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Histone acetyltransferase KAT5 (EC 2.3.1.48) (60 kDa Tat-interactive protein) (Tip60) (Histone acetyltransferase HTATIP) (HIV-1 Tat interactive protein) (Lysine acetyltransferase 5) (cPLA(2)-interacting protein)

 KAT5_HUMAN              Reviewed;         513 AA.
Q92993; B4E3C7; C9JL99; O95624; Q13430; Q17RW5; Q561W3; Q6GSE8;
Q9BWK7;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
16-MAY-2003, sequence version 2.
30-AUG-2017, entry version 187.
RecName: Full=Histone acetyltransferase KAT5;
EC=2.3.1.48 {ECO:0000269|PubMed:10096020, ECO:0000269|PubMed:12468530};
AltName: Full=60 kDa Tat-interactive protein;
Short=Tip60;
AltName: Full=Histone acetyltransferase HTATIP;
Short=HIV-1 Tat interactive protein;
AltName: Full=Lysine acetyltransferase 5;
AltName: Full=cPLA(2)-interacting protein;
Name=KAT5; Synonyms=HTATIP, TIP60;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HIV-1
TAT.
TISSUE=Lymphoblast;
PubMed=8607265; DOI=10.1006/viro.1996.0071;
Kamine J., Elangovan B., Subramanian T., Coleman D., Chinnadurai G.;
"Identification of a cellular protein that specifically interacts with
the essential cysteine region of the HIV-1 Tat transactivator.";
Virology 216:357-366(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PLA2G4A, AND
SUBCELLULAR LOCATION.
TISSUE=Fibroblast, and Placenta;
PubMed=11416127; DOI=10.1128/MCB.21.14.4470-4481.2001;
Sheridan A.M., Force T., Yoon H.J., O'Leary E., Choukroun G.,
Taheri M.R., Bonventre J.V.;
"PLIP, a novel splice variant of Tip60, interacts with group IV
cytosolic phospholipase A(2), induces apoptosis, and potentiates
prostaglandin production.";
Mol. Cell. Biol. 21:4470-4481(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=12801643; DOI=10.1016/S0378-1119(03)00547-X;
Legube G., Trouche D.;
"Identification of a larger form of the histone acetyl transferase
Tip60.";
Gene 310:161-168(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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., 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.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cervix, Liver, Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 19-35; 150-177 AND 297-307, IDENTIFICATION IN NUA4
COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12963728; DOI=10.1074/jbc.C300389200;
Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
Conaway R.C., Conaway J.W.;
"Identification of new subunits of the multiprotein mammalian
TRRAP/TIP60-containing histone acetyltransferase complex.";
J. Biol. Chem. 278:42733-42736(2003).
[10]
CATALYTIC ACTIVITY IN VITRO.
PubMed=10096020; DOI=10.1046/j.1365-2443.1998.00229.x;
Kimura A., Horikoshi M.;
"Tip60 acetylates six lysines of a specific class in core histones in
vitro.";
Genes Cells 3:789-800(1998).
[11]
IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=10966108; DOI=10.1016/S0092-8674(00)00051-9;
Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J.,
Horikoshi M., Scully R., Qin J., Nakatani Y.;
"Involvement of the TIP60 histone acetylase complex in DNA repair and
apoptosis.";
Cell 102:463-473(2000).
[12]
INTERACTION WITH EDNRA.
PubMed=11262386; DOI=10.1074/jbc.C000909200;
Lee H.-J., Chun M., Kandror K.V.;
"Tip60 and HDAC7 interact with the endothelin receptor a and may be
involved in downstream signaling.";
J. Biol. Chem. 276:16597-16600(2001).
[13]
UBIQUITINATION.
PubMed=11927554; DOI=10.1093/emboj/21.7.1704;
Legube G., Linares L.K., Lemercier C., Scheffner M., Khochbin S.,
Trouche D.;
"Tip60 is targeted to proteasome-mediated degradation by Mdm2 and
accumulates after UV irradiation.";
EMBO J. 21:1704-1712(2002).
[14]
ROLE IN MYC-DEPENDENT TRANSCRIPTION.
PubMed=12776177; DOI=10.1038/sj.embor.embor861;
Frank S.R., Parisi T., Taubert S., Fernandez P., Fuchs M., Chan H.M.,
Livingston D.M., Amati B.;
"MYC recruits the TIP60 histone acetyltransferase complex to
chromatin.";
EMBO Rep. 4:575-580(2003).
