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Q5RBG4

- KAT5_PONAB

UniProt

Q5RBG4 - KAT5_PONAB

Protein

Histone acetyltransferase KAT5

Gene

KAT5

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    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. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei275 – 2751By similarity
    Active sitei317 – 3171NucleophileBy similarity
    Binding sitei320 – 3201Acetyl-CoABy similarity
    Binding sitei355 – 3551Acetyl-CoABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri209 – 23123C2HC-typeAdd
    BLAST

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
    2. histone acetylation Source: GOC
    3. positive regulation of transcription, DNA-templated Source: UniProtKB
    4. regulation of growth Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Acyltransferase, Chromatin regulator, Transferase

    Keywords - Biological processi

    Growth regulation, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    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
    Lysine acetyltransferase 5
    Gene namesi
    Name:KAT5
    Synonyms:HTATIP, TIP60
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Nucleus By similarity. Nucleusnucleolus By similarity. Cytoplasmperinuclear region By similarity
    Note: Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region.By similarity

    GO - Cellular componenti

    1. NuA4 histone acetyltransferase complex Source: UniProtKB
    2. nucleolus Source: UniProtKB
    3. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    4. Piccolo NuA4 histone acetyltransferase complex Source: UniProtKB
    5. Swr1 complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Histone acetyltransferase KAT5PRO_0000245806Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei52 – 521N6-acetyllysineBy similarity
    Modified residuei86 – 861PhosphoserineBy similarity
    Modified residuei90 – 901PhosphoserineBy similarity
    Modified residuei275 – 2751N6-acetyllysine; by autocatalysisBy similarity
    Cross-linki378 – 378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki399 – 399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Sumoylated by UBE2I at Lys-378 and Lys-399, leading to increase of its histone acetyltransferase activity in UV-induced DNA damage response, as well as its translocation to nuclear bodies.By similarity
    Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase. Phosphorylated form has a higher activity By similarity.By similarity
    Ubiquitinated by MDM2, leading to its proteasome-dependent degradation.By similarity
    Autoacetylation at Lys-275 is required for proper function.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ5RBG4.

    Interactioni

    Subunit structurei

    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 By similarity. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4 By similarity. The NuA4 complex interacts with MYC By similarity. Interacts with ATM By similarity. Interacts with JADE1 By similarity. Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7 By similarity. Interacts with the cytoplasmic tail of APP. Interacts with the cytoplasmic tail of APP and APBB1/FE65 By similarity. Interacts with TRIM24 and TRIM68 By similarity. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Identified in a complex with HINT1 By similarity. Interacts with ATF2 and CUL3. Interacts with NR1D2 (via N-terminus). Component of a SWR1-like complex By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5RBG4.
    SMRiQ5RBG4. Positions 11-79, 178-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini175 – 452278MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni316 – 461146Interaction with ATF2By similarityAdd
    BLAST
    Regioni325 – 3317Acetyl-CoA bindingBy similarity

    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 fingeri209 – 23123C2HC-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    KOiK11304.

    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]

    Sequencei

    Sequence statusi: Complete.

    Q5RBG4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF    50
    NKRLDEWVTH ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVKRKVE 100
    VVSPATPVPS ETAPASVFPQ NGAARRAVAA QPGRKRKSNC LGTDEDSQDS 150
    SDGIPSAPRM TGSLVSDRSH DDIVTRMKNI ECIELGRHRL KPWYFSPYPQ 200
    ELTTLPVLYL CEFCLKYGRS LKCLQRHLTK CDLRHPPGNE IYRKGTISFF 250
    EIDGRKNKSY SQNLCLLAKC FLDHKTLYYD TDPFLFYVMT EYDCKGFHIV 300
    GYFSKEKEST EDYNVACILT LPPYQRRGYG KLLIEFSYEL SKVEGKTGTP 350
    EKPLSDLGLL SYRSYWSQTI LEILMGLKSE SGERPQITIN EISEITSIKK 400
    EDVISTLQYL NLINYYKGQY ILTLSEDIVD GHERAMLKRL LRIDSKCLHF 450
    TPKDWSKRGK W 461
    Length:461
    Mass (Da):53,077
    Last modified:December 21, 2004 - v1
    Checksum:i5A0E9324550AF246
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR858684 mRNA. Translation: CAH90896.1.
    RefSeqiNP_001127347.1. NM_001133875.1.
    UniGeneiPab.13524.

    Genome annotation databases

    GeneIDi100174410.
    KEGGipon:100174410.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR858684 mRNA. Translation: CAH90896.1 .
    RefSeqi NP_001127347.1. NM_001133875.1.
    UniGenei Pab.13524.

    3D structure databases

    ProteinModelPortali Q5RBG4.
    SMRi Q5RBG4. Positions 11-79, 178-452.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5RBG4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100174410.
    KEGGi pon:100174410.

    Organism-specific databases

    CTDi 10524.

    Phylogenomic databases

    KOi K11304.

    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Heart.

    Entry informationi

    Entry nameiKAT5_PONAB
    AccessioniPrimary (citable) accession number: Q5RBG4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3