GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Hepatocyte growth factor receptor (HGF receptor) (EC 2 7 10 1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)

 MET_HUMAN               Reviewed;        1390 AA.
P08581; A1L467; B5A932; E7EQ94; O60366; Q12875; Q9UDX7; Q9UPL8;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 4.
17-JUN-2020, entry version 256.
RecName: Full=Hepatocyte growth factor receptor;
Short=HGF receptor;
EC=2.7.10.1;
AltName: Full=HGF/SF receptor;
AltName: Full=Proto-oncogene c-Met;
AltName: Full=Scatter factor receptor;
Short=SF receptor;
AltName: Full=Tyrosine-protein kinase Met;
Flags: Precursor;
Name=MET;
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).
PubMed=2819873; DOI=10.1073/pnas.84.18.6379;
Park M., Dean M., Kaul K., Braun M.J., Gonda M.A., Vande Woude G.;
"Sequence of MET protooncogene cDNA has features characteristic of the
tyrosine kinase family of growth-factor receptors.";
Proc. Natl. Acad. Sci. U.S.A. 84:6379-6383(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Giordano S.;
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
PubMed=18593464; DOI=10.1186/ar2447;
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
"Novel splice variants derived from the receptor tyrosine kinase
superfamily are potential therapeutics for rheumatoid arthritis.";
Arthritis Res. Ther. 10:R73-R73(2008).
[4]
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).
[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]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1010-1390.
PubMed=3325883;
Chan A.M.-L., King H.W.S., Tempest P.R., Deakin E.A., Cooper C.S.,
Brookes P.;
"Primary structure of the met protein tyrosine kinase domain.";
Oncogene 1:229-233(1987).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1206-1264.
PubMed=8247543;
Lee S.-T., Strunk K.M., Spritz R.A.;
"A survey of protein tyrosine kinase mRNAs expressed in normal human
melanocytes.";
Oncogene 8:3403-3410(1993).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1267-1390.
PubMed=4069211; DOI=10.1038/318385a0;
Dean M., Park M., le Beau M.M., Robins T.S., Diaz M.O., Rowley J.D.,
Blair D.G., Vande Woude G.F.;
"The human met oncogene is related to the tyrosine kinase oncogenes.";
Nature 318:385-388(1985).
[11]
TISSUE SPECIFICITY.
PubMed=1917129; DOI=10.1002/ijc.2910490302;
Prat M., Narsimhan R.P., Crepaldi T., Nicotra M.R., Natali P.G.,
Comoglio P.M.;
"The receptor encoded by the human c-MET oncogene is expressed in
hepatocytes, epithelial cells and solid tumors.";
Int. J. Cancer 49:323-328(1991).
[12]
INTERACTION WITH PIK3R1.
PubMed=1718989;
Graziani A., Gramaglia D., Cantley L.C., Comoglio P.M.;
"The tyrosine-phosphorylated hepatocyte growth factor/scatter factor
receptor associates with phosphatidylinositol 3-kinase.";
J. Biol. Chem. 266:22087-22090(1991).
[13]
TISSUE SPECIFICITY.
PubMed=1719465;
Di Renzo M.F., Narsimhan R.P., Olivero M., Bretti S., Giordano S.,
Medico E., Gaglia P., Zara P., Comoglio P.M.;
"Expression of the Met/HGF receptor in normal and neoplastic human
tissues.";
Oncogene 6:1997-2003(1991).
[14]
FUNCTION.
PubMed=1846706; DOI=10.1126/science.1846706;
Bottaro D.P., Rubin J.S., Faletto D.L., Chan A.M.-L., Kmiecik T.E.,
Vande Woude G.F., Aaronson S.A.;
"Identification of the hepatocyte growth factor receptor as the c-met
proto-oncogene product.";
Science 251:802-804(1991).
[15]
PHOSPHORYLATION AT TYR-1235, AND ATP-BINDING SITE LYS-1110.
PubMed=1655790;
Ferracini R., Longati P., Naldini L., Vigna E., Comoglio P.M.;
"Identification of the major autophosphorylation site of the Met/hepatocyte
growth factor receptor tyrosine kinase.";
J. Biol. Chem. 266:19558-19564(1991).
[16]
PHOSPHORYLATION AT TYR-1349 AND TYR-1356, AND INTERACTION WITH SRC; PLCG1
AND GRB2.
PubMed=7513258; DOI=10.1016/0092-8674(94)90318-2;
Ponzetto C., Bardelli A., Zhen Z., Maina F., dalla Zonca P., Giordano S.,
Graziani A., Panayotou G., Comoglio P.M.;
"A multifunctional docking site mediates signaling and transformation by
the hepatocyte growth factor/scatter factor receptor family.";
Cell 77:261-271(1994).
[17]
FUNCTION IN WOUND HEALING.
PubMed=8182137; DOI=10.1172/jci117200;
Nusrat A., Parkos C.A., Bacarra A.E., Godowski P.J., Delp-Archer C.,
Rosen E.M., Madara J.L.;
"Hepatocyte growth factor/scatter factor effects on epithelia. Regulation
of intercellular junctions in transformed and nontransformed cell lines,
basolateral polarization of c-met receptor in transformed and natural
intestinal epithelia, and induction of rapid wound repair in a transformed
model epithelium.";
J. Clin. Invest. 93:2056-2065(1994).
[18]
INTERACTION WITH STAT3.
PubMed=9440692; DOI=10.1038/34657;
Boccaccio C., Ando M., Tamagnone L., Bardelli A., Michieli P.,
Battistini C., Comoglio P.M.;
"Induction of epithelial tubules by growth factor HGF depends on the STAT
pathway.";
Nature 391:285-288(1998).
[19]
INTERACTION WITH GRB10.
PubMed=10454568; DOI=10.1128/mcb.19.9.6217;
Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A.,
Swamy O.R., Leone M.E., Riedel H.;
"Grb10, a positive, stimulatory signaling adapter in platelet-derived
growth factor BB-, insulin-like growth factor I-, and insulin-mediated
mitogenesis.";
Mol. Cell. Biol. 19:6217-6228(1999).
[20]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH L.MONOCYTOGENES INLB
(MICROBIAL INFECTION), AND PHOSPHORYLATION (MICROBIAL INFECTION).
PubMed=11081636; DOI=10.1016/s0092-8674(00)00141-0;
Shen Y., Naujokas M., Park M., Ireton K.;
"InIB-dependent internalization of Listeria is mediated by the Met receptor
tyrosine kinase.";
Cell 103:501-510(2000).
[21]
INTERACTION WITH RANBP9.
PubMed=12147692; DOI=10.1074/jbc.m205111200;
Wang D., Li Z., Messing E.M., Wu G.;
"Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM.";
J. Biol. Chem. 277:36216-36222(2002).
[22]
UBIQUITINATION, MUTAGENESIS OF TYR-1234; TYR-1235; TYR-1313; TYR-1349;
TYR-1356 AND TYR-1365, AND CHARACTERIZATION OF VARIANT SER-1003.
PubMed=12244174; DOI=10.4049/jimmunol.169.7.3793;
Taher T.E., Tjin E.P., Beuling E.A., Borst J., Spaargaren M., Pals S.T.;
"c-Cbl is involved in Met signaling in B cells and mediates hepatocyte
growth factor-induced receptor ubiquitination.";
J. Immunol. 169:3793-3800(2002).
[23]
INTERACTION WITH PLXNB1.
PubMed=12198496; DOI=10.1038/ncb843;
Giordano S., Corso S., Conrotto P., Artigiani S., Gilestro G., Barberis D.,
Tamagnone L., Comoglio P.M.;
"The semaphorin 4D receptor controls invasive growth by coupling with
Met.";
Nat. Cell Biol. 4:720-724(2002).
[24]
PHOSPHORYLATION AT TYR-1230; TYR-1234; TYR-1235; TYR-1349 AND TYR-1365, AND
DEPHOSPHORYLATION AT TYR-1349 AND TYR-1365 BY PTPRJ.
PubMed=12475979; DOI=10.1074/jbc.m210656200;
Palka H.L., Park M., Tonks N.K.;
"Hepatocyte growth factor receptor tyrosine kinase met is a substrate of
the receptor protein-tyrosine phosphatase DEP-1.";
J. Biol. Chem. 278:5728-5735(2003).
[25]
INTERACTION WITH RANBP9 AND RANBP10.
PubMed=14684163; DOI=10.1016/j.bbrc.2003.11.124;
Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.;
"A novel MET-interacting protein shares high sequence similarity with
RanBPM, but fails to stimulate MET-induced Ras/Erk signaling.";
Biochem. Biophys. Res. Commun. 313:320-326(2004).
[26]
FUNCTION, AND INTERACTION WITH MUC20.
PubMed=15314156; DOI=10.1128/mcb.24.17.7456-7468.2004;
Higuchi T., Orita T., Katsuya K., Yamasaki Y., Akiyama K., Li H.,
Yamamoto T., Saito Y., Nakamura M.;
"MUC20 suppresses the hepatocyte growth factor-induced Grb2-Ras pathway by
binding to a multifunctional docking site of met.";
Mol. Cell. Biol. 24:7456-7468(2004).
[27]
PHOSPHORYLATION AT TYR-1356, AND INTERACTION WITH INPPL1.
PubMed=15735664; DOI=10.1038/sj.onc.1208558;
Koch A., Mancini A., El Bounkari O., Tamura T.;
"The SH2-domain-containing inositol 5-phosphatase (SHIP)-2 binds to c-Met
directly via tyrosine residue 1356 and involves hepatocyte growth factor
(HGF)-induced lamellipodium formation, cell scattering and cell
spreading.";
Oncogene 24:3436-3447(2005).
[28]
REVIEW ON FUNCTION IN ANGIOGENESIS.
PubMed=16862193; DOI=10.1038/nrc1912;
Boccaccio C., Comoglio P.M.;
"Invasive growth: a MET-driven genetic programme for cancer and stem
cells.";
Nat. Rev. Cancer 6:637-645(2006).
[29]
PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN1 AND PTPN2, INTERACTION WITH
PTPN1 AND PTPN2, AND MUTAGENESIS OF TYR-1234 AND TYR-1235.
PubMed=18819921; DOI=10.1074/jbc.m805916200;
Sangwan V., Paliouras G.N., Abella J.V., Dube N., Monast A., Tremblay M.L.,
Park M.;
"Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine
phosphatase 1B and T-cell phosphatase.";
J. Biol. Chem. 283:34374-34383(2008).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-977 AND TYR-1003, 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).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-990; SER-997 AND SER-1000,
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).
[32]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106.
TISSUE=Hepatoma;
PubMed=19196183; DOI=10.1021/pr800826u;
Cao J., Shen C., Wang H., Shen H., Chen Y., Nie A., Yan G., Lu H., Liu Y.,
Yang P.;
"Identification of N-glycosylation sites on secreted proteins of human
hepatocellular carcinoma cells with a complementary proteomics approach.";
J. Proteome Res. 8:662-672(2009).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1003 AND THR-1289, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[34]
REVIEW ON FUNCTION.
