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P08581

- MET_HUMAN

UniProt

P08581 - MET_HUMAN

Protein

Hepatocyte growth factor receptor

Gene

MET

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 199 (01 Oct 2014)
      Sequence version 4 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    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.
    Acts as a receptor for Listeria internalin inlB, mediating entry of the pathogen into cells.

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei307 – 3082CleavageSequence Analysis
    Sitei1009 – 10102Breakpoint for translocation to form TPR-MET oncogene
    Binding sitei1110 – 11101ATP
    Active sitei1204 – 12041Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1084 – 10929ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hepatocyte growth factor-activated receptor activity Source: ProtInc
    3. protein binding Source: UniProtKB
    4. protein phosphatase binding Source: UniProtKB
    5. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: Ensembl
    2. adult behavior Source: Ensembl
    3. axon guidance Source: Reactome
    4. brain development Source: Ensembl
    5. branching morphogenesis of an epithelial tube Source: UniProtKB
    6. cell proliferation Source: ProtInc
    7. cell surface receptor signaling pathway Source: UniProtKB
    8. glucose homeostasis Source: Ensembl
    9. liver development Source: Ensembl
    10. muscle cell migration Source: Ensembl
    11. myoblast proliferation Source: Ensembl
    12. myotube differentiation Source: Ensembl
    13. negative regulation of hydrogen peroxide-mediated programmed cell death Source: BHF-UCL
    14. peptidyl-tyrosine phosphorylation Source: GOC
    15. placenta development Source: Ensembl
    16. positive chemotaxis Source: UniProtKB
    17. positive regulation of endothelial cell chemotaxis Source: UniProtKB
    18. positive regulation of glucose transport Source: Ensembl
    19. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    20. protein autophosphorylation Source: Ensembl
    21. regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling Source: Ensembl
    22. semaphorin-plexin signaling pathway Source: UniProtKB
    23. signal transduction Source: ProtInc
    24. skeletal muscle tissue development Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    ReactomeiREACT_19266. Sema4D mediated inhibition of cell attachment and migration.
    SignaLinkiP08581.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hepatocyte growth factor receptor (EC:2.7.10.1)
    Short name:
    HGF receptor
    Alternative name(s):
    HGF/SF receptor
    Proto-oncogene c-Met
    Scatter factor receptor
    Short name:
    SF receptor
    Tyrosine-protein kinase Met
    Gene namesi
    Name:MET
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:7029. MET.

    Subcellular locationi

    GO - Cellular componenti

    1. basal plasma membrane Source: MGI
    2. extracellular region Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB
    4. integral component of plasma membrane Source: ProtInc
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Activation of MET after rearrangement with the TPR gene produces an oncogenic protein.
    Defects in MET may be associated with gastric cancer.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1173 – 11731T → I in HCC. 1 Publication
    VAR_032490
    Natural varianti1244 – 12441K → R in HCC. 1 Publication
    VAR_032492
    Natural varianti1250 – 12501M → I in HCC. 1 Publication
    VAR_032493
    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.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1092 – 10921V → I in RCCP; constitutive autophosphorylation. 3 Publications
    VAR_032485
    Natural varianti1094 – 10941H → L in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 1 Publication
    VAR_032486
    Natural varianti1094 – 10941H → R in RCCP; causes malignant transformation in cell lines. 2 Publications
    VAR_032487
    Natural varianti1094 – 10941H → Y in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 1 Publication
    VAR_032488
    Natural varianti1106 – 11061H → D in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 2 Publications
    VAR_032489
    Natural varianti1131 – 11311M → T in RCCP; germline mutation. 2 Publications
    VAR_006286
    Natural varianti1188 – 11881V → L in RCCP; germline mutation. 2 Publications
    VAR_006287
    Natural varianti1195 – 11951L → V in RCCP; somatic mutation. 1 Publication
    VAR_006288
    Natural varianti1220 – 12201V → I in RCCP; germline mutation. 1 Publication
    VAR_006289
    Natural varianti1228 – 12281D → H in RCCP; somatic mutation. 1 Publication
    VAR_006291
    Natural varianti1228 – 12281D → N in RCCP; germline mutation. 1 Publication
    VAR_006290
    Natural varianti1230 – 12301Y → C in RCCP; germline mutation. 2 Publications
    VAR_006292
    Natural varianti1230 – 12301Y → D in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 2 Publications
    VAR_032491
    Natural varianti1230 – 12301Y → H in RCCP; somatic mutation. 1 Publication
    VAR_006293
    Natural varianti1250 – 12501M → T in RCCP; somatic mutation. 2 Publications
    VAR_006294
    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.
    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1234 – 12341Y → F: Alters interaction with PTPN1 and PTPN2. Loss of interaction with PTPN1 and PTPN2; when associated with F-1235. 1 Publication
    Mutagenesisi1235 – 12351Y → F: Alters interaction with PTPN1 and PTPN2. Loss of interaction with PTPN1 and PTPN2; when associated with F-1234. 1 Publication