[15]
PHOSPHORYLATION AT SER-86 AND SER-90, MUTAGENESIS OF SER-86; SER-90;
LEU-254; LEU-257 AND GLY-380, AND CATALYTIC ACTIVITY.
PubMed=12468530; DOI=10.1074/jbc.M211811200;
Lemercier C., Legube G., Caron C., Louwagie M., Garin J., Trouche D.,
Khochbin S.;
"Tip60 acetyltransferase activity is controlled by phosphorylation.";
J. Biol. Chem. 278:4713-4718(2003).
[16]
SUBCELLULAR LOCATION, AND INTERACTION WITH HDAC7.
PubMed=12551922; DOI=10.1074/jbc.M210816200;
Xiao H., Chung J., Kao H.-Y., Yang Y.-C.;
"Tip60 is a co-repressor for STAT3.";
J. Biol. Chem. 278:11197-11204(2003).
[17]
REVIEW ON NUA4 COMPLEX.
PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
Doyon Y., Cote J.;
"The highly conserved and multifunctional NuA4 HAT complex.";
Curr. Opin. Genet. Dev. 14:147-154(2004).
[18]
ROLE IN TP53-DEPENDENT TRANSCRIPTION.
PubMed=15310756; DOI=10.1074/jbc.M407478200;
Legube G., Linares L.K., Tyteca S., Caron C., Scheffner M.,
Chevillard-Briet M., Trouche D.;
"Role of the histone acetyl transferase Tip60 in the p53 pathway.";
J. Biol. Chem. 279:44825-44833(2004).
[19]
INTERACTION WITH JADE1.
PubMed=15502158; DOI=10.1074/jbc.M410487200;
Panchenko M.V., Zhou M.I., Cohen H.T.;
"von Hippel-Lindau partner Jade-1 is a transcriptional co-activator
associated with histone acetyltransferase activity.";
J. Biol. Chem. 279:56032-56041(2004).
[20]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN
THE NUA4 COMPLEX.
PubMed=14966270; DOI=10.1128/MCB.24.5.1884-1896.2004;
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
"Structural and functional conservation of the NuA4 histone
acetyltransferase complex from yeast to humans.";
Mol. Cell. Biol. 24:1884-1896(2004).
[21]
ROLE IN E2F1-DEPENDENT TRANSCRIPTION.
PubMed=15121871; DOI=10.1128/MCB.24.10.4546-4556.2004;
Taubert S., Gorrini C., Frank S.R., Parisi T., Fuchs M., Chan H.M.,
Livingston D.M., Amati B.;
"E2F-dependent histone acetylation and recruitment of the Tip60
acetyltransferase complex to chromatin in late G1.";
Mol. Cell. Biol. 24:4546-4556(2004).
[22]
ROLE IN TP53-DEPENDENT TRANSCRIPTION.
PubMed=15042092; DOI=10.1038/nature02371;
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.;
"A large-scale RNAi screen in human cells identifies new components of
the p53 pathway.";
Nature 428:431-437(2004).
[23]
INTERACTION WITH HIV-1 TAT.
PubMed=16001085; DOI=10.1038/sj.emboj.7600734;
Col E., Caron C., Chable-Bessia C., Legube G., Gazzeri S., Komatsu Y.,
Yoshida M., Benkirane M., Trouche D., Khochbin S.;
"HIV-1 Tat targets Tip60 to impair the apoptotic cell response to
genotoxic stresses.";
EMBO J. 24:2634-2645(2005).
[24]
INTERACTION WITH ATM, AND FUNCTION.
PubMed=16141325; DOI=10.1073/pnas.0504211102;
Sun Y., Jiang X., Chen S., Fernandes N., Price B.D.;
"A role for the Tip60 histone acetyltransferase in the acetylation and
activation of ATM.";
Proc. Natl. Acad. Sci. U.S.A. 102:13182-13187(2005).
[25]
IDENTIFICATION IN A COMPLEX WITH HINT1.
PubMed=16835243; DOI=10.1074/jbc.M513452200;
Weiske J., Huber O.;
"The histidine triad protein Hint1 triggers apoptosis independent of
its enzymatic activity.";
J. Biol. Chem. 281:27356-27366(2006).
[26]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
Lane W.S., Tan S., Yang X.-J., Cote J.;
"ING tumor suppressor proteins are critical regulators of chromatin
acetylation required for genome expression and perpetuation.";
Mol. Cell 21:51-64(2006).
