TRIP6_HUMAN
ID TRIP6_HUMAN Reviewed; 476 AA.
AC Q15654; A4D2E7; F2ZC07; F2ZC08; O15170; O15275; Q9BTB2; Q9BUE5; Q9BXP3;
AC Q9UNT4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Thyroid receptor-interacting protein 6;
DE Short=TR-interacting protein 6;
DE Short=TRIP-6;
DE AltName: Full=Opa-interacting protein 1;
DE Short=OIP-1;
DE AltName: Full=Zyxin-related protein 1;
DE Short=ZRP-1;
GN Name=TRIP6; Synonyms=OIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9598321; DOI=10.1006/geno.1998.5248;
RA Yi J., Beckerle M.C.;
RT "The human TRIP6 gene encodes a LIM domain protein and maps to chromosome
RT 7q22, a region associated with tumorigenesis.";
RL Genomics 49:314-316(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND INTERACTION WITH
RP PTPN13.
RX PubMed=10400701; DOI=10.1074/jbc.274.29.20679;
RA Murthy K.K., Clark K., Fortin Y., Shen S.-H., Banville D.;
RT "ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of
RT the cytosolic protein tyrosine phosphatase hPTP1E.";
RL J. Biol. Chem. 274:20679-20687(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Kojima H., Masuhiro Y., Hanazawa S.;
RT "Identification and characterization of novel isoforms of human TRIP6.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLN-111;
RP ILE-230 AND PHE-296.
RC TISSUE=Cervix, Kidney, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 310-476 (ISOFORM 1).
RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence of
RT thyroid hormone for interaction with the thyroid hormone receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [11]
RP INTERACTION WITH PDLIM4 AND PTPN13, AND SUBCELLULAR LOCATION.
RX PubMed=10826496; DOI=10.1078/s0171-9335(04)70031-x;
RA Cuppen E., van Ham M., Wansink D.G., de Leeuw A., Wieringa B., Hendriks W.;
RT "The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor
RT protein RIL and the protein tyrosine phosphatase PTP-BL.";
RL Eur. J. Cell Biol. 79:283-293(2000).
RN [12]
RP FUNCTION.
RX PubMed=15489293; DOI=10.1101/gad.322404;
RA Kassel O., Schneider S., Heilbock C., Litfin M., Goettlicher M.,
RA Herrlich P.;
RT "A nuclear isoform of the focal adhesion LIM-domain protein Trip6
RT integrates activating and repressing signals at AP-1- and NF-kappaB-
RT regulated promoters.";
RL Genes Dev. 18:2518-2528(2004).
RN [13]
RP INTERACTION WITH LPAR2, AND FUNCTION.
RX PubMed=14688263; DOI=10.1074/jbc.m311891200;
RA Xu J., Lai Y.-J., Lin W.-C., Lin F.-T.;
RT "TRIP6 enhances lysophosphatidic acid-induced cell migration by interacting
RT with the lysophosphatidic acid 2 receptor.";
RL J. Biol. Chem. 279:10459-10468(2004).
RN [14]
RP INTERACTION WITH SCRIB.
RX PubMed=16137684; DOI=10.1016/j.febslet.2005.08.012;
RA Petit M.M.R., Crombez K.R.M.O., Vervenne H.B.V.K., Weyns N.,
RA Van de Ven W.J.M.;
RT "The tumor suppressor Scrib selectively interacts with specific members of
RT the zyxin family of proteins.";
RL FEBS Lett. 579:5061-5068(2005).
RN [15]
RP PHOSPHORYLATION AT TYR-55.
RX PubMed=15988003; DOI=10.1128/mcb.25.14.5859-5868.2005;
RA Lai Y.-J., Chen C.-S., Lin W.-C., Lin F.-T.;
RT "c-Src-mediated phosphorylation of TRIP6 regulates its function in
RT lysophosphatidic acid-induced cell migration.";
RL Mol. Cell. Biol. 25:5859-5868(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [17]
RP INTERACTION WITH PRKAA2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-101 AND
RP SER-102, AND FUNCTION.
