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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.
22-NOV-2017, entry version 232.
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]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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).
[44]
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).
[45]
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).
[46]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-740 IN COMPLEX WITH
L.MONOCYTOGENES INLB, 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).
[47]
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).
[48]
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).
[49]
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).
[50]
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).
[51]
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).
[52]
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).
[53]
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).
[54]
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).
[55]
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).
[56]
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).
[57]
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).
[58]
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).
[59]
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: Acts as a receptor for Listeria internalin inlB,
mediating entry of the pathogen into cells.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME 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}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1039152, EBI-1039152;
P22681:CBL; NbExp=15; IntAct=EBI-1039152, EBI-518228;
Q96EY1-2:DNAJA3; NbExp=2; IntAct=EBI-1039152, EBI-3952284;
P00533:EGFR; NbExp=8; IntAct=EBI-1039152, EBI-297353;
P09769:FGR; NbExp=2; IntAct=EBI-1039152, EBI-1383732;
P14210:HGF; NbExp=7; IntAct=EBI-1039152, EBI-1039104;
P14210-6:HGF; NbExp=3; IntAct=EBI-1039152, EBI-6280319;
Q08048:Hgf (xeno); NbExp=3; IntAct=EBI-1039152, EBI-15655650;
P25147:inlB (xeno); NbExp=4; IntAct=EBI-1039152, EBI-1379295;
O15357:INPPL1; NbExp=2; IntAct=EBI-1039152, EBI-1384248;
P35968:KDR; NbExp=3; IntAct=EBI-1039152, EBI-1005487;
P35918:Kdr (xeno); NbExp=3; IntAct=EBI-1039152, EBI-1555005;
P06239:LCK; NbExp=3; IntAct=EBI-1039152, EBI-1348;
P07948:LYN; NbExp=2; IntAct=EBI-1039152, EBI-79452;
P15941:MUC1; NbExp=2; IntAct=EBI-1039152, EBI-2804728;
P16333:NCK1; NbExp=2; IntAct=EBI-1039152, EBI-389883;
O43639:NCK2; NbExp=2; IntAct=EBI-1039152, EBI-713635;
P27986:PIK3R1; NbExp=6; IntAct=EBI-1039152, EBI-79464;
O00459:PIK3R2; NbExp=11; IntAct=EBI-1039152, EBI-346930;
Q92569:PIK3R3; NbExp=11; IntAct=EBI-1039152, EBI-79893;
P19174:PLCG1; NbExp=10; IntAct=EBI-1039152, EBI-79387;
O43157:PLXNB1; NbExp=7; IntAct=EBI-1039152, EBI-1111488;
O15031:PLXNB2; NbExp=2; IntAct=EBI-1039152, EBI-722004;
Q9ULL4:PLXNB3; NbExp=2; IntAct=EBI-1039152, EBI-311073;
Q00944:PTK2 (xeno); NbExp=5; IntAct=EBI-1039152, EBI-2896409;
P18031:PTPN1; NbExp=3; IntAct=EBI-1039152, EBI-968788;
Q06124:PTPN11; NbExp=13; IntAct=EBI-1039152, EBI-297779;
P23467:PTPRB; NbExp=2; IntAct=EBI-1039152, EBI-1265766;
Q12913:PTPRJ; NbExp=5; IntAct=EBI-1039152, EBI-2264500;