[27]
FUNCTION, INTERACTION WITH FOXP3, AND SUBCELLULAR LOCATION.
PubMed=17360565; DOI=10.1073/pnas.0700298104;
Li B., Samanta A., Song X., Iacono K.T., Bembas K., Tao R., Basu S.,
Riley J.L., Hancock W.W., Shen Y., Saouaf S.J., Greene M.I.;
"FOXP3 interactions with histone acetyltransferase and class II
histone deacetylases are required for repression.";
Proc. Natl. Acad. Sci. U.S.A. 104:4571-4576(2007).
[28]
FUNCTION, INTERACTION WITH NR1D2, AND SUBCELLULAR LOCATION.
PubMed=17996965; DOI=10.1016/j.bbamcr.2007.09.004;
Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X.,
Lu H.;
"The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to
regulate apolipoprotein CIII promoter.";
Biochim. Biophys. Acta 1783:224-236(2008).
[29]
INTERACTION WITH TRIM68.
PubMed=18451177; DOI=10.1158/0008-5472.CAN-07-6059;
Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M.,
Shinohara N., Nonomura K., Hatakeyama S.;
"TRIM68 regulates ligand-dependent transcription of androgen receptor
in prostate cancer cells.";
Cancer Res. 68:3486-3494(2008).
[30]
INTERACTION WITH ATF2 AND CUL3, AND PROTEASOMAL DEGRADATION.
PubMed=18397884; DOI=10.1074/jbc.M802030200;
Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.;
"Regulation of TIP60 by ATF2 modulates ATM activation.";
J. Biol. Chem. 283:17605-17614(2008).
[31]
SUMOYLATION AT LYS-430 AND LYS-451, MUTAGENESIS OF LYS-430 AND
LYS-451, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
AND IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX.
PubMed=17704809; DOI=10.1038/sj.onc.1210710;
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., Hu R., Huang H., Jin C., Yao X.;
"Functional characterization of TIP60 sumoylation in UV-irradiated DNA
damage response.";
Oncogene 27:931-941(2008).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[33]
FUNCTION, AND INTERACTION WITH TRIM24.
PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001;
Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N.,
Tanaka J., Imamura M., Hatakeyama S.;
"TRIM24 mediates ligand-dependent activation of androgen receptor and
is repressed by a bromodomain-containing protein, BRD7, in prostate
cancer cells.";
Biochim. Biophys. Acta 1793:1828-1836(2009).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-90 AND SER-199,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[37]
INTERACTION WITH ZBTB49.
PubMed=25245946; DOI=10.1093/nar/gku857;
Jeon B.N., Kim M.K., Yoon J.H., Kim M.Y., An H., Noh H.J., Choi W.I.,
Koh D.I., Hur M.W.;
"Two ZNF509 (ZBTB49) isoforms induce cell-cycle arrest by activating
transcription of p21/CDKN1A and RB upon exposure to genotoxic
stress.";
Nucleic Acids Res. 42:11447-11461(2014).
[38]
FUNCTION, AND IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
PubMed=24463511; DOI=10.1038/nature12922;
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.;
"ANP32E is a histone chaperone that removes H2A.Z from chromatin.";
Nature 505:648-653(2014).
[39]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 227-506 IN COMPLEX WITH
ACETYL-COA AND ZINC IONS, AND ACETYLATION AT LYS-327.
Structural genomics consortium (SGC);
"The crystal structure of acetyltransferase domain of human HIV-1 TAT
interacting protein in complex with acetylcoenzyme A.";
Submitted (FEB-2009) to the PDB data bank.
[40]
STRUCTURE BY NMR OF 5-78.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RUH-073, a pseudo chromo domain from human
cDNA.";
Submitted (FEB-2009) to the PDB data bank.
-!- 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. Promotes FOXP3 acetylation and
positively regulates its transcriptional repressor activity
(PubMed:17360565). {ECO:0000269|PubMed:12776177,
ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:15042092,
ECO:0000269|PubMed:15121871, ECO:0000269|PubMed:15310756,
ECO:0000269|PubMed:16141325, ECO:0000269|PubMed:16387653,
ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17996965,
ECO:0000269|PubMed:19909775, ECO:0000269|PubMed:24463511}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000269|PubMed:10096020,
ECO:0000269|PubMed:12468530}.