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi114550. phenotype.
    605074. phenotype.
    Orphaneti106. Autism.
    47044. Familial papillary renal cell carcinoma.
    33402. Hepatocellular carcinoma, childhood-onset.
    PharmGKBiPA30763.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 13901366Hepatocyte growth factor receptorPRO_0000024440Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi95 ↔ 101
    Disulfide bondi98 ↔ 160
    Glycosylationi106 – 1061N-linked (GlcNAc...)1 Publication
    Disulfide bondi133 ↔ 141
    Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi172 ↔ 175
    Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi298 ↔ 363
    Disulfide bondi385 ↔ 397
    Glycosylationi399 – 3991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi520 ↔ 538
    Disulfide bondi526 ↔ 561
    Disulfide bondi529 ↔ 545
    Disulfide bondi541 ↔ 551
    Glycosylationi607 – 6071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi635 – 6351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi785 – 7851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi879 – 8791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi930 – 9301N-linked (GlcNAc...)Sequence Analysis
    Modified residuei977 – 9771Phosphothreonine2 Publications
    Modified residuei990 – 9901Phosphoserine2 Publications
    Modified residuei997 – 9971Phosphoserine2 Publications
    Modified residuei1000 – 10001Phosphoserine2 Publications
    Modified residuei1003 – 10031Phosphotyrosine3 Publications
    Modified residuei1230 – 12301Phosphotyrosine2 Publications
    Modified residuei1234 – 12341Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei1235 – 12351Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei1289 – 12891Phosphothreonine2 Publications
    Modified residuei1349 – 13491Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei1356 – 13561Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei1365 – 13651Phosphotyrosine2 Publications

    Post-translational modificationi

    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 PTPN2.8 Publications
    Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP08581.
    PaxDbiP08581.
    PRIDEiP08581.

    2D gel databases

    OGPiP08581.

    PTM databases

    PhosphoSiteiP08581.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Gene expression databases

    ArrayExpressiP08581.
    BgeeiP08581.
    CleanExiHS_MET.
    GenevestigatoriP08581.

    Organism-specific databases

    HPAiCAB005282.
    CAB018577.
    HPA055607.