PubMed=20655987; DOI=10.1016/j.bbcan.2010.07.006;
Mahtouk K., Tjin E.P., Spaargaren M., Pals S.T.;
"The HGF/MET pathway as target for the treatment of multiple myeloma and B-
cell lymphomas.";
Biochim. Biophys. Acta 1806:208-219(2010).
[35]
FUNCTION (MICROBIAL INFECTION), AND SUBUNIT (MICROBIAL INFECTION).
PubMed=19900460; DOI=10.1016/j.jmb.2009.10.074;
Ferraris D.M., Gherardi E., Di Y., Heinz D.W., Niemann H.H.;
"Ligand-mediated dimerization of the Met receptor tyrosine kinase by the
bacterial invasion protein InlB.";
J. Mol. Biol. 395:522-532(2010).
[36]
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).
[37]
INTERACTION WITH GAB1.
PubMed=21784853; DOI=10.1074/jbc.m111.239384;
Chaudhuri A., Xie M.H., Yang B., Mahapatra K., Liu J., Marsters S.,
Bodepudi S., Ashkenazi A.;
"Distinct involvement of the Gab1 and Grb2 adaptor proteins in signal
transduction by the related receptor tyrosine kinases RON and MET.";
J. Biol. Chem. 286:32762-32774(2011).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-990, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-966, AND 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).
[40]
INVOLVEMENT IN OSFD, VARIANT OSFD 964-LEU--ASP-1010 DEL, TISSUE
SPECIFICITY, AND UBIQUITINATION.
PubMed=26637977; DOI=10.1016/j.ajhg.2015.11.001;
Gray M.J., Kannu P., Sharma S., Neyt C., Zhang D., Paria N., Daniel P.B.,
Whetstone H., Sprenger H.G., Hammerschmidt P., Weng A., Dupuis L.,
Jobling R., Mendoza-Londono R., Dray M., Su P., Wilson M.J., Kapur R.P.,
McCarthy E.F., Alman B.A., Howard A., Somers G.R., Marshall C.R.,
Manners S., Flanagan A.M., Rathjen K.E., Karol L.A., Crawford H.,
Markie D.M., Rios J.J., Wise C.A., Robertson S.P.;
"Mutations preventing regulated exon skipping in MET cause osteofibrous
dysplasia.";
Am. J. Hum. Genet. 97:837-847(2015).
[41]
INVOLVEMENT IN DFNB97, AND VARIANT DFNB97 VAL-841.
PubMed=25941349; DOI=10.1136/jmedgenet-2015-103023;
Mujtaba G., Schultz J.M., Imtiaz A., Morell R.J., Friedman T.B., Naz S.;
"A mutation of MET, encoding hepatocyte growth factor receptor, is
associated with human DFNB97 hearing loss.";
J. Med. Genet. 52:548-552(2015).
[42]
INTERACTION WITH HSP90AA1 AND HSP90AB1.
PubMed=26517842; DOI=10.1371/journal.pone.0141786;
Prince T.L., Kijima T., Tatokoro M., Lee S., Tsutsumi S., Yim K., Rivas C.,
Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T., Beebe K.,
Trepel J.B., Neckers L.;
"Client proteins and small molecule inhibitors display distinct binding
preferences for constitutive and stress-induced HSP90 isoforms and their
conformationally restricted mutants.";
PLoS ONE 10:E0141786-E0141786(2015).
[43]
INTERACTION WITH LECT2.
PubMed=27334921; DOI=10.1074/jbc.m116.720375;
Zheng H., Miyakawa T., Sawano Y., Asano A., Okumura A., Yamagoe S.,
Tanokura M.;
"Crystal structure of human leukocyte cell-derived chemotaxin 2 (LECT2)
reveals a mechanistic basis of functional evolution in a mammalian protein
with an M23 metalloendopeptidase fold.";
J. Biol. Chem. 291:17133-17142(2016).
[44]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1356-1359 IN COMPLEX WITH GRB2.
PubMed=11063574; DOI=10.1021/bi0012336;
Schiering N., Casale E., Caccia P., Giordano P., Battistini C.;
"Dimer formation through domain swapping in the crystal structure of the
Grb2-SH2-Ac-pYVNV complex.";
Biochemistry 39:13376-13382(2000).
[45]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1049-1360 IN COMPLEX WITH
INHIBITOR.
PubMed=14559966; DOI=10.1073/pnas.1734128100;
Schiering N., Knapp S., Marconi M., Flocco M.M., Cui J., Perego R.,
Rusconi L., Cristiani C.;
"Crystal structure of the tyrosine kinase domain of the hepatocyte growth
factor receptor c-Met and its complex with the microbial alkaloid K-252a.";
Proc. Natl. Acad. Sci. U.S.A. 100:12654-12659(2003).
[46]
STRUCTURE BY NMR OF 519-562, AND DISULFIDE BONDS.
PubMed=15358240; DOI=10.1016/j.bbrc.2004.06.132;
Kozlov G., Perreault A., Schrag J.D., Park M., Cygler M., Gehring K.,
Ekiel I.;
"Insights into function of PSI domains from structure of the Met receptor
PSI domain.";
Biochem. Biophys. Res. Commun. 321:234-240(2004).
[47]
X-RAY CRYSTALLOGRAPHY (3.22 ANGSTROMS) OF 25-567 IN COMPLEX WITH HGF, AND
DISULFIDE BONDS.
PubMed=15167892; DOI=10.1038/sj.emboj.7600243;
Stamos J., Lazarus R.A., Yao X., Kirchhofer D., Wiesmann C.;
"Crystal structure of the HGF beta-chain in complex with the Sema domain of
the Met receptor.";
EMBO J. 23:2325-2335(2004).
[48]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-740 IN COMPLEX WITH
L.MONOCYTOGENES INLB, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH
L.MONOCYTOGENES INLB (MICROBIAL INFECTION), AND DISULFIDE BONDS.
PubMed=17662939; DOI=10.1016/j.cell.2007.05.037;
Niemann H.H., Jager V., Butler P.J., van den Heuvel J., Schmidt S.,
Ferraris D., Gherardi E., Heinz D.W.;
"Structure of the human receptor tyrosine kinase Met in complex with the
Listeria invasion protein InlB.";
Cell 130:235-246(2007).
[49]
VARIANTS RCCP THR-1131; LEU-1188; VAL-1195; ILE-1220; HIS-1228; ASN-1228;
CYS-1230; HIS-1230 AND THR-1250, AND VARIANT VAL-320.
PubMed=9140397; DOI=10.1038/ng0597-68;
Schmidt L., Duh F.-M., Chen F., Kishida T., Glenn G., Choyke P.,
Scherer S.W., Zhuang Z., Lubensky I., Dean M., Allikmets R.,
Chidambaram A., Bergerheim U.R., Feltis J.T., Casadevall C., Zamarron A.,
Bernues M., Richard S., Lips C.J.M., Walther M.M., Tsui L.-C., Geil L.,
Orcutt M.L., Stackhouse T., Lipan J., Slife L., Brauch H., Decker J.,
Niehans G., Hughson M.D., Moch H., Storkel S., Lerman M.I., Linehan W.M.,
Zbar B.;
"Germline and somatic mutations in the tyrosine kinase domain of the MET
proto-oncogene in papillary renal carcinomas.";
Nat. Genet. 16:68-73(1997).
[50]
VARIANT RCCP ARG-1094, AND CHARACTERIZATION OF VARIANT RCCP ARG-1094.
PubMed=9563489;
Schmidt L., Junker K., Weirich G., Glenn G., Choyke P., Lubensky I.,
Zhuang Z., Jeffers M., Vande Woude G., Neumann H., Walther M.,
Linehan W.M., Zbar B.;
"Two North American families with hereditary papillary renal carcinoma and
identical novel mutations in the MET proto-oncogene.";
Cancer Res. 58:1719-1722(1998).
[51]
VARIANTS RCCP ILE-1092; ARG-1094; ASP-1106; THR-1131; LEU-1188; ASP-1230;
CYS-1230 AND THR-1250.
PubMed=10433944; DOI=10.1016/s0002-9440(10)65147-4;
Lubensky I.A., Schmidt L., Zhuang Z., Weirich G., Pack S., Zambrano N.,
Walther M.M., Choyke P., Linehan W.M., Zbar B.;
"Hereditary and sporadic papillary renal carcinomas with c-met mutations
share a distinct morphological phenotype.";
Am. J. Pathol. 155:517-526(1999).
[52]
VARIANTS HCC ILE-1173; ARG-1244 AND ILE-1250.
PubMed=9927037;
Park W.S., Dong S.M., Kim S.Y., Na E.Y., Shin M.S., Pi J.H., Kim B.J.,
Bae J.H., Hong Y.K., Lee K.S., Lee S.H., Yoo N.J., Jang J.J., Pack S.,
Zhuang Z., Schmidt L., Zbar B., Lee J.Y.;
"Somatic mutations in the kinase domain of the Met/hepatocyte growth factor
receptor gene in childhood hepatocellular carcinomas.";
Cancer Res. 59:307-310(1999).
[53]
VARIANT RCCP ILE-1092, AND CHARACTERIZATION OF VARIANT RCCP ILE-1092.
PubMed=10417759;
DOI=10.1002/(sici)1097-0215(19990827)82:5<640::aid-ijc4>3.0.co;2-6;
Olivero M., Valente G., Bardelli A., Longati P., Ferrero N., Cracco C.,
Terrone C., Rocca-Rossetti S., Comoglio P.M., Di Renzo M.F.;
"Novel mutation in the ATP-binding site of the MET oncogene tyrosine kinase
in a HPRCC family.";
Int. J. Cancer 82:640-643(1999).
[54]
VARIANTS RCCP ILE-1092; LEU-1094; TYR-1094; ASP-1106 AND ASP-1230, AND
CHARACTERIZATION OF VARIANTS RCCP ILE-1092; LEU-1094; TYR-1094; ASP-1106
AND ASP-1230.
PubMed=10327054; DOI=10.1038/sj.onc.1202547;
Schmidt L., Junker K., Nakaigawa N., Kinjerski T., Weirich G., Miller M.,
Lubensky I., Neumann H.P.H., Brauch H., Decker J., Vocke C., Brown J.A.,
Jenkins R., Richard S., Bergerheim U., Gerrard B., Dean M., Linehan W.M.,
Zbar B.;
"Novel mutations of the MET proto-oncogene in papillary renal carcinomas.";
Oncogene 18:2343-2350(1999).
[55]
VARIANT GASTRIC CANCER SER-991, VARIANT ILE-992, CHARACTERIZATION OF
VARIANT GASTRIC CANCER SER-991, AND CHARACTERIZATION OF VARIANT ILE-992.
PubMed=11042681; DOI=10.1038/sj.onc.1203874;
Lee J.-H., Han S.-U., Cho H., Jennings B., Gerrard B., Dean M., Schmidt L.,
Zbar B., Vande Woude G.F.V.;
"A novel germ line juxtamembrane Met mutation in human gastric cancer.";
Oncogene 19:4947-4953(2000).
[56]
VARIANT GASTRIC CANCER LEU-773.
