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Thyroid receptor-interacting protein 6 (TR-interacting protein 6) (TRIP-6) (Opa-interacting protein 1) (OIP-1) (Zyxin-related protein 1) (ZRP-1)

 TRIP6_HUMAN             Reviewed;         476 AA.
Q15654; A4D2E7; F2ZC07; F2ZC08; O15170; O15275; Q9BTB2; Q9BUE5;
Q9BXP3; Q9UNT4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-MAY-2002, sequence version 3.
25-OCT-2017, entry version 167.
RecName: Full=Thyroid receptor-interacting protein 6;
Short=TR-interacting protein 6;
Short=TRIP-6;
AltName: Full=Opa-interacting protein 1;
Short=OIP-1;
AltName: Full=Zyxin-related protein 1;
Short=ZRP-1;
Name=TRIP6; Synonyms=OIP1;
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).
PubMed=9598321; DOI=10.1006/geno.1998.5248;
Yi J., Beckerle M.C.;
"The human TRIP6 gene encodes a LIM domain protein and maps to
chromosome 7q22, a region associated with tumorigenesis.";
Genomics 49:314-316(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND INTERACTION
WITH PTPN13.
PubMed=10400701; DOI=10.1074/jbc.274.29.20679;
Murthy K.K., Clark K., Fortin Y., Shen S.-H., Banville D.;
"ZRP-1, a zyxin-related protein, interacts with the second PDZ domain
of the cytosolic protein tyrosine phosphatase hPTP1E.";
J. Biol. Chem. 274:20679-20687(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11239002; DOI=10.1093/nar/29.6.1352;
Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C.,
Miller W., Koop B.F.;
"Comparative analysis of the gene-dense ACHE/TFR2 region on human
chromosome 7q22 with the orthologous region on mouse chromosome 5.";
Nucleic Acids Res. 29:1352-1365(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Kojima H., Masuhiro Y., Hanazawa S.;
"Identification and characterization of novel isoforms of human
TRIP6.";
Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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=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).
[7]
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).
[8]
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLN-111; ILE-230 AND PHE-296.
TISSUE=Cervix, Kidney, and Pancreas;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 310-476 (ISOFORM 1).
PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
"Two classes of proteins dependent on either the presence or absence
of thyroid hormone for interaction with the thyroid hormone
receptor.";
Mol. Endocrinol. 9:243-254(1995).
[11]
FUNCTION.
PubMed=15489293; DOI=10.1101/gad.322404;
Kassel O., Schneider S., Heilbock C., Litfin M., Goettlicher M.,
Herrlich P.;
"A nuclear isoform of the focal adhesion LIM-domain protein Trip6
integrates activating and repressing signals at AP-1- and NF-kappaB-
regulated promoters.";
Genes Dev. 18:2518-2528(2004).
[12]
INTERACTION WITH LPAR2, AND FUNCTION.
PubMed=14688263; DOI=10.1074/jbc.M311891200;
Xu J., Lai Y.-J., Lin W.-C., Lin F.-T.;
"TRIP6 enhances lysophosphatidic acid-induced cell migration by
interacting with the lysophosphatidic acid 2 receptor.";
J. Biol. Chem. 279:10459-10468(2004).
[13]
INTERACTION WITH SCRIB.
PubMed=16137684; DOI=10.1016/j.febslet.2005.08.012;
Petit M.M.R., Crombez K.R.M.O., Vervenne H.B.V.K., Weyns N.,
Van de Ven W.J.M.;
"The tumor suppressor Scrib selectively interacts with specific
members of the zyxin family of proteins.";
FEBS Lett. 579:5061-5068(2005).
[14]
PHOSPHORYLATION AT TYR-55.
PubMed=15988003; DOI=10.1128/MCB.25.14.5859-5868.2005;
Lai Y.-J., Chen C.-S., Lin W.-C., Lin F.-T.;
"c-Src-mediated phosphorylation of TRIP6 regulates its function in
lysophosphatidic acid-induced cell migration.";
Mol. Cell. Biol. 25:5859-5868(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
INTERACTION WITH PRKAA2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-101
AND SER-102, AND FUNCTION.
PubMed=16624523; DOI=10.1016/j.cellsig.2006.01.021;
Solaz-Fuster M.C., Gimeno-Alcaniz J.V., Casado M., Sanz P.;
"TRIP6 transcriptional co-activator is a novel substrate of AMP-
activated protein kinase.";
Cell. Signal. 18:1702-1712(2006).