RX PubMed=16624523; DOI=10.1016/j.cellsig.2006.01.021;
RA Solaz-Fuster M.C., Gimeno-Alcaniz J.V., Casado M., Sanz P.;
RT "TRIP6 transcriptional co-activator is a novel substrate of AMP-activated
RT protein kinase.";
RL Cell. Signal. 18:1702-1712(2006).
RN [18]
RP INTERACTION WITH SVIL.
RX PubMed=16880273; DOI=10.1083/jcb.200512051;
RA Takizawa N., Smith T.C., Nebl T., Crowley J.L., Palmieri S.J.,
RA Lifshitz L.M., Ehrhardt A.G., Hoffman L.M., Beckerle M.C., Luna E.J.;
RT "Supervillin modulation of focal adhesions involving TRIP6/ZRP-1.";
RL J. Cell Biol. 174:447-458(2006).
RN [19]
RP INTERACTION WITH SALMONELLA TYPHIMURIUM SSEI.
RX PubMed=17095609; DOI=10.1073/pnas.0604054103;
RA Worley M.J., Nieman G.S., Geddes K., Heffron F.;
RT "Salmonella typhimurium disseminates within its host by manipulating the
RT motility of infected cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17915-17920(2006).
RN [20]
RP INTERACTION WITH PTPN13, AND PHOSPHORYLATION AT TYR-55.
RX PubMed=17591779; DOI=10.1074/jbc.m701499200;
RA Lai Y.-J., Lin W.-C., Lin F.-T.;
RT "PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic acid-
RT induced cell migration.";
RL J. Biol. Chem. 282:24381-24387(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP INTERACTION WITH MAGI1 AND PTPN13, MUTAGENESIS OF THR-474, TISSUE
RP SPECIFICITY, AND FUNCTION.
RX PubMed=19017743; DOI=10.1096/fj.08-106344;
RA Chastre E., Abdessamad M., Kruglov A., Bruyneel E., Bracke M., Di Gioia Y.,
RA Beckerle M.C., van Roy F., Kotelevets L.;
RT "TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule,
RT promotes invasiveness.";
RL FASEB J. 23:916-928(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-189 AND SER-249, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-25; ARG-111; ARG-179; ARG-186;
RP ARG-205; ARG-236 AND ARG-238, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [28]
RP STRUCTURE BY NMR OF 279-396.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first and second LIM domain of thyroid receptor
RT interacting protein 6 (TRIP6).";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Relays signals from the cell surface to the nucleus to weaken
CC adherens junction and promote actin cytoskeleton reorganization and
CC cell invasiveness. Involved in lysophosphatidic acid-induced cell
CC adhesion and migration. Acts as a transcriptional coactivator for NF-
CC kappa-B and JUN, and mediates the transrepression of these
CC transcription factors induced by glucocorticoid receptor.
CC {ECO:0000269|PubMed:14688263, ECO:0000269|PubMed:15489293,
CC ECO:0000269|PubMed:16624523, ECO:0000269|PubMed:19017743}.
CC -!- SUBUNIT: Specifically interacts with the ligand binding domain of the
CC thyroid receptor (TR) in the presence of thyroid hormone
CC (PubMed:14688263). Interacts (via the third LIM domain and C-terminus)
CC with PTPN13 (via the second PDZ domain) (PubMed:10400701,
CC PubMed:17591779, PubMed:19017743, PubMed:10826496). Interacts (via the
CC second LIM domain or via the third LIM domain plus C-terminus) with
CC PDLIM4 (via PDZ domain) (PubMed:10826496). Found in a complex with
CC PTPN13 and PDLIM4 (By similarity). Interacts with SVIL isoform 2
CC (PubMed:16880273). Interacts with LPAR2 but not other LPA receptors
CC (PubMed:14688263). Interacts with PRKAA2 (PubMed:16624523). Interacts
CC with MAGI1 (PubMed:19017743). Interacts with SCRIB (PubMed:16137684).
