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UniProtKB/Swiss-Prot entry P08581

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MET_HUMAN
Primary accession number P08581
Secondary accession numbers O60366 Q12875 Q9UDX7 Q9UPL8
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on December 1, 1992 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 135)
Name and origin of the protein
Protein name Hepatocyte growth factor receptor [Precursor]
Synonyms HGF receptor
EC 2.7.10.1
Scatter factor receptor
SF receptor
HGF/SF receptor
Met proto-oncogene tyrosine kinase
c-Met
Gene name
Name: MET
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1073/pnas.84.18.6379; PubMed=2819873 [NCBI, ExPASy, EBI, Israel, Japan]
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 [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1010-1390.
PubMed=3325883 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1206-1264.
PubMed=8247543 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1267-1390.
DOI=10.1038/318385a0; PubMed=4069211 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
 FUNCTION.
DOI=10.1126/science.1846706; PubMed=1846706 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
 PHOSPHORYLATION AT TYR-1235, AND ATP-BINDING SITE LYS-1110.
PubMed=1655790 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
 INTERACTION WITH RANBP9.
DOI=10.1074/jbc.M205111200; PubMed=12147692 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
 INTERACTION WITH PLXNB1.
DOI=10.1038/ncb843; PubMed=12198496 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
 INTERACTION WITH RANBP9 AND RANBP10.
DOI=10.1016/j.bbrc.2003.11.124; PubMed=14684163 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
 FUNCTION, AND INTERACTION WITH MUC20.
DOI=10.1128/MCB.24.17.7456-7468.2004; PubMed=15314156 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
 PHOSPHORYLATION AT TYR-1356, AND INTERACTION WITH INPPL1.
DOI=10.1038/sj.onc.1208558; PubMed=15735664 [NCBI, ExPASy, EBI, Israel, Japan]
Koch A., Mancini A., El Bounkari O., Tamura T.;
"The SH2-domian-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).
[14]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1003; TYR-1230; TYR-1234 AND TYR-1235, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[15]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-977; SER-988; SER-990 AND TYR-1003, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[16]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-966; THR-977; SER-988; SER-990; SER-997; SER-1000 AND TYR-1003, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-990; SER-997 AND SER-1000, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[19]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106, AND MASS SPECTROMETRY.
DOI=10.1021/pr800826u; PubMed=19196183 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1356-1359 IN COMPLEX WITH GRB2.
DOI=10.1021/bi0012336; PubMed=11063574 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[21]
 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1049-1360 IN COMPLEX WITH INHIBITOR.
DOI=10.1073/pnas.1734128100; PubMed=14559966 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[22]
 VARIANTS HPRC THR-1131; LEU-1188; VAL-1195; ILE-1220; HIS-1228; ASN-1228; CYS-1230; HIS-1230 AND THR-1250, AND VARIANT VAL-320.
DOI=10.1038/ng0597-68; PubMed=9140397 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[23]
