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Q99MK2

- KAT5_RAT

UniProt

Q99MK2 - KAT5_RAT

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Protein
Histone acetyltransferase KAT5
Gene
Kat5, Htatip, Tip60, Tip60b
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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. 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 activityi

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

Sites

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

Regions

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

GO - Molecular functioni

  1. histone acetyltransferase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: UniProtKB
  4. protein complex binding Source: RGD
  5. transcription coactivator activity Source: UniProtKB
  6. transcription factor binding Source: RGD
Complete GO annotation...

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
  2. double-strand break repair Source: Ensembl
  3. histone H4 acetylation Source: UniProtKB
  4. histone acetylation Source: RGD
  5. negative regulation of interleukin-2 production Source: Ensembl
  6. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  7. positive regulation of transcription from RNA polymerase II promoter Source: RGD
  8. positive regulation of transcription, DNA-templated Source: UniProtKB
  9. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  10. response to ionizing radiation Source: Ensembl
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198384. HATs acetylate histones.
REACT_226234. formation of the beta-catenin:TCF transactivating complex.

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, Tip60b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi621061. Kat5.

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. Piccolo NuA4 histone acetyltransferase complex Source: UniProtKB
  3. Swr1 complex Source: UniProtKB
  4. chromatin Source: RGD
  5. cytosol Source: RGD
  6. histone acetyltransferase complex Source: RGD
  7. nucleolus Source: UniProtKB
  8. nucleus Source: RGD
  9. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  10. protein complex Source: RGD
  11. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513Histone acetyltransferase KAT5
PRO_0000051582Add
BLAST

Amino acid modifications

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

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 By similarity.
Phosphorylated. 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.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ99MK2.

Expressioni

Gene expression databases

GenevestigatoriQ99MK2.

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 and APBB1/FE65. 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.2 Publications

Protein-protein interaction databases

BioGridi251357. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ99MK2.
SMRiQ99MK2. Positions 11-79, 230-504.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 513146Interaction with ATF2 By similarity
Add
BLAST
Regioni377 – 3837Acetyl-CoA binding By similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000182457.
KOiK11304.
OMAiHDDIITR.
OrthoDBiEOG7ZKS9R.
PhylomeDBiQ99MK2.

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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99MK2-1) [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 PQNGSARRAV 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):58,598
Last modified:July 11, 2006 - v2
Checksum:iEACEE4D544C0DB60
GO
Isoform 2 (identifier: Q99MK2-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:461
Mass (Da):53,093
Checksum:iD3B238AF01737EF3
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei96 – 14752Missing in isoform 2.
VSP_019781Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC083879 mRNA. Translation: AAH83879.1.
AF333984 mRNA. Translation: AAK20836.1.
RefSeqiNP_001005872.1. NM_001005872.1. [Q99MK2-1]
XP_006230725.1. XM_006230663.1. [Q99MK2-2]
UniGeneiRn.6629.

Genome annotation databases

EnsembliENSRNOT00000028107; ENSRNOP00000028107; ENSRNOG00000020707. [Q99MK2-2]
ENSRNOT00000041916; ENSRNOP00000039632; ENSRNOG00000020707. [Q99MK2-1]
GeneIDi192218.
KEGGirno:192218.
UCSCiRGD:621061. rat. [Q99MK2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC083879 mRNA. Translation: AAH83879.1 .
AF333984 mRNA. Translation: AAK20836.1 .
RefSeqi NP_001005872.1. NM_001005872.1. [Q99MK2-1 ]
XP_006230725.1. XM_006230663.1. [Q99MK2-2 ]
UniGenei Rn.6629.

3D structure databases

ProteinModelPortali Q99MK2.
SMRi Q99MK2. Positions 11-79, 230-504.
ModBasei Search...

Protein-protein interaction databases

BioGridi 251357. 1 interaction.

Chemistry

ChEMBLi CHEMBL1932911.

Proteomic databases

PaxDbi Q99MK2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000028107 ; ENSRNOP00000028107 ; ENSRNOG00000020707 . [Q99MK2-2 ]
ENSRNOT00000041916 ; ENSRNOP00000039632 ; ENSRNOG00000020707 . [Q99MK2-1 ]
GeneIDi 192218.
KEGGi rno:192218.
UCSCi RGD:621061. rat. [Q99MK2-1 ]

Organism-specific databases

CTDi 10524.
RGDi 621061. Kat5.

Phylogenomic databases

eggNOGi COG5027.
GeneTreei ENSGT00550000074503.
HOGENOMi HOG000182457.
KOi K11304.
OMAi HDDIITR.
OrthoDBi EOG7ZKS9R.
PhylomeDBi Q99MK2.

Enzyme and pathway databases

Reactomei REACT_198384. HATs acetylate histones.
REACT_226234. formation of the beta-catenin:TCF transactivating complex.

Miscellaneous databases

NextBioi 622815.
PROi Q99MK2.

Gene expression databases

Genevestigatori Q99MK2.

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.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 1).
    Tissue: Kidney.
  2. "A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60."
    Cao X., Suedhof T.C.
    Science 293:115-120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-506 (ISOFORM 2), INTERACTION WITH APP.
  3. "Fe65 is required for Tip60-directed histone H4 acetylation at DNA strand breaks."
    Stante M., Minopoli G., Passaro F., Raia M., Vecchio L.D., Russo T.
    Proc. Natl. Acad. Sci. U.S.A. 106:5093-5098(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APBB1.

Entry informationi

Entry nameiKAT5_RAT
AccessioniPrimary (citable) accession number: Q99MK2
Secondary accession number(s): Q5XI16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: July 11, 2006
Last modified: September 3, 2014
This is version 101 of the entry and version 2 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

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