CC In case of infection, interacts with S.typhimurium protein sseI
CC (PubMed:17095609). {ECO:0000250|UniProtKB:Q9Z1Y4,
CC ECO:0000269|PubMed:10400701, ECO:0000269|PubMed:10826496,
CC ECO:0000269|PubMed:14688263, ECO:0000269|PubMed:16137684,
CC ECO:0000269|PubMed:16624523, ECO:0000269|PubMed:16880273,
CC ECO:0000269|PubMed:17095609, ECO:0000269|PubMed:17591779,
CC ECO:0000269|PubMed:19017743}.
CC -!- INTERACTION:
CC Q15654; Q9NYB9: ABI2; NbExp=5; IntAct=EBI-742327, EBI-743598;
CC Q15654; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-742327, EBI-10173507;
CC Q15654; P29972: AQP1; NbExp=7; IntAct=EBI-742327, EBI-745213;
CC Q15654; P54259: ATN1; NbExp=2; IntAct=EBI-742327, EBI-945980;
CC Q15654; P48047: ATP5PO; NbExp=3; IntAct=EBI-742327, EBI-355815;
CC Q15654; P54253: ATXN1; NbExp=7; IntAct=EBI-742327, EBI-930964;
CC Q15654; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-742327, EBI-16429430;
CC Q15654; O15169: AXIN1; NbExp=6; IntAct=EBI-742327, EBI-710484;
CC Q15654; O95817: BAG3; NbExp=3; IntAct=EBI-742327, EBI-747185;
CC Q15654; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-742327, EBI-745073;
CC Q15654; Q13895: BYSL; NbExp=6; IntAct=EBI-742327, EBI-358049;
CC Q15654; Q6NUJ2: C11orf87; NbExp=3; IntAct=EBI-742327, EBI-6660291;
CC Q15654; Q8NEC5: CATSPER1; NbExp=7; IntAct=EBI-742327, EBI-744545;
CC Q15654; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-742327, EBI-744556;
CC Q15654; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-742327, EBI-1104933;
CC Q15654; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-742327, EBI-10181988;
CC Q15654; P26441: CNTF; NbExp=3; IntAct=EBI-742327, EBI-1050897;
CC Q15654; Q02930-3: CREB5; NbExp=3; IntAct=EBI-742327, EBI-10192698;
CC Q15654; P53673: CRYBA4; NbExp=3; IntAct=EBI-742327, EBI-7519711;
CC Q15654; O75638: CTAG2; NbExp=4; IntAct=EBI-742327, EBI-10188927;
CC Q15654; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-742327, EBI-9679045;
CC Q15654; Q86UW9: DTX2; NbExp=3; IntAct=EBI-742327, EBI-740376;
CC Q15654; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-742327, EBI-743105;
CC Q15654; Q9UM22: EPDR1; NbExp=3; IntAct=EBI-742327, EBI-946972;
CC Q15654; Q8N2X6: EXOC3-AS1; NbExp=4; IntAct=EBI-742327, EBI-749333;
CC Q15654; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-742327, EBI-2807642;
CC Q15654; O95363: FARS2; NbExp=3; IntAct=EBI-742327, EBI-2513774;
CC Q15654; P48023: FASLG; NbExp=3; IntAct=EBI-742327, EBI-495538;
CC Q15654; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-742327, EBI-11320806;
CC Q15654; O43559: FRS3; NbExp=6; IntAct=EBI-742327, EBI-725515;
CC Q15654; A0A0S2Z4D9: GAD1; NbExp=3; IntAct=EBI-742327, EBI-16430771;
CC Q15654; P15976-2: GATA1; NbExp=4; IntAct=EBI-742327, EBI-9090198;