Q16827:PTPRO; NbExp=2; IntAct=EBI-1039152, EBI-723739;
P20936:RASA1; NbExp=15; IntAct=EBI-1039152, EBI-1026476;
Q9UQQ2:SH2B3; NbExp=2; IntAct=EBI-1039152, EBI-7879749;
O60880:SH2D1A; NbExp=3; IntAct=EBI-1039152, EBI-6983382;
O14796:SH2D1B; NbExp=6; IntAct=EBI-1039152, EBI-3923013;
Q9NP31:SH2D2A; NbExp=7; IntAct=EBI-1039152, EBI-490630;
Q8N5H7:SH2D3C; NbExp=4; IntAct=EBI-1039152, EBI-745980;
Q15464:SHB; NbExp=4; IntAct=EBI-1039152, EBI-4402156;
P29353:SHC1; NbExp=5; IntAct=EBI-1039152, EBI-78835;
P98077:SHC2; NbExp=2; IntAct=EBI-1039152, EBI-7256023;
Q6S5L8:SHC4; NbExp=3; IntAct=EBI-1039152, EBI-9453524;
Q96IW2:SHD; NbExp=2; IntAct=EBI-1039152, EBI-4402781;
Q9H6Q3:SLA2; NbExp=4; IntAct=EBI-1039152, EBI-1222854;
O75159:SOCS5; NbExp=2; IntAct=EBI-1039152, EBI-970130;
O14544:SOCS6; NbExp=4; IntAct=EBI-1039152, EBI-3929549;
P12931:SRC; NbExp=4; IntAct=EBI-1039152, EBI-621482;
Q9ULZ2:STAP1; NbExp=3; IntAct=EBI-1039152, EBI-6083058;
P43405:SYK; NbExp=3; IntAct=EBI-1039152, EBI-78302;
P42680:TEC; NbExp=2; IntAct=EBI-1039152, EBI-1383480;
Q9HBL0:TNS1; NbExp=2; IntAct=EBI-1039152, EBI-3389814;
Q63HR2:TNS2; NbExp=2; IntAct=EBI-1039152, EBI-949753;
Q68CZ2:TNS3; NbExp=3; IntAct=EBI-1039152, EBI-1220488;
Q9UKW4:VAV3; NbExp=2; IntAct=EBI-1039152, EBI-297568;
P07947:YES1; NbExp=3; IntAct=EBI-1039152, EBI-515331;
P43403:ZAP70; NbExp=2; IntAct=EBI-1039152, EBI-1211276;
-!- 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;
Note=No experimental confirmation available.;
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}.
-!- 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";
-----------------------------------------------------------------------
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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]
UniGene; Hs.132966; -.
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; 5UAF; X-ray; 2.25 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; 5UAF; -.
ProteinModelPortal; P08581; -.
SMR; P08581; -.
BioGrid; 110391; 46.
CORUM; P08581; -.
DIP; DIP-6023N; -.
ELM; P08581; -.
IntAct; P08581; 90.
MINT; MINT-4837114; -.
STRING; 9606.ENSP00000317272; -.
BindingDB; P08581; -.
ChEMBL; CHEMBL3717; -.
DrugBank; DB07969; 3-[3-(4-methylpiperazin-1-yl)-7-(trifluoromethyl)quinoxalin-5-yl]phenol.
DrugBank; DB08875; Cabozantinib.
DrugBank; DB08865; Crizotinib.
DrugBank; DB02152; K-252a.
DrugBank; DB05216; MP470.
DrugBank; DB06995; N-({4-[(2-aminopyridin-4-yl)oxy]-3-fluorophenyl}carbamoyl)-2-(4-fluorophenyl)acetamide.
DrugBank; DB05153; XL184.
GuidetoPHARMACOLOGY; 1815; -.
iPTMnet; P08581; -.
PhosphoSitePlus; P08581; -.
SwissPalm; P08581; -.
UniCarbKB; P08581; -.
BioMuta; MET; -.
DMDM; 251757497; -.
OGP; P08581; -.
EPD; P08581; -.
MaxQB; P08581; -.
PaxDb; P08581; -.
PeptideAtlas; P08581; -.
PRIDE; P08581; -.
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; CAB005282; -.
HPA; CAB018577; -.
HPA; HPA055607; -.
MalaCards; MET; -.
MIM; 114550; phenotype.
MIM; 164860; gene.
MIM; 605074; phenotype.
MIM; 607278; phenotype.
MIM; 616705; phenotype.
neXtProt; NX_P08581; -.
OpenTargets; ENSG00000105976; -.
Orphanet; 106; Autism.
Orphanet; 47044; Familial papillary renal cell carcinoma.
