Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q92993

- KAT5_HUMAN

UniProt

Q92993 - KAT5_HUMAN

Protein

Histone acetyltransferase KAT5

Gene

KAT5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (16 May 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2.10 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei327 – 3271By similarity
    Active sitei369 – 3691NucleophileBy similarity
    Binding sitei372 – 3721Acetyl-CoA
    Binding sitei407 – 4071Acetyl-CoA

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri261 – 28323C2HC-typeAdd
    BLAST

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. histone acetyltransferase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. repressing transcription factor binding Source: BHF-UCL
    6. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. cellular response to estradiol stimulus Source: UniProt
    3. chromatin organization Source: Reactome
    4. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
    5. double-strand break repair Source: UniProtKB
    6. histone acetylation Source: UniProtKB
    7. negative regulation of interleukin-2 production Source: BHF-UCL
    8. negative regulation of transcription, DNA-templated Source: BHF-UCL
    9. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    10. positive regulation of transcription, DNA-templated Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: UniProt
    12. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    13. regulation of growth Source: UniProtKB-KW
    14. response to ionizing radiation Source: UniProtKB
    15. transcription, DNA-templated Source: UniProtKB-KW
    16. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Acyltransferase, Chromatin regulator, Transferase

    Keywords - Biological processi

    Growth regulation, Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    SignaLinkiQ92993.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase KAT5 (EC:2.3.1.48)
    Alternative name(s):
    60 kDa Tat-interactive protein
    Short name:
    Tip60
    Histone acetyltransferase HTATIP
    Short name:
    HIV-1 Tat interactive protein
    Lysine acetyltransferase 5
    cPLA(2)-interacting protein
    Gene namesi
    Name:KAT5
    Synonyms:HTATIP, TIP60
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:5275. KAT5.

    Subcellular locationi

    Nucleus. Nucleusnucleolus. Cytoplasmperinuclear region
    Note: Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region and UV irradiation induces translocation into punctuate subnuclear structures named nuclear bodies.

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. NuA4 histone acetyltransferase complex Source: UniProtKB
    3. nucleolus Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. Piccolo NuA4 histone acetyltransferase complex Source: UniProtKB
    8. Swr1 complex Source: UniProtKB
    9. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 861S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-90. Reduced activity. 1 Publication
    Mutagenesisi90 – 901S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-86. Reduced activity. 1 Publication
    Mutagenesisi254 – 2541L → A: Does not affect phosphorylation; when associated with A-257. 1 Publication
    Mutagenesisi257 – 2571L → A: Does not affect phosphorylation; when associated with A-254. 1 Publication
    Mutagenesisi380 – 3801G → A: Loss of function. Does not affect phosphorylation. 1 Publication
    Mutagenesisi430 – 4301K → R: Abrogates sumoylation. 1 Publication
    Mutagenesisi451 – 4511K → R: Abrogates sumoylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA162392746.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 513513Histone acetyltransferase KAT5PRO_0000051580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei52 – 521N6-acetyllysine1 Publication
    Modified residuei86 – 861Phosphoserine1 Publication
    Modified residuei90 – 901Phosphoserine; by CDK11 Publication
    Modified residuei327 – 3271N6-acetyllysine; by autocatalysisBy similarity
    Cross-linki430 – 430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki451 – 451Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of its histone acetyltransferase activity in UV-induced DNA damage response, as well as its translocation to nuclear bodies.1 Publication
    Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase. Phosphorylated form has a higher activity.1 Publication
    Ubiquitinated by MDM2, leading to its proteasome-dependent degradation.1 Publication
    Autoacetylation at Lys-327 is required for proper function.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ92993.
    PaxDbiQ92993.
    PRIDEiQ92993.

    PTM databases

    PhosphoSiteiQ92993.

    Expressioni

    Gene expression databases

    ArrayExpressiQ92993.
    BgeeiQ92993.
    CleanExiHS_KAT5.
    GenevestigatoriQ92993.

    Organism-specific databases

    HPAiHPA016953.