CC Q15654; Q9HBR3: GDPD5; NbExp=3; IntAct=EBI-742327, EBI-10310206;
CC Q15654; Q8NEA6-2: GLIS3; NbExp=3; IntAct=EBI-742327, EBI-12232117;
CC Q15654; P04899: GNAI2; NbExp=3; IntAct=EBI-742327, EBI-353997;
CC Q15654; Q9Y223-2: GNE; NbExp=3; IntAct=EBI-742327, EBI-11975289;
CC Q15654; Q13227: GPS2; NbExp=3; IntAct=EBI-742327, EBI-713355;
CC Q15654; Q14687: GSE1; NbExp=5; IntAct=EBI-742327, EBI-372619;
CC Q15654; P08631-2: HCK; NbExp=3; IntAct=EBI-742327, EBI-9834454;
CC Q15654; V9HWD0: HEL-S-42; NbExp=3; IntAct=EBI-742327, EBI-10330219;
CC Q15654; P31269: HOXA9; NbExp=4; IntAct=EBI-742327, EBI-742314;
CC Q15654; P17482: HOXB9; NbExp=3; IntAct=EBI-742327, EBI-745290;
CC Q15654; P31273: HOXC8; NbExp=3; IntAct=EBI-742327, EBI-1752118;
CC Q15654; P42858: HTT; NbExp=3; IntAct=EBI-742327, EBI-466029;
CC Q15654; A0A0C4DGM4: HYKK; NbExp=3; IntAct=EBI-742327, EBI-10236738;
CC Q15654; Q0VD86: INCA1; NbExp=3; IntAct=EBI-742327, EBI-6509505;
CC Q15654; Q96PC2: IP6K3; NbExp=3; IntAct=EBI-742327, EBI-10990676;
CC Q15654; P16144-2: ITGB4; NbExp=3; IntAct=EBI-742327, EBI-11051601;
CC Q15654; Q7L273: KCTD9; NbExp=3; IntAct=EBI-742327, EBI-4397613;
CC Q15654; Q99706: KIR2DL4; NbExp=3; IntAct=EBI-742327, EBI-10294579;
CC Q15654; Q9H2R5: KLK15; NbExp=3; IntAct=EBI-742327, EBI-8645371;
CC Q15654; Q5T749: KPRP; NbExp=3; IntAct=EBI-742327, EBI-10981970;
CC Q15654; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-742327, EBI-3957672;
CC Q15654; P25791: LMO2; NbExp=3; IntAct=EBI-742327, EBI-739696;
CC Q15654; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-742327, EBI-739832;
CC Q15654; O60336: MAPKBP1; NbExp=3; IntAct=EBI-742327, EBI-947402;
CC Q15654; Q9Y316: MEMO1; NbExp=3; IntAct=EBI-742327, EBI-1104564;
CC Q15654; Q9H7H0: METTL17; NbExp=5; IntAct=EBI-742327, EBI-749353;
CC Q15654; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-742327, EBI-14086479;
CC Q15654; Q9BRT3: MIEN1; NbExp=3; IntAct=EBI-742327, EBI-6137472;
CC Q15654; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-742327, EBI-2801965;
CC Q15654; Q8IVT2: MISP; NbExp=3; IntAct=EBI-742327, EBI-2555085;
CC Q15654; Q8IXL7: MSRB3; NbExp=3; IntAct=EBI-742327, EBI-8634060;
CC Q15654; O43639: NCK2; NbExp=8; IntAct=EBI-742327, EBI-713635;
CC Q15654; Q14511: NEDD9; NbExp=3; IntAct=EBI-742327, EBI-2108053;
CC Q15654; Q8WWR8-2: NEU4; NbExp=3; IntAct=EBI-742327, EBI-10277551;
CC Q15654; Q6NSM0: NR1D2; NbExp=3; IntAct=EBI-742327, EBI-10250949;
CC Q15654; Q6X4W1-2: NSMF; NbExp=3; IntAct=EBI-742327, EBI-12028784;
CC Q15654; O43482: OIP5; NbExp=4; IntAct=EBI-742327, EBI-536879;
CC Q15654; Q9BWI9: OTUB2; NbExp=3; IntAct=EBI-742327, EBI-10300896;
CC Q15654; P32242: OTX1; NbExp=3; IntAct=EBI-742327, EBI-740446;
CC Q15654; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-742327, EBI-11022007;