[17]
INTERACTION WITH SVIL.
PubMed=16880273; DOI=10.1083/jcb.200512051;
Takizawa N., Smith T.C., Nebl T., Crowley J.L., Palmieri S.J.,
Lifshitz L.M., Ehrhardt A.G., Hoffman L.M., Beckerle M.C., Luna E.J.;
"Supervillin modulation of focal adhesions involving TRIP6/ZRP-1.";
J. Cell Biol. 174:447-458(2006).
[18]
INTERACTION WITH SALMONELLA TYPHIMURIUM SSEI.
PubMed=17095609; DOI=10.1073/pnas.0604054103;
Worley M.J., Nieman G.S., Geddes K., Heffron F.;
"Salmonella typhimurium disseminates within its host by manipulating
the motility of infected cells.";
Proc. Natl. Acad. Sci. U.S.A. 103:17915-17920(2006).
[19]
INTERACTION WITH PTPN13, AND PHOSPHORYLATION AT TYR-55.
PubMed=17591779; DOI=10.1074/jbc.M701499200;
Lai Y.-J., Lin W.-C., Lin F.-T.;
"PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic
acid-induced cell migration.";
J. Biol. Chem. 282:24381-24387(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, 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]
INTERACTION WITH MAGI1 AND PTPN13, MUTAGENESIS OF THR-474, TISSUE
SPECIFICITY, AND FUNCTION.
PubMed=19017743; DOI=10.1096/fj.08-106344;
Chastre E., Abdessamad M., Kruglov A., Bruyneel E., Bracke M.,
Di Gioia Y., Beckerle M.C., van Roy F., Kotelevets L.;
"TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule,
promotes invasiveness.";
FASEB J. 23:916-928(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND 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).
[23]
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-189 AND
SER-249, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=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).
[25]
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).
[26]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-25; ARG-111; ARG-179;
ARG-186; ARG-205; ARG-236 AND ARG-238, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[27]
STRUCTURE BY NMR OF 279-396.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first and second LIM domain of thyroid
receptor interacting protein 6 (TRIP6).";
Submitted (OCT-2006) to the PDB data bank.
-!- FUNCTION: Relays signals from the cell surface to the nucleus to
weaken adherens junction and promote actin cytoskeleton
reorganization and cell invasiveness. Involved in lysophosphatidic
acid-induced cell adhesion and migration. Acts as a
transcriptional coactivator for NF-kappa-B and JUN, and mediates
the transrepression of these transcription factors induced by
glucocorticoid receptor. {ECO:0000269|PubMed:14688263,
ECO:0000269|PubMed:15489293, ECO:0000269|PubMed:16624523,
ECO:0000269|PubMed:19017743}.
-!- SUBUNIT: Specifically interacts with the ligand binding domain of
the thyroid receptor (TR) in the presence of thyroid hormone.
Interacts with PTPN13. Interacts with SVIL isoform 2. Interacts
with LPAR2 but not other LPA receptors. Interacts with PRKAA2.
Interacts with MAGI1. Interacts with SCRIB (By similarity). Binds
to S.typhimurium protein sseI. {ECO:0000250,
ECO:0000269|PubMed:10400701, ECO:0000269|PubMed:14688263,
ECO:0000269|PubMed:16137684, ECO:0000269|PubMed:16624523,
ECO:0000269|PubMed:16880273, ECO:0000269|PubMed:17095609,
ECO:0000269|PubMed:17591779, ECO:0000269|PubMed:19017743}.
-!- INTERACTION:
Q5W150:-; NbExp=3; IntAct=EBI-742327, EBI-10248148;
Q95HA4:-; NbExp=3; IntAct=EBI-742327, EBI-10236795;
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-742327, EBI-743598;
Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-742327, EBI-10173507;
P29972:AQP1; NbExp=6; IntAct=EBI-742327, EBI-745213;
P54259:ATN1; NbExp=2; IntAct=EBI-742327, EBI-945980;
P48047:ATP5O; NbExp=3; IntAct=EBI-742327, EBI-355815;
Q13895:BYSL; NbExp=6; IntAct=EBI-742327, EBI-358049;
Q8NEC5:CATSPER1; NbExp=6; IntAct=EBI-742327, EBI-744545;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-742327, EBI-10181988;
P26441:CNTF; NbExp=3; IntAct=EBI-742327, EBI-1050897;
Q02930-3:CREB5; NbExp=3; IntAct=EBI-742327, EBI-10192698;
P53673:CRYBA4; NbExp=3; IntAct=EBI-742327, EBI-7519711;
O75638:CTAG2; NbExp=3; IntAct=EBI-742327, EBI-10188927;
Q9NQL9:DMRT3; NbExp=3; IntAct=EBI-742327, EBI-9679045;
Q86UW9:DTX2; NbExp=3; IntAct=EBI-742327, EBI-740376;
Q5JVL4:EFHC1; NbExp=3; IntAct=EBI-742327, EBI-743105;
Q8N2X6:EXOC3-AS1; NbExp=6; IntAct=EBI-742327, EBI-749333;
P48023:FASLG; NbExp=3; IntAct=EBI-742327, EBI-495538;
O43559:FRS3; NbExp=5; IntAct=EBI-742327, EBI-725515;
P15976-2:GATA1; NbExp=3; IntAct=EBI-742327, EBI-9090198;
Q9HBR3:GDPD5; NbExp=3; IntAct=EBI-742327, EBI-10310206;
P04899:GNAI2; NbExp=3; IntAct=EBI-742327, EBI-353997;
Q9Y223-2:GNE; NbExp=4; IntAct=EBI-742327, EBI-11975289;
Q13227:GPS2; NbExp=4; IntAct=EBI-742327, EBI-713355;
Q14687:GSE1; NbExp=3; IntAct=EBI-742327, EBI-372619;
V9HWD0:HEL-S-42; NbExp=3; IntAct=EBI-742327, EBI-10330219;
P09022:Hoxa1 (xeno); NbExp=3; IntAct=EBI-742327, EBI-3957603;
P31269:HOXA9; NbExp=4; IntAct=EBI-742327, EBI-742314;
P17482:HOXB9; NbExp=3; IntAct=EBI-742327, EBI-745290;
A0A0C4DGM4:HYKK; NbExp=3; IntAct=EBI-742327, EBI-10236738;
Q0VD86:INCA1; NbExp=3; IntAct=EBI-742327, EBI-6509505;
Q99706:KIR2DL4; NbExp=3; IntAct=EBI-742327, EBI-10294579;
Q9H2R5:KLK15; NbExp=3; IntAct=EBI-742327, EBI-8645371;
Q6PEX3:KRTAP26-1; NbExp=3; IntAct=EBI-742327, EBI-3957672;
P25791:LMO2; NbExp=3; IntAct=EBI-742327, EBI-739696;
O60336:MAPKBP1; NbExp=3; IntAct=EBI-742327, EBI-947402;
Q9Y316:MEMO1; NbExp=3; IntAct=EBI-742327, EBI-1104564;
Q9H7H0:METTL17; NbExp=4; IntAct=EBI-742327, EBI-749353;
Q8IXL7:MSRB3; NbExp=3; IntAct=EBI-742327, EBI-8634060;
O43639:NCK2; NbExp=6; IntAct=EBI-742327, EBI-713635;
Q14511:NEDD9; NbExp=3; IntAct=EBI-742327, EBI-2108053;
Q8WWR8-2:NEU4; NbExp=3; IntAct=EBI-742327, EBI-10277551;
O43482:OIP5; NbExp=3; IntAct=EBI-742327, EBI-536879;
Q9BWI9:OTUB2; NbExp=3; IntAct=EBI-742327, EBI-10300896;
P09619:PDGFRB; NbExp=3; IntAct=EBI-742327, EBI-641237;
Q13526:PIN1; NbExp=3; IntAct=EBI-742327, EBI-714158;
Q3SYA9:POM121L1P; NbExp=3; IntAct=EBI-742327, EBI-10241319;
Q96I34:PPP1R16A; NbExp=3; IntAct=EBI-742327, EBI-710402;
Q13131:PRKAA1; NbExp=3; IntAct=EBI-742327, EBI-1181405;
P54646:PRKAA2; NbExp=3; IntAct=EBI-742327, EBI-1383852;
Q15678:PTPN14; NbExp=4; IntAct=EBI-742327, EBI-1237156;
P54725:RAD23A; NbExp=3; IntAct=EBI-742327, EBI-746453;