    Interactioni

    Subunit structurei

    Interacts with the cytoplasmic tail of APP and APBB1/FE65 By similarity. Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. The NuA4 complex interacts with MYC and the adenovirus E1A protein. Interacts with ATM. Interacts with JADE1. Interacts with HIV-1 Tat. Interacts with TRIM24 and TRIM68. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Identified in a complex with HINT1. Interacts with ATF2 and CUL3. Interacts with NR1D2 (via N-terminus). Component of a SWR1-like complex.By similarity17 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN1P542533EBI-399080,EBI-930964
    CBX8Q9HC522EBI-399080,EBI-712912
    DLEU1O432612EBI-399080,EBI-710057
    GADD45GO952572EBI-399080,EBI-448202
    KIAA1377Q9P2H02EBI-399080,EBI-473176
    Myod1P100855EBI-399080,EBI-4405734From a different organism.
    PTPN4P290742EBI-399080,EBI-710431
    SRSF2Q011303EBI-399080,EBI-627047
    TP53P046373EBI-399080,EBI-366083

    Protein-protein interaction databases

    BioGridi115779. 178 interactions.
    DIPiDIP-5998N.
    IntActiQ92993. 69 interactions.
    MINTiMINT-94861.
    STRINGi9606.ENSP00000340330.

    Structurei

    Secondary structure

    1
    513
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 154
    Beta strandi28 – 347
    Beta strandi37 – 393
    Beta strandi43 – 475
    Beta strandi56 – 583
    Turni60 – 623
    Helixi65 – 673
    Beta strandi235 – 2373
    Beta strandi240 – 2423
    Helixi252 – 2543
    Beta strandi260 – 2623
    Turni264 – 2663
    Beta strandi269 – 2713
    Helixi273 – 28210
    Beta strandi289 – 2968
    Beta strandi299 – 3057
    Turni306 – 3083
    Helixi310 – 32112
    Turni328 – 3314
    Beta strandi336 – 34510
    Beta strandi348 – 36013
    Beta strandi365 – 3684
    Beta strandi370 – 3723
    Helixi374 – 3763
    Helixi381 – 39515
    Beta strandi400 – 4023
    Helixi408 – 42518
    Helixi441 – 4488
    Helixi452 – 46110
    Beta strandi469 – 4746
    Helixi497 – 4993

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EKONMR-A5-78[»]
    2OU2X-ray2.30A227-506[»]
    ProteinModelPortaliQ92993.
    SMRiQ92993. Positions 11-79, 230-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92993.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini227 – 504278MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni368 – 513146Interaction with ATF2Add
    BLAST
    Regioni377 – 3837Acetyl-CoA binding

    Sequence similaritiesi

    Belongs to the MYST (SAS/MOZ) family.Curated
    Contains 1 C2HC-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri261 – 28323C2HC-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5027.
    HOGENOMiHOG000182457.
    KOiK11304.
    OMAiHDDIITR.
    OrthoDBiEOG7ZKS9R.
    PhylomeDBiQ92993.
    TreeFamiTF317619.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR002717. MOZ_SAS.
    IPR025995. Tudor-knot.
    [Graphical view]
    PfamiPF01853. MOZ_SAS. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view]
    SMARTiSM00298. CHROMO. 1 hit.
    [Graphical view]
    SUPFAMiSSF54160. SSF54160. 1 hit.
    SSF55729. SSF55729. 1 hit.
    PROSITEiPS51726. MYST_HAT. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92993-1) [UniParc]FASTAAdd to Basket

    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

    MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF    50
    NKRLDEWVTH ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVPASAQ 100
    ASGKTLPIPV QITLRFNLPK EREAIPGGEP DQPLSSSSCL QPNHRSTKRK 150
    VEVVSPATPV PSETAPASVF PQNGAARRAV AAQPGRKRKS NCLGTDEDSQ 200
    DSSDGIPSAP RMTGSLVSDR SHDDIVTRMK NIECIELGRH RLKPWYFSPY 250
    PQELTTLPVL YLCEFCLKYG RSLKCLQRHL TKCDLRHPPG NEIYRKGTIS 300
    FFEIDGRKNK SYSQNLCLLA KCFLDHKTLY YDTDPFLFYV MTEYDCKGFH 350
    IVGYFSKEKE STEDYNVACI LTLPPYQRRG YGKLLIEFSY ELSKVEGKTG 400
    TPEKPLSDLG LLSYRSYWSQ TILEILMGLK SESGERPQIT INEISEITSI 450
    KKEDVISTLQ YLNLINYYKG QYILTLSEDI VDGHERAMLK RLLRIDSKCL 500
    HFTPKDWSKR GKW 513
    Length:513
    Mass (Da):58,582
    Last modified:May 16, 2003 - v2
    Checksum:i63724F5E10B957D5
    GO
    Isoform 2 (identifier: Q92993-2) [UniParc]FASTAAdd to Basket

    Also known as: PLIP

    The sequence of this isoform differs from the canonical sequence as follows:
         96-147: Missing.