 VARIANT HPRC ARG-1094, AND CHARACTERIZATION OF VARIANT HPRC ARG-1094.
PubMed=9563489 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[24]
 VARIANTS HPRC ILE-1092; ARG-1094; ASP-1106; THR-1131; LEU-1188; ASP-1230; CYS-1230 AND THR-1250.
PubMed=10433944 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[25]
 VARIANTS HCC ILE-1173; ARG-1244 AND ILE-1250.
PubMed=9927037 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[26]
 VARIANT HPRC ILE-1092, AND CHARACTERIZATION OF VARIANT HPRC ILE-1092.
DOI=10.1002/(SICI)1097-0215(19990827)82:5<640::AID-IJC4>3.0.CO;2-6; PubMed=10417759 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[27]
 VARIANTS HPRC ILE-1092; LEU-1094; TYR-1094; ASP-1106 AND ASP-1230, AND CHARACTERIZATION OF VARIANTS HPRC ILE-1092; LEU-1094; TYR-1094; ASP-1106 AND ASP-1230.
DOI=10.1038/sj.onc.1202547; PubMed=10327054 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[28]
 VARIANT GASTRIC CANCER SER-991, VARIANT ILE-992, CHARACTERIZATION OF VARIANT GASTRIC CANCER SER-991, AND CHARACTERIZATION OF VARIANT ILE-992.
DOI=10.1038/sj.onc.1203874; PubMed=11042681 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[29]
 VARIANT GASTRIC CANCER LEU-773.
DOI=10.1136/jmg.40.8.e97; PubMed=12920089 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[30]
 INTERACTION WITH SPSB1; SPSB2; SPSB3 AND SPSB4.
DOI=10.1074/jbc.M413897200; PubMed=15713673 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[31]
 INVOLVEMENT IN SUSCEPTIBILITY TO AUTS9, AND VARIANTS CYS-970 AND ILE-992.
DOI=10.1073/pnas.0605296103; PubMed=17053076 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[32]
 VARIANTS [LARGE SCALE ANALYSIS] GLN-143; LEU-156; ASP-168; SER-375; CYS-970 AND ILE-992.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J02958; AAA59591.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54559; CAB56793.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002080; AAB54047.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002543; AAC60383.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004416; AAF66137.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U08818; AAB60323.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M35074; AAA59590.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00029273; -.
IPI00294528; -.
PIR A40175; TVHUME.
RefSeq NP_000236.2; -.
NP_001120972.1; -.
UniGene Hs.132966
3D structure databases
PDB
1FYR; X-ray; 2.40 A; I/J/K/L=1356-1359.[ExPASy / RCSB / EBI]
1R0P; X-ray; 1.80 A; A=1049-1360.[ExPASy / RCSB / EBI]
1R1W; X-ray; 1.80 A; A=1049-1360.[ExPASy / RCSB / EBI]
1SHY; X-ray; 3.22 A; B=25-567.[ExPASy / RCSB / EBI]
1SSL; NMR; -; A=519-562.[ExPASy / RCSB / EBI]
1UX3; Model; -; A=25-656.[ExPASy / RCSB / EBI]
2G15; X-ray; 2.15 A; A=1038-1346.[ExPASy / RCSB / EBI]
2RFN; X-ray; 2.50 A; A/B=1048-1351.[ExPASy / RCSB / EBI]
2RFS; X-ray; 2.20 A; A=1048-1351.[ExPASy / RCSB / EBI]
2UZX; X-ray; 2.80 A; B/D=25-740.[ExPASy / RCSB / EBI]
2UZY; X-ray; 4.00 A; B/D=25-740.[ExPASy / RCSB / EBI]
2WD1; X-ray; 2.00 A; A=1055-1346.[ExPASy / RCSB / EBI]
3BUX; X-ray; 1.35 A; A/C=997-1009.[ExPASy / RCSB / EBI]
3CE3; X-ray; 2.40 A; A=1049-1360.[ExPASy / RCSB / EBI]
3CTH; X-ray; 2.30 A; A=1049-1360.[ExPASy / RCSB / EBI]
3CTJ; X-ray; 2.50 A; A=1049-1360.[ExPASy / RCSB / EBI]
3EFJ; X-ray; 2.60 A; A/B=1048-1351.[ExPASy / RCSB / EBI]
3EFK; X-ray; 2.20 A; A/B=1048-1351.[ExPASy / RCSB / EBI]
3F66; X-ray; 1.40 A; A/B=1052-1349.[ExPASy / RCSB / EBI]
3F82; X-ray; 2.50 A; A=1049-1360.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FYR; -.
1R0P; -.
1R1W; -.
1SHY; -.
1SSL; -.
1UX3; -.
2G15; -.
2RFN; -.
2RFS; -.
2UZX; -.
2UZY; -.
2WD1; -.
3BUX; -.
3CE3; -.
3CTH; -.
3CTJ; -.
3EFJ; -.
3EFK; -.
3F66; -.
3F82; -.
DisProt DP00317; -.
ModBase P08581.
Protein-protein interaction databases
DIP DIP:6023N; -.
IntAct P08581; 11.
PTM databases
PhosphoSite P08581; -.
Enzyme and pathway databases
BRENDA 2.7.10.1; 247.
Pathway_Interaction_DB a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
arf6cyclingpathway; Arf6 signaling events.
faspathway; FAS signaling pathway (CD95).
fgf_pathway; FGF signaling pathway.
met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
syndecan_1_pathway; Syndecan-1-mediated signaling events.
2D gel databases
OGP P08581; -.
Organism-specific databases
GeneCards GC07P116099; -.
H-InvDB HIX0007019; -.
HGNC HGNC:7029; MET.
GenAtlas MET.
HPA CAB005282; -.
MIM 114550; phenotype. [NCBI / EBI]
164860; gene. [NCBI / EBI]
605074; phenotype. [NCBI / EBI]
611015; phenotype. [NCBI / EBI]
Orphanet 106; Autism.
33402; Hepatocellular carcinoma of childhood.
47044; Renal cell carcinoma, papillary, familial.
PharmGKB PA24993; -.
Gene expression databases
ArrayExpress P08581; -.
Bgee P08581; -.
CleanEx HS_MET; -.
GermOnline ENSG00000105976; Homo sapiens.
Ontologies
GO
GO:0009925; Cellular component: basal plasma membrane (inferred from direct assay from MGI).
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005008; Molecular function: hepatocyte growth factor receptor activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002909; IPT_TIG_rcpt.
IPR003659; Plexin-like.
IPR002165; Plexin_repeat.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR001627; Semaphorin/CD100_Ag.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
IPR016244; TyrPK_HGF-R.
IPR015943; WD40/YVTN_repeat-like.
Graphical view of domain structure.
Gene3D G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
Pfam PF07714; Pkinase_Tyr; 1.
PF01437; PSI; 1.
PF01403; Sema; 1.
PF01833; TIG; 3.
Pfam graphical view of domain structure.
PIRSF PIRSF000617; TyrPK_HGF-R; 1.
PRINTS PR00109; TYRKINASE.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00429; IPT; 4.
SM00423; PSI; 1.
SM00630; Sema; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS51004; SEMA; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P08581; -.
Genome annotation databases
Ensembl ENSG00000105976; Homo sapiens. [Contig view]
GeneID 4233; -.
KEGG hsa:4233; -.
Phylogenomic databases
HOGENOM P08581; -.
HOVERGEN P08581; -.
Other
NextBio 16689; -.
SOURCE MET; Homo sapiens.
ProtoNet P08581.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Chromosomal rearrangement; Disease mutation; Disulfide bond; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene; Receptor; Repeat; Signal; Transferase; Transmembrane; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     24  24     Potential. 
CHAIN   25   1390  1366     Hepatocyte growth factor receptor. PRO_0000024440
TOPO_DOM   25    932  908     Extracellular (Potential). 
TRANSMEM   933    955  23     Potential. 
TOPO_DOM   956   1390  435     Cytoplasmic (Potential). 
DOMAIN   27    515  489     Sema. 
DOMAIN   563    655  93     IPT/TIG 1. 
DOMAIN   657    739  83     IPT/TIG 2. 
DOMAIN   742    836  95     IPT/TIG 3. 
DOMAIN   1078   1345  268     Protein kinase. 
NP_BIND   1084   1092  9     ATP (By similarity). 
REGION   1212   1390  179     Interaction with RANBP9. 
REGION   1320   1359  40     Interaction with MUC20. 
ACT_SITE   1204   1204        Proton acceptor (By similarity). 
BINDING   1110   1110        ATP. 
SITE   307    308  2     Cleavage (Potential). 
SITE   1009   1010  2     Breakpoint for translocation to form TPR-MET oncogene. 
MOD_RES   966    966        Phosphoserine. 
MOD_RES   977    977        Phosphothreonine. 
MOD_RES   988    988        Phosphoserine. 
MOD_RES   990    990        Phosphoserine. 
MOD_RES   997    997        Phosphoserine. 
MOD_RES   1000   1000        Phosphoserine. 
MOD_RES   1003   1003        Phosphotyrosine. 
MOD_RES   1230   1230        Phosphotyrosine. 
MOD_RES   1234   1234        Phosphotyrosine. 
MOD_RES   1235   1235        Phosphotyrosine; by autocatalysis. 
MOD_RES   1356   1356        Phosphotyrosine. 
CARBOHYD   45     45        N-linked (GlcNAc...) (Potential). 
CARBOHYD   106    106        N-linked (GlcNAc...). 
CARBOHYD   149    149        N-linked (GlcNAc...) (Potential). 
CARBOHYD   202    202        N-linked (GlcNAc...). 
CARBOHYD   399    399        N-linked (GlcNAc...) (Potential). 
CARBOHYD   405    405        N-linked (GlcNAc...) (Potential). 
CARBOHYD   607    607        N-linked (GlcNAc...) (Potential). 
CARBOHYD   635    635        N-linked (GlcNAc...) (Potential). 
CARBOHYD   785    785        N-linked (GlcNAc...) (Potential). 
CARBOHYD   879    879        N-linked (GlcNAc...) (Potential). 
CARBOHYD   930    930        N-linked (GlcNAc...) (Potential). 
VAR_SEQ   755    755        S -> STWWKEPLNIVSFLFCFAS (in isoform 2). VSP_005005
VARIANT   143    143  1     R -> Q. VAR_041738 
VARIANT   156    156  1     S -> L. VAR_041739 
VARIANT   168    168  1     E -> D. VAR_041740 
VARIANT   238    238  1     L -> S (in dbSNP:rs34349517 [NCBI]). VAR_032478 
VARIANT   316    316  1     I -> M (in dbSNP:rs35225896 [NCBI]). VAR_032479 
VARIANT   320    320  1     A -> V (in dbSNP:rs35776110 [NCBI]). VAR_006285 
VARIANT   375    375  1     N -> S (in dbSNP:rs33917957 [NCBI]). VAR_032480 
VARIANT   773    773  1     P -> L (in gastric cancer). VAR_032481 
VARIANT   970    970  1     R -> C (in dbSNP:rs34589476 [NCBI]). VAR_032482 
VARIANT   991    991  1     P -> S (in gastric cancer; prolonged tyrosine phosphorylation in response to HGF/SF; transforming activity in athymic nude mice). VAR_032483 
VARIANT   992    992  1     T -> I (low transforming activity in athymic nude mice). VAR_032484 
VARIANT   1092   1092  1     V -> I (in HPRC; constitutive autophosphorylation). VAR_032485 [3D]
VARIANT   1094   1094  1     H -> L (in HPRC; constitutive autophosphorylation; causes malignant transformation in cell lines). VAR_032486 [3D]
VARIANT   1094   1094  1     H -> R (in HPRC; causes malignant transformation in cell lines). VAR_032487 [3D]
VARIANT   1094   1094  1     H -> Y (in HPRC; constitutive autophosphorylation; causes malignant transformation in cell lines). VAR_032488 [3D]
VARIANT   1106   1106  1     H -> D (in HPRC; constitutive autophosphorylation; causes malignant transformation in cell lines). VAR_032489 [3D]
VARIANT   1131   1131  1     M -> T (in HPRC; germline mutation). VAR_006286 [3D]
VARIANT   1173   1173  1     T -> I (in HCC). VAR_032490 [3D]
VARIANT   1188   1188  1     V -> L (in HPRC; germline mutation). VAR_006287 [3D]
VARIANT   1195   1195  1     L -> V (in HPRC; somatic mutation). VAR_006288 [3D]
VARIANT   1220   1220  1     V -> I (in HPRC; germline mutation). VAR_006289 [3D]
VARIANT   1228   1228  1     D -> H (in HPRC; somatic mutation). VAR_006291 [3D]
VARIANT   1228   1228  1     D -> N (in HPRC; germline mutation). VAR_006290 [3D]
VARIANT   1230   1230  1     Y -> C (in HPRC; germline mutation). VAR_006292 [3D]
VARIANT   1230   1230  1     Y -> D (in HPRC; constitutive autophosphorylation; causes malignant transformation in cell lines). VAR_032491 [3D]
VARIANT   1230   1230  1     Y -> H (in HPRC; somatic mutation). VAR_006293 [3D]
VARIANT   1244   1244  1     K -> R (in HCC). VAR_032492 [3D]
VARIANT   1250   1250  1     M -> I (in HCC). VAR_032493 [3D]
VARIANT   1250   1250  1     M -> T (in HPRC; somatic mutation). VAR_006294 [3D]
CONFLICT   1191   1191        G -> A (in Ref. 2; AAA59591). 
CONFLICT   1272   1272        V -> L (in Ref. 3; AAC60383 and 4). 
STRAND   45     47  3      
STRAND   52     58  7      
STRAND   61     66  6      
STRAND   69     74  6      
TURN   75     77  3      
STRAND   80     85  6      
STRAND   89     91  3      
STRAND   93     95  3      
STRAND   97     99  3      
STRAND   102    104  3      
STRAND   111    113  3      
STRAND   117    123  7      
STRAND   125    145  21      
STRAND   154    160  7      
STRAND   182    189  8      
STRAND   192    199  8      
STRAND   213    219  7      
HELIX   231    233  3      
HELIX   241    244  4      
STRAND   248    255  8      
STRAND   258    264  7      
STRAND   276    282  7      
STRAND   292    299  8      
STRAND   319    323  5      
HELIX   327    332  6      
STRAND   341    349  9      
STRAND   353    366  14      
HELIX   367    375  9      
TURN   387    389  3      
STRAND   392    394  3      
TURN   395    398  4      
STRAND   418    422  5      
STRAND   424    427  4      
TURN   431    436  6      
STRAND   439    447  9      
STRAND   450    457  8      
STRAND   460    466  7      
STRAND   469    471  3      
STRAND   486    495  10      
TURN   496    498  3      
STRAND   499    506  8      
STRAND   509    516  8      
HELIX   517    520  4      
HELIX   526    530  5      
HELIX   534    536  3      
STRAND   539    541  3      
STRAND   544    546  3      
HELIX   548    550  3      
HELIX   1055   1057  3      
HELIX   1060   1066  7      
HELIX   1067   1069  3      
HELIX   1073   1075  3      
STRAND   1076   1087  12      
STRAND   1090   1097  8      
STRAND   1105   1112  8      
HELIX   1118   1132  15      
STRAND   1144   1148  5      
TURN   1149   1151  3      
STRAND   1152   1158  7      
HELIX   1165   1170  6      
HELIX   1178   1197  20      
HELIX   1207   1209  3      
STRAND   1210   1212  3      
STRAND   1218   1220  3      
HELIX   1224   1226  3      
TURN   1229   1233  5      
HELIX   1247   1249  3      
HELIX   1252   1257  6      
HELIX   1262   1277  16      
HELIX   1293   1297  5      
HELIX   1310   1319  10      
HELIX   1324   1326  3      
HELIX   1330   1342  13      
TURN   1354   1358  5      
Sequence information
Length: 1390 AA [This is the length of the unprocessed precursor] Molecular weight: 155527 Da [This is the MW of the unprocessed precursor] CRC64: 96F896D13D390E04 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKAPAVLAPG ILVLLFTLVQ RSNGECKEAL AKSEMNVNMK YQLPNFTAET PIQNVILHEH 

        70         80         90        100        110        120 
HIFLGATNYI YVLNEEDLQK VAEYKTGPVL EHPDCFPCQD CSSKANLSGG VWKDNINMAL 

       130        140        150        160        170        180 
VVDTYYDDQL ISCGSVNRGT CQRHVFPHNH TADIQSEVHC IFSPQIEEPS QCPDCVVSAL 

       190        200        210        220        230        240 
GAKVLSSVKD RFINFFVGNT INSSYFPDHP LHSISVRRLK ETKDGFMFLT DQSYIDVLPE 

       250        260        270        280        290        300 
FRDSYPIKYV HAFESNNFIY FLTVQRETLD AQTFHTRIIR FCSINSGLHS YMEMPLECIL 

       310        320        330        340        350        360 
TEKRKKRSTK KEVFNILQAA YVSKPGAQLA RQIGASLNDD ILFGVFAQSK PDSAEPMDRS 

       370        380        390        400        410        420 
AMCAFPIKYV NDFFNKIVNK NNVRCLQHFY GPNHEHCFNR TLLRNSSGCE ARRDEYRTEF 

       430        440        450        460        470        480 
TTALQRVDLF MGQFSEVLLT SISTFIKGDL TIANLGTSEG RFMQVVVSRS GPSTPHVNFL 

       490        500        510        520        530        540 
LDSHPVSPEV IVEHTLNQNG YTLVITGKKI TKIPLNGLGC RHFQSCSQCL SAPPFVQCGW 

       550        560        570        580        590        600 
CHDKCVRSEE CLSGTWTQQI CLPAIYKVFP NSAPLEGGTR LTICGWDFGF RRNNKFDLKK 

       610        620        630        640        650        660 
TRVLLGNESC TLTLSESTMN TLKCTVGPAM NKHFNMSIII SNGHGTTQYS TFSYVDPVIT 

       670        680        690        700        710        720 
SISPKYGPMA GGTLLTLTGN YLNSGNSRHI SIGGKTCTLK SVSNSILECY TPAQTISTEF 

       730        740        750        760        770        780 
AVKLKIDLAN RETSIFSYRE DPIVYEIHPT KSFISGGSTI TGVGKNLNSV SVPRMVINVH 

       790        800        810        820        830        840 
EAGRNFTVAC QHRSNSEIIC CTTPSLQQLN LQLPLKTKAF FMLDGILSKY FDLIYVHNPV 

       850        860        870        880        890        900 
FKPFEKPVMI SMGNENVLEI KGNDIDPEAV KGEVLKVGNK SCENIHLHSE AVLCTVPNDL 

       910        920        930        940        950        960 
LKLNSELNIE WKQAISSTVL GKVIVQPDQN FTGLIAGVVS ISTALLLLLG FFLWLKKRKQ 

       970        980        990       1000       1010       1020 
IKDLGSELVR YDARVHTPHL DRLVSARSVS PTTEMVSNES VDYRATFPED QFPNSSQNGS 

      1030       1040       1050       1060       1070       1080 
CRQVQYPLTD MSPILTSGDS DISSPLLQNT VHIDLSALNP ELVQAVQHVV IGPSSLIVHF 

      1090       1100       1110       1120       1130       1140 
NEVIGRGHFG CVYHGTLLDN DGKKIHCAVK SLNRITDIGE VSQFLTEGII MKDFSHPNVL 

      1150       1160       1170       1180       1190       1200 
SLLGICLRSE GSPLVVLPYM KHGDLRNFIR NETHNPTVKD LIGFGLQVAK GMKYLASKKF 

      1210       1220       1230       1240       1250       1260 
VHRDLAARNC MLDEKFTVKV ADFGLARDMY DKEYYSVHNK TGAKLPVKWM ALESLQTQKF 

      1270       1280       1290       1300       1310       1320 
TTKSDVWSFG VVLWELMTRG APPYPDVNTF DITVYLLQGR RLLQPEYCPD PLYEVMLKCW 

      1330       1340       1350       1360       1370       1380 
HPKAEMRPSF SELVSRISAI FSTFIGEHYV HVNATYVNVK CVAPYPSLLS SEDNADDEVD 

      1390 
TRPASFWETS
P08581 in FASTA format

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