CC Q15654; P09619: PDGFRB; NbExp=3; IntAct=EBI-742327, EBI-641237;
CC Q15654; J3QSH9: PER1; NbExp=3; IntAct=EBI-742327, EBI-10178671;
CC Q15654; Q96S52: PIGS; NbExp=3; IntAct=EBI-742327, EBI-2908273;
CC Q15654; Q13526: PIN1; NbExp=3; IntAct=EBI-742327, EBI-714158;
CC Q15654; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-742327, EBI-12014286;
CC Q15654; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-742327, EBI-11956563;
CC Q15654; Q3SYA9: POM121L1P; NbExp=3; IntAct=EBI-742327, EBI-10241319;
CC Q15654; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-742327, EBI-710402;
CC Q15654; Q13131: PRKAA1; NbExp=3; IntAct=EBI-742327, EBI-1181405;
CC Q15654; P54646: PRKAA2; NbExp=3; IntAct=EBI-742327, EBI-1383852;
CC Q15654; Q15678: PTPN14; NbExp=3; IntAct=EBI-742327, EBI-1237156;
CC Q15654; P54725: RAD23A; NbExp=3; IntAct=EBI-742327, EBI-746453;
CC Q15654; Q86VV4: RANBP3L; NbExp=3; IntAct=EBI-742327, EBI-12028066;
CC Q15654; P48380: RFX3; NbExp=3; IntAct=EBI-742327, EBI-742557;
CC Q15654; P61586: RHOA; NbExp=3; IntAct=EBI-742327, EBI-446668;
CC Q15654; Q63HN8-6: RNF213; NbExp=3; IntAct=EBI-742327, EBI-10248548;
CC Q15654; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-742327, EBI-3957636;
CC Q15654; P57086: SCAND1; NbExp=3; IntAct=EBI-742327, EBI-745846;
CC Q15654; Q15047-3: SETDB1; NbExp=3; IntAct=EBI-742327, EBI-11149962;
CC Q15654; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-742327, EBI-12037847;
CC Q15654; Q9Y2K2-7: SIK3; NbExp=3; IntAct=EBI-742327, EBI-17172855;
CC Q15654; Q05CH4: SLC15A3; NbExp=3; IntAct=EBI-742327, EBI-10223741;
CC Q15654; P12236: SLC25A6; NbExp=3; IntAct=EBI-742327, EBI-356254;
CC Q15654; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-742327, EBI-2872322;
CC Q15654; O95863: SNAI1; NbExp=4; IntAct=EBI-742327, EBI-1045459;
CC Q15654; O75716: STK16; NbExp=3; IntAct=EBI-742327, EBI-749295;
CC Q15654; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-742327, EBI-8787464;
CC Q15654; Q9Y4C2: TCAF1; NbExp=3; IntAct=EBI-742327, EBI-750484;
CC Q15654; Q8WW24: TEKT4; NbExp=4; IntAct=EBI-742327, EBI-750487;
CC Q15654; P35590: TIE1; NbExp=3; IntAct=EBI-742327, EBI-2256865;
CC Q15654; Q08117-2: TLE5; NbExp=3; IntAct=EBI-742327, EBI-11741437;
CC Q15654; Q0P5Q0: TMSB4X; NbExp=3; IntAct=EBI-742327, EBI-10226570;
CC Q15654; Q5VU62: TPM3; NbExp=3; IntAct=EBI-742327, EBI-10184033;
CC Q15654; O43734: TRAF3IP2; NbExp=3; IntAct=EBI-742327, EBI-744798;
CC Q15654; Q9UL33: TRAPPC2L; NbExp=3; IntAct=EBI-742327, EBI-747601;
CC Q15654; Q14134: TRIM29; NbExp=3; IntAct=EBI-742327, EBI-702370;
CC Q15654; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-742327, EBI-10241197;
CC Q15654; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-742327, EBI-3918381;