    Show »
    Length:461
    Mass (Da):53,077
    Checksum:i5A0E9324550AF246
    GO
    Isoform 3 (identifier: Q92993-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         4-4: V → VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ

    Show »
    Length:546
    Mass (Da):61,798
    Checksum:i0CEB1A8E8C8D3E24
    GO
    Isoform 4 (identifier: Q92993-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         4-4: V → VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ
         96-147: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:494
    Mass (Da):56,292
    Checksum:i761BF5859BE89793
    GO

    Sequence cautioni

    The sequence AAB02683.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti382 – 3821G → R in AAB18236. (PubMed:8607265)Curated
    Sequence conflicti382 – 3821G → R in AAB02683. (PubMed:8607265)Curated
    Isoform 3 (identifier: Q92993-3)
    Sequence conflicti32 – 321V → A no nucleotide entry (PubMed:12801643)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti78 – 781P → T.
    Corresponds to variant rs11541271 [ dbSNP | Ensembl ].
    VAR_059456

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei4 – 41V → VVSPVPGAGRREPGEVGRAR GPPVADPGVALSPQ in isoform 3 and isoform 4. 2 PublicationsVSP_009104
    Alternative sequencei96 – 14752Missing in isoform 2 and isoform 4. 3 PublicationsVSP_007438Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U74667 mRNA. Translation: AAB18236.1.
    U40989 mRNA. Translation: AAB02683.1. Different initiation.
    U67734 mRNA. Translation: AAD00163.1.
    AY214165 Genomic DNA. Translation: AAO21130.1.
    AK304664 mRNA. Translation: BAG65439.1.
    AP001266 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74427.1.
    CH471076 Genomic DNA. Translation: EAW74429.1.
    BC000166 mRNA. Translation: AAH00166.3.
    BC064912 mRNA. Translation: AAH64912.1.
    BC093032 mRNA. Translation: AAH93032.1.
    BC143296 mRNA. Translation: AAI43297.1.
    BC117167 mRNA. Translation: AAI17168.1.
    CCDSiCCDS31610.1. [Q92993-1]
    CCDS55771.1. [Q92993-4]
    CCDS8109.1. [Q92993-2]
    CCDS8110.1. [Q92993-3]
    RefSeqiNP_001193762.1. NM_001206833.1. [Q92993-4]
    NP_006379.2. NM_006388.3. [Q92993-1]
    NP_874368.1. NM_182709.2. [Q92993-2]
    NP_874369.1. NM_182710.2. [Q92993-3]
    UniGeneiHs.397010.

    Genome annotation databases

    EnsembliENST00000341318; ENSP00000340330; ENSG00000172977. [Q92993-3]
    ENST00000352980; ENSP00000344955; ENSG00000172977. [Q92993-2]
    ENST00000377046; ENSP00000366245; ENSG00000172977. [Q92993-1]
    ENST00000530446; ENSP00000434765; ENSG00000172977. [Q92993-4]
    GeneIDi10524.
    KEGGihsa:10524.
    UCSCiuc001ofi.3. human. [Q92993-1]
    uc001ofj.3. human. [Q92993-2]
    uc001ofk.3. human. [Q92993-3]
    uc010roo.2. human. [Q92993-4]

    Polymorphism databases

    DMDMi30923328.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U74667 mRNA. Translation: AAB18236.1 .
    U40989 mRNA. Translation: AAB02683.1 . Different initiation.
    U67734 mRNA. Translation: AAD00163.1 .
    AY214165 Genomic DNA. Translation: AAO21130.1 .
    AK304664 mRNA. Translation: BAG65439.1 .
    AP001266 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74427.1 .
    CH471076 Genomic DNA. Translation: EAW74429.1 .
    BC000166 mRNA. Translation: AAH00166.3 .
    BC064912 mRNA. Translation: AAH64912.1 .
    BC093032 mRNA. Translation: AAH93032.1 .
    BC143296 mRNA. Translation: AAI43297.1 .
    BC117167 mRNA. Translation: AAI17168.1 .
    CCDSi CCDS31610.1. [Q92993-1 ]
    CCDS55771.1. [Q92993-4 ]
    CCDS8109.1. [Q92993-2 ]
    CCDS8110.1. [Q92993-3 ]
    RefSeqi NP_001193762.1. NM_001206833.1. [Q92993-4 ]
    NP_006379.2. NM_006388.3. [Q92993-1 ]
    NP_874368.1. NM_182709.2. [Q92993-2 ]
    NP_874369.1. NM_182710.2. [Q92993-3 ]
    UniGenei Hs.397010.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EKO NMR - A 5-78 [» ]
    2OU2 X-ray 2.30 A 227-506 [» ]
    ProteinModelPortali Q92993.
    SMRi Q92993. Positions 11-79, 230-504.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115779. 178 interactions.
    DIPi DIP-5998N.
    IntActi Q92993. 69 interactions.
    MINTi MINT-94861.
    STRINGi 9606.ENSP00000340330.

