nameiKAT2B_HUMAN
    AccessioniPrimary (citable) accession number: Q92831
    Secondary accession number(s): Q6NSK1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2002
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 158 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 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3