CC Q15654; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-742327, EBI-9090990;
CC Q15654; Q6ZVT0: TTLL10; NbExp=3; IntAct=EBI-742327, EBI-7844656;
CC Q15654; Q99757: TXN2; NbExp=3; IntAct=EBI-742327, EBI-2932492;
CC Q15654; Q86UY0: TXNDC5; NbExp=3; IntAct=EBI-742327, EBI-2825190;
CC Q15654; O75604: USP2; NbExp=3; IntAct=EBI-742327, EBI-743272;
CC Q15654; Q6EMK4: VASN; NbExp=3; IntAct=EBI-742327, EBI-10249550;
CC Q15654; Q06250: WT1-AS; NbExp=3; IntAct=EBI-742327, EBI-10223946;
CC Q15654; Q8N4L5: XRCC6BP1; NbExp=3; IntAct=EBI-742327, EBI-10265517;
CC Q15654; A2RRL9: ZBP1; NbExp=3; IntAct=EBI-742327, EBI-10173066;
CC Q15654; Q15915: ZIC1; NbExp=3; IntAct=EBI-742327, EBI-11963196;
CC Q15654; Q9H0D2: ZNF541; NbExp=3; IntAct=EBI-742327, EBI-3957075;
CC Q15654; Q9UK33: ZNF580; NbExp=3; IntAct=EBI-742327, EBI-746277;
CC Q15654; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-742327, EBI-745520;
CC Q15654; A0A0S2Z5X4: ZNF688; NbExp=6; IntAct=EBI-742327, EBI-16429014;
CC Q15654; A8K8V0: ZNF785; NbExp=3; IntAct=EBI-742327, EBI-3925400;
CC Q15654; Q5W150; NbExp=3; IntAct=EBI-742327, EBI-10248148;
CC Q15654; Q95HA4; NbExp=3; IntAct=EBI-742327, EBI-10236795;
CC Q15654; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-742327, EBI-3957603;
CC Q15654; O46385: SVIL; Xeno; NbExp=5; IntAct=EBI-742327, EBI-6995105;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16624523}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:16624523}. Nucleus {ECO:0000269|PubMed:10826496,
CC ECO:0000269|PubMed:16624523}. Cytoplasm {ECO:0000269|PubMed:16624523}.
CC Note=Shuttles between nucleus and cytoplasm (PubMed:16624523).
CC Colocalizes with actin (PubMed:10826496). {ECO:0000269|PubMed:10826496,
CC ECO:0000269|PubMed:16624523}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15654-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15654-2; Sequence=VSP_047621, VSP_047624;
CC Name=3;
CC IsoId=Q15654-3; Sequence=VSP_047622, VSP_047623;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in kidney, liver and lung.
CC Lower levels in heart, placenta and pancreas. Expressed in colonic
CC epithelial cells. Up-regulated in colonic tumors.
CC {ECO:0000269|PubMed:19017743}.
CC -!- DOMAIN: The LIM zinc-binding domains mediate interaction with LPAR2 and
CC with S.typhimurium protein sseI.
CC -!- PTM: Phosphorylation at Tyr-55 by SRC is required for enhancement of
CC lysophosphatidic acid-induced cell migration. Tyr-55 is
CC dephosphorylated by PTPN13. {ECO:0000269|PubMed:15988003,
CC ECO:0000269|PubMed:17591779}.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC41740.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ001902; CAA05080.1; -; mRNA.
DR EMBL; AF000974; AAB62222.1; -; mRNA.