    Chemistry

    BindingDBi Q92993.
    ChEMBLi CHEMBL5750.
    GuidetoPHARMACOLOGYi 2664.

    PTM databases

    PhosphoSitei Q92993.

    Polymorphism databases

    DMDMi 30923328.

    Proteomic databases

    MaxQBi Q92993.
    PaxDbi Q92993.
    PRIDEi Q92993.

    Protocols and materials databases

    DNASUi 10524.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341318 ; ENSP00000340330 ; ENSG00000172977 . [Q92993-3 ]
    ENST00000352980 ; ENSP00000344955 ; ENSG00000172977 . [Q92993-2 ]
    ENST00000377046 ; ENSP00000366245 ; ENSG00000172977 . [Q92993-1 ]
    ENST00000530446 ; ENSP00000434765 ; ENSG00000172977 . [Q92993-4 ]
    GeneIDi 10524.
    KEGGi hsa:10524.
    UCSCi uc001ofi.3. human. [Q92993-1 ]
    uc001ofj.3. human. [Q92993-2 ]
    uc001ofk.3. human. [Q92993-3 ]
    uc010roo.2. human. [Q92993-4 ]

    Organism-specific databases

    CTDi 10524.
    GeneCardsi GC11P065479.
    HGNCi HGNC:5275. KAT5.
    HPAi HPA016953.
    MIMi 601409. gene.
    neXtProti NX_Q92993.
    PharmGKBi PA162392746.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5027.
    HOGENOMi HOG000182457.
    KOi K11304.
    OMAi HDDIITR.
    OrthoDBi EOG7ZKS9R.
    PhylomeDBi Q92993.
    TreeFami TF317619.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    SignaLinki Q92993.