Q86VV4:RANBP3L; NbExp=4; IntAct=EBI-742327, EBI-12028066;
P48380:RFX3; NbExp=3; IntAct=EBI-742327, EBI-742557;
P61586:RHOA; NbExp=3; IntAct=EBI-742327, EBI-446668;
Q63HN8-6:RNF213; NbExp=3; IntAct=EBI-742327, EBI-10248548;
Q8IYX7:SAXO1; NbExp=3; IntAct=EBI-742327, EBI-3957636;
Q9Y2K2-3:SIK3; NbExp=3; IntAct=EBI-742327, EBI-10326390;
Q05CH4:SLC15A3; NbExp=3; IntAct=EBI-742327, EBI-10223741;
P12236:SLC25A6; NbExp=3; IntAct=EBI-742327, EBI-356254;
O75716:STK16; NbExp=3; IntAct=EBI-742327, EBI-749295;
O46385:SVIL (xeno); NbExp=5; IntAct=EBI-742327, EBI-6995105;
Q9Y4C2:TCAF1; NbExp=3; IntAct=EBI-742327, EBI-750484;
Q8WW24:TEKT4; NbExp=3; IntAct=EBI-742327, EBI-750487;
Q0P5Q0:TMSB4X; NbExp=3; IntAct=EBI-742327, EBI-10226570;
Q5VU62:TPM3; NbExp=3; IntAct=EBI-742327, EBI-10184033;
O43734:TRAF3IP2; NbExp=3; IntAct=EBI-742327, EBI-744798;
Q9UL33:TRAPPC2L; NbExp=3; IntAct=EBI-742327, EBI-747601;
Q14134:TRIM29; NbExp=3; IntAct=EBI-742327, EBI-702370;
Q6ZVT0:TTLL10; NbExp=3; IntAct=EBI-742327, EBI-7844656;
Q99757:TXN2; NbExp=3; IntAct=EBI-742327, EBI-2932492;
Q86UY0:TXNDC5; NbExp=3; IntAct=EBI-742327, EBI-2825190;
Q06250:WT1-AS; NbExp=3; IntAct=EBI-742327, EBI-10223946;
Q8N4L5:XRCC6BP1; NbExp=3; IntAct=EBI-742327, EBI-10265517;
A2RRL9:ZBP1; NbExp=3; IntAct=EBI-742327, EBI-10173066;
Q9H0D2:ZNF541; NbExp=4; IntAct=EBI-742327, EBI-3957075;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:16624523}. Cell junction, focal adhesion
{ECO:0000269|PubMed:16624523}. Nucleus
{ECO:0000269|PubMed:16624523}. Cytoplasm
{ECO:0000269|PubMed:16624523}. Note=Shuttles between nucleus and
cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q15654-1; Sequence=Displayed;
Name=2;
IsoId=Q15654-2; Sequence=VSP_047621, VSP_047624;
Name=3;
IsoId=Q15654-3; Sequence=VSP_047622, VSP_047623;
-!- TISSUE SPECIFICITY: Abundantly expressed in kidney, liver and
lung. Lower levels in heart, placenta and pancreas. Expressed in
colonic epithelial cells. Up-regulated in colonic tumors.
{ECO:0000269|PubMed:19017743}.
-!- DOMAIN: The LIM zinc-binding domains mediate interaction with
LPAR2 and with S.typhimurium protein sseI.
-!- PTM: Phosphorylation at Tyr-55 by SRC is required for enhancement
of lysophosphatidic acid-induced cell migration. Tyr-55 is
dephosphorylated by PTPN13. {ECO:0000269|PubMed:15988003,
ECO:0000269|PubMed:17591779}.
-!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC41740.1; Type=Frameshift; Positions=461; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ001902; CAA05080.1; -; mRNA.
EMBL; AF000974; AAB62222.1; -; mRNA.
EMBL; AF093836; AAD03037.1; -; Genomic_DNA.
EMBL; AF093834; AAD03037.1; JOINED; Genomic_DNA.
EMBL; AF093835; AAD03037.1; JOINED; Genomic_DNA.
EMBL; AF312032; AAK21007.1; -; Genomic_DNA.
EMBL; AB628086; BAK20497.1; -; mRNA.
EMBL; AB628087; BAK20498.1; -; mRNA.
EMBL; AK291906; BAF84595.1; -; mRNA.
EMBL; AC011895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236956; EAL23817.1; -; Genomic_DNA.
EMBL; CH471091; EAW76472.1; -; Genomic_DNA.
EMBL; BC002680; AAH02680.1; -; mRNA.