DR EMBL; AF093836; AAD03037.1; -; Genomic_DNA.
DR EMBL; AF093834; AAD03037.1; JOINED; Genomic_DNA.
DR EMBL; AF093835; AAD03037.1; JOINED; Genomic_DNA.
DR EMBL; AF312032; AAK21007.1; -; Genomic_DNA.
DR EMBL; AB628086; BAK20497.1; -; mRNA.
DR EMBL; AB628087; BAK20498.1; -; mRNA.
DR EMBL; AK291906; BAF84595.1; -; mRNA.
DR EMBL; AC011895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23817.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76472.1; -; Genomic_DNA.
DR EMBL; BC002680; AAH02680.1; -; mRNA.
DR EMBL; BC004249; AAH04249.1; -; mRNA.
DR EMBL; BC004999; AAH04999.1; -; mRNA.
DR EMBL; BC021540; AAH21540.1; -; mRNA.
DR EMBL; BC028985; AAH28985.1; -; mRNA.
DR EMBL; L40374; AAC41740.1; ALT_FRAME; mRNA.
DR CCDS; CCDS5708.1; -. [Q15654-1]
DR RefSeq; NP_003293.2; NM_003302.2. [Q15654-1]
DR PDB; 1X61; NMR; -; A=279-337.
DR PDB; 2DLO; NMR; -; A=329-396.
DR PDBsum; 1X61; -.
DR PDBsum; 2DLO; -.
DR AlphaFoldDB; Q15654; -.
DR SMR; Q15654; -.
DR BioGRID; 113056; 328.
DR CORUM; Q15654; -.
DR DIP; DIP-34466N; -.
DR IntAct; Q15654; 221.
DR MINT; Q15654; -.
DR STRING; 9606.ENSP00000200457; -.
DR GlyGen; Q15654; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15654; -.
DR PhosphoSitePlus; Q15654; -.
DR BioMuta; TRIP6; -.
DR DMDM; 20981729; -.
DR EPD; Q15654; -.
DR jPOST; Q15654; -.
DR MassIVE; Q15654; -.
DR MaxQB; Q15654; -.
DR PaxDb; Q15654; -.
DR PeptideAtlas; Q15654; -.
DR PRIDE; Q15654; -.
DR ProteomicsDB; 24045; -.
DR ProteomicsDB; 24046; -.
DR ProteomicsDB; 60696; -. [Q15654-1]
DR Antibodypedia; 16676; 410 antibodies from 38 providers.
DR DNASU; 7205; -.
DR Ensembl; ENST00000200457.9; ENSP00000200457.4; ENSG00000087077.14. [Q15654-1]
DR Ensembl; ENST00000417475.5; ENSP00000413817.1; ENSG00000087077.14. [Q15654-2]
DR Ensembl; ENST00000437505.5; ENSP00000410736.1; ENSG00000087077.14. [Q15654-3]
DR Ensembl; ENST00000619988.4; ENSP00000479865.1; ENSG00000087077.14. [Q15654-3]
DR GeneID; 7205; -.
DR KEGG; hsa:7205; -.
DR MANE-Select; ENST00000200457.9; ENSP00000200457.4; NM_003302.3; NP_003293.2.
DR UCSC; uc003uww.4; human. [Q15654-1]
DR CTD; 7205; -.
DR DisGeNET; 7205; -.
DR GeneCards; TRIP6; -.
DR HGNC; HGNC:12311; TRIP6.
DR HPA; ENSG00000087077; Low tissue specificity.
DR MIM; 602933; gene.
DR neXtProt; NX_Q15654; -.
DR OpenTargets; ENSG00000087077; -.
DR PharmGKB; PA36989; -.
DR VEuPathDB; HostDB:ENSG00000087077; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000154273; -.
DR HOGENOM; CLU_001357_10_1_1; -.
DR InParanoid; Q15654; -.