    Miscellaneous databases

    EvolutionaryTracei Q92993.
    GeneWikii KAT5.
    GenomeRNAii 10524.
    NextBioi 39922.
    PROi Q92993.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92993.
    Bgeei Q92993.
    CleanExi HS_KAT5.
    Genevestigatori Q92993.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR002717. MOZ_SAS.
    IPR025995. Tudor-knot.
    [Graphical view ]
    Pfami PF01853. MOZ_SAS. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view ]
    SMARTi SM00298. CHROMO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54160. SSF54160. 1 hit.
    SSF55729. SSF55729. 1 hit.
    PROSITEi PS51726. MYST_HAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator."
      Kamine J., Elangovan B., Subramanian T., Coleman D., Chinnadurai G.
      Virology 216:357-366(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HIV-1 TAT.
      Tissue: Lymphoblast.
    2. "PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production."
      Sheridan A.M., Force T., Yoon H.J., O'Leary E., Choukroun G., Taheri M.R., Bonventre J.V.
      Mol. Cell. Biol. 21:4470-4481(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PLA2G4A, SUBCELLULAR LOCATION.
      Tissue: Fibroblast and Placenta.
    3. "Identification of a larger form of the histone acetyl transferase Tip60."
      Legube G., Trouche D.
      Gene 310:161-168(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    4. NIEHS SNPs program
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Uterus.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1 AND 2).
      Tissue: Cervix, Liver, Placenta and Testis.
    9. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
      Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
      J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-35; 150-177 AND 297-307, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Tip60 acetylates six lysines of a specific class in core histones in vitro."
      Kimura A., Horikoshi M.
      Genes Cells 3:789-800(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY IN VITRO.
    11. "Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis."
      Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M., Scully R., Qin J., Nakatani Y.
      Cell 102:463-473(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling."
      Lee H.-J., Chun M., Kandror K.V.
      J. Biol. Chem. 276:16597-16600(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EDNRA.
    13. "Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation."
      Legube G., Linares L.K., Lemercier C., Scheffner M., Khochbin S., Trouche D.
      EMBO J. 21:1704-1712(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    14. "MYC recruits the TIP60 histone acetyltransferase complex to chromatin."
      Frank S.R., Parisi T., Taubert S., Fernandez P., Fuchs M., Chan H.M., Livingston D.M., Amati B.
      EMBO Rep. 4:575-580(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN MYC-DEPENDENT TRANSCRIPTION.
    15. "Tip60 acetyltransferase activity is controlled by phosphorylation."
      Lemercier C., Legube G., Caron C., Louwagie M., Garin J., Trouche D., Khochbin S.
      J. Biol. Chem. 278:4713-4718(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-86 AND SER-90, MUTAGENESIS OF SER-86; SER-90; LEU-254; LEU-257 AND GLY-380.
    16. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HDAC7.
    17. "The highly conserved and multifunctional NuA4 HAT complex."
      Doyon Y., Cote J.
      Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON NUA4 COMPLEX.
    18. Cited for: ROLE IN TP53-DEPENDENT TRANSCRIPTION.
    19. "von Hippel-Lindau partner Jade-1 is a transcriptional co-activator associated with histone acetyltransferase activity."
      Panchenko M.V., Zhou M.I., Cohen H.T.
      J. Biol. Chem. 279:56032-56041(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH JADE1.
    20. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
      Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
      Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 COMPLEX.
    21. "E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1."
      Taubert S., Gorrini C., Frank S.R., Parisi T., Fuchs M., Chan H.M., Livingston D.M., Amati B.
      Mol. Cell. Biol. 24:4546-4556(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN E2F1-DEPENDENT TRANSCRIPTION.
    22. Cited for: ROLE IN TP53-DEPENDENT TRANSCRIPTION.
    23. "HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses."
      Col E., Caron C., Chable-Bessia C., Legube G., Gazzeri S., Komatsu Y., Yoshida M., Benkirane M., Trouche D., Khochbin S.
      EMBO J. 24:2634-2645(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    24. "A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM."
      Sun Y., Jiang X., Chen S., Fernandes N., Price B.D.
      Proc. Natl. Acad. Sci. U.S.A. 102:13182-13187(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATM, FUNCTION.
    25. "The histidine triad protein Hint1 triggers apoptosis independent of its enzymatic activity."
      Weiske J., Huber O.
      J. Biol. Chem. 281:27356-27366(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH HINT1.
    26. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
      Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
      Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    27. "The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter."
      Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X., Lu H.
      Biochim. Biophys. Acta 1783:224-236(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NR1D2, SUBCELLULAR LOCATION.
    28. "TRIM68 regulates ligand-dependent transcription of androgen receptor in prostate cancer cells."
      Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M., Shinohara N., Nonomura K., Hatakeyama S.
      Cancer Res. 68:3486-3494(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM68.
    29. "Regulation of TIP60 by ATF2 modulates ATM activation."
      Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.
      J. Biol. Chem. 283:17605-17614(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF2 AND CUL3, PROTEASOMAL DEGRADATION.
    30. "Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response."
      Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z., Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M., Liang S., Wu Q., Reddy S.E.
      , Hu R., Huang H., Jin C., Yao X.
      Oncogene 27:931-941(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-430 AND LYS-451, MUTAGENESIS OF LYS-430 AND LYS-451, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. "TRIM24 mediates ligand-dependent activation of androgen receptor and is repressed by a bromodomain-containing protein, BRD7, in prostate cancer cells."
      Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J., Imamura M., Hatakeyama S.
      Biochim. Biophys. Acta 1793:1828-1836(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TRIM24.
    33. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    34. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
    36. "The crystal structure of acetyltransferase domain of human HIV-1 TAT interacting protein in complex with acetylcoenzyme A."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 227-506 IN COMPLEX WITH ACETYL COENZYME A AND ZINC IONS.
    37. "Solution structure of RUH-073, a pseudo chromo domain from human cDNA."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 5-78.

    Entry informationi

    Entry nameiKAT5_HUMAN
    AccessioniPrimary (citable) accession number: Q92993
    Secondary accession number(s): B4E3C7
    , C9JL99, O95624, Q13430, Q17RW5, Q561W3, Q6GSE8, Q9BWK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 16, 2003
    Last modified: October 1, 2014
    This is version 158 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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