EMBL; BC004249; AAH04249.1; -; mRNA.
EMBL; BC004999; AAH04999.1; -; mRNA.
EMBL; BC021540; AAH21540.1; -; mRNA.
EMBL; BC028985; AAH28985.1; -; mRNA.
EMBL; L40374; AAC41740.1; ALT_FRAME; mRNA.
CCDS; CCDS5708.1; -. [Q15654-1]
RefSeq; NP_003293.2; NM_003302.2. [Q15654-1]
UniGene; Hs.534360; -.
PDB; 1X61; NMR; -; A=279-337.
PDB; 2DLO; NMR; -; A=329-396.
PDBsum; 1X61; -.
PDBsum; 2DLO; -.
ProteinModelPortal; Q15654; -.
SMR; Q15654; -.
BioGrid; 113056; 197.
CORUM; Q15654; -.
DIP; DIP-34466N; -.
IntAct; Q15654; 167.
MINT; MINT-1366827; -.
STRING; 9606.ENSP00000200457; -.
iPTMnet; Q15654; -.
PhosphoSitePlus; Q15654; -.
BioMuta; TRIP6; -.
DMDM; 20981729; -.
EPD; Q15654; -.
MaxQB; Q15654; -.
PaxDb; Q15654; -.
PeptideAtlas; Q15654; -.
PRIDE; Q15654; -.
DNASU; 7205; -.
Ensembl; ENST00000200457; ENSP00000200457; ENSG00000087077. [Q15654-1]
Ensembl; ENST00000417475; ENSP00000413817; ENSG00000087077. [Q15654-2]
Ensembl; ENST00000437505; ENSP00000410736; ENSG00000087077. [Q15654-3]
Ensembl; ENST00000619988; ENSP00000479865; ENSG00000087077. [Q15654-3]
GeneID; 7205; -.
KEGG; hsa:7205; -.
UCSC; uc003uww.4; human. [Q15654-1]
CTD; 7205; -.
DisGeNET; 7205; -.
EuPathDB; HostDB:ENSG00000087077.11; -.
GeneCards; TRIP6; -.
H-InvDB; HIX0167828; -.
HGNC; HGNC:12311; TRIP6.
HPA; CAB046454; -.
HPA; CAB046460; -.
HPA; HPA052813; -.
MIM; 602933; gene.
neXtProt; NX_Q15654; -.
OpenTargets; ENSG00000087077; -.
PharmGKB; PA36989; -.
eggNOG; KOG1701; Eukaryota.
eggNOG; ENOG410Y3GP; LUCA.
GeneTree; ENSGT00760000119039; -.
HOVERGEN; HBG093602; -.
InParanoid; Q15654; -.
KO; K12792; -.
OrthoDB; EOG091G085F; -.
PhylomeDB; Q15654; -.
TreeFam; TF320310; -.
SignaLink; Q15654; -.
SIGNOR; Q15654; -.
ChiTaRS; TRIP6; human.
EvolutionaryTrace; Q15654; -.
GeneWiki; TRIP6; -.
GenomeRNAi; 7205; -.
PRO; PR:Q15654; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000087077; -.
CleanEx; HS_TRIP6; -.
ExpressionAtlas; Q15654; baseline and differential.
Genevisible; Q15654; HS.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005149; F:interleukin-1 receptor binding; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0046966; F:thyroid hormone receptor binding; NAS:UniProtKB.
GO; GO:0048041; P:focal adhesion assembly; NAS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0008588; P:release of cytoplasmic sequestered NF-kappaB; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR001781; Znf_LIM.
Pfam; PF00412; LIM; 3.
SMART; SM00132; LIM; 3.
PROSITE; PS00478; LIM_DOMAIN_1; 2.
PROSITE; PS50023; LIM_DOMAIN_2; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Complete proteome; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation;
Zinc.
CHAIN 1 476 Thyroid receptor-interacting protein 6.
/FTId=PRO_0000075908.
DOMAIN 279 316 LIM zinc-binding 1. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 339 398 LIM zinc-binding 2. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 399 467 LIM zinc-binding 3. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
REGION 469 476 Interaction with MAGI1 and PTPN13.
{ECO:0000269|PubMed:19017743}.
MOD_RES 25 25 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q9Z1Y4}.
MOD_RES 25 25 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 55 55 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:15988003,
ECO:0000269|PubMed:17591779}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231}.
