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Q92993 (KAT5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
Short name=HIV-1 Tat interactive protein
Lysine acetyltransferase 5
cPLA(2)-interacting protein
Gene names
Name:KAT5
Synonyms:HTATIP, TIP60
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2. Ref.14 Ref.18 Ref.20 Ref.21 Ref.22 Ref.24 Ref.26 Ref.27 Ref.32 Ref.35

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.10

Subunit structure

Interacts with the cytoplasmic tail of APP and APBB1/FE65 By similarity. Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7. 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. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. The NuA4 complex interacts with MYC and the adenovirus E1A protein. Interacts with ATM. Interacts with JADE1. Interacts with HIV-1 Tat. Interacts with TRIM24 and TRIM68. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Identified in a complex with HINT1. Interacts with ATF2 and CUL3. Interacts with NR1D2 (via N-terminus). Component of a SWR1-like complex. Ref.1 Ref.2 Ref.9 Ref.11 Ref.12 Ref.16 Ref.19 Ref.20 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.32 Ref.35

Subcellular location

Nucleus. Nucleusnucleolus. Cytoplasmperinuclear region. Note: Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region and UV irradiation induces translocation into punctuate subnuclear structures named nuclear bodies. Ref.2 Ref.16 Ref.26 Ref.27 Ref.30

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. Ref.30

Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase. Phosphorylated form has a higher activity. Ref.15

Ubiquitinated by MDM2, leading to its proteasome-dependent degradation. Ref.13 Ref.29

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.

Sequence caution

The sequence AAB02683.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processGrowth regulation
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Transferase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from direct assay Ref.20. Source: UniProtKB

androgen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

chromatin organization

Traceable author statement. Source: Reactome

double-strand break repair

Inferred from mutant phenotype Ref.11. Source: UniProtKB

histone acetylation

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of interleukin-2 production

Inferred from direct assay PubMed 17360565. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17360565. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 17360565. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.20. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.29. Source: UniProtKB

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

response to ionizing radiation

Inferred from direct assay Ref.29. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuA4 histone acetyltransferase complex

Inferred from direct assay Ref.11Ref.20. Source: UniProtKB

Piccolo NuA4 histone acetyltransferase complex

Inferred from direct assay Ref.20. Source: UniProtKB

Swr1 complex

Inferred from direct assay Ref.35. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from direct assay Ref.26. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.27. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionandrogen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

histone acetyltransferase activity

Inferred from direct assay Ref.29. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

repressing transcription factor binding

Inferred from physical interaction PubMed 17360565. Source: BHF-UCL

transcription coactivator activity

Inferred from direct assay Ref.20. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92993-1)

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: Q92993-2)

Also known as: PLIP;

The sequence of this isoform differs from the canonical sequence as follows:
     96-147: Missing.
Isoform 3 (identifier: Q92993-3)

The sequence of this isoform differs from the canonical sequence as follows:
     4-4: V → VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ
Isoform 4 (identifier: Q92993-4)

The sequence of this isoform differs from the canonical sequence as follows:
     4-4: V → VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ
     96-147: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513Histone acetyltransferase KAT5
PRO_0000051580

Regions

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

Sites

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

Amino acid modifications

Modified residue521N6-acetyllysine Ref.34
Modified residue861Phosphoserine Ref.15
Modified residue901Phosphoserine; by CDK1 Ref.15
Modified residue3271N6-acetyllysine; by autocatalysis By similarity
Cross-link430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.30
Cross-link451Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.30

Natural variations

Alternative sequence41V → VVSPVPGAGRREPGEVGRAR GPPVADPGVALSPQ in isoform 3 and isoform 4.
VSP_009104
Alternative sequence96 – 14752Missing in isoform 2 and isoform 4.
VSP_007438
Natural variant781P → T.
Corresponds to variant rs11541271 [ dbSNP | Ensembl ].
VAR_059456

Experimental info

Mutagenesis861S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-90. Reduced activity. Ref.15
Mutagenesis901S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-86. Reduced activity. Ref.15
Mutagenesis2541L → A: Does not affect phosphorylation; when associated with A-257. Ref.15
Mutagenesis2571L → A: Does not affect phosphorylation; when associated with A-254. Ref.15
Mutagenesis3801G → A: Loss of function. Does not affect phosphorylation. Ref.15
Mutagenesis4301K → R: Abrogates sumoylation. Ref.30
Mutagenesis4511K → R: Abrogates sumoylation. Ref.30
Sequence conflict3821G → R in AAB18236. Ref.1
Sequence conflict3821G → R in AAB02683. Ref.1
Isoform 3:
Sequence conflict321V → A no nucleotide entry Ref.3

Secondary structure

.............................................................. 513
Helix Strand Turn

Details...

Sequences

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

Last modified May 16, 2003. Version 2.
Checksum: 63724F5E10B957D5

FASTA51358,582
        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 PQNGAARRAV 

       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 (PLIP) [UniParc].