PubMed=12920089; DOI=10.1136/jmg.40.8.e97;
Kim I.-J., Park J.-H., Kang H.C., Shin Y., Lim S.-B., Ku J.-L., Yang H.-K.,
Lee K.U., Park J.-G.;
"A novel germline mutation in the MET extracellular domain in a Korean
patient with the diffuse type of familial gastric cancer.";
J. Med. Genet. 40:E97-E97(2003).
[57]
INTERACTION WITH SPSB1; SPSB2; SPSB3 AND SPSB4.
PubMed=15713673; DOI=10.1074/jbc.m413897200;
Wang D., Li Z., Messing E.M., Wu G.;
"The SPRY domain-containing SOCS box protein 1 (SSB-1) interacts with MET
and enhances the hepatocyte growth factor-induced Erk-Elk-1-serum response
element pathway.";
J. Biol. Chem. 280:16393-16401(2005).
[58]
POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO AUTS9, AND VARIANTS CYS-970 AND
ILE-992.
PubMed=17053076; DOI=10.1073/pnas.0605296103;
Campbell D.B., Sutcliffe J.S., Ebert P.J., Militerni R., Bravaccio C.,
Trillo S., Elia M., Schneider C., Melmed R., Sacco R., Persico A.M.,
Levitt P.;
"A genetic variant that disrupts MET transcription is associated with
autism.";
Proc. Natl. Acad. Sci. U.S.A. 103:16834-16839(2006).
[59]
VARIANTS [LARGE SCALE ANALYSIS] GLN-143; LEU-156; ASP-168; SER-375; CYS-970
AND ILE-992.
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).
[60]
VARIANTS TYR-150; ASP-168; TYR-385; ILE-992 AND ILE-1294, CHARACTERIZATION
OF VARIANTS TYR-150; ASP-168; TYR-385; ILE-992 AND ILE-1294, AND POSSIBLE
INVOLVEMENT IN CUP.
PubMed=20949619; DOI=10.1002/humu.21374;
Stella G.M., Benvenuti S., Gramaglia D., Scarpa A., Tomezzoli A.,
Cassoni P., Senetta R., Venesio T., Pozzi E., Bardelli A., Comoglio P.M.;
"MET mutations in cancers of unknown primary origin (CUPs).";
Hum. Mutat. 32:44-50(2011).
[61]
VARIANT LYS-375, AND CHARACTERIZATION OF VARIANT LYS-375.
PubMed=28294470; DOI=10.1111/cas.13233;
Tode N., Kikuchi T., Sakakibara T., Hirano T., Inoue A., Ohkouchi S.,
Tamada T., Okazaki T., Koarai A., Sugiura H., Niihori T., Aoki Y.,
Nakayama K., Matsumoto K., Matsubara Y., Yamamoto M., Watanabe A.,
Nukiwa T., Ichinose M.;
"Exome sequencing deciphers a germline MET mutation in familial epidermal
growth factor receptor-mutant lung cancer.";
Cancer Sci. 108:1263-1270(2017).
-!- FUNCTION: Receptor tyrosine kinase that transduces signals from the
extracellular matrix into the cytoplasm by binding to hepatocyte growth
factor/HGF ligand. Regulates many physiological processes including
proliferation, scattering, morphogenesis and survival. Ligand binding
at the cell surface induces autophosphorylation of MET on its
intracellular domain that provides docking sites for downstream
signaling molecules. Following activation by ligand, interacts with the
PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1.
Recruitment of these downstream effectors by MET leads to the
activation of several signaling cascades including the RAS-ERK, PI3
kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with
the morphogenetic effects while PI3K/AKT coordinates prosurvival
effects. During embryonic development, MET signaling plays a role in
gastrulation, development and migration of muscles and neuronal
precursors, angiogenesis and kidney formation. In adults, participates
in wound healing as well as organ regeneration and tissue remodeling.
Promotes also differentiation and proliferation of hematopoietic cells.
May regulate cortical bone osteogenesis (By similarity).
{ECO:0000250|UniProtKB:P16056}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Listeria
monocytogenes internalin InlB, mediating entry of the pathogen into
cells. {ECO:0000269|PubMed:11081636, ECO:0000305|PubMed:17662939,
ECO:0000305|PubMed:19900460}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
-!- ACTIVITY REGULATION: In its inactive state, the C-terminal tail
interacts with the catalytic domain and inhibits the kinase activity.
Upon ligand binding, the C-terminal tail is displaced and becomes
phosphorylated, thus increasing the kinase activity.
-!- SUBUNIT: Heterodimer made of an alpha chain (50 kDa) and a beta chain
(145 kDa) which are disulfide linked. Binds PLXNB1. Interacts when
phosphorylated with downstream effectors including STAT3, PIK3R1, SRC,
PCLG1, GRB2 and GAB1. Interacts with SPSB1, SPSB2 and SPSB4 (By
similarity). Interacts with INPP5D/SHIP1. When phosphorylated at Tyr-
1356, interacts with INPPL1/SHIP2. Interacts with RANBP9 and RANBP10,
as well as SPSB1, SPSB2, SPSB3 and SPSB4. SPSB1 binding occurs in the
presence and in the absence of HGF, however HGF treatment has a
positive effect on this interaction. Interacts with MUC20; prevents
interaction with GRB2 and suppresses hepatocyte growth factor-induced
cell proliferation. Interacts with GRB10. Interacts with PTPN1 and
PTPN2. Interacts with LECT2; this interaction may have an antagonistic
effect on receptor activation (PubMed:27334921). Interacts with
HSP90AA1 and HSP90AB1; the interaction suppresses MET kinase activity
(PubMed:26517842). {ECO:0000250|UniProtKB:P16056,
ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:11063574,
ECO:0000269|PubMed:12147692, ECO:0000269|PubMed:12198496,
ECO:0000269|PubMed:14559966, ECO:0000269|PubMed:14684163,
ECO:0000269|PubMed:15167892, ECO:0000269|PubMed:15314156,
ECO:0000269|PubMed:15713673, ECO:0000269|PubMed:15735664,
ECO:0000269|PubMed:1718989, ECO:0000269|PubMed:17662939,
ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:21784853,
ECO:0000269|PubMed:26517842, ECO:0000269|PubMed:27334921,
ECO:0000269|PubMed:7513258, ECO:0000269|PubMed:9440692}.
-!- SUBUNIT: (Microbial infection) Interacts via extracytoplasmic residues
25-656 with L.monocytogenes InlB; MET can bind HGF, its endogenous
ligand, and InlB simultaneously (PubMed:11081636, PubMed:17662939).
InlB probably dimerizes upon binding to MET, which encourages
subsequent dimerization of MET (Probable).
{ECO:0000269|PubMed:11081636, ECO:0000269|PubMed:17662939,
ECO:0000305|PubMed:19900460}.
-!- INTERACTION:
P08581; P22681: CBL; NbExp=15; IntAct=EBI-1039152, EBI-518228;
P08581; Q96EY1-2: DNAJA3; NbExp=2; IntAct=EBI-1039152, EBI-3952284;
P08581; P00533: EGFR; NbExp=8; IntAct=EBI-1039152, EBI-297353;
P08581; P09769: FGR; NbExp=2; IntAct=EBI-1039152, EBI-1383732;
P08581; P14210: HGF; NbExp=7; IntAct=EBI-1039152, EBI-1039104;
P08581; P14210-6: HGF; NbExp=3; IntAct=EBI-1039152, EBI-6280319;
P08581; O15357: INPPL1; NbExp=2; IntAct=EBI-1039152, EBI-1384248;
P08581; P35968: KDR; NbExp=3; IntAct=EBI-1039152, EBI-1005487;
P08581; P06239: LCK; NbExp=3; IntAct=EBI-1039152, EBI-1348;
P08581; P07948: LYN; NbExp=2; IntAct=EBI-1039152, EBI-79452;
P08581; P08581: MET; NbExp=2; IntAct=EBI-1039152, EBI-1039152;
P08581; P15941: MUC1; NbExp=2; IntAct=EBI-1039152, EBI-2804728;
P08581; P16333: NCK1; NbExp=2; IntAct=EBI-1039152, EBI-389883;
P08581; O43639: NCK2; NbExp=2; IntAct=EBI-1039152, EBI-713635;
P08581; P27986: PIK3R1; NbExp=6; IntAct=EBI-1039152, EBI-79464;
P08581; O00459: PIK3R2; NbExp=11; IntAct=EBI-1039152, EBI-346930;
P08581; Q92569: PIK3R3; NbExp=11; IntAct=EBI-1039152, EBI-79893;
P08581; P19174: PLCG1; NbExp=10; IntAct=EBI-1039152, EBI-79387;
P08581; O43157: PLXNB1; NbExp=7; IntAct=EBI-1039152, EBI-1111488;
P08581; O15031: PLXNB2; NbExp=2; IntAct=EBI-1039152, EBI-722004;
P08581; Q9ULL4: PLXNB3; NbExp=2; IntAct=EBI-1039152, EBI-311073;
P08581; P18031: PTPN1; NbExp=3; IntAct=EBI-1039152, EBI-968788;
P08581; Q06124: PTPN11; NbExp=13; IntAct=EBI-1039152, EBI-297779;
P08581; P23467: PTPRB; NbExp=2; IntAct=EBI-1039152, EBI-1265766;
P08581; Q12913: PTPRJ; NbExp=5; IntAct=EBI-1039152, EBI-2264500;
P08581; Q16827: PTPRO; NbExp=2; IntAct=EBI-1039152, EBI-723739;
P08581; P20936: RASA1; NbExp=15; IntAct=EBI-1039152, EBI-1026476;
P08581; Q9UQQ2: SH2B3; NbExp=2; IntAct=EBI-1039152, EBI-7879749;
P08581; O60880: SH2D1A; NbExp=3; IntAct=EBI-1039152, EBI-6983382;
P08581; O14796: SH2D1B; NbExp=6; IntAct=EBI-1039152, EBI-3923013;
P08581; Q9NP31: SH2D2A; NbExp=7; IntAct=EBI-1039152, EBI-490630;
P08581; Q8N5H7: SH2D3C; NbExp=4; IntAct=EBI-1039152, EBI-745980;
P08581; Q15464: SHB; NbExp=4; IntAct=EBI-1039152, EBI-4402156;
P08581; P29353: SHC1; NbExp=5; IntAct=EBI-1039152, EBI-78835;
P08581; P98077: SHC2; NbExp=2; IntAct=EBI-1039152, EBI-7256023;
P08581; Q6S5L8: SHC4; NbExp=3; IntAct=EBI-1039152, EBI-9453524;
P08581; Q96IW2: SHD; NbExp=2; IntAct=EBI-1039152, EBI-4402781;
P08581; Q9H6Q3: SLA2; NbExp=4; IntAct=EBI-1039152, EBI-1222854;
P08581; O75159: SOCS5; NbExp=2; IntAct=EBI-1039152, EBI-970130;
P08581; O14544: SOCS6; NbExp=4; IntAct=EBI-1039152, EBI-3929549;
P08581; P12931: SRC; NbExp=4; IntAct=EBI-1039152, EBI-621482;
P08581; Q9ULZ2: STAP1; NbExp=3; IntAct=EBI-1039152, EBI-6083058;
P08581; P43405: SYK; NbExp=3; IntAct=EBI-1039152, EBI-78302;
P08581; P42680: TEC; NbExp=2; IntAct=EBI-1039152, EBI-1383480;
P08581; Q9HBL0: TNS1; NbExp=2; IntAct=EBI-1039152, EBI-3389814;
P08581; Q63HR2: TNS2; NbExp=2; IntAct=EBI-1039152, EBI-949753;
P08581; Q68CZ2: TNS3; NbExp=3; IntAct=EBI-1039152, EBI-1220488;
P08581; Q9UKW4: VAV3; NbExp=2; IntAct=EBI-1039152, EBI-297568;
P08581; P07947: YES1; NbExp=3; IntAct=EBI-1039152, EBI-515331;
P08581; P43403: ZAP70; NbExp=2; IntAct=EBI-1039152, EBI-1211276;
P08581; Q08048: Hgf; Xeno; NbExp=3; IntAct=EBI-1039152, EBI-15655650;
P08581; P0DQD2: inlB; Xeno; NbExp=4; IntAct=EBI-1039152, EBI-1379295;
P08581; P35918: Kdr; Xeno; NbExp=3; IntAct=EBI-1039152, EBI-1555005;
P08581; Q00944: PTK2; Xeno; NbExp=5; IntAct=EBI-1039152, EBI-2896409;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
-!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional soluble isoforms seem to exist.;
Name=1;
IsoId=P08581-1; Sequence=Displayed;
Name=2;
IsoId=P08581-2; Sequence=VSP_005005;
Name=3; Synonyms=Soluble MET variant 4;
IsoId=P08581-3; Sequence=VSP_042447, VSP_042448;
-!- TISSUE SPECIFICITY: Expressed in normal hepatocytes as well as in
epithelial cells lining the stomach, the small and the large intestine.