MOD_RES 111 111 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 179 179 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 186 186 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 189 189 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 205 205 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 236 236 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 238 238 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 37 106 ALQPHPRVNFCPLPSEQCYQAPGGPEDRGPAWVGSHGVLQH
TQGLPADRGGLRPGSLDAEIDLLSSTLAE -> VLPGPRGT
GGSGAGVGGVPWSTPAHAGAPCRQGGPSPWKPGRRDRLAEQ
HAGRAEWGSGSCVTATRPTGI (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_047621.
VAR_SEQ 37 80 ALQPHPRVNFCPLPSEQCYQAPGGPEDRGPAWVGSHGVLQH
TQG -> GAPCRQGGPSPWKPGRRDRLAEQHAGRAEWGSGS
CVTATRPTGI (in isoform 3). {ECO:0000305}.
/FTId=VSP_047622.
VAR_SEQ 81 476 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_047623.
VAR_SEQ 107 476 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_047624.
VARIANT 111 111 R -> Q (in dbSNP:rs2437100).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_062262.
VARIANT 230 230 V -> I (in dbSNP:rs2075756).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_050171.
VARIANT 296 296 L -> F (in dbSNP:rs17855370).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_013309.
MUTAGEN 101 101 S->A: Exclusively located in nucleus.
{ECO:0000269|PubMed:16624523}.
MUTAGEN 102 102 S->A: Exclusively located in nucleus.
{ECO:0000269|PubMed:16624523}.
MUTAGEN 474 474 T->A: Reduces interaction with MAGI1.
{ECO:0000269|PubMed:19017743}.
CONFLICT 39 40 Missing (in Ref. 9; AAH02680).
{ECO:0000305}.
CONFLICT 102 102 S -> T (in Ref. 2; AAB62222).
{ECO:0000305}.
CONFLICT 106 106 E -> K (in Ref. 2; AAB62222).
{ECO:0000305}.
CONFLICT 135 135 S -> C (in Ref. 1; CAA05080).
{ECO:0000305}.
CONFLICT 310 313 CRAQ -> MPGP (in Ref. 10; AAC41740).
{ECO:0000305}.
STRAND 280 282 {ECO:0000244|PDB:1X61}.
STRAND 288 290 {ECO:0000244|PDB:1X61}.
STRAND 296 300 {ECO:0000244|PDB:1X61}.
TURN 302 304 {ECO:0000244|PDB:1X61}.
STRAND 308 310 {ECO:0000244|PDB:1X61}.
STRAND 319 324 {ECO:0000244|PDB:1X61}.
STRAND 326 328 {ECO:0000244|PDB:1X61}.
HELIX 329 337 {ECO:0000244|PDB:1X61}.
TURN 340 342 {ECO:0000244|PDB:2DLO}.
STRAND 351 353 {ECO:0000244|PDB:2DLO}.
STRAND 356 358 {ECO:0000244|PDB:2DLO}.
TURN 360 362 {ECO:0000244|PDB:2DLO}.
STRAND 366 368 {ECO:0000244|PDB:2DLO}.
HELIX 388 394 {ECO:0000244|PDB:2DLO}.
SEQUENCE 476 AA; 50288 MW; 2BA7C747DF30A8FD CRC64;
MSGPTWLPPK QPEPARAPQG RAIPRGTPGP PPAHGAALQP HPRVNFCPLP SEQCYQAPGG
PEDRGPAWVG SHGVLQHTQG LPADRGGLRP GSLDAEIDLL SSTLAELNGG RGHASRRPDR
QAYEPPPPPA YRTGSLKPNP ASPLPASPYG GPTPASYTTA STPAGPAFPV QVKVAQPVRG
CGPPRRGASQ ASGPLPGPHF PLPGRGEVWG PGYRSQREPG PGAKEEAAGV SGPAGRGRGG
EHGPQVPLSQ PPEDELDRLT KKLVHDMNHP PSGEYFGQCG GCGEDVVGDG AGVVALDRVF
HVGCFVCSTC RAQLRGQHFY AVERRAYCEG CYVATLEKCA TCSQPILDRI LRAMGKAYHP
GCFTCVVCHR GLDGIPFTVD ATSQIHCIED FHRKFAPRCS VCGGAIMPEP GQEETVRIVA
LDRSFHIGCY KCEECGLLLS SEGECQGCYP LDGHILCKAC SAWRIQELSA TVTTDC


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