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Protein

Histone acetyltransferase KAT5

Gene

KAT5

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei351 – 3511Proton donor/acceptorBy similarity
Binding sitei355 – 3551Acetyl-CoABy similarity
Binding sitei364 – 3641Acetyl-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
Complete GO annotation...

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:2.3.1.48By similarity)
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
Complete GO annotation...

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. The phosphorylated form has a higher HAT activity.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
Regioni318 – 3203Acetyl-CoA bindingBy similarity
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

InParanoidiQ5RBG4.
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

        10         20         30         40         50
MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF
60 70 80 90 100
NKRLDEWVTH ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVKRKVE
110 120 130 140 150
VVSPATPVPS ETAPASVFPQ NGAARRAVAA QPGRKRKSNC LGTDEDSQDS
160 170 180 190 200
SDGIPSAPRM TGSLVSDRSH DDIVTRMKNI ECIELGRHRL KPWYFSPYPQ
210 220 230 240 250
ELTTLPVLYL CEFCLKYGRS LKCLQRHLTK CDLRHPPGNE IYRKGTISFF
260 270 280 290 300
EIDGRKNKSY SQNLCLLAKC FLDHKTLYYD TDPFLFYVMT EYDCKGFHIV
310 320 330 340 350
GYFSKEKEST EDYNVACILT LPPYQRRGYG KLLIEFSYEL SKVEGKTGTP
360 370 380 390 400
EKPLSDLGLL SYRSYWSQTI LEILMGLKSE SGERPQITIN EISEITSIKK
410 420 430 440 450
EDVISTLQYL NLINYYKGQY ILTLSEDIVD GHERAMLKRL LRIDSKCLHF
460
TPKDWSKRGK W
Length:461
Mass (Da):53,077
Last modified:December 21, 2004 - v1
Checksum:i5A0E9324550AF246
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CR858684 mRNA. Translation: CAH90896.1.
RefSeqiNP_001127347.1. NM_001133875.1.
UniGeneiPab.13524.

3D structure databases

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

Proteomic databases

PRIDEiQ5RBG4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100174410.
KEGGipon:100174410.

Organism-specific databases

CTDi10524.

Phylogenomic databases

InParanoidiQ5RBG4.
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]
ProtoNetiSearch...

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: January 7, 2015
This is version 77 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.