Found also in basal keratinocytes of esophagus and skin. High levels
are found in liver, gastrointestinal tract, thyroid and kidney. Also
present in the brain. Expressed in metaphyseal bone (at protein level)
(PubMed:26637977). {ECO:0000269|PubMed:1719465,
ECO:0000269|PubMed:1917129, ECO:0000269|PubMed:26637977}.
-!- DOMAIN: The kinase domain is involved in SPSB1 binding.
-!- DOMAIN: The beta-propeller Sema domain mediates binding to HGF.
-!- PTM: Autophosphorylated in response to ligand binding on Tyr-1234 and
Tyr-1235 in the kinase domain leading to further phosphorylation of
Tyr-1349 and Tyr-1356 in the C-terminal multifunctional docking site.
Dephosphorylated by PTPRJ at Tyr-1349 and Tyr-1365. Dephosphorylated by
PTPN1 and PTPN2. {ECO:0000269|PubMed:12475979,
ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:1655790,
ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:7513258}.
-!- PTM: Ubiquitinated. Ubiquitination by CBL regulates MET endocytosis,
resulting in decreasing plasma membrane receptor abundance, and in
endosomal degradation and/or recycling of internalized receptors.
{ECO:0000269|PubMed:12244174, ECO:0000305|PubMed:26637977}.
-!- PTM: (Microbial infection) Tyrosine phosphorylation is stimulated by
L.monocytogenes InlB. Tyrosine phosphorylation is maximal 10-20 minutes
after treatment with InlB and disappears by 60 minutes. The
phosphorylated residues were not identified.
{ECO:0000269|PubMed:11081636}.
-!- DISEASE: Note=Activation of MET after rearrangement with the TPR gene
produces an oncogenic protein.
-!- DISEASE: Note=Defects in MET may be associated with gastric cancer.
-!- DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary
malignant neoplasm of epithelial liver cells. The major risk factors
for HCC are chronic hepatitis B virus (HBV) infection, chronic
hepatitis C virus (HCV) infection, prolonged dietary aflatoxin
exposure, alcoholic cirrhosis, and cirrhosis due to other causes.
{ECO:0000269|PubMed:9927037}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Renal cell carcinoma papillary (RCCP) [MIM:605074]: A subtype
of renal cell carcinoma tending to show a tubulo-papillary architecture
formed by numerous, irregular, finger-like projections of connective
tissue. Renal cell carcinoma is a heterogeneous group of sporadic or
hereditary carcinoma derived from cells of the proximal renal tubular
epithelium. {ECO:0000269|PubMed:10327054, ECO:0000269|PubMed:10417759,
ECO:0000269|PubMed:10433944, ECO:0000269|PubMed:9140397,
ECO:0000269|PubMed:9563489}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Note=A common allele in the promoter region of the MET shows
genetic association with susceptibility to autism in some families.
Functional assays indicate a decrease in MET promoter activity and
altered binding of specific transcription factor complexes.
-!- DISEASE: Note=MET activating mutations may be involved in the
development of a highly malignant, metastatic syndrome known as cancer
of unknown primary origin (CUP) or primary occult malignancy. Systemic
neoplastic spread is generally a late event in cancer progression.
However, in some instances, distant dissemination arises at a very
early stage, so that metastases reach clinical relevance before primary
lesions. Sometimes, the primary lesions cannot be identified in spite
of the progresses in the diagnosis of malignancies.
-!- DISEASE: Deafness, autosomal recessive, 97 (DFNB97) [MIM:616705]: A
form of non-syndromic sensorineural hearing loss with prelingual onset.
Sensorineural deafness results from damage to the neural receptors of
the inner ear, the nerve pathways to the brain, or the area of the
brain that receives sound information. {ECO:0000269|PubMed:25941349}.
Note=The disease is caused by mutations affecting the gene represented
in this entry.
-!- DISEASE: Osteofibrous dysplasia (OSFD) [MIM:607278]: A congenital
disorder of osteogenesis characterized by non-neoplastic, radiolucent
lesions that affect the cortical bone immediately under the periosteum.
It usually manifests as a painless swelling or anterior bowing of the
long bones, most commonly the tibia and fibula.
{ECO:0000269|PubMed:26637977}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. Disease-associated variants identified in 4 families cause the
deletion of exon 14. This results in the exclusion of an ubiquitination
target site within the cytoplasmic domain, hence in protein
stabilization. The persistent presence of MET at the cell surface in
conditions of ligand-dependent activation retards osteoblastic
differentiation. {ECO:0000269|PubMed:26637977}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/METID131.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=C-MET entry;
URL="https://en.wikipedia.org/wiki/C-MET";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; J02958; AAA59591.1; -; mRNA.
EMBL; X54559; CAB56793.1; -; mRNA.
EMBL; EU826570; ACF47606.1; -; mRNA.
EMBL; AC002080; AAB54047.1; -; Genomic_DNA.
EMBL; AC002543; AAC60383.1; -; Genomic_DNA.
EMBL; AC004416; AAF66137.2; -; Genomic_DNA.
EMBL; CH236947; EAL24359.1; -; Genomic_DNA.
EMBL; CH471070; EAW83509.1; -; Genomic_DNA.
EMBL; BC130420; AAI30421.1; -; mRNA.
EMBL; U08818; AAB60323.1; ALT_SEQ; mRNA.
EMBL; M35074; AAA59590.1; -; mRNA.
CCDS; CCDS43636.1; -. [P08581-1]
CCDS; CCDS47689.1; -. [P08581-2]
PIR; A40175; TVHUME.
RefSeq; NP_000236.2; NM_000245.3. [P08581-1]
RefSeq; NP_001120972.1; NM_001127500.2. [P08581-2]
PDB; 1FYR; X-ray; 2.40 A; I/J/K/L=1356-1359.
PDB; 1R0P; X-ray; 1.80 A; A=1049-1360.
PDB; 1R1W; X-ray; 1.80 A; A=1049-1360.
PDB; 1SHY; X-ray; 3.22 A; B=25-567.
PDB; 1SSL; NMR; -; A=519-562.
PDB; 1UX3; Model; -; A=25-656.
PDB; 2G15; X-ray; 2.15 A; A=1038-1346.
PDB; 2RFN; X-ray; 2.50 A; A/B=1048-1351.
PDB; 2RFS; X-ray; 2.20 A; A=1048-1351.
PDB; 2UZX; X-ray; 2.80 A; B/D=25-740.
PDB; 2UZY; X-ray; 4.00 A; B/D=25-740.
PDB; 2WD1; X-ray; 2.00 A; A=1055-1346.
PDB; 2WGJ; X-ray; 2.00 A; A=1051-1348.
PDB; 2WKM; X-ray; 2.20 A; A=1051-1348.
PDB; 3A4P; X-ray; 2.54 A; A=1049-1360.
PDB; 3BUX; X-ray; 1.35 A; A/C=997-1009.
PDB; 3C1X; X-ray; 2.17 A; A=1049-1360.
PDB; 3CCN; X-ray; 1.90 A; A=1048-1350.
PDB; 3CD8; X-ray; 2.00 A; A=1048-1350.
PDB; 3CE3; X-ray; 2.40 A; A=1049-1360.
PDB; 3CTH; X-ray; 2.30 A; A=1049-1360.
PDB; 3CTJ; X-ray; 2.50 A; A=1049-1360.
PDB; 3DKC; X-ray; 1.52 A; A=1049-1360.
PDB; 3DKF; X-ray; 1.80 A; A=1049-1360.
PDB; 3DKG; X-ray; 1.91 A; A=1049-1360.
PDB; 3EFJ; X-ray; 2.60 A; A/B=1048-1351.
PDB; 3EFK; X-ray; 2.20 A; A/B=1048-1351.
PDB; 3F66; X-ray; 1.40 A; A/B=1052-1349.
PDB; 3F82; X-ray; 2.50 A; A=1049-1360.
PDB; 3I5N; X-ray; 2.00 A; A=1048-1350.
PDB; 3L8V; X-ray; 2.40 A; A=1049-1360.
PDB; 3LQ8; X-ray; 2.02 A; A=1051-1348.
PDB; 3Q6U; X-ray; 1.60 A; A=1048-1348.
PDB; 3Q6W; X-ray; 1.75 A; A=1048-1348.
PDB; 3QTI; X-ray; 2.00 A; A/B=1050-1360.
PDB; 3R7O; X-ray; 2.30 A; A=1048-1348.
PDB; 3RHK; X-ray; 1.94 A; A/B=1038-1346.
PDB; 3U6H; X-ray; 2.00 A; A=1048-1351.
PDB; 3U6I; X-ray; 2.10 A; A=1048-1351.
PDB; 3VW8; X-ray; 2.10 A; A=1024-1352.
PDB; 3ZBX; X-ray; 2.20 A; A=1051-1348.
PDB; 3ZC5; X-ray; 2.20 A; A=1051-1348.
PDB; 3ZCL; X-ray; 1.40 A; A=1051-1348.
PDB; 3ZXZ; X-ray; 1.80 A; A=1051-1348.
PDB; 3ZZE; X-ray; 1.87 A; A=1051-1348.
PDB; 4AOI; X-ray; 1.90 A; A=1051-1348.
PDB; 4AP7; X-ray; 1.80 A; A=1051-1348.
PDB; 4DEG; X-ray; 2.00 A; A=1048-1351.
PDB; 4DEH; X-ray; 2.00 A; A=1048-1351.
PDB; 4DEI; X-ray; 2.05 A; A=1048-1351.
PDB; 4EEV; X-ray; 1.80 A; A=1038-1346.