PharmGKB; PA30763; -.
eggNOG; KOG1095; Eukaryota.
eggNOG; KOG3610; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00810000125384; -.
HOGENOM; HOG000220900; -.
HOVERGEN; HBG006348; -.
InParanoid; P08581; -.
KO; K05099; -.
OMA; QCPDCVV; -.
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.
SignaLink; P08581; -.
SIGNOR; P08581; -.
ChiTaRS; MET; human.
EvolutionaryTrace; P08581; -.
GeneWiki; C-Met; -.
GenomeRNAi; 4233; -.
PRO; PR:P08581; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000105976; -.
CleanEx; HS_MET; -.
ExpressionAtlas; P08581; baseline and differential.
Genevisible; P08581; HS.
GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA: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; TAS:ProtInc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005008; F:hepatocyte growth factor-activated receptor activity; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
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:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
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:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IMP:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:CAFA.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT.
InterPro; IPR011009; Kinase-like_dom_sf.
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.
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; Complete proteome; 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 {ECO:0000255}.
CHAIN 25 1390 Hepatocyte growth factor receptor.
/FTId=PRO_0000024440.
TOPO_DOM 25 932 Extracellular. {ECO:0000255}.
TRANSMEM 933 955 Helical. {ECO:0000255}.
TOPO_DOM 956 1390 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 515 Sema. {ECO:0000255|PROSITE-
ProRule:PRU00352}.
DOMAIN 563 655 IPT/TIG 1.
DOMAIN 657 739 IPT/TIG 2.
DOMAIN 742 836 IPT/TIG 3.
DOMAIN 1078 1345 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1084 1092 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1212 1390 Interaction with RANBP9.
REGION 1320 1359 Interaction with MUC20.
{ECO:0000269|PubMed:15314156}.
ACT_SITE 1204 1204 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 1110 1110 ATP.
SITE 307 308 Cleavage. {ECO:0000255}.
SITE 1003 1003 Required for ligand-induced CBL-mediated
ubiquitination.
{ECO:0000269|PubMed:12244174}.
SITE 1009 1010 Breakpoint for translocation to form TPR-
MET oncogene.
MOD_RES 966 966 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 977 977 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 990 990 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 997 997 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1000 1000 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1003 1003 Phosphotyrosine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 1230 1230 Phosphotyrosine.
{ECO:0000269|PubMed:12475979}.
MOD_RES 1234 1234 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12475979}.
MOD_RES 1235 1235 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12475979,
ECO:0000269|PubMed:1655790}.
MOD_RES 1289 1289 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 1349 1349 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12475979,
ECO:0000269|PubMed:7513258}.
MOD_RES 1356 1356 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15735664,
ECO:0000269|PubMed:7513258}.
MOD_RES 1365 1365 Phosphotyrosine.
{ECO:0000269|PubMed:12475979}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19196183}.
CARBOHYD 149 149 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 405 405 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 607 607 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 635 635 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 785 785 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 879 879 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 930 930 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 95 101
DISULFID 98 160
DISULFID 133 141
DISULFID 172 175
DISULFID 298 363
DISULFID 385 397
DISULFID 520 538
DISULFID 526 561
DISULFID 529 545
DISULFID 541 551
VAR_SEQ 755 764 SGGSTITGVG -> RHVNIALIQR (in isoform 3).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_042447.
VAR_SEQ 755 755 S -> STWWKEPLNIVSFLFCFAS (in isoform 2).
{ECO:0000303|PubMed:2819873}.
/FTId=VSP_005005.
VAR_SEQ 765 1390 Missing (in isoform 3).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_042448.
VARIANT 143 143 R -> Q (in dbSNP:rs35469582).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041738.
VARIANT 150 150 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).
{ECO:0000269|PubMed:20949619}.
/FTId=VAR_064855.
VARIANT 156 156 S -> L (in dbSNP:rs56311081).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041739.
VARIANT 168 168 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).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:20949619}.
/FTId=VAR_041740.
VARIANT 238 238 L -> S (in dbSNP:rs34349517).
/FTId=VAR_032478.
VARIANT 316 316 I -> M (in dbSNP:rs35225896).
/FTId=VAR_032479.
VARIANT 320 320 A -> V (in dbSNP:rs35776110).
{ECO:0000269|PubMed:9140397}.
/FTId=VAR_006285.
VARIANT 375 375 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).
{ECO:0000269|PubMed:28294470}.
/FTId=VAR_079370.
VARIANT 375 375 N -> S (in dbSNP:rs33917957).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_032480.
VARIANT 385 385 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).
{ECO:0000269|PubMed:20949619}.
/FTId=VAR_064856.
VARIANT 773 773 P -> L (in gastric cancer;
dbSNP:rs771333219).
{ECO:0000269|PubMed:12920089}.
/FTId=VAR_032481.
VARIANT 841 841 F -> V (in DFNB97; dbSNP:rs794728016).
{ECO:0000269|PubMed:25941349}.
/FTId=VAR_075757.
VARIANT 964 1010 Missing (in OSFD; loss of CBL-mediated
destabilization).
{ECO:0000269|PubMed:26637977}.
/FTId=VAR_076584.
VARIANT 970 970 R -> C (in dbSNP:rs34589476).
{ECO:0000269|PubMed:17053076,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_032482.
VARIANT 991 991 P -> S (in gastric cancer; prolonged
tyrosine phosphorylation in response to
HGF/SF; transforming activity in athymic
nude mice; dbSNP:rs768678989).
{ECO:0000269|PubMed:11042681}.
/FTId=VAR_032483.
VARIANT 992 992 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).
{ECO:0000269|PubMed:11042681,
ECO:0000269|PubMed:17053076,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:20949619}.
/FTId=VAR_032484.
VARIANT 1003 1003 Y -> S (probable disease-associated
mutation 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).
{ECO:0000269|PubMed:12244174}.
/FTId=VAR_076585.
VARIANT 1092 1092 V -> I (in RCCP; constitutive
autophosphorylation; dbSNP:rs786202724).
{ECO:0000269|PubMed:10327054,
ECO:0000269|PubMed:10417759,
ECO:0000269|PubMed:10433944}.
/FTId=VAR_032485.
VARIANT 1094 1094 H -> L (in RCCP; constitutive
autophosphorylation; causes malignant
transformation in cell lines).
{ECO:0000269|PubMed:10327054}.
/FTId=VAR_032486.
VARIANT 1094 1094 H -> R (in RCCP; causes malignant
transformation in cell lines;
dbSNP:rs121913243).
{ECO:0000269|PubMed:10433944,
ECO:0000269|PubMed:9563489}.
/FTId=VAR_032487.
VARIANT 1094 1094 H -> Y (in RCCP; constitutive
autophosphorylation; causes malignant
transformation in cell lines;
dbSNP:rs121913244).
{ECO:0000269|PubMed:10327054}.
/FTId=VAR_032488.
VARIANT 1106 1106 H -> D (in RCCP; constitutive
autophosphorylation; causes malignant
transformation in cell lines).
{ECO:0000269|PubMed:10327054,
ECO:0000269|PubMed:10433944}.
/FTId=VAR_032489.
VARIANT 1131 1131 M -> T (in RCCP; germline mutation;
dbSNP:rs121913668).
{ECO:0000269|PubMed:10433944,
ECO:0000269|PubMed:9140397}.
/FTId=VAR_006286.
VARIANT 1173 1173 T -> I (in HCC; dbSNP:rs121913675).
{ECO:0000269|PubMed:9927037}.
/FTId=VAR_032490.
VARIANT 1188 1188 V -> L (in RCCP; germline mutation;
dbSNP:rs121913669).
{ECO:0000269|PubMed:10433944,
ECO:0000269|PubMed:9140397}.
/FTId=VAR_006287.
VARIANT 1195 1195 L -> V (in RCCP; somatic mutation;
dbSNP:rs121913673).
{ECO:0000269|PubMed:9140397}.
/FTId=VAR_006288.
VARIANT 1220 1220 V -> I (in RCCP; germline mutation;
dbSNP:rs121913670).
{ECO:0000269|PubMed:9140397}.
/FTId=VAR_006289.
VARIANT 1228 1228 D -> H (in RCCP; somatic mutation).
{ECO:0000269|PubMed:9140397}.
/FTId=VAR_006291.
VARIANT 1228 1228 D -> N (in RCCP; germline mutation;
dbSNP:rs121913671).
{ECO:0000269|PubMed:9140397}.
/FTId=VAR_006290.
VARIANT 1230 1230 Y -> C (in RCCP; germline mutation;
dbSNP:rs121913246).
{ECO:0000269|PubMed:10433944,
ECO:0000269|PubMed:9140397}.
/FTId=VAR_006292.
VARIANT 1230 1230 Y -> D (in RCCP; constitutive
autophosphorylation; causes malignant
transformation in cell lines).
{ECO:0000269|PubMed:10327054,
ECO:0000269|PubMed:10433944}.
/FTId=VAR_032491.
VARIANT 1230 1230 Y -> H (in RCCP; somatic mutation;
dbSNP:rs121913247).
{ECO:0000269|PubMed:9140397}.
/FTId=VAR_006293.
VARIANT 1244 1244 K -> R (in HCC; dbSNP:rs121913677).
{ECO:0000269|PubMed:9927037}.
/FTId=VAR_032492.
VARIANT 1250 1250 M -> I (in HCC; dbSNP:rs121913676).
{ECO:0000269|PubMed:9927037}.
/FTId=VAR_032493.
VARIANT 1250 1250 M -> T (in RCCP; somatic mutation;
dbSNP:rs121913245).
{ECO:0000269|PubMed:10433944,
ECO:0000269|PubMed:9140397}.
/FTId=VAR_006294.
VARIANT 1294 1294 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).
{ECO:0000269|PubMed:20949619}.
/FTId=VAR_064857.
MUTAGEN 1234 1234 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.
{ECO:0000269|PubMed:12244174,
ECO:0000269|PubMed:18819921}.
MUTAGEN 1235 1235 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.
{ECO:0000269|PubMed:12244174,
ECO:0000269|PubMed:18819921}.
MUTAGEN 1313 1313 Y->F: No effect on ligand-induced CBL-
mediated ubiquitination; when associated
with F-1349, F-1356 and F-1365.
{ECO:0000269|PubMed:12244174}.
MUTAGEN 1349 1349 Y->F: No effect on ligand-induced CBL-
mediated ubiquitination; when associated
with F-1313, F-1356 and F-1365.
{ECO:0000269|PubMed:12244174}.
MUTAGEN 1356 1356 Y->F: No effect on ligand-induced CBL-
mediated ubiquitination; when associated
with F-1313, F-1349 and F-1365.
{ECO:0000269|PubMed:12244174}.
MUTAGEN 1365 1365 Y->F: No effect on ligand-induced CBL-
mediated ubiquitination; when associated
with F-1313, F-1349 and F-1356.
{ECO:0000269|PubMed:12244174}.
CONFLICT 237 237 V -> A (in Ref. 3; ACF47606).
{ECO:0000305}.
CONFLICT 508 508 K -> R (in Ref. 3; ACF47606).
{ECO:0000305}.
CONFLICT 720 720 F -> S (in Ref. 3; ACF47606).
{ECO:0000305}.
CONFLICT 1191 1191 G -> A (in Ref. 1; AAA59591).
{ECO:0000305}.
CONFLICT 1272 1272 L -> V (in Ref. 1; AAA59591, 2; CAB56793
and 6; AAA59590). {ECO:0000305}.
HELIX 25 30 {ECO:0000244|PDB:5LSP}.
STRAND 45 47 {ECO:0000244|PDB:2UZX}.
STRAND 52 58 {ECO:0000244|PDB:2UZX}.
STRAND 61 66 {ECO:0000244|PDB:2UZX}.
STRAND 69 74 {ECO:0000244|PDB:2UZX}.
TURN 75 77 {ECO:0000244|PDB:2UZX}.
STRAND 80 84 {ECO:0000244|PDB:2UZX}.
STRAND 89 91 {ECO:0000244|PDB:4K3J}.
STRAND 93 95 {ECO:0000244|PDB:4K3J}.
STRAND 97 99 {ECO:0000244|PDB:1SHY}.
HELIX 103 105 {ECO:0000244|PDB:4O3T}.
STRAND 111 113 {ECO:0000244|PDB:4K3J}.
STRAND 119 123 {ECO:0000244|PDB:2UZX}.
STRAND 125 133 {ECO:0000244|PDB:2UZX}.
STRAND 135 139 {ECO:0000244|PDB:2UZX}.
STRAND 141 145 {ECO:0000244|PDB:2UZX}.
STRAND 155 160 {ECO:0000244|PDB:4K3J}.
STRAND 182 189 {ECO:0000244|PDB:2UZX}.
STRAND 192 199 {ECO:0000244|PDB:2UZX}.
STRAND 213 219 {ECO:0000244|PDB:2UZX}.
HELIX 231 233 {ECO:0000244|PDB:2UZX}.
HELIX 239 241 {ECO:0000244|PDB:2UZX}.
TURN 242 244 {ECO:0000244|PDB:2UZX}.
STRAND 247 255 {ECO:0000244|PDB:2UZX}.
STRAND 258 268 {ECO:0000244|PDB:2UZX}.
STRAND 272 274 {ECO:0000244|PDB:2UZX}.
STRAND 277 281 {ECO:0000244|PDB:2UZX}.
STRAND 284 286 {ECO:0000244|PDB:2UZX}.
STRAND 292 300 {ECO:0000244|PDB:2UZX}.
STRAND 312 314 {ECO:0000244|PDB:2UZX}.
STRAND 316 323 {ECO:0000244|PDB:2UZX}.
HELIX 327 333 {ECO:0000244|PDB:2UZX}.
STRAND 341 349 {ECO:0000244|PDB:2UZX}.
STRAND 356 366 {ECO:0000244|PDB:2UZX}.
HELIX 367 374 {ECO:0000244|PDB:2UZX}.
HELIX 380 382 {ECO:0000244|PDB:4K3J}.
STRAND 383 385 {ECO:0000244|PDB:4K3J}.
HELIX 387 390 {ECO:0000244|PDB:2UZX}.
STRAND 392 394 {ECO:0000244|PDB:1SHY}.
TURN 395 397 {ECO:0000244|PDB:4O3T}.
STRAND 418 422 {ECO:0000244|PDB:2UZX}.
STRAND 424 427 {ECO:0000244|PDB:2UZX}.
TURN 429 436 {ECO:0000244|PDB:2UZX}.
STRAND 439 447 {ECO:0000244|PDB:2UZX}.
STRAND 450 457 {ECO:0000244|PDB:2UZX}.
STRAND 462 466 {ECO:0000244|PDB:2UZX}.
STRAND 469 471 {ECO:0000244|PDB:4K3J}.
STRAND 476 480 {ECO:0000244|PDB:4K3J}.
STRAND 490 493 {ECO:0000244|PDB:2UZX}.
TURN 496 498 {ECO:0000244|PDB:4O3T}.
STRAND 501 506 {ECO:0000244|PDB:2UZX}.
STRAND 509 514 {ECO:0000244|PDB:2UZX}.
HELIX 520 522 {ECO:0000244|PDB:5LSP}.
HELIX 526 529 {ECO:0000244|PDB:5LSP}.
HELIX 534 536 {ECO:0000244|PDB:5LSP}.
STRAND 539 541 {ECO:0000244|PDB:5LSP}.
STRAND 544 546 {ECO:0000244|PDB:5LSP}.
HELIX 548 550 {ECO:0000244|PDB:5LSP}.
STRAND 552 554 {ECO:0000244|PDB:2UZX}.
STRAND 557 559 {ECO:0000244|PDB:5LSP}.
STRAND 564 574 {ECO:0000244|PDB:5LSP}.
STRAND 580 586 {ECO:0000244|PDB:5LSP}.
STRAND 589 592 {ECO:0000244|PDB:5LSP}.
STRAND 595 598 {ECO:0000244|PDB:5LSP}.
STRAND 602 605 {ECO:0000244|PDB:5LSP}.
HELIX 614 616 {ECO:0000244|PDB:5LSP}.
STRAND 619 625 {ECO:0000244|PDB:5LSP}.
STRAND 633 641 {ECO:0000244|PDB:5LSP}.
STRAND 646 655 {ECO:0000244|PDB:5LSP}.
STRAND 658 663 {ECO:0000244|PDB:5LSP}.
STRAND 665 668 {ECO:0000244|PDB:5LSP}.
STRAND 674 681 {ECO:0000244|PDB:5LSP}.
STRAND 688 692 {ECO:0000244|PDB:5LSP}.
STRAND 698 702 {ECO:0000244|PDB:5LSP}.
STRAND 704 710 {ECO:0000244|PDB:5LSP}.
STRAND 718 726 {ECO:0000244|PDB:5LSP}.
STRAND 729 739 {ECO:0000244|PDB:5LSP}.
HELIX 1048 1050 {ECO:0000244|PDB:4EEV}.
HELIX 1055 1057 {ECO:0000244|PDB:3F66}.
HELIX 1060 1066 {ECO:0000244|PDB:4R1V}.
HELIX 1067 1069 {ECO:0000244|PDB:4R1V}.
HELIX 1073 1075 {ECO:0000244|PDB:4R1V}.
STRAND 1076 1087 {ECO:0000244|PDB:4R1V}.
STRAND 1090 1098 {ECO:0000244|PDB:4R1V}.
STRAND 1100 1102 {ECO:0000244|PDB:4EEV}.
STRAND 1104 1111 {ECO:0000244|PDB:4R1V}.
HELIX 1118 1132 {ECO:0000244|PDB:4R1V}.
STRAND 1144 1146 {ECO:0000244|PDB:4R1V}.
STRAND 1149 1151 {ECO:0000244|PDB:3F66}.
STRAND 1154 1158 {ECO:0000244|PDB:4R1V}.
HELIX 1165 1170 {ECO:0000244|PDB:4R1V}.
TURN 1172 1174 {ECO:0000244|PDB:3ZCL}.
HELIX 1178 1197 {ECO:0000244|PDB:4R1V}.
HELIX 1207 1209 {ECO:0000244|PDB:4R1V}.
STRAND 1210 1212 {ECO:0000244|PDB:4R1V}.
STRAND 1218 1220 {ECO:0000244|PDB:4R1V}.
HELIX 1224 1226 {ECO:0000244|PDB:4R1V}.
HELIX 1232 1234 {ECO:0000244|PDB:4R1V}.
STRAND 1236 1238 {ECO:0000244|PDB:4KNB}.
TURN 1239 1241 {ECO:0000244|PDB:4R1V}.
STRAND 1243 1245 {ECO:0000244|PDB:4KNB}.
HELIX 1247 1249 {ECO:0000244|PDB:4R1V}.
HELIX 1252 1257 {ECO:0000244|PDB:4R1V}.
HELIX 1262 1277 {ECO:0000244|PDB:4R1V}.
STRAND 1283 1287 {ECO:0000244|PDB:4EEV}.
HELIX 1289 1291 {ECO:0000244|PDB:4R1V}.
HELIX 1292 1297 {ECO:0000244|PDB:4R1V}.
HELIX 1310 1319 {ECO:0000244|PDB:4R1V}.
HELIX 1324 1326 {ECO:0000244|PDB:4R1V}.
HELIX 1330 1342 {ECO:0000244|PDB:4R1V}.
TURN 1354 1358 {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


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