Checksum: 5A0E9324550AF246
Show »

FASTA46153,077
Isoform 3 [UniParc].

Checksum: 0CEB1A8E8C8D3E24
Show »

FASTA54661,798
Isoform 4 [UniParc].

Checksum: 761BF5859BE89793
Show »

FASTA49456,292

References

« Hide 'large scale' references
[1]"Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator."
Kamine J., Elangovan B., Subramanian T., Coleman D., Chinnadurai G.
Virology 216:357-366(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HIV-1 TAT.
Tissue: Lymphoblast.
[2]"PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production."
Sheridan A.M., Force T., Yoon H.J., O'Leary E., Choukroun G., Taheri M.R., Bonventre J.V.
Mol. Cell. Biol. 21:4470-4481(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PLA2G4A, SUBCELLULAR LOCATION.
Tissue: Fibroblast and Placenta.
[3]"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 [MRNA] (ISOFORM 3).
[4]NIEHS SNPs program
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Uterus.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 1 AND 2).
Tissue: Cervix, Liver, Placenta and Testis.
[9]"Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-35; 150-177 AND 297-307, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Tip60 acetylates six lysines of a specific class in core histones in vitro."
Kimura A., Horikoshi M.
Genes Cells 3:789-800(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY IN VITRO.
[11]"Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis."
Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M., Scully R., Qin J., Nakatani Y.
Cell 102:463-473(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling."
Lee H.-J., Chun M., Kandror K.V.
J. Biol. Chem. 276:16597-16600(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EDNRA.
[13]"Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation."
Legube G., Linares L.K., Lemercier C., Scheffner M., Khochbin S., Trouche D.
EMBO J. 21:1704-1712(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[14]"MYC recruits the TIP60 histone acetyltransferase complex to chromatin."
Frank S.R., Parisi T., Taubert S., Fernandez P., Fuchs M., Chan H.M., Livingston D.M., Amati B.
EMBO Rep. 4:575-580(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN MYC-DEPENDENT TRANSCRIPTION.
[15]"Tip60 acetyltransferase activity is controlled by phosphorylation."
Lemercier C., Legube G., Caron C., Louwagie M., Garin J., Trouche D., Khochbin S.
J. Biol. Chem. 278:4713-4718(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-86 AND SER-90, MUTAGENESIS OF SER-86; SER-90; LEU-254; LEU-257 AND GLY-380.
[16]"Tip60 is a co-repressor for STAT3."
Xiao H., Chung J., Kao H.-Y., Yang Y.-C.
J. Biol. Chem. 278:11197-11204(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HDAC7.
[17]"The highly conserved and multifunctional NuA4 HAT complex."
Doyon Y., Cote J.
Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON NUA4 COMPLEX.
[18]"Role of the histone acetyl transferase Tip60 in the p53 pathway."
Legube G., Linares L.K., Tyteca S., Caron C., Scheffner M., Chevillard-Briet M., Trouche D.
J. Biol. Chem. 279:44825-44833(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN TP53-DEPENDENT TRANSCRIPTION.
[19]"von Hippel-Lindau partner Jade-1 is a transcriptional co-activator associated with histone acetyltransferase activity."
Panchenko M.V., Zhou M.I., Cohen H.T.
J. Biol. Chem. 279:56032-56041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH JADE1.
[20]"Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 COMPLEX.
[21]"E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1."
Taubert S., Gorrini C., Frank S.R., Parisi T., Fuchs M., Chan H.M., Livingston D.M., Amati B.
Mol. Cell. Biol. 24:4546-4556(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN E2F1-DEPENDENT TRANSCRIPTION.
[22]"A large-scale RNAi screen in human cells identifies new components of the p53 pathway."
Berns K., Hijmans E.M., Mullenders J., Brummelkamp T.R., Velds A., Heimerikx M., Kerkhoven R.M., Madiredjo M., Nijkamp W., Weigelt B., Agami R., Ge W., Cavet G., Linsley P.S., Beijersbergen R.L., Bernards R.
Nature 428:431-437(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN TP53-DEPENDENT TRANSCRIPTION.
[23]"HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses."
Col E., Caron C., Chable-Bessia C., Legube G., Gazzeri S., Komatsu Y., Yoshida M., Benkirane M., Trouche D., Khochbin S.
EMBO J. 24:2634-2645(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[24]"A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM."
Sun Y., Jiang X., Chen S., Fernandes N., Price B.D.
Proc. Natl. Acad. Sci. U.S.A. 102:13182-13187(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATM, FUNCTION.
[25]"The histidine triad protein Hint1 triggers apoptosis independent of its enzymatic activity."
Weiske J., Huber O.
J. Biol. Chem. 281:27356-27366(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH HINT1.
[26]"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[27]"The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter."
Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X., Lu H.
Biochim. Biophys. Acta 1783:224-236(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NR1D2, SUBCELLULAR LOCATION.
[28]"TRIM68 regulates ligand-dependent transcription of androgen receptor in prostate cancer cells."
Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M., Shinohara N., Nonomura K., Hatakeyama S.
Cancer Res. 68:3486-3494(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM68.
[29]"Regulation of TIP60 by ATF2 modulates ATM activation."
Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.
J. Biol. Chem. 283:17605-17614(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF2 AND CUL3, PROTEASOMAL DEGRADATION.
[30]"Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response."
Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z., Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M., Liang S., Wu Q., Reddy S.E. expand/collapse author list , Hu R., Huang H., Jin C., Yao X.
Oncogene 27:931-941(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-430 AND LYS-451, MUTAGENESIS OF LYS-430 AND LYS-451, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX.
[31]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"TRIM24 mediates ligand-dependent activation of androgen receptor and is repressed by a bromodomain-containing protein, BRD7, in prostate cancer cells."
Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J., Imamura M., Hatakeyama S.
Biochim. Biophys. Acta 1793:1828-1836(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TRIM24.
[33]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[34]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"ANP32E is a histone chaperone that removes H2A.Z from chromatin."
Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M., Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C., Hamiche A.
Nature 505:648-653(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
[36]"The crystal structure of acetyltransferase domain of human HIV-1 TAT interacting protein in complex with acetylcoenzyme A."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 227-506 IN COMPLEX WITH ACETYL COENZYME A AND ZINC IONS.
[37]"Solution structure of RUH-073, a pseudo chromo domain from human cDNA."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 5-78.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U74667 mRNA. Translation: AAB18236.1.
U40989 mRNA. Translation: AAB02683.1. Different initiation.
U67734 mRNA. Translation: AAD00163.1.
AY214165 Genomic DNA. Translation: AAO21130.1.
AK304664 mRNA. Translation: BAG65439.1.
AP001266 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74427.1.
CH471076 Genomic DNA. Translation: EAW74429.1.
BC000166 mRNA. Translation: AAH00166.3.
BC064912 mRNA. Translation: AAH64912.1.
BC093032 mRNA. Translation: AAH93032.1.
BC143296 mRNA. Translation: AAI43297.1.
BC117167 mRNA. Translation: AAI17168.1.
RefSeqNP_001193762.1. NM_001206833.1.
NP_006379.2. NM_006388.3.
NP_874368.1. NM_182709.2.
NP_874369.1. NM_182710.2.
UniGeneHs.397010.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EKONMR-A5-78[»]
2OU2X-ray2.30A227-506[»]
ProteinModelPortalQ92993.
SMRQ92993. Positions 11-79, 230-504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115779. 178 interactions.
DIPDIP-5998N.
IntActQ92993. 66 interactions.
MINTMINT-94861.
STRING9606.ENSP00000340330.