PDB; 4GG5; X-ray; 2.42 A; A=1038-1346.
PDB; 4GG7; X-ray; 2.27 A; A=1038-1346.
PDB; 4IWD; X-ray; 1.99 A; A=1048-1348.
PDB; 4K3J; X-ray; 2.80 A; B=39-564.
PDB; 4KNB; X-ray; 2.40 A; A/B/C/D=1060-1346.
PDB; 4MXC; X-ray; 1.63 A; A=1038-1346.
PDB; 4O3T; X-ray; 2.99 A; B=25-567.
PDB; 4O3U; X-ray; 3.04 A; B=25-567.
PDB; 4R1V; X-ray; 1.20 A; A=1055-1345.
PDB; 4R1Y; X-ray; 2.00 A; A=1055-1346.
PDB; 4XMO; X-ray; 1.75 A; A=1048-1350.
PDB; 4XYF; X-ray; 1.85 A; A=1048-1351.
PDB; 5DG5; X-ray; 2.60 A; A/B=1038-1346.
PDB; 5EOB; X-ray; 1.75 A; A=1038-1346.
PDB; 5EYC; X-ray; 1.80 A; A=1048-1351.
PDB; 5EYD; X-ray; 1.85 A; A=1048-1351.
PDB; 5HLW; X-ray; 1.97 A; A=1057-1355.
PDB; 5HNI; X-ray; 1.71 A; X/Y=1049-1360.
PDB; 5HO6; X-ray; 1.97 A; A=1049-1360.
PDB; 5HOA; X-ray; 2.14 A; A=1049-1360.
PDB; 5HOR; X-ray; 2.20 A; A=1049-1360.
PDB; 5HTI; X-ray; 1.66 A; A=1038-1346.
PDB; 5LSP; X-ray; 2.60 A; A/P=519-743, X/Y=25-35.
PDB; 5T3Q; X-ray; 2.00 A; A=1048-1350.
PDB; 5UAB; X-ray; 1.90 A; A=1023-1360.
PDB; 5UAD; X-ray; 2.25 A; A=1023-1360.
PDB; 5YA5; X-ray; 1.89 A; A=1038-1346.
PDB; 6GCU; X-ray; 6.00 A; A/D=25-741.
PDB; 6I04; X-ray; 3.10 A; A/B=25-564.
PDB; 6SD9; X-ray; 2.35 A; A=1038-1346.
PDB; 6SDC; X-ray; 1.67 A; A=1038-1346.
PDB; 6SDD; X-ray; 1.93 A; A=1038-1346.
PDB; 6SDE; X-ray; 2.49 A; A=1038-1346.
PDB; 6UBW; X-ray; 2.00 A; A=1023-1360.
PDBsum; 1FYR; -.
PDBsum; 1R0P; -.
PDBsum; 1R1W; -.
PDBsum; 1SHY; -.
PDBsum; 1SSL; -.
PDBsum; 1UX3; -.
PDBsum; 2G15; -.
PDBsum; 2RFN; -.
PDBsum; 2RFS; -.
PDBsum; 2UZX; -.
PDBsum; 2UZY; -.
PDBsum; 2WD1; -.
PDBsum; 2WGJ; -.
PDBsum; 2WKM; -.
PDBsum; 3A4P; -.
PDBsum; 3BUX; -.
PDBsum; 3C1X; -.
PDBsum; 3CCN; -.
PDBsum; 3CD8; -.
PDBsum; 3CE3; -.
PDBsum; 3CTH; -.
PDBsum; 3CTJ; -.
PDBsum; 3DKC; -.
PDBsum; 3DKF; -.
PDBsum; 3DKG; -.
PDBsum; 3EFJ; -.
PDBsum; 3EFK; -.
PDBsum; 3F66; -.
PDBsum; 3F82; -.
PDBsum; 3I5N; -.
PDBsum; 3L8V; -.
PDBsum; 3LQ8; -.
PDBsum; 3Q6U; -.
PDBsum; 3Q6W; -.
PDBsum; 3QTI; -.
PDBsum; 3R7O; -.
PDBsum; 3RHK; -.
PDBsum; 3U6H; -.
PDBsum; 3U6I; -.
PDBsum; 3VW8; -.
PDBsum; 3ZBX; -.
PDBsum; 3ZC5; -.
PDBsum; 3ZCL; -.
PDBsum; 3ZXZ; -.
PDBsum; 3ZZE; -.
PDBsum; 4AOI; -.
PDBsum; 4AP7; -.
PDBsum; 4DEG; -.
PDBsum; 4DEH; -.
PDBsum; 4DEI; -.
PDBsum; 4EEV; -.
PDBsum; 4GG5; -.
PDBsum; 4GG7; -.
PDBsum; 4IWD; -.
PDBsum; 4K3J; -.
PDBsum; 4KNB; -.
PDBsum; 4MXC; -.
PDBsum; 4O3T; -.
PDBsum; 4O3U; -.
PDBsum; 4R1V; -.
PDBsum; 4R1Y; -.
PDBsum; 4XMO; -.
PDBsum; 4XYF; -.
PDBsum; 5DG5; -.
PDBsum; 5EOB; -.
PDBsum; 5EYC; -.
PDBsum; 5EYD; -.
PDBsum; 5HLW; -.
PDBsum; 5HNI; -.
PDBsum; 5HO6; -.
PDBsum; 5HOA; -.
PDBsum; 5HOR; -.
PDBsum; 5HTI; -.
PDBsum; 5LSP; -.
PDBsum; 5T3Q; -.
PDBsum; 5UAB; -.
PDBsum; 5UAD; -.
PDBsum; 5YA5; -.
PDBsum; 6GCU; -.
PDBsum; 6I04; -.
PDBsum; 6SD9; -.
PDBsum; 6SDC; -.
PDBsum; 6SDD; -.
PDBsum; 6SDE; -.
PDBsum; 6UBW; -.
SMR; P08581; -.
BioGRID; 110391; 74.
CORUM; P08581; -.
DIP; DIP-6023N; -.
ELM; P08581; -.
IntAct; P08581; 96.
MINT; P08581; -.
STRING; 9606.ENSP00000317272; -.
BindingDB; P08581; -.
ChEMBL; CHEMBL3717; -.
DrugBank; DB06896; 1-(4-fluorophenyl)-N-[3-fluoro-4-(1H-pyrrolo[2,3-b]pyridin-4-yloxy)phenyl]-2-oxo-1,2-dihydropyridine-3-carboxamide.
DrugBank; DB08791; 1-[(2-NITROPHENYL)SULFONYL]-1H-PYRROLO[3,2-B]PYRIDINE-6-CARBOXAMIDE.
DrugBank; DB06997; 2-(4-fluorophenyl)-N-{[3-fluoro-4-(1H-pyrrolo[2,3-b]pyridin-4-yloxy)phenyl]carbamoyl}acetamide.
DrugBank; DB07969; 3-[3-(4-methylpiperazin-1-yl)-7-(trifluoromethyl)quinoxalin-5-yl]phenol.
DrugBank; DB08584; 6-{[6-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-b]pyridazin-3-yl]sulfanyl}quinoline.
DrugBank; DB08079; AMG-208.
DrugBank; DB12742; Amuvatinib.
DrugBank; DB12267; Brigatinib.
DrugBank; DB08875; Cabozantinib.
DrugBank; DB08865; Crizotinib.
DrugBank; DB12010; Fostamatinib.
DrugBank; DB02152; K-252a.
DrugBank; DB07369; N-(3-chlorophenyl)-N-methyl-2-oxo-3-[(3,4,5-trimethyl-1H-pyrrol-2-yl)methyl]-2H-indole-5-sulfonamide.
DrugBank; DB06995; N-({4-[(2-aminopyridin-4-yl)oxy]-3-fluorophenyl}carbamoyl)-2-(4-fluorophenyl)acetamide.
DrugBank; DB06314; SGX-523.
DrugBank; DB12200; Tivantinib.
DrugCentral; P08581; -.
GuidetoPHARMACOLOGY; 1815; -.
GlyConnect; 680; -.
iPTMnet; P08581; -.
PhosphoSitePlus; P08581; -.
SwissPalm; P08581; -.
UniCarbKB; P08581; -.
BioMuta; MET; -.
DMDM; 251757497; -.
OGP; P08581; -.
CPTAC; CPTAC-1496; -.
CPTAC; CPTAC-2784; -.
EPD; P08581; -.
jPOST; P08581; -.
MassIVE; P08581; -.
MaxQB; P08581; -.
PaxDb; P08581; -.
PeptideAtlas; P08581; -.
PRIDE; P08581; -.
ProteomicsDB; 52128; -. [P08581-1]
ProteomicsDB; 52129; -. [P08581-2]
ProteomicsDB; 52130; -. [P08581-3]
ABCD; P08581; 42 sequenced antibodies.
Antibodypedia; 3939; 2787 antibodies.
DNASU; 4233; -.
Ensembl; ENST00000318493; ENSP00000317272; ENSG00000105976. [P08581-2]
Ensembl; ENST00000397752; ENSP00000380860; ENSG00000105976. [P08581-1]
Ensembl; ENST00000436117; ENSP00000410980; ENSG00000105976. [P08581-3]
GeneID; 4233; -.
KEGG; hsa:4233; -.
UCSC; uc003vij.4; human. [P08581-1]
CTD; 4233; -.
DisGeNET; 4233; -.
EuPathDB; HostDB:ENSG00000105976.14; -.
GeneCards; MET; -.
HGNC; HGNC:7029; MET.
HPA; ENSG00000105976; Low tissue specificity.
MalaCards; MET; -.
MIM; 114550; phenotype.
MIM; 164860; gene.
MIM; 605074; phenotype.
MIM; 607278; phenotype.
MIM; 616705; phenotype.
neXtProt; NX_P08581; -.
OpenTargets; ENSG00000105976; -.
Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
Orphanet; 47044; Hereditary papillary renal cell carcinoma.
Orphanet; 106; NON RARE IN EUROPE: Autism.
Orphanet; 488265; Osteofibrous dysplasia.
Orphanet; 319298; Papillary renal cell carcinoma.
Orphanet; 33402; Pediatric hepatocellular carcinoma.
Orphanet; 357191; Selection of therapeutic option in non-small cell lung carcinoma.
PharmGKB; PA30763; -.
eggNOG; KOG1095; Eukaryota.
eggNOG; KOG3610; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000158022; -.
HOGENOM; CLU_005158_0_0_1; -.
InParanoid; P08581; -.
KO; K05099; -.
OMA; DEEPGQC; -.
OrthoDB; 408584at2759; -.
PhylomeDB; P08581; -.
TreeFam; TF317402; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-416550; Sema4D mediated inhibition of cell attachment and migration.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6806942; MET Receptor Activation.
Reactome; R-HSA-6807004; Negative regulation of MET activity.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8851805; MET activates RAS signaling.
Reactome; R-HSA-8851907; MET activates PI3K/AKT signaling.
Reactome; R-HSA-8865999; MET activates PTPN11.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
Reactome; R-HSA-8875513; MET interacts with TNS proteins.
Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
Reactome; R-HSA-8875656; MET receptor recycling.
Reactome; R-HSA-8875791; MET activates STAT3.
Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
SignaLink; P08581; -.
SIGNOR; P08581; -.
BioGRID-ORCS; 4233; 20 hits in 824 CRISPR screens.
ChiTaRS; MET; human.
EvolutionaryTrace; P08581; -.
GeneWiki; C-Met; -.
GenomeRNAi; 4233; -.
Pharos; P08581; Tclin.
PRO; PR:P08581; -.
Proteomes; UP000005640; Chromosome 7.
RNAct; P08581; protein.
Bgee; ENSG00000105976; Expressed in pigmented layer of retina and 206 other tissues.
ExpressionAtlas; P08581; baseline and differential.
Genevisible; P08581; HS.
GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
GO; GO:0009986; C:cell surface; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005008; F:hepatocyte growth factor-activated receptor activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
GO; GO:0001886; P:endothelial cell morphogenesis; IDA:UniProtKB.
GO; GO:0035635; P:entry of bacterium into host cell; TAS:Reactome.
GO; GO:0061436; P:establishment of skin barrier; IMP:CAFA.
GO; GO:0001889; P:liver development; IBA:GO_Central.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0010507; P:negative regulation of autophagy; NAS:ParkinsonsUK-UCL.
GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; IDA:CAFA.
GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; IMP:BHF-UCL.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IDA:CAFA.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:CAFA.
GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; IDA:CAFA.
GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
GO; GO:0031016; P:pancreas development; IBA:GO_Central.
GO; GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IMP:UniProtKB.
GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:CAFA.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR031148; Plexin.
InterPro; IPR002165; Plexin_repeat.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR016201; PSI.
InterPro; IPR001627; Semap_dom.
InterPro; IPR036352; Semap_dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PANTHER; PTHR22625; PTHR22625; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01437; PSI; 1.
Pfam; PF01403; Sema; 1.
Pfam; PF01833; TIG; 3.
PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00429; IPT; 4.
SMART; SM00423; PSI; 1.
SMART; SM00630; Sema; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF101912; SSF101912; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF81296; SSF81296; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS51004; SEMA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Chromosomal rearrangement;
Deafness; Disease mutation; Disulfide bond; Glycoprotein; Kinase; Membrane;
Non-syndromic deafness; Nucleotide-binding; Phosphoprotein; Polymorphism;
Proto-oncogene; Receptor; Reference proteome; Repeat; Secreted; Signal;
Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
Ubl conjugation.
SIGNAL 1..24
/evidence="ECO:0000255"
CHAIN 25..1390
/note="Hepatocyte growth factor receptor"
/id="PRO_0000024440"
TOPO_DOM 25..932
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 933..955
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 956..1390
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 27..515
/note="Sema"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
DOMAIN 563..655
/note="IPT/TIG 1"
DOMAIN 657..739
/note="IPT/TIG 2"
DOMAIN 742..836
/note="IPT/TIG 3"
DOMAIN 1078..1345
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 1084..1092
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 1212..1390
/note="Interaction with RANBP9"
REGION 1320..1359
/note="Interaction with MUC20"
/evidence="ECO:0000269|PubMed:15314156"
ACT_SITE 1204
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
BINDING 1110
/note="ATP"
SITE 307..308
/note="Cleavage"
/evidence="ECO:0000255"
SITE 1003
/note="Required for ligand-induced CBL-mediated
ubiquitination"
/evidence="ECO:0000269|PubMed:12244174"
SITE 1009..1010
/note="Breakpoint for translocation to form TPR-MET
oncogene"
MOD_RES 966
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 977
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18691976"
MOD_RES 990
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163"
MOD_RES 997
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 1000
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 1003
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195"
MOD_RES 1230
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:12475979"
MOD_RES 1234
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:12475979"
MOD_RES 1235
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:12475979,
ECO:0000269|PubMed:1655790"
MOD_RES 1289
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:19369195"
MOD_RES 1349
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:12475979,
ECO:0000269|PubMed:7513258"
MOD_RES 1356
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:15735664,
ECO:0000269|PubMed:7513258"
MOD_RES 1365
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:12475979"
CARBOHYD 45
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 106
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19196183"
CARBOHYD 149
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 202
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 399
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 405
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 607
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 635
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 785
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 879
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 930
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 95..101
DISULFID 98..160
DISULFID 133..141
/evidence="ECO:0000244|PDB:2UZX, ECO:0000244|PDB:2UZY,
ECO:0000269|PubMed:17662939"
DISULFID 172..175
/evidence="ECO:0000244|PDB:2UZX, ECO:0000244|PDB:2UZY,
ECO:0000269|PubMed:17662939"
DISULFID 298..363
/evidence="ECO:0000244|PDB:2UZX, ECO:0000244|PDB:2UZY,
ECO:0000269|PubMed:17662939"
DISULFID 385..397
/evidence="ECO:0000244|PDB:2UZY,
ECO:0000269|PubMed:17662939"
DISULFID 520..538
/evidence="ECO:0000244|PDB:2UZX, ECO:0000244|PDB:2UZY,
ECO:0000269|PubMed:17662939"
DISULFID 526..561
/evidence="ECO:0000244|PDB:2UZX, ECO:0000244|PDB:2UZY,
ECO:0000269|PubMed:17662939"
DISULFID 529..545
/evidence="ECO:0000244|PDB:2UZX, ECO:0000244|PDB:2UZY,
ECO:0000269|PubMed:17662939"
DISULFID 541..551
/evidence="ECO:0000244|PDB:2UZX, ECO:0000244|PDB:2UZY,
ECO:0000269|PubMed:17662939"
DISULFID 610..624
/evidence="ECO:0000244|PDB:2UZX, ECO:0000244|PDB:2UZY,
ECO:0000269|PubMed:17662939"
DISULFID 697..709
/evidence="ECO:0000244|PDB:2UZY,
ECO:0000269|PubMed:17662939"
VAR_SEQ 755..764
/note="SGGSTITGVG -> RHVNIALIQR (in isoform 3)"
/evidence="ECO:0000303|PubMed:18593464"
/id="VSP_042447"
VAR_SEQ 755
/note="S -> STWWKEPLNIVSFLFCFAS (in isoform 2)"
/evidence="ECO:0000303|PubMed:2819873"
/id="VSP_005005"
VAR_SEQ 765..1390
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:18593464"
/id="VSP_042448"
VARIANT 143
/note="R -> Q (in dbSNP:rs35469582)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041738"
VARIANT 150
/note="H -> Y (found in a case of cancer of unknown primary
origin; the mutated receptor is still functional and can
sustain the transformed phenotype; somatic mutation;
dbSNP:rs1436957498)"
/evidence="ECO:0000269|PubMed:20949619"
/id="VAR_064855"
VARIANT 156
/note="S -> L (in dbSNP:rs56311081)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041739"
VARIANT 168
/note="E -> D (found in a case of cancer of unknown primary
origin; the mutated receptor is still functional and can
sustain the transformed phenotype; somatic mutation;
dbSNP:rs55985569)"
/evidence="ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:20949619"
/id="VAR_041740"
VARIANT 238
/note="L -> S (in dbSNP:rs34349517)"
/id="VAR_032478"
VARIANT 316
/note="I -> M (in dbSNP:rs35225896)"
/id="VAR_032479"
VARIANT 320
/note="A -> V (in dbSNP:rs35776110)"
/evidence="ECO:0000269|PubMed:9140397"
/id="VAR_006285"
VARIANT 375
/note="N -> K (found in lung cancer also including cases
carrying EGFR mutations; unknown pathological significance;
decreased hepatocyte growth factor-activated receptor
activity; decreased interaction with HGF;
dbSNP:rs776693512)"
/evidence="ECO:0000269|PubMed:28294470"
/id="VAR_079370"
VARIANT 375
/note="N -> S (in dbSNP:rs33917957)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_032480"
VARIANT 385
/note="C -> Y (found in a case of cancer of unknown primary
origin; the mutated receptor is still functional and can
sustain the transformed phenotype; somatic mutation;
dbSNP:rs752055485)"
/evidence="ECO:0000269|PubMed:20949619"
/id="VAR_064856"
VARIANT 773
/note="P -> L (in gastric cancer; dbSNP:rs771333219)"
/evidence="ECO:0000269|PubMed:12920089"
/id="VAR_032481"
VARIANT 841
/note="F -> V (in DFNB97; dbSNP:rs794728016)"
/evidence="ECO:0000269|PubMed:25941349"
/id="VAR_075757"
VARIANT 964..1010
/note="Missing (in OSFD; loss of CBL-mediated
destabilization)"
/evidence="ECO:0000269|PubMed:26637977"
/id="VAR_076584"
VARIANT 970
/note="R -> C (in dbSNP:rs34589476)"
/evidence="ECO:0000269|PubMed:17053076,
ECO:0000269|PubMed:17344846"
/id="VAR_032482"
VARIANT 991
/note="P -> S (in gastric cancer; prolonged tyrosine
phosphorylation in response to HGF/SF; transforming
activity in athymic nude mice; dbSNP:rs768678989)"
/evidence="ECO:0000269|PubMed:11042681"
/id="VAR_032483"
VARIANT 992
/note="T -> I (found in a case of cancer of unknown primary
origin; the mutated receptor is still functional and can
sustain the transformed phenotype; somatic mutation;
dbSNP:rs56391007)"
/evidence="ECO:0000269|PubMed:11042681,
ECO:0000269|PubMed:17053076, ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:20949619"
/id="VAR_032484"
VARIANT 1003
/note="Y -> S (probable disease-associated variant found in
lesional sample from a patient with sporadically occurring,
unilateral osteofibrous dysplasia; somatic mutation;
complete loss of ligand-induced CBL-mediated
ubiquitination, resulting in protein stabilization)"
/evidence="ECO:0000269|PubMed:12244174"
/id="VAR_076585"
VARIANT 1092
/note="V -> I (in RCCP; constitutive autophosphorylation;
dbSNP:rs786202724)"
/evidence="ECO:0000269|PubMed:10327054,
ECO:0000269|PubMed:10417759, ECO:0000269|PubMed:10433944"
/id="VAR_032485"
VARIANT 1094
/note="H -> L (in RCCP; constitutive autophosphorylation;
causes malignant transformation in cell lines)"
/evidence="ECO:0000269|PubMed:10327054"
/id="VAR_032486"
VARIANT 1094
/note="H -> R (in RCCP; causes malignant transformation in
cell lines; dbSNP:rs121913243)"
/evidence="ECO:0000269|PubMed:10433944,
ECO:0000269|PubMed:9563489"
/id="VAR_032487"
VARIANT 1094
/note="H -> Y (in RCCP; constitutive autophosphorylation;
causes malignant transformation in cell lines;
dbSNP:rs121913244)"
/evidence="ECO:0000269|PubMed:10327054"
/id="VAR_032488"
VARIANT 1106
/note="H -> D (in RCCP; constitutive autophosphorylation;
causes malignant transformation in cell lines)"
/evidence="ECO:0000269|PubMed:10327054,
ECO:0000269|PubMed:10433944"
/id="VAR_032489"
VARIANT 1131
/note="M -> T (in RCCP; germline mutation;
dbSNP:rs121913668)"
/evidence="ECO:0000269|PubMed:10433944,
ECO:0000269|PubMed:9140397"
/id="VAR_006286"
VARIANT 1173
/note="T -> I (in HCC; dbSNP:rs121913675)"
/evidence="ECO:0000269|PubMed:9927037"
/id="VAR_032490"
VARIANT 1188
/note="V -> L (in RCCP; germline mutation;
dbSNP:rs121913669)"
/evidence="ECO:0000269|PubMed:10433944,
ECO:0000269|PubMed:9140397"
/id="VAR_006287"
VARIANT 1195
/note="L -> V (in RCCP; somatic mutation;
dbSNP:rs121913673)"
/evidence="ECO:0000269|PubMed:9140397"
/id="VAR_006288"
VARIANT 1220
/note="V -> I (in RCCP; germline mutation;
dbSNP:rs121913670)"
/evidence="ECO:0000269|PubMed:9140397"
/id="VAR_006289"
VARIANT 1228
/note="D -> H (in RCCP; somatic mutation;
dbSNP:rs121913671)"
/evidence="ECO:0000269|PubMed:9140397"
/id="VAR_006291"
VARIANT 1228
/note="D -> N (in RCCP; germline mutation;
dbSNP:rs121913671)"
/evidence="ECO:0000269|PubMed:9140397"
/id="VAR_006290"
VARIANT 1230
/note="Y -> C (in RCCP; germline mutation;
dbSNP:rs121913246)"
/evidence="ECO:0000269|PubMed:10433944,
ECO:0000269|PubMed:9140397"
/id="VAR_006292"
VARIANT 1230
/note="Y -> D (in RCCP; constitutive autophosphorylation;
causes malignant transformation in cell lines)"
/evidence="ECO:0000269|PubMed:10327054,
ECO:0000269|PubMed:10433944"
/id="VAR_032491"
VARIANT 1230
/note="Y -> H (in RCCP; somatic mutation;
dbSNP:rs121913247)"
/evidence="ECO:0000269|PubMed:9140397"
/id="VAR_006293"
VARIANT 1244
/note="K -> R (in HCC; dbSNP:rs121913677)"
/evidence="ECO:0000269|PubMed:9927037"
/id="VAR_032492"
VARIANT 1250
/note="M -> I (in HCC; dbSNP:rs121913676)"
/evidence="ECO:0000269|PubMed:9927037"
/id="VAR_032493"
VARIANT 1250
/note="M -> T (in RCCP; somatic mutation;
dbSNP:rs121913245)"
/evidence="ECO:0000269|PubMed:10433944,
ECO:0000269|PubMed:9140397"
/id="VAR_006294"
VARIANT 1294
/note="V -> I (found in a case of cancer of unknown primary
origin; the mutated receptor is still functional and can
sustain the transformed phenotype; somatic mutation;
dbSNP:rs1263785859)"
/evidence="ECO:0000269|PubMed:20949619"
/id="VAR_064857"
MUTAGEN 1234
/note="Y->F: Complete loss of kinase activity and of
ligand-induced ubiquitination. Alters interaction with
PTPN1 and PTPN2. Loss of interaction with PTPN1 and PTPN2;
when associated with F-1235."
/evidence="ECO:0000269|PubMed:12244174,
ECO:0000269|PubMed:18819921"
MUTAGEN 1235
/note="Y->F: Complete loss of kinase activity. Alters
interaction with PTPN1 and PTPN2. Loss of interaction with
PTPN1 and PTPN2; when associated with F-1234."
/evidence="ECO:0000269|PubMed:12244174,
ECO:0000269|PubMed:18819921"
MUTAGEN 1313
/note="Y->F: No effect on ligand-induced CBL-mediated
ubiquitination; when associated with F-1349, F-1356 and F-
1365."
/evidence="ECO:0000269|PubMed:12244174"
MUTAGEN 1349
/note="Y->F: No effect on ligand-induced CBL-mediated
ubiquitination; when associated with F-1313, F-1356 and F-
1365."
/evidence="ECO:0000269|PubMed:12244174"
MUTAGEN 1356
/note="Y->F: No effect on ligand-induced CBL-mediated
ubiquitination; when associated with F-1313, F-1349 and F-
1365."
/evidence="ECO:0000269|PubMed:12244174"
MUTAGEN 1365
/note="Y->F: No effect on ligand-induced CBL-mediated
ubiquitination; when associated with F-1313, F-1349 and F-
1356."
/evidence="ECO:0000269|PubMed:12244174"
CONFLICT 237
/note="V -> A (in Ref. 3; ACF47606)"
/evidence="ECO:0000305"
CONFLICT 508
/note="K -> R (in Ref. 3; ACF47606)"
/evidence="ECO:0000305"
CONFLICT 720
/note="F -> S (in Ref. 3; ACF47606)"
/evidence="ECO:0000305"
CONFLICT 1191
/note="G -> A (in Ref. 1; AAA59591)"
/evidence="ECO:0000305"
CONFLICT 1272
/note="L -> V (in Ref. 1; AAA59591, 2; CAB56793 and 6;
AAA59590)"
/evidence="ECO:0000305"
HELIX 25..30
/evidence="ECO:0000244|PDB:5LSP"
STRAND 45..47
/evidence="ECO:0000244|PDB:2UZX"
STRAND 52..58
/evidence="ECO:0000244|PDB:2UZX"
STRAND 61..66
/evidence="ECO:0000244|PDB:2UZX"
STRAND 69..74
/evidence="ECO:0000244|PDB:2UZX"
TURN 75..77
/evidence="ECO:0000244|PDB:2UZX"
STRAND 80..84
/evidence="ECO:0000244|PDB:2UZX"
STRAND 89..91
/evidence="ECO:0000244|PDB:4K3J"
STRAND 93..95
/evidence="ECO:0000244|PDB:4K3J"
STRAND 97..99
/evidence="ECO:0000244|PDB:1SHY"
HELIX 103..105
/evidence="ECO:0000244|PDB:4O3T"
STRAND 111..113
/evidence="ECO:0000244|PDB:4K3J"
STRAND 119..123
/evidence="ECO:0000244|PDB:2UZX"
STRAND 125..133
/evidence="ECO:0000244|PDB:2UZX"
STRAND 135..139
/evidence="ECO:0000244|PDB:2UZX"
STRAND 141..145
/evidence="ECO:0000244|PDB:2UZX"
STRAND 155..160
/evidence="ECO:0000244|PDB:4K3J"
STRAND 173..175
/evidence="ECO:0000244|PDB:6I04"
STRAND 182..189
/evidence="ECO:0000244|PDB:2UZX"
STRAND 192..199
/evidence="ECO:0000244|PDB:2UZX"
STRAND 213..219
/evidence="ECO:0000244|PDB:2UZX"
HELIX 231..233
/evidence="ECO:0000244|PDB:2UZX"
HELIX 239..241
/evidence="ECO:0000244|PDB:2UZX"
TURN 242..244
/evidence="ECO:0000244|PDB:2UZX"
STRAND 247..255
/evidence="ECO:0000244|PDB:2UZX"
STRAND 258..268
/evidence="ECO:0000244|PDB:2UZX"
STRAND 272..274
/evidence="ECO:0000244|PDB:2UZX"
STRAND 277..281
/evidence="ECO:0000244|PDB:2UZX"
STRAND 284..286
/evidence="ECO:0000244|PDB:2UZX"
STRAND 292..300
/evidence="ECO:0000244|PDB:2UZX"
STRAND 312..314
/evidence="ECO:0000244|PDB:2UZX"
STRAND 316..323
/evidence="ECO:0000244|PDB:2UZX"
HELIX 327..333
/evidence="ECO:0000244|PDB:2UZX"
STRAND 341..349
/evidence="ECO:0000244|PDB:2UZX"
STRAND 356..366
/evidence="ECO:0000244|PDB:2UZX"
HELIX 367..374
/evidence="ECO:0000244|PDB:2UZX"
HELIX 380..382
/evidence="ECO:0000244|PDB:4K3J"
STRAND 383..385
/evidence="ECO:0000244|PDB:4K3J"
HELIX 387..390
/evidence="ECO:0000244|PDB:2UZX"
STRAND 392..394
/evidence="ECO:0000244|PDB:1SHY"
TURN 395..397
/evidence="ECO:0000244|PDB:4O3T"
STRAND 418..422
/evidence="ECO:0000244|PDB:2UZX"
STRAND 424..427
/evidence="ECO:0000244|PDB:2UZX"
TURN 429..436
/evidence="ECO:0000244|PDB:2UZX"
STRAND 439..447
/evidence="ECO:0000244|PDB:2UZX"
STRAND 450..457
/evidence="ECO:0000244|PDB:2UZX"
STRAND 462..466
/evidence="ECO:0000244|PDB:2UZX"
STRAND 469..471
/evidence="ECO:0000244|PDB:4K3J"
STRAND 476..480
/evidence="ECO:0000244|PDB:4K3J"
STRAND 490..493
/evidence="ECO:0000244|PDB:2UZX"
TURN 496..498
/evidence="ECO:0000244|PDB:4O3T"
STRAND 501..506
/evidence="ECO:0000244|PDB:2UZX"
STRAND 509..514
/evidence="ECO:0000244|PDB:2UZX"
HELIX 520..522
/evidence="ECO:0000244|PDB:5LSP"
HELIX 526..529
/evidence="ECO:0000244|PDB:5LSP"
HELIX 534..536
/evidence="ECO:0000244|PDB:5LSP"
STRAND 539..541
/evidence="ECO:0000244|PDB:5LSP"
STRAND 544..546
/evidence="ECO:0000244|PDB:5LSP"
HELIX 548..550
/evidence="ECO:0000244|PDB:5LSP"
STRAND 552..554
/evidence="ECO:0000244|PDB:2UZX"
STRAND 557..559
/evidence="ECO:0000244|PDB:5LSP"
STRAND 564..574
/evidence="ECO:0000244|PDB:5LSP"
STRAND 580..586
/evidence="ECO:0000244|PDB:5LSP"
STRAND 589..592
/evidence="ECO:0000244|PDB:5LSP"
STRAND 595..598
/evidence="ECO:0000244|PDB:5LSP"
STRAND 602..605
/evidence="ECO:0000244|PDB:5LSP"
HELIX 614..616
/evidence="ECO:0000244|PDB:5LSP"
STRAND 619..625
/evidence="ECO:0000244|PDB:5LSP"
STRAND 633..641
/evidence="ECO:0000244|PDB:5LSP"
STRAND 646..655
/evidence="ECO:0000244|PDB:5LSP"
STRAND 658..663
/evidence="ECO:0000244|PDB:5LSP"
STRAND 665..668
/evidence="ECO:0000244|PDB:5LSP"
STRAND 674..681
/evidence="ECO:0000244|PDB:5LSP"
STRAND 688..692
/evidence="ECO:0000244|PDB:5LSP"
STRAND 698..702
/evidence="ECO:0000244|PDB:5LSP"
STRAND 704..710
/evidence="ECO:0000244|PDB:5LSP"
STRAND 718..726
/evidence="ECO:0000244|PDB:5LSP"
STRAND 729..739
/evidence="ECO:0000244|PDB:5LSP"
HELIX 1048..1050
/evidence="ECO:0000244|PDB:4EEV"
HELIX 1055..1057
/evidence="ECO:0000244|PDB:3F66"
HELIX 1060..1066
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1067..1069
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1073..1075
/evidence="ECO:0000244|PDB:4R1V"
STRAND 1076..1087
/evidence="ECO:0000244|PDB:4R1V"
STRAND 1090..1098
/evidence="ECO:0000244|PDB:4R1V"
STRAND 1100..1102
/evidence="ECO:0000244|PDB:4EEV"
STRAND 1104..1111
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1118..1132
/evidence="ECO:0000244|PDB:4R1V"
STRAND 1144..1146
/evidence="ECO:0000244|PDB:4R1V"
STRAND 1149..1151
/evidence="ECO:0000244|PDB:3F66"
STRAND 1154..1158
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1165..1170
/evidence="ECO:0000244|PDB:4R1V"
TURN 1172..1174
/evidence="ECO:0000244|PDB:3ZCL"
HELIX 1178..1197
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1207..1209
/evidence="ECO:0000244|PDB:4R1V"
STRAND 1210..1212
/evidence="ECO:0000244|PDB:4R1V"
STRAND 1218..1220
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1224..1226
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1232..1234
/evidence="ECO:0000244|PDB:4R1V"
STRAND 1236..1238
/evidence="ECO:0000244|PDB:4KNB"
TURN 1239..1241
/evidence="ECO:0000244|PDB:4R1V"
STRAND 1243..1245
/evidence="ECO:0000244|PDB:4KNB"
HELIX 1247..1249
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1252..1257
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1262..1277
/evidence="ECO:0000244|PDB:4R1V"
STRAND 1283..1287
/evidence="ECO:0000244|PDB:4EEV"
HELIX 1289..1291
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1292..1297
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1310..1319
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1324..1326
/evidence="ECO:0000244|PDB:4R1V"
HELIX 1330..1342
/evidence="ECO:0000244|PDB:4R1V"
TURN 1354..1358
/evidence="ECO:0000244|PDB:1R0P"
SEQUENCE 1390 AA; 155541 MW; 9CF896D1273905C3 CRC64;
MKAPAVLAPG ILVLLFTLVQ RSNGECKEAL AKSEMNVNMK YQLPNFTAET PIQNVILHEH
HIFLGATNYI YVLNEEDLQK VAEYKTGPVL EHPDCFPCQD CSSKANLSGG VWKDNINMAL
VVDTYYDDQL ISCGSVNRGT CQRHVFPHNH TADIQSEVHC IFSPQIEEPS QCPDCVVSAL
GAKVLSSVKD RFINFFVGNT INSSYFPDHP LHSISVRRLK ETKDGFMFLT DQSYIDVLPE
FRDSYPIKYV HAFESNNFIY FLTVQRETLD AQTFHTRIIR FCSINSGLHS YMEMPLECIL
TEKRKKRSTK KEVFNILQAA YVSKPGAQLA RQIGASLNDD ILFGVFAQSK PDSAEPMDRS
AMCAFPIKYV NDFFNKIVNK NNVRCLQHFY GPNHEHCFNR TLLRNSSGCE ARRDEYRTEF
TTALQRVDLF MGQFSEVLLT SISTFIKGDL TIANLGTSEG RFMQVVVSRS GPSTPHVNFL
LDSHPVSPEV IVEHTLNQNG YTLVITGKKI TKIPLNGLGC RHFQSCSQCL SAPPFVQCGW
CHDKCVRSEE CLSGTWTQQI CLPAIYKVFP NSAPLEGGTR LTICGWDFGF RRNNKFDLKK
TRVLLGNESC TLTLSESTMN TLKCTVGPAM NKHFNMSIII SNGHGTTQYS TFSYVDPVIT
SISPKYGPMA GGTLLTLTGN YLNSGNSRHI SIGGKTCTLK SVSNSILECY TPAQTISTEF
AVKLKIDLAN RETSIFSYRE DPIVYEIHPT KSFISGGSTI TGVGKNLNSV SVPRMVINVH
EAGRNFTVAC QHRSNSEIIC CTTPSLQQLN LQLPLKTKAF FMLDGILSKY FDLIYVHNPV
FKPFEKPVMI SMGNENVLEI KGNDIDPEAV KGEVLKVGNK SCENIHLHSE AVLCTVPNDL
LKLNSELNIE WKQAISSTVL GKVIVQPDQN FTGLIAGVVS ISTALLLLLG FFLWLKKRKQ
IKDLGSELVR YDARVHTPHL DRLVSARSVS PTTEMVSNES VDYRATFPED QFPNSSQNGS
CRQVQYPLTD MSPILTSGDS DISSPLLQNT VHIDLSALNP ELVQAVQHVV IGPSSLIVHF
NEVIGRGHFG CVYHGTLLDN DGKKIHCAVK SLNRITDIGE VSQFLTEGII MKDFSHPNVL
SLLGICLRSE GSPLVVLPYM KHGDLRNFIR NETHNPTVKD LIGFGLQVAK GMKYLASKKF
VHRDLAARNC MLDEKFTVKV ADFGLARDMY DKEYYSVHNK TGAKLPVKWM ALESLQTQKF
TTKSDVWSFG VLLWELMTRG APPYPDVNTF DITVYLLQGR RLLQPEYCPD PLYEVMLKCW
HPKAEMRPSF SELVSRISAI FSTFIGEHYV HVNATYVNVK CVAPYPSLLS SEDNADDEVD
TRPASFWETS


Related products :

Catalog number Product name Quantity
18-785-210279 Met (Ab-1234) - EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.05 mg
18-785-210279 Met (Ab-1234) - EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.1 mg
18-785-210280 Met (Ab-1349) - EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.05 mg
10-054-165010 cMet HUMAN - EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met 0.01 mg
18-785-210280 Met (Ab-1349) - EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.1 mg
18-785-210277 Met (Phospho-Tyr1234) - EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.05 mg
18-785-210278 Met (Phospho-Tyr1349) - EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.1 mg
18-785-210277 Met (Phospho-Tyr1234) - EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.1 mg
18-785-210278 Met (Phospho-Tyr1349) - EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.05 mg
18-272-196210 Met ( c - Met ) - Rabbit polyclonal to Met ( c - Met ); EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.05 mg
18-272-195200 Met (c-Met) - Goat polyclonal to Met (c-Met); EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.025 mg
U0978r CLIA Epidermal growth factor receptor-related protein,Erbb2,Neu,p185erbB2,p185neu,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-2 96T
E0978r ELISA Epidermal growth factor receptor-related protein,Erbb2,Neu,p185erbB2,p185neu,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-2 96T
E0978r ELISA kit Epidermal growth factor receptor-related protein,Erbb2,Neu,p185erbB2,p185neu,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-2 96T
20-272-191078 Met ( c - Met ) ( phospho Y1234 ) - Mouse monoclonal [3i20] to Met ( c - Met ) ( phospho Y1234 ); EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene t 0.05 ml
U0757h CLIA EGFR,Epidermal growth factor receptor,ERBB1,Homo sapiens,Human,Proto-oncogene c-ErbB-1,Receptor tyrosine-protein kinase erbB-1 96T
E0757h ELISA EGFR,Epidermal growth factor receptor,ERBB1,Homo sapiens,Human,Proto-oncogene c-ErbB-1,Receptor tyrosine-protein kinase erbB-1 96T
E0757h ELISA kit EGFR,Epidermal growth factor receptor,ERBB1,Homo sapiens,Human,Proto-oncogene c-ErbB-1,Receptor tyrosine-protein kinase erbB-1 96T
EIAAB13163 Erbb3,Glial growth factor receptor,Mouse,Mus musculus,Proto-oncogene-like protein c-ErbB-3,Receptor tyrosine-protein kinase erbB-3
U0147m CLIA Embryonic receptor kinase 2,Emrk2,Flt,Flt1,FLT-1,Fms-like tyrosine kinase 1,Mouse,Mus musculus,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,VEGFR-1 96T
E0147m ELISA Embryonic receptor kinase 2,Emrk2,Flt,Flt1,FLT-1,Fms-like tyrosine kinase 1,Mouse,Mus musculus,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,VEGFR-1 96T
E0147m ELISA kit Embryonic receptor kinase 2,Emrk2,Flt,Flt1,FLT-1,Fms-like tyrosine kinase 1,Mouse,Mus musculus,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,VEGFR-1 96T
18-783-75623 RABBIT ANTI HUMAN EGF RECEPTOR - EPIDERMAL GROWTH FACTOR RECEPTOR; EC 2.7.10.1; Receptor tyrosine-protein kinase ErbB-1 Polyclonal 0.05 mg
15-288-21181 Vascular endothelial growth factor receptor 2 - EC 2.7.10.1; VEGFR-2; Kinase insert domain receptor; Protein-tyrosine kinase receptor Flk-1; CD309 antigen Polyclonal 0.1 mg
15-288-21181 Vascular endothelial growth factor receptor 2 - EC 2.7.10.1; VEGFR-2; Kinase insert domain receptor; Protein-tyrosine kinase receptor Flk-1; CD309 antigen Polyclonal 0.05 mg
Pathways :
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP2292: Chemokine signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP474: Endochondral Ossification
WP1354: B Cell Receptor Signaling Pathway
WP2079: Serotonin Receptor 2 and STAT3 Signaling
WP878: EPO Receptor Signaling
WP2328: Allograft rejection
WP1004: Kit Receptor Signaling Pathway
WP2355: Corticotropin-releasing hormone
WP733: Serotonin Receptor 2 and STAT3 Signaling
WP1025: B Cell Receptor Signaling Pathway
WP138: Androgen receptor signaling pathway
WP2118: Arrhythmogenic right ventricular cardiomyopathy
WP352: T Cell Receptor Signaling Pathway
WP894: T Cell Receptor Signaling Pathway

Related Genes :
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[Met] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[Met] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)

Bibliography :
[30930049] Inhibition of the MET Kinase Activity and Cell Growth in MET-Addicted Cancer Cells by Bi-Paratopic Linking.
[30670153] Proteolytic cleavages of MET: the divide-and-conquer strategy of a receptor tyrosine kinase.
[30401749] Activation of hepatocyte growth factor/MET signaling initiates oncogenic transformation and enhances tumor aggressiveness in the murine prostate.
[28827556] Characterization and structural determination of a new anti-MET function-blocking antibody with binding epitope distinct from the ligand binding domain.
[28212658] c-Met expression and activity in urogenital cancers - novel aspects of signal transduction and medical implications.
[28107696] A mini-review of c-Met as a potential therapeutic target in melanoma.
[28061464] MET receptor variant R970C favors calpain-dependent generation of a fragment promoting epithelial cell scattering.
[27864331] Role of Sphingosine Kinase 1 and S1P Transporter Spns2 in HGF-mediated Lamellipodia Formation in Lung Endothelium.
[26712116] Developing Antagonists for the Met-HGF/SF Protein-Protein Interaction Using a Fragment-Based Approach.
[26260789] Impact of Cell-surface Antigen Expression on Target Engagement and Function of an Epidermal Growth Factor Receptor × c-MET Bispecific Antibody.