-!- SUBUNIT: 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. Interacts with
FOXP3. Interacts with ZBTB49 (PubMed:25245946).
{ECO:0000250|UniProtKB:Q99MK2, ECO:0000269|PubMed:10966108,
ECO:0000269|PubMed:11262386, ECO:0000269|PubMed:11416127,
ECO:0000269|PubMed:12551922, ECO:0000269|PubMed:12963728,
ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:15502158,
ECO:0000269|PubMed:16001085, ECO:0000269|PubMed:16141325,
ECO:0000269|PubMed:16835243, ECO:0000269|PubMed:17360565,
ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:18397884,
ECO:0000269|PubMed:18451177, ECO:0000269|PubMed:19909775,
ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:25245946,
ECO:0000269|PubMed:8607265, ECO:0000269|Ref.39}.
-!- INTERACTION:
P54253:ATXN1; NbExp=3; IntAct=EBI-399080, EBI-930964;
Q9HC52:CBX8; NbExp=2; IntAct=EBI-399080, EBI-712912;
Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-399080, EBI-10171416;
Q9P2H0:CEP126; NbExp=2; IntAct=EBI-399080, EBI-473176;
O43261:DLEU1; NbExp=2; IntAct=EBI-399080, EBI-710057;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-399080, EBI-10172181;
Q9BZS1-1:FOXP3; NbExp=2; IntAct=EBI-399080, EBI-9695448;
O95257:GADD45G; NbExp=2; IntAct=EBI-399080, EBI-448202;
Q5VSY0:GKAP1; NbExp=4; IntAct=EBI-399080, EBI-743722;
Q96IK5:GMCL1; NbExp=4; IntAct=EBI-399080, EBI-2548508;
Q8NEA9:GMCL1P1; NbExp=3; IntAct=EBI-399080, EBI-745707;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-399080, EBI-618309;
Q6NT76:HMBOX1; NbExp=5; IntAct=EBI-399080, EBI-2549423;
Q9UKT9:IKZF3; NbExp=5; IntAct=EBI-399080, EBI-747204;
Q6A162:KRT40; NbExp=3; IntAct=EBI-399080, EBI-10171697;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-399080, EBI-10172052;
Q17RB8:LONRF1; NbExp=3; IntAct=EBI-399080, EBI-2341787;
Q9BRK4:LZTS2; NbExp=5; IntAct=EBI-399080, EBI-741037;
Q99750:MDFI; NbExp=3; IntAct=EBI-399080, EBI-724076;
P50222:MEOX2; NbExp=3; IntAct=EBI-399080, EBI-748397;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-399080, EBI-742948;
P10085:Myod1 (xeno); NbExp=5; IntAct=EBI-399080, EBI-4405734;
Q9Y2I6:NINL; NbExp=3; IntAct=EBI-399080, EBI-719716;
Q9HC29:NOD2; NbExp=2; IntAct=EBI-399080, EBI-7445625;
P11926:ODC1; NbExp=7; IntAct=EBI-399080, EBI-1044287;
Q8IXK0:PHC2; NbExp=3; IntAct=EBI-399080, EBI-713786;
Q9NQM4:PIH1D3; NbExp=5; IntAct=EBI-399080, EBI-10239299;
P29074:PTPN4; NbExp=2; IntAct=EBI-399080, EBI-710431;
P35711:SOX5; NbExp=3; IntAct=EBI-399080, EBI-3505701;
Q01130:SRSF2; NbExp=3; IntAct=EBI-399080, EBI-627047;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-399080, EBI-2212028;
O75558:STX11; NbExp=7; IntAct=EBI-399080, EBI-714135;
O75069-4:TMCC2; NbExp=3; IntAct=EBI-399080, EBI-10177480;
P04637:TP53; NbExp=3; IntAct=EBI-399080, EBI-366083;
P36406:TRIM23; NbExp=3; IntAct=EBI-399080, EBI-740098;
P14373:TRIM27; NbExp=3; IntAct=EBI-399080, EBI-719493;
O94972:TRIM37; NbExp=3; IntAct=EBI-399080, EBI-741602;
Q9NNX1:TUFT1; NbExp=3; IntAct=EBI-399080, EBI-2557363;
Q15672:TWIST1; NbExp=2; IntAct=EBI-399080, EBI-1797287;
O43829:ZBTB14; NbExp=3; IntAct=EBI-399080, EBI-10176632;
Q96BR9:ZBTB8A; NbExp=4; IntAct=EBI-399080, EBI-742740;
Q8N8E2:ZNF513; NbExp=3; IntAct=EBI-399080, EBI-10279993;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17360565}.
Nucleus, nucleolus. Cytoplasm, perinuclear 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q92993-1; Sequence=Displayed;
Name=2; Synonyms=PLIP;
IsoId=Q92993-2; Sequence=VSP_007438;
Name=3;
IsoId=Q92993-3; Sequence=VSP_009104;
Note=Ref.3 (no nucleotide entry) sequence is in conflict in
position: 32:V->A. {ECO:0000305};
Name=4;
IsoId=Q92993-4; Sequence=VSP_009104, VSP_007438;
Note=No experimental confirmation available.;
-!- PTM: 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. {ECO:0000269|PubMed:17704809}.
-!- PTM: Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M
phase. The phosphorylated form has a higher HAT activity.
{ECO:0000269|PubMed:12468530}.
-!- PTM: Ubiquitinated by MDM2, leading to its proteasome-dependent
degradation. {ECO:0000269|PubMed:11927554}.
-!- PTM: Autoacetylation at Lys-327 is required for proper function.
{ECO:0000250|UniProtKB:Q9H7Z6}.
-!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB02683.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/htatip/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HTATIPID40893ch11q13.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U74667; AAB18236.1; -; mRNA.
EMBL; U40989; AAB02683.1; ALT_INIT; mRNA.
EMBL; U67734; AAD00163.1; -; mRNA.
EMBL; AY214165; AAO21130.1; -; Genomic_DNA.
EMBL; AK304664; BAG65439.1; -; mRNA.
EMBL; AP001266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW74427.1; -; Genomic_DNA.
EMBL; CH471076; EAW74429.1; -; Genomic_DNA.
EMBL; BC000166; AAH00166.3; -; mRNA.
EMBL; BC064912; AAH64912.1; -; mRNA.
EMBL; BC093032; AAH93032.1; -; mRNA.
EMBL; BC143296; AAI43297.1; -; mRNA.
EMBL; BC117167; AAI17168.1; -; mRNA.
CCDS; CCDS31610.1; -. [Q92993-1]
CCDS; CCDS55771.1; -. [Q92993-4]
CCDS; CCDS8109.1; -. [Q92993-2]
CCDS; CCDS8110.1; -. [Q92993-3]
RefSeq; NP_001193762.1; NM_001206833.1. [Q92993-4]
RefSeq; NP_006379.2; NM_006388.3. [Q92993-1]
RefSeq; NP_874368.1; NM_182709.2. [Q92993-2]
RefSeq; NP_874369.1; NM_182710.2. [Q92993-3]
UniGene; Hs.397010; -.
PDB; 2EKO; NMR; -; A=5-78.
PDB; 2OU2; X-ray; 2.30 A; A=227-506.
PDB; 4QQG; X-ray; 2.80 A; A/B/C/D/E/F/G=1-80.
PDBsum; 2EKO; -.
PDBsum; 2OU2; -.
PDBsum; 4QQG; -.
ProteinModelPortal; Q92993; -.
SMR; Q92993; -.
BioGrid; 115779; 228.
DIP; DIP-5998N; -.
IntAct; Q92993; 141.
MINT; MINT-94861; -.
STRING; 9606.ENSP00000340330; -.
BindingDB; Q92993; -.
ChEMBL; CHEMBL5750; -.
DrugBank; DB01992; Coenzyme A.
DrugBank; DB02039; S-Acetyl-Cysteine.
GuidetoPHARMACOLOGY; 2664; -.
iPTMnet; Q92993; -.
PhosphoSitePlus; Q92993; -.
BioMuta; KAT5; -.
DMDM; 30923328; -.
EPD; Q92993; -.
MaxQB; Q92993; -.
PaxDb; Q92993; -.
PeptideAtlas; Q92993; -.
PRIDE; Q92993; -.
DNASU; 10524; -.
Ensembl; ENST00000341318; ENSP00000340330; ENSG00000172977. [Q92993-3]
Ensembl; ENST00000352980; ENSP00000344955; ENSG00000172977. [Q92993-2]
Ensembl; ENST00000377046; ENSP00000366245; ENSG00000172977. [Q92993-1]
Ensembl; ENST00000530446; ENSP00000434765; ENSG00000172977. [Q92993-4]
GeneID; 10524; -.
KEGG; hsa:10524; -.
UCSC; uc001ofi.4; human. [Q92993-1]
CTD; 10524; -.
DisGeNET; 10524; -.
GeneCards; KAT5; -.
HGNC; HGNC:5275; KAT5.
HPA; HPA016953; -.
MIM; 601409; gene.
neXtProt; NX_Q92993; -.
OpenTargets; ENSG00000172977; -.
PharmGKB; PA162392746; -.
eggNOG; KOG2747; Eukaryota.
eggNOG; COG5027; LUCA.
GeneTree; ENSGT00550000074503; -.
HOGENOM; HOG000182457; -.
InParanoid; Q92993; -.
KO; K11304; -.
OMA; ITHADVM; -.
OrthoDB; EOG091G0B73; -.
PhylomeDB; Q92993; -.
TreeFam; TF317619; -.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693548; Sensing of DNA Double Strand Breaks.
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
SignaLink; Q92993; -.
SIGNOR; Q92993; -.
ChiTaRS; KAT5; human.
EvolutionaryTrace; Q92993; -.
GeneWiki; KAT5; -.
GenomeRNAi; 10524; -.
PRO; PR:Q92993; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000172977; -.
CleanEx; HS_KAT5; -.
ExpressionAtlas; Q92993; baseline and differential.
Genevisible; Q92993; HS.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0000812; C:Swr1 complex; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0016407; F:acetyltransferase activity; TAS:Reactome.
GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:UniProtKB.
GO; GO:0000729; P:DNA double-strand break processing; TAS:Reactome.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome.
GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:1901985; P:positive regulation of protein acetylation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR016197; Chromodomain-like.
InterPro; IPR002717; HAT_MYST-type.
InterPro; IPR025995; Tudor-knot.
Pfam; PF01853; MOZ_SAS; 1.
Pfam; PF11717; Tudor-knot; 1.
SMART; SM00298; CHROMO; 1.
SUPFAM; SSF54160; SSF54160; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51726; MYST_HAT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Acyltransferase;
Alternative splicing; Chromatin regulator; Complete proteome;
Cytoplasm; Direct protein sequencing; Growth regulation;
Host-virus interaction; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Transferase; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 513 Histone acetyltransferase KAT5.
/FTId=PRO_0000051580.
DOMAIN 227 504 MYST-type HAT. {ECO:0000255|PROSITE-
ProRule:PRU01063}.
ZN_FING 260 285 C2HC MYST-type. {ECO:0000255|PROSITE-
ProRule:PRU01063, ECO:0000305|Ref.39}.
REGION 368 513 Interaction with ATF2.
{ECO:0000269|PubMed:18397884}.
REGION 370 372 Acetyl-CoA binding. {ECO:0000269|Ref.39}.
REGION 377 383 Acetyl-CoA binding. {ECO:0000269|Ref.39}.
ACT_SITE 403 403 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q9H7Z6}.
BINDING 407 407 Acetyl-CoA. {ECO:0000269|Ref.39}.
BINDING 416 416 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q9H7Z6}.
MOD_RES 52 52 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12468530}.
MOD_RES 90 90 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12468530}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 327 327 N6-acetyllysine; by autocatalysis.
{ECO:0000269|Ref.39}.
CROSSLNK 430 430 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:17704809}.
CROSSLNK 451 451 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:17704809}.
VAR_SEQ 4 4 V -> VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ
(in isoform 3 and isoform 4).
{ECO:0000303|PubMed:12801643,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_009104.
VAR_SEQ 96 147 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11416127,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007438.
VARIANT 78 78 P -> T (in dbSNP:rs11541271).
/FTId=VAR_059456.
MUTAGEN 86 86 S->A: Reduces phosphorylation. Abolishes
phosphorylation; when associated with A-
90. Reduced HAT activity.
{ECO:0000269|PubMed:12468530}.
MUTAGEN 90 90 S->A: Reduces phosphorylation. Abolishes
phosphorylation; when associated with A-
86. Reduced HAT activity.
{ECO:0000269|PubMed:12468530}.
MUTAGEN 254 254 L->A: Does not affect phosphorylation;
when associated with A-257.
{ECO:0000269|PubMed:12468530}.
MUTAGEN 257 257 L->A: Does not affect phosphorylation;
when associated with A-254.
{ECO:0000269|PubMed:12468530}.
MUTAGEN 380 380 G->A: Loss of function. Does not affect
phosphorylation.
{ECO:0000269|PubMed:12468530}.
MUTAGEN 430 430 K->R: Abrogates sumoylation.
{ECO:0000269|PubMed:17704809}.
MUTAGEN 451 451 K->R: Abrogates sumoylation.
{ECO:0000269|PubMed:17704809}.
CONFLICT 382 382 G -> R (in Ref. 1; AAB18236/AAB02683).
{ECO:0000305}.
HELIX 4 6 {ECO:0000244|PDB:4QQG}.
STRAND 12 15 {ECO:0000244|PDB:4QQG}.
STRAND 28 35 {ECO:0000244|PDB:4QQG}.
STRAND 37 40 {ECO:0000244|PDB:4QQG}.
STRAND 42 47 {ECO:0000244|PDB:4QQG}.
HELIX 52 54 {ECO:0000244|PDB:4QQG}.
STRAND 56 58 {ECO:0000244|PDB:4QQG}.
HELIX 60 62 {ECO:0000244|PDB:4QQG}.
HELIX 65 67 {ECO:0000244|PDB:2EKO}.
STRAND 235 237 {ECO:0000244|PDB:2OU2}.
STRAND 240 242 {ECO:0000244|PDB:2OU2}.
HELIX 252 254 {ECO:0000244|PDB:2OU2}.
STRAND 260 262 {ECO:0000244|PDB:2OU2}.
TURN 264 266 {ECO:0000244|PDB:2OU2}.
STRAND 269 271 {ECO:0000244|PDB:2OU2}.
HELIX 273 282 {ECO:0000244|PDB:2OU2}.
STRAND 289 296 {ECO:0000244|PDB:2OU2}.
STRAND 299 305 {ECO:0000244|PDB:2OU2}.
TURN 306 308 {ECO:0000244|PDB:2OU2}.
HELIX 310 321 {ECO:0000244|PDB:2OU2}.
TURN 328 331 {ECO:0000244|PDB:2OU2}.
STRAND 336 345 {ECO:0000244|PDB:2OU2}.
STRAND 348 360 {ECO:0000244|PDB:2OU2}.
STRAND 365 368 {ECO:0000244|PDB:2OU2}.
STRAND 370 372 {ECO:0000244|PDB:2OU2}.
HELIX 374 376 {ECO:0000244|PDB:2OU2}.
HELIX 381 395 {ECO:0000244|PDB:2OU2}.
STRAND 400 402 {ECO:0000244|PDB:2OU2}.
HELIX 408 425 {ECO:0000244|PDB:2OU2}.
HELIX 441 448 {ECO:0000244|PDB:2OU2}.
HELIX 452 461 {ECO:0000244|PDB:2OU2}.
STRAND 469 474 {ECO:0000244|PDB:2OU2}.
HELIX 497 499 {ECO:0000244|PDB:2OU2}.
SEQUENCE 513 AA; 58582 MW; 63724F5E10B957D5 CRC64;
MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF NKRLDEWVTH
ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVPASAQ ASGKTLPIPV QITLRFNLPK
EREAIPGGEP DQPLSSSSCL QPNHRSTKRK VEVVSPATPV PSETAPASVF PQNGAARRAV
AAQPGRKRKS NCLGTDEDSQ DSSDGIPSAP RMTGSLVSDR SHDDIVTRMK NIECIELGRH
RLKPWYFSPY PQELTTLPVL YLCEFCLKYG RSLKCLQRHL TKCDLRHPPG NEIYRKGTIS
FFEIDGRKNK SYSQNLCLLA KCFLDHKTLY YDTDPFLFYV MTEYDCKGFH IVGYFSKEKE
STEDYNVACI LTLPPYQRRG YGKLLIEFSY ELSKVEGKTG TPEKPLSDLG LLSYRSYWSQ
TILEILMGLK SESGERPQIT INEISEITSI KKEDVISTLQ YLNLINYYKG QYILTLSEDI
VDGHERAMLK RLLRIDSKCL HFTPKDWSKR GKW


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