DR OMA; SMGYPPH; -.
DR OrthoDB; 483341at2759; -.
DR PhylomeDB; Q15654; -.
DR TreeFam; TF320310; -.
DR PathwayCommons; Q15654; -.
DR SignaLink; Q15654; -.
DR SIGNOR; Q15654; -.
DR BioGRID-ORCS; 7205; 71 hits in 1080 CRISPR screens.
DR ChiTaRS; TRIP6; human.
DR EvolutionaryTrace; Q15654; -.
DR GeneWiki; TRIP6; -.
DR GenomeRNAi; 7205; -.
DR Pharos; Q15654; Tbio.
DR PRO; PR:Q15654; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q15654; protein.
DR Bgee; ENSG00000087077; Expressed in endometrium epithelium and 201 other tissues.
DR ExpressionAtlas; Q15654; baseline and differential.
DR Genevisible; Q15654; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0005149; F:interleukin-1 receptor binding; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; NAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0043009; P:chordate embryonic development; IEA:Ensembl.
DR GO; GO:0048041; P:focal adhesion assembly; NAS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cytoplasm; Cytoskeleton; LIM domain; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..476
FT /note="Thyroid receptor-interacting protein 6"
FT /id="PRO_0000075908"
FT DOMAIN 279..316
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 339..398
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 399..467
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..476
FT /note="Interaction with MAGI1 and PTPN13"
FT /evidence="ECO:0000269|PubMed:19017743"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Y4"
FT MOD_RES 25
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 55
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:15988003,
FT ECO:0000269|PubMed:17591779"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 111
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 179
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 186
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 236
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 238
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 37..106
FT /note="ALQPHPRVNFCPLPSEQCYQAPGGPEDRGPAWVGSHGVLQHTQGLPADRGGL
FT RPGSLDAEIDLLSSTLAE -> VLPGPRGTGGSGAGVGGVPWSTPAHAGAPCRQGGPSP
FT WKPGRRDRLAEQHAGRAEWGSGSCVTATRPTGI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047621"
FT VAR_SEQ 37..80
FT /note="ALQPHPRVNFCPLPSEQCYQAPGGPEDRGPAWVGSHGVLQHTQG -> GAPC
FT RQGGPSPWKPGRRDRLAEQHAGRAEWGSGSCVTATRPTGI (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047622"
FT VAR_SEQ 81..476
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047623"
FT VAR_SEQ 107..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047624"
FT VARIANT 111
FT /note="R -> Q (in dbSNP:rs2437100)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_062262"
FT VARIANT 230
FT /note="V -> I (in dbSNP:rs2075756)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_050171"
FT VARIANT 296
FT /note="L -> F (in dbSNP:rs17855370)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_013309"
FT MUTAGEN 101
FT /note="S->A: Exclusively located in nucleus."
FT /evidence="ECO:0000269|PubMed:16624523"
FT MUTAGEN 102
FT /note="S->A: Exclusively located in nucleus."
FT /evidence="ECO:0000269|PubMed:16624523"
FT MUTAGEN 474
FT /note="T->A: Reduces interaction with MAGI1."
FT /evidence="ECO:0000269|PubMed:19017743"
FT CONFLICT 39..40
FT /note="Missing (in Ref. 9; AAH02680)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="S -> T (in Ref. 2; AAB62222)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="E -> K (in Ref. 2; AAB62222)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="S -> C (in Ref. 1; CAA05080)"
FT /evidence="ECO:0000305"
FT CONFLICT 310..313
FT /note="CRAQ -> MPGP (in Ref. 10; AAC41740)"
FT /evidence="ECO:0000305"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:1X61"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1X61"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1X61"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1X61"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1X61"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:1X61"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1X61"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:1X61"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:2DLO"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:2DLO"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:2DLO"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2DLO"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:2DLO"
FT HELIX 388..394
FT /evidence="ECO:0007829|PDB:2DLO"
SQ 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