Chemistry

BindingDBQ92993.
ChEMBLCHEMBL5750.

PTM databases

PhosphoSiteQ92993.

Polymorphism databases

DMDM30923328.

Proteomic databases

PaxDbQ92993.
PRIDEQ92993.

Protocols and materials databases

DNASU10524.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341318; ENSP00000340330; ENSG00000172977. [Q92993-3]
ENST00000352980; ENSP00000344955; ENSG00000172977. [Q92993-2]
ENST00000377046; ENSP00000366245; ENSG00000172977. [Q92993-1]
ENST00000530446; ENSP00000434765; ENSG00000172977. [Q92993-4]
GeneID10524.
KEGGhsa:10524.
UCSCuc001ofi.3. human. [Q92993-1]
uc001ofj.3. human. [Q92993-2]
uc001ofk.3. human. [Q92993-3]
uc010roo.2. human. [Q92993-4]

Organism-specific databases

CTD10524.
GeneCardsGC11P065479.
HGNCHGNC:5275. KAT5.
HPAHPA016953.
MIM601409. gene.
neXtProtNX_Q92993.
PharmGKBPA162392746.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000182457.
KOK11304.
OMAHDDIITR.
OrthoDBEOG7ZKS9R.
PhylomeDBQ92993.
TreeFamTF317619.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.
SignaLinkQ92993.

Gene expression databases

ArrayExpressQ92993.
BgeeQ92993.
CleanExHS_KAT5.
GenevestigatorQ92993.

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

EvolutionaryTraceQ92993.
GeneWikiKAT5.
GenomeRNAi10524.
NextBio39922.
PROQ92993.
SOURCESearch...

Entry information

Entry nameKAT5_HUMAN
AccessionPrimary (citable) accession number: Q92993
Secondary accession number(s): B4E3C7 expand/collapse secondary AC list , C9JL99, O95624, Q13430, Q17RW5, Q561W3, Q6GSE8, Q9BWK7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 16, 2003
Last modified: April 16, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM