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Q8CHK4 (KAT5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. 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 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. Cytoplasmperinuclear region By similarity. Note: Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region By similarity. Ref.1

Tissue specificity

Expressed in testis, heart, brain, kidney and liver. Weakly expressed in lung. Ref.1

Post-translational modification

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 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-327 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
   Coding sequence diversityAlternative splicing
   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

double-strand break repair

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-2 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 15944124. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12464179. Source: MGI

response to ionizing radiation

Inferred from electronic annotation. Source: Ensembl

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

cytosol

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

transcription factor complex

Inferred from direct assay PubMed 12464179. Source: MGI

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 17110330. Source: IntAct

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Atxn1P542542EBI-1169948,EBI-1169713

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CHK4-1)

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.
Isoform 2 (identifier: Q8CHK4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     96-147: Missing.
Isoform 3 (identifier: Q8CHK4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     4-4: V → VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ
Isoform 4 (identifier: Q8CHK4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-211: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513Histone acetyltransferase KAT5
PRO_0000051581

Regions

Zinc finger261 – 28323C2HC-type
Region368 – 513146Interaction with ATF2 By similarity
Region377 – 3837Acetyl-CoA binding By similarity

Sites

Active site3271 By similarity
Active site3691Nucleophile By similarity
Binding site3721Acetyl-CoA By similarity
Binding site4071Acetyl-CoA By similarity

Amino acid modifications

Modified residue521N6-acetyllysine By similarity
Modified residue861Phosphoserine By similarity
Modified residue901Phosphoserine; by CDK1 By similarity
Modified residue3271N6-acetyllysine; by autocatalysis By similarity
Cross-link430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link451Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 211211Missing in isoform 4.
VSP_009105
Alternative sequence41V → VVSPVPGAGRREPGEVGRAR GPPVADPGVALSPQ in isoform 3.
VSP_009106
Alternative sequence96 – 14752Missing in isoform 2.
VSP_009107

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2003. Version 2.
Checksum: EACEE4D544C0DB60

FASTA51358,598
        10         20         30         40         50         60 
MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF NKRLDEWVTH 

        70         80         90        100        110        120 
ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVPASAQ ASGKTLPIPV QITLRFNLPK 

       130        140        150        160        170        180 
EREAIPGGEP DQPLSSSSCL QPNHRSTKRK VEVVSPATPV PSETAPASVF PQNGSARRAV 

       190        200        210        220        230        240 
AAQPGRKRKS NCLGTDEDSQ DSSDGIPSAP RMTGSLVSDR SHDDIVTRMK NIECIELGRH 

       250        260        270        280        290        300 
RLKPWYFSPY PQELTTLPVL YLCEFCLKYG RSLKCLQRHL TKCDLRHPPG NEIYRKGTIS 

       310        320        330        340        350        360 
FFEIDGRKNK SYSQNLCLLA KCFLDHKTLY YDTDPFLFYV MTEYDCKGFH IVGYFSKEKE 

       370        380        390        400        410        420 
STEDYNVACI LTLPPYQRRG YGKLLIEFSY ELSKVEGKTG TPEKPLSDLG LLSYRSYWSQ 

       430        440        450        460        470        480 
TILEILMGLK SESGERPQIT INEISEITSI KKEDVISTLQ YLNLINYYKG QYILTLSEDI 

       490        500        510 
VDGHERAMLK RLLRIDSKCL HFTPKDWSKR GKW 

« Hide

Isoform 2 [UniParc].

Checksum: D3B238AF01737EF3
Show »

FASTA46153,093
Isoform 3 [UniParc].

Checksum: 8557B105D8F4B291
Show »

FASTA54661,814
Isoform 4 [UniParc].

Checksum: D96A7FCCB49FA85D
Show »

FASTA30235,396

References

« Hide 'large scale' references
[1]"Characterization and expression of the mouse tat interactive protein 60 kD (TIP60) gene."
McAllister D., Merlo X., Lough J.W.
Gene 289:169-176(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: 129/SvJ.
[2]"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 (ISOFORM 3).
[3]"Cloning of mouse Tip60."
Szendro P.I., Cadenas C., Eichele G.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6.
[4]"Isolation and characterization of novel human and mouse genes, which are expressed in the digestive tract."
Daigo Y., Takayama I., Fujino M.A.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Strain: W/Wv.
[5]"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] (ISOFORM 2).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY061983 Genomic DNA. Translation: AAL34981.1.
AF528194 mRNA. Translation: AAN77140.1.
AF528195 mRNA. Translation: AAN77141.1.
AF528196 mRNA. Translation: AAN77142.1.
AB055409 mRNA. Translation: BAC53807.1.
BC129968 mRNA. Translation: AAI29969.1.
CCDSCCDS29472.1. [Q8CHK4-1]
RefSeqNP_001186176.1. NM_001199247.1. [Q8CHK4-2]
NP_001186177.1. NM_001199248.1.
NP_848752.1. NM_178637.2. [Q8CHK4-1]
UniGeneMm.228930.

3D structure databases

ProteinModelPortalQ8CHK4.
SMRQ8CHK4. Positions 11-79, 230-504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid219884. 11 interactions.
IntActQ8CHK4. 24 interactions.
MINTMINT-4302182.

PTM databases

PhosphoSiteQ8CHK4.

Proteomic databases

MaxQBQ8CHK4.
PaxDbQ8CHK4.
PRIDEQ8CHK4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113641; ENSMUSP00000109271; ENSMUSG00000024926. [Q8CHK4-1]
GeneID81601.
KEGGmmu:81601.
UCSCuc008gdy.2. mouse. [Q8CHK4-1]
uc008geb.2. mouse. [Q8CHK4-2]

Organism-specific databases

CTD10524.
MGIMGI:1932051. Kat5.

Phylogenomic databases

eggNOGCOG5027.
GeneTreeENSGT00550000074503.
HOGENOMHOG000182457.
KOK11304.
OMAHDDIITR.
OrthoDBEOG7ZKS9R.
PhylomeDBQ8CHK4.
TreeFamTF317619.

Gene expression databases

BgeeQ8CHK4.
GenevestigatorQ8CHK4.

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...

Other

ChiTaRSKAT5. mouse.
NextBio350414.
PROQ8CHK4.
SOURCESearch...

Entry information

Entry nameKAT5_MOUSE
AccessionPrimary (citable) accession number: Q8CHK4
Secondary accession number(s): A1L394 expand/collapse secondary AC list , Q8CGZ3, Q8CGZ4, Q8VIH0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: July 9, 2014
This is version 111 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot