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Transformation/transcription domain-associated protein (350/400 kDa PCAF-associated factor) (PAF350/400) (STAF40) (Tra1 homolog)

 TRRAP_HUMAN             Reviewed;        3859 AA.
Q9Y4A5; A4D265; O75218; Q9Y631; Q9Y6H4;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
22-NOV-2017, entry version 177.
RecName: Full=Transformation/transcription domain-associated protein;
AltName: Full=350/400 kDa PCAF-associated factor;
Short=PAF350/400;
AltName: Full=STAF40;
AltName: Full=Tra1 homolog;
Name=TRRAP; Synonyms=PAF400;
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 2), PARTIAL PROTEIN SEQUENCE,
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYC AND E2F1.
TISSUE=Cervix carcinoma;
PubMed=9708738; DOI=10.1016/S0092-8674(00)81479-8;
McMahon S.B., Van Buskirk H.A., Dugan K.A., Copeland T.D., Cole M.D.;
"The novel ATM-related protein TRRAP is an essential cofactor for the
c-Myc and E2F oncoproteins.";
Cell 94:363-374(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 41-90;
337-344; 369-387; 879-892; 997-1005; 1171-1184; 1237-1247; 1545-1560;
1815-1820; 1922-1934; 2211-2218; 2260-2275; 2534-2547; 2583-2594;
2706-2726; 2830-2844; 3567-3573; 3583-3598; 3604-3614; 3712-3730 AND
3822-3834, AND IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L;
TAF5L; TAF6L; TAF10; SUPT3H; TAF12 AND TAF9.
TISSUE=Fetal heart;
PubMed=9885574; DOI=10.1016/S1097-2765(00)80301-9;
Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L.,
Qin J., Nakatani Y.;
"The 400 kDa subunit of the PCAF histone acetylase complex belongs to
the ATM superfamily.";
Mol. Cell 2:869-875(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[6]
SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H;
GCN5L2; KIAA0764; TAF5L; TAF6L; TADA3L; TAF10; TAF12 AND TAF9, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11564863; DOI=10.1128/MCB.21.20.6782-6795.2001;
Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
Kundu T.K., Chait B.T., Roeder R.G.;
"Human STAGA complex is a chromatin-acetylating transcription
coactivator that interacts with pre-mRNA splicing and DNA damage-
binding factors in vivo.";
Mol. Cell. Biol. 21:6782-6795(2001).
[7]
IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L;
SUPT3H; TAF2; TAF4; TAF5; GCN5L2 AND TAF10.
PubMed=10373431; DOI=10.1074/jbc.274.26.18285;
Brand M., Yamamoto K., Staub A., Tora L.;
"Identification of TATA-binding protein-free TAFII-containing complex
subunits suggests a role in nucleosome acetylation and signal
transduction.";
J. Biol. Chem. 274:18285-18289(1999).
[8]
IDENTIFICATION IN THE TIP60 HAT COMPLEX WITH KAT5; RUVBL1 AND RUVBL2.
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).
[9]
INTERACTION WITH GCN5L2.
PubMed=10611234; DOI=10.1128/MCB.20.2.556-562.2000;
McMahon S.B., Wood M.A., Cole M.D.;
"The essential cofactor TRRAP recruits the histone acetyltransferase
hGCN5 to c-Myc.";
Mol. Cell. Biol. 20:556-562(2000).
[10]
INTERACTION WITH E2F1 AND E2F4, AND FUNCTION.
PubMed=11418595; DOI=10.1074/jbc.M102067200;
Lang S.E., McMahon S.B., Cole M.D., Hearing P.;
"E2F transcriptional activation requires TRRAP and GCN5 cofactors.";
J. Biol. Chem. 276:32627-32634(2001).
[11]
DOMAIN.
PubMed=11445536; DOI=10.1101/gad.900101;
Park J., Kunjibettu S., McMahon S.B., Cole M.D.;
"The ATM-related domain of TRRAP is required for histone
acetyltransferase recruitment and Myc-dependent oncogenesis.";
Genes Dev. 15:1619-1624(2001).
[12]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=12138177; DOI=10.1128/MCB.22.16.5650-5661.2002;
Ard P.G., Chatterjee C., Kunjibettu S., Adside L.R., Gralinski L.E.,
McMahon S.B.;
"Transcriptional regulation of the mdm2 oncogene by p53 requires TRRAP
acetyltransferase complexes.";
Mol. Cell. Biol. 22:5650-5661(2002).
[13]
IDENTIFICATION IN THE BAF53 COMPLEX WITH BAF53A; RUVBL1 AND SMARCA4.
PubMed=11839798; DOI=10.1128/MCB.22.5.1307-1316.2002;
Park J., Wood M.A., Cole M.D.;
"BAF53 forms distinct nuclear complexes and functions as a critical c-
Myc-interacting nuclear cofactor for oncogenic transformation.";
Mol. Cell. Biol. 22:1307-1316(2002).
[14]
FUNCTION.
PubMed=12743606; DOI=10.1038/sj.onc.1206376;
Lang S.E., Hearing P.;
"The adenovirus E1A oncoprotein recruits the cellular TRRAP/GCN5
histone acetyltransferase complex.";
Oncogene 22:2836-2841(2003).
[15]
FUNCTION.
PubMed=12660246; DOI=10.1074/jbc.M211795200;
Liu X., Tesfai J., Evrard Y.A., Dent S.Y.R., Martinez E.;
"c-Myc transformation domain recruits the human STAGA complex and
requires TRRAP and GCN5 acetylase activity for transcription
activation.";
J. Biol. Chem. 278:20405-20412(2003).
[16]
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).
[17]
IDENTIFICATION IN STAGA COMPLEX.
PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A.,
Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
"A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
coactivates nuclear receptors, and counteracts heterochromatin
silencing.";
Mol. Cell 29:92-101(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2051, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
NPAT.
PubMed=17967892; DOI=10.1128/MCB.00607-07;
DeRan M., Pulvino M., Greene E., Su C., Zhao J.;
"Transcriptional activation of histone genes requires NPAT-dependent
recruitment of TRRAP-Tip60 complex to histone promoters during the
G1/S phase transition.";
Mol. Cell. Biol. 28:435-447(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2051 AND SER-2077, AND
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).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3078, 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).
[22]
INTERACTION WITH TELO2 AND TTI1.
PubMed=20427287; DOI=10.1074/jbc.M110.121699;
Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K.,
Iemura S., Natsume T., Mizushima N.;
"Tti1 and Tel2 are critical factors in mammalian target of rapamycin
complex assembly.";
J. Biol. Chem. 285:20109-20116(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
PROBABLE INVOLVEMENT IN MELANOMA, VARIANT PHE-722, AND
CHARACTERIZATION OF VARIANT PHE-722.
PubMed=21499247; DOI=10.1038/ng.810;
Wei X., Walia V., Lin J.C., Teer J.K., Prickett T.D., Gartner J.,
Davis S., Stemke-Hale K., Davies M.A., Gershenwald J.E., Robinson W.,
Robinson S., Rosenberg S.A., Samuels Y.;
"Exome sequencing identifies GRIN2A as frequently mutated in
melanoma.";
Nat. Genet. 43:442-446(2011).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1628; SER-2051 AND
SER-2077, 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).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[29]
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).
[30]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2543, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[31]
VARIANTS [LARGE SCALE ANALYSIS] CYS-893; GLY-1070; HIS-1669; HIS-1724;
VAL-1925; LEU-1932; LEU-1947; GLY-2139; TRP-2302; GLY-2433; LEU-2690;
ASP-2750; GLU-2801 AND MET-2931.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Adapter protein, which is found in various multiprotein
chromatin complexes with histone acetyltransferase activity (HAT),
which gives a specific tag for epigenetic transcription
activation. Component of the NuA4 histone acetyltransferase
complex which is responsible for acetylation of nucleosomal
histones H4 and H2A. Plays a central role in MYC transcription
activation, and also participates in cell transformation by MYC.
Required for p53/TP53-, E2F1- and E2F4-mediated transcription
activation. Also involved in transcription activation mediated by
the adenovirus E1A, a viral oncoprotein that deregulates
transcription of key genes. Probably acts by linking transcription
factors such as E1A, MYC or E2F1 to HAT complexes such as STAGA
thereby allowing transcription activation. Probably not required
in the steps following histone acetylation in processes of
transcription activation. May be required for the mitotic
checkpoint and normal cell cycle progression. Component of a SWR1-
like complex that specifically mediates the removal of histone
H2A.Z/H2AFZ from the nucleosome. {ECO:0000269|PubMed:11418595,
ECO:0000269|PubMed:12138177, ECO:0000269|PubMed:12660246,
ECO:0000269|PubMed:12743606, ECO:0000269|PubMed:14966270,
ECO:0000269|PubMed:17967892, ECO:0000269|PubMed:24463511,
ECO:0000269|PubMed:9708738}.
-!- SUBUNIT: Interacts with MYC, E2F1 and E2F4 transcription factors.
Interacts directly with p53/TP53. Interacts with GCN5L2. Component
of various HAT complexes. Component of the PCAF complex, at least
composed of TADA2L/ADA2, SUPT3H, TADA3L/ADA3, TAF5L/PAF65-beta,
TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and
TRRAP. Component of the TFTC-HAT complex, at least composed of
TAF5L, TAF6L, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135,
TAF5/TAFII100, GCN5L2/GCN5, TAF10 and TRRAP. 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. Component of the STAGA complex, at least
composed of SUPT3H, GCN5L2, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L,
TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is associated
with a subcomplex required for histone deubiquitination composed
of ATXN7L3, ENY2 and USP22. Component of the BAF53 complex, at
least composed of BAF53A, RUVBL1, SMARCA4/BRG1, and TRRAP, which
preferentially acetylates histone H4 (and H2A) within nucleosomes.
Interacts with NPAT. Interaction with TELO2 AND TTI1. Component of
a SWR1-like complex. {ECO:0000269|PubMed:10373431,
ECO:0000269|PubMed:10611234, ECO:0000269|PubMed:10966108,
ECO:0000269|PubMed:11418595, ECO:0000269|PubMed:11564863,
ECO:0000269|PubMed:11839798, ECO:0000269|PubMed:12138177,
ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:17967892,
ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:20427287,
ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:9708738,
ECO:0000269|PubMed:9885574}.
-!- INTERACTION:
O15265:ATXN7; NbExp=6; IntAct=EBI-399128, EBI-708350;
P38398:BRCA1; NbExp=8; IntAct=EBI-399128, EBI-349905;
P11474:ESRRA; NbExp=3; IntAct=EBI-399128, EBI-372412;
P01106:MYC; NbExp=4; IntAct=EBI-399128, EBI-447544;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
ECO:0000269|PubMed:9708738}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y4A5-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y4A5-2; Sequence=VSP_009102, VSP_009103;
-!- DOMAIN: The PI3K/PI4K domain is required for the recruitment of
HAT complexes, and the MYC-dependent transactivation. Although it
is strongly related to the PI3/PI4-kinase family, it lacks the
typical motifs that constitute the catalytic site of PI3/PI4-
kinase proteins, and lacks such activity.
{ECO:0000269|PubMed:11445536}.
-!- DISEASE: Note=TRRAP mutation Phe-722 has been frequently found in
cutaneous malignant melanoma, suggesting that TRRAP may play a
role in the pathogenesis of melanoma.
{ECO:0000269|PubMed:21499247}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. TRA1 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC62433.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AF076974; AAD09420.1; -; mRNA.
EMBL; AF110377; AAD04629.1; -; mRNA.
EMBL; AC004893; AAC62433.1; ALT_SEQ; Genomic_DNA.
EMBL; AC004991; AAC27675.2; -; Genomic_DNA.
EMBL; CH471091; EAW76694.1; -; Genomic_DNA.
EMBL; CH236956; EAL23887.1; -; Genomic_DNA.
CCDS; CCDS5659.1; -. [Q9Y4A5-2]
CCDS; CCDS59066.1; -. [Q9Y4A5-1]
PIR; T02632; T02632.
RefSeq; NP_001231509.1; NM_001244580.1. [Q9Y4A5-1]
RefSeq; NP_003487.1; NM_003496.3. [Q9Y4A5-2]
UniGene; Hs.203952; -.
ProteinModelPortal; Q9Y4A5; -.
BioGrid; 113900; 116.
CORUM; Q9Y4A5; -.
DIP; DIP-28149N; -.
IntAct; Q9Y4A5; 52.
MINT; MINT-1955478; -.
STRING; 9606.ENSP00000347733; -.
iPTMnet; Q9Y4A5; -.
PhosphoSitePlus; Q9Y4A5; -.
BioMuta; TRRAP; -.
DMDM; 116242829; -.
EPD; Q9Y4A5; -.
PaxDb; Q9Y4A5; -.
PeptideAtlas; Q9Y4A5; -.
PRIDE; Q9Y4A5; -.
Ensembl; ENST00000355540; ENSP00000347733; ENSG00000196367. [Q9Y4A5-2]
Ensembl; ENST00000359863; ENSP00000352925; ENSG00000196367. [Q9Y4A5-1]
GeneID; 8295; -.
KEGG; hsa:8295; -.
UCSC; uc003upp.3; human. [Q9Y4A5-1]
CTD; 8295; -.
DisGeNET; 8295; -.
EuPathDB; HostDB:ENSG00000196367.12; -.
GeneCards; TRRAP; -.
HGNC; HGNC:12347; TRRAP.
HPA; HPA054376; -.
MIM; 603015; gene.
neXtProt; NX_Q9Y4A5; -.
OpenTargets; ENSG00000196367; -.
PharmGKB; PA37020; -.
eggNOG; KOG0889; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00390000017961; -.
HOGENOM; HOG000252997; -.
HOVERGEN; HBG079283; -.
InParanoid; Q9Y4A5; -.
KO; K08874; -.
OMA; EHAFLIG; -.
OrthoDB; EOG091G0024; -.
PhylomeDB; Q9Y4A5; -.
TreeFam; TF106414; -.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SIGNOR; Q9Y4A5; -.
ChiTaRS; TRRAP; human.
GenomeRNAi; 8295; -.
PRO; PR:Q9Y4A5; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000196367; -.
CleanEx; HS_TRRAP; -.
ExpressionAtlas; Q9Y4A5; baseline and differential.
Genevisible; Q9Y4A5; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000125; C:PCAF complex; NAS:UniProtKB.
GO; GO:0030914; C:STAGA complex; IDA:UniProtKB.
GO; GO:0000812; C:Swr1 complex; IDA:UniProtKB.
GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; IBA:GO_Central.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
GO; GO:0003712; F:transcription cofactor activity; IDA:UniProtKB.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0016573; P:histone acetylation; NAS:UniProtKB.
GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 1.25.10.10; -; 2.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR003152; FATC_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR003151; PIK-rel_kinase_FAT.
InterPro; IPR014009; PIK_FAT.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR033317; TRA1/TRRAP.
PANTHER; PTHR11139:SF1; PTHR11139:SF1; 1.
Pfam; PF02259; FAT; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
SMART; SM01343; FATC; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF48371; SSF48371; 13.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51189; FAT; 1.
PROSITE; PS51190; FATC; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Chromatin regulator;
Complete proteome; Direct protein sequencing; Isopeptide bond;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 3859 Transformation/transcription domain-
associated protein.
/FTId=PRO_0000088851.
DOMAIN 2704 3275 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
DOMAIN 3528 3826 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 3827 3859 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
REGION 2010 2388 Interaction with TP53.
{ECO:0000269|PubMed:12138177}.
MOTIF 2047 2062 Bipartite nuclear localization signal.
{ECO:0000255}.
COMPBIAS 485 526 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 1628 1628 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2051 2051 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 2077 2077 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 3078 3078 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 2543 2543 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1492 1509 Missing (in isoform 2).
{ECO:0000303|PubMed:9708738}.
/FTId=VSP_009102.
VAR_SEQ 3001 3012 GKPTWSGMHSSS -> A (in isoform 2).
{ECO:0000303|PubMed:9708738}.
/FTId=VSP_009103.
VARIANT 722 722 S -> F (found in a cutaneous malignant
melanoma sample; somatic mutation;
induces cell transformation and confers
resistance to apoptosis;
dbSNP:rs147405090).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067754.
VARIANT 878 878 R -> L (in dbSNP:rs17161510).
/FTId=VAR_028359.
VARIANT 893 893 R -> C (in an ovarian serous carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041658.
VARIANT 1070 1070 S -> G (in dbSNP:rs55920979).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041659.
VARIANT 1669 1669 R -> H (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs373632999).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041660.
VARIANT 1724 1724 R -> H (in a gastric adenocarcinoma
sample; somatic mutation;
dbSNP:rs782203759).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041661.
VARIANT 1925 1925 A -> V (in dbSNP:rs56197298).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041662.
VARIANT 1932 1932 P -> L (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041663.
VARIANT 1947 1947 R -> L (in an ovarian mucinous carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041664.
VARIANT 2139 2139 W -> G (in dbSNP:rs34185633).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041665.
VARIANT 2302 2302 R -> W (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs528967912).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041666.
VARIANT 2433 2433 S -> G (in dbSNP:rs35634065).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041667.
VARIANT 2690 2690 P -> L (in a lung large cell carcinoma
sample; somatic mutation;
dbSNP:rs753661271).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041668.
VARIANT 2750 2750 E -> D (in dbSNP:rs55755466).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041669.
VARIANT 2801 2801 K -> E (in dbSNP:rs56341061).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041670.
VARIANT 2931 2931 T -> M (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041671.
CONFLICT 660 660 E -> D (in Ref. 2; AAD04629).
{ECO:0000305}.
SEQUENCE 3859 AA; 437600 MW; 391E467C0047B00B CRC64;
MAFVATQGAT VVDQTTLMKK YLQFVAALTD VNTPDETKLK MMQEVSENFE NVTSSPQYST
FLEHIIPRFL TFLQDGEVQF LQEKPAQQLR KLVLEIIHRI PTNEHLRPHT KNVLSVMFRF
LETENEENVL ICLRIIIELH KQFRPPITQE IHHFLDFVKQ IYKELPKVVN RYFENPQVIP
ENTVPPPEMV GMITTIAVKV NPEREDSETR THSIIPRGSL SLKVLAELPI IVVLMYQLYK
LNIHNVVAEF VPLIMNTIAI QVSAQARQHK LYNKELYADF IAAQIKTLSF LAYIIRIYQE
LVTKYSQQMV KGMLQLLSNC PAETAHLRKE LLIAAKHILT TELRNQFIPC MDKLFDESIL
IGSGYTARET LRPLAYSTLA DLVHHVRQHL PLSDLSLAVQ LFAKNIDDES LPSSIQTMSC
KLLLNLVDCI RSKSEQESGN GRDVLMRMLE VFVLKFHTIA RYQLSAIFKK CKPQSELGAV
EAALPGVPTA PAAPGPAPSP APVPAPPPPP PPPPPATPVT PAPVPPFEKQ GEKDKEDKQT
FQVTDCRSLV KTLVCGVKTI TWGITSCKAP GEAQFIPNKQ LQPKETQIYI KLVKYAMQAL
DIYQVQIAGN GQTYIRVANC QTVRMKEEKE VLEHFAGVFT MMNPLTFKEI FQTTVPYMVE
RISKNYALQI VANSFLANPT TSALFATILV EYLLDRLPEM GSNVELSNLY LKLFKLVFGS
VSLFAAENEQ MLKPHLHKIV NSSMELAQTA KEPYNYFLLL RALFRSIGGG SHDLLYQEFL
PLLPNLLQGL NMLQSGLHKQ HMKDLFVELC LTVPVRLSSL LPYLPMLMDP LVSALNGSQT
LVSQGLRTLE LCVDNLQPDF LYDHIQPVRA ELMQALWRTL RNPADSISHV AYRVLGKFGG
SNRKMLKESQ KLHYVVTEVQ GPSITVEFSD CKASLQLPME KAIETALDCL KSANTEPYYR
RQAWEVIKCF LVAMMSLEDN KHALYQLLAH PNFTEKTIPN VIISHRYKAQ DTPARKTFEQ
ALTGAFMSAV IKDLRPSALP FVASLIRHYT MVAVAQQCGP FLLPCYQVGS QPSTAMFHSE
ENGSKGMDPL VLIDAIAICM AYEEKELCKI GEVALAVIFD VASIILGSKE RACQLPLFSY
IVERLCACCY EQAWYAKLGG VVSIKFLMER LPLTWVLQNQ QTFLKALLFV MMDLTGEVSN
GAVAMAKTTL EQLLMRCATP LKDEERAEEI VAAQEKSFHH VTHDLVREVT SPNSTVRKQA
MHSLQVLAQV TGKSVTVIME PHKEVLQDMV PPKKHLLRHQ PANAQIGLME GNTFCTTLQP
RLFTMDLNVV EHKVFYTELL NLCEAEDSAL TKLPCYKSLP SLVPLRIAAL NALAACNYLP
QSREKIIAAL FKALNSTNSE LQEAGEACMR KFLEGATIEV DQIHTHMRPL LMMLGDYRSL
TLNVVNRLTS VTRLFPNSFN DKFCDQMMQH LRKWMEVVVI THKGGQRSDG NESISECGRC
PLSPFCQFEE MKICSAIINL FHLIPAAPQT LVKPLLEVVM KTERAMLIEA GSPFREPLIK
FLTRHPSQTV ELFMMEATLN DPQWSRMFMS FLKHKDARPL RDVLAANPNR FITLLLPGGA
QTAVRPGSPS TSTMRLDLQF QAIKIISIIV KNDDSWLASQ HSLVSQLRRV WVSENFQERH
RKENMAATNW KEPKLLAYCL LNYCKRNYGD IELLFQLLRA FTGRFLCNMT FLKEYMEEEI
PKNYSIAQKR ALFFRFVDFN DPNFGDELKA KVLQHILNPA FLYSFEKGEG EQLLGPPNPE
GDNPESITSV FITKVLDPEK QADMLDSLRI YLLQYATLLV EHAPHHIHDN NKNRNSKLRR
LMTFAWPCLL SKACVDPACK YSGHLLLAHI IAKFAIHKKI VLQVFHSLLK AHAMEARAIV
RQAMAILTPA VPARMEDGHQ MLTHWTRKII VEEGHTVPQL VHILHLIVQH FKVYYPVRHH
LVQHMVSAMQ RLGFTPSVTI EQRRLAVDLS EVVIKWELQR IKDQQPDSDM DPNSSGEGVN
SVSSSIKRGL SVDSAQEVKR FRTATGAISA VFGRSQSLPG ADSLLAKPID KQHTDTVVNF
LIRVACQVND NTNTAGSPGE VLSRRCVNLL KTALRPDMWP KSELKLQWFD KLLMTVEQPN
QVNYGNICTG LEVLSFLLTV LQSPAILSSF KPLQRGIAAC MTCGNTKVLR AVHSLLSRLM
SIFPTEPSTS SVASKYEELE CLYAAVGKVI YEGLTNYEKA TNANPSQLFG TLMILKSACS
NNPSYIDRLI SVFMRSLQKM VREHLNPQAA SGSTEATSGT SELVMLSLEL VKTRLAVMSM
EMRKNFIQAI LTSLIEKSPD AKILRAVVKI VEEWVKNNSP MAANQTPTLR EKSILLVKMM
TYIEKRFPED LELNAQFLDL VNYVYRDETL SGSELTAKLE PAFLSGLRCA QPLIRAKFFE
VFDNSMKRRV YERLLYVTCS QNWEAMGNHF WIKQCIELLL AVCEKSTPIG TSCQGAMLPS
ITNVINLADS HDRAAFAMVT HVKQEPRERE NSESKEEDVE IDIELAPGDQ TSTPKTKELS
EKDIGNQLHM LTNRHDKFLD TLREVKTGAL LSAFVQLCHI STTLAEKTWV QLFPRLWKIL
SDRQQHALAG EISPFLCSGS HQVQRDCQPS ALNCFVEAMS QCVPPIPIRP CVLKYLGKTH
NLWFRSTLML EHQAFEKGLS LQIKPKQTTE FYEQESITPP QQEILDSLAE LYSLLQEEDM
WAGLWQKRCK YSETATAIAY EQHGFFEQAQ ESYEKAMDKA KKEHERSNAS PAIFPEYQLW
EDHWIRCSKE LNQWEALTEY GQSKGHINPY LVLECAWRVS NWTAMKEALV QVEVSCPKEM
AWKVNMYRGY LAICHPEEQQ LSFIERLVEM ASSLAIREWR RLPHVVSHVH TPLLQAAQQI
IELQEAAQIN AGLQPTNLGR NNSLHDMKTV VKTWRNRLPI VSDDLSHWSS IFMWRQHHYQ
GKPTWSGMHS SSIVTAYENS SQHDPSSNNA MLGVHASASA IIQYGKIARK QGLVNVALDI
LSRIHTIPTV PIVDCFQKIR QQVKCYLQLA GVMGKNECMQ GLEVIESTNL KYFTKEMTAE
FYALKGMFLA QINKSEEANK AFSAAVQMHD VLVKAWAMWG DYLENIFVKE RQLHLGVSAI
TCYLHACRHQ NESKSRKYLA KVLWLLSFDD DKNTLADAVD KYCIGVPPIQ WLAWIPQLLT
CLVGSEGKLL LNLISQVGRV YPQAVYFPIR TLYLTLKIEQ RERYKSDPGP IRATAPMWRC
SRIMHMQREL HPTLLSSLEG IVDQMVWFRE NWHEEVLRQL QQGLAKCYSV AFEKSGAVSD
AKITPHTLNF VKKLVSTFGV GLENVSNVST MFSSAASESL ARRAQATAQD PVFQKLKGQF
TTDFDFSVPG SMKLHNLISK LKKWIKILEA KTKQLPKFFL IEEKCRFLSN FSAQTAEVEI
PGEFLMPKPT HYYIKIARFM PRVEIVQKHN TAARRLYIRG HNGKIYPYLV MNDACLTESR
REERVLQLLR LLNPCLEKRK ETTKRHLFFT VPRVVAVSPQ MRLVEDNPSS LSLVEIYKQR
CAKKGIEHDN PISRYYDRLA TVQARGTQAS HQVLRDILKE VQSNMVPRSM LKEWALHTFP
NATDYWTFRK MFTIQLALIG FAEFVLHLNR LNPEMLQIAQ DTGKLNVAYF RFDINDATGD
LDANRPVPFR LTPNISEFLT TIGVSGPLTA SMIAVARCFA QPNFKVDGIL KTVLRDEIIA
WHKKTQEDTS SPLSAAGQPE NMDSQQLVSL VQKAVTAIMT RLHNLAQFEG GESKVNTLVA
AANSLDNLCR MDPAWHPWL


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