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Q5RBG4 (KAT5_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KAT5
Synonyms:HTATIP, TIP60
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Subunit structure

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.

Subcellular location

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.

Post-translational modification

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.

Ubiquitinated by MDM2, leading to its proteasome-dependent degradation By similarity.

Autoacetylation at Lys-275 is required for proper function By similarity.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Contains 1 C2HC-type zinc finger.

Ontologies

Keywords
   Biological processGrowth regulation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Transferase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetylation

Inferred from sequence or structural similarity. Source: GOC

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuA4 histone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

Piccolo NuA4 histone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

Swr1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Histone acetyltransferase KAT5
PRO_0000245806

Regions

Zinc finger209 – 23123C2HC-type
Region316 – 461146Interaction with ATF2 By similarity
Region325 – 3317Acetyl-CoA binding By similarity

Sites

Active site2751 By similarity
Active site3171Nucleophile By similarity
Binding site3201Acetyl-CoA By similarity
Binding site3551Acetyl-CoA By similarity

Amino acid modifications

Modified residue521N6-acetyllysine By similarity
Modified residue861Phosphoserine By similarity
Modified residue901Phosphoserine By similarity
Modified residue2751N6-acetyllysine; by autocatalysis By similarity
Cross-link378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RBG4 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 5A0E9324550AF246

FASTA46153,077
        10         20         30         40         50         60 
MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF NKRLDEWVTH 

        70         80         90        100        110        120 
ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVKRKVE VVSPATPVPS ETAPASVFPQ 

       130        140        150        160        170        180 
NGAARRAVAA QPGRKRKSNC LGTDEDSQDS SDGIPSAPRM TGSLVSDRSH DDIVTRMKNI 

       190        200        210        220        230        240 
ECIELGRHRL KPWYFSPYPQ ELTTLPVLYL CEFCLKYGRS LKCLQRHLTK CDLRHPPGNE 

       250        260        270        280        290        300 
IYRKGTISFF EIDGRKNKSY SQNLCLLAKC FLDHKTLYYD TDPFLFYVMT EYDCKGFHIV 

       310        320        330        340        350        360 
GYFSKEKEST EDYNVACILT LPPYQRRGYG KLLIEFSYEL SKVEGKTGTP EKPLSDLGLL 

       370        380        390        400        410        420 
SYRSYWSQTI LEILMGLKSE SGERPQITIN EISEITSIKK EDVISTLQYL NLINYYKGQY 

       430        440        450        460 
ILTLSEDIVD GHERAMLKRL LRIDSKCLHF TPKDWSKRGK W 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858684 mRNA. Translation: CAH90896.1.
RefSeqNP_001127347.1. NM_001133875.1.
UniGenePab.13524.

3D structure databases

ProteinModelPortalQ5RBG4.
SMRQ5RBG4. Positions 11-79, 178-452.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5RBG4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174410.
KEGGpon:100174410.

Organism-specific databases

CTD10524.

Phylogenomic databases

KOK11304.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKAT5_PONAB
AccessionPrimary (citable) accession number: Q5RBG4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families