    Interactioni

    Subunit structurei

    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.By similarity16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBLP2268115EBI-1039152,EBI-518228
    DNAJA3Q96EY1-22EBI-1039152,EBI-3952284
    EGFRP005337EBI-1039152,EBI-297353
    FGRP097692EBI-1039152,EBI-1383732
    HGFP142104EBI-1039152,EBI-1039104
    HGFP14210-62EBI-1039152,EBI-6280319
    inlBP251474EBI-1039152,EBI-1379295From a different organism.
    INPPL1O153572EBI-1039152,EBI-1384248
    KDRP359683EBI-1039152,EBI-1005487
    KdrP359183EBI-1039152,EBI-1555005From a different organism.
    LCKP062393EBI-1039152,EBI-1348
    LYNP079482EBI-1039152,EBI-79452
    MUC1P159412EBI-1039152,EBI-2804728
    NCK1P163332EBI-1039152,EBI-389883
    NCK2O436392EBI-1039152,EBI-713635
    PIK3R1P279866EBI-1039152,EBI-79464
    PIK3R2O0045911EBI-1039152,EBI-346930
    PIK3R3Q9256911EBI-1039152,EBI-79893
    PLCG1P1917410EBI-1039152,EBI-79387
    PLXNB1O431577EBI-1039152,EBI-1111488
    PLXNB2O150312EBI-1039152,EBI-722004
    PLXNB3Q9ULL42EBI-1039152,EBI-311073
    PTK2Q009445EBI-1039152,EBI-2896409From a different organism.
    PTPN1P180313EBI-1039152,EBI-968788
    PTPN11Q0612413EBI-1039152,EBI-297779
    PTPRBP234672EBI-1039152,EBI-1265766
    PTPRJQ129135EBI-1039152,EBI-2264500
    RASA1P2093615EBI-1039152,EBI-1026476
    SH2B3Q9UQQ22EBI-1039152,EBI-7879749
    SH2D1AO608803EBI-1039152,EBI-6983382
    SH2D1BO147966EBI-1039152,EBI-3923013
    SH2D2AQ9NP317EBI-1039152,EBI-490630
    SH2D3CQ8N5H74EBI-1039152,EBI-745980
    SHBQ154644EBI-1039152,EBI-4402156
    SHC1P293535EBI-1039152,EBI-78835
    SHC2P980772EBI-1039152,EBI-7256023
    SHC4Q6S5L83EBI-1039152,EBI-9453524
    SHDQ96IW22EBI-1039152,EBI-4402781
    SLA2Q9H6Q34EBI-1039152,EBI-1222854
    SOCS5O751592EBI-1039152,EBI-970130
    SOCS6O145444EBI-1039152,EBI-3929549
    SRCP129314EBI-1039152,EBI-621482
    STAP1Q9ULZ23EBI-1039152,EBI-6083058
    SYKP434053EBI-1039152,EBI-78302
    TECP426802EBI-1039152,EBI-1383480
    TENC1Q63HR22EBI-1039152,EBI-949753
    TNS1Q9HBL02EBI-1039152,EBI-3389814
    TNS3Q68CZ23EBI-1039152,EBI-1220488
    VAV3Q9UKW42EBI-1039152,EBI-297568
    YES1P079473EBI-1039152,EBI-515331
    ZAP70P434032EBI-1039152,EBI-1211276

    Protein-protein interaction databases

    BioGridi110391. 34 interactions.
    DIPiDIP-6023N.
    IntActiP08581. 85 interactions.
    MINTiMINT-4837114.
    STRINGi9606.ENSP00000317272.

    Structurei

    Secondary structure

    1
    1390
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi45 – 473
    Beta strandi52 – 587
    Beta strandi61 – 666
    Beta strandi69 – 746
    Turni75 – 773
    Beta strandi80 – 845
    Beta strandi89 – 913
    Beta strandi93 – 953
    Beta strandi97 – 993
    Beta strandi102 – 1043
    Beta strandi111 – 1133
    Beta strandi119 – 1235
    Beta strandi125 – 1339
    Beta strandi135 – 1395
    Beta strandi141 – 1455
    Beta strandi155 – 1606
    Beta strandi182 – 1898
    Beta strandi192 – 1998
    Beta strandi213 – 2197
    Helixi231 – 2333
    Helixi239 – 2413
    Turni242 – 2443
    Beta strandi247 – 2559
    Beta strandi258 – 26811
    Beta strandi272 – 2743
    Beta strandi277 – 2815
    Beta strandi284 – 2863
    Beta strandi292 – 3009
    Beta strandi312 – 3143
    Beta strandi316 – 3238
    Helixi327 – 3337
    Beta strandi341 – 3499
    Beta strandi356 – 36611
    Helixi367 – 3748
    Helixi380 – 3823
    Beta strandi383 – 3853
    Helixi387 – 3904
    Beta strandi392 – 3943
    Turni395 – 3984
    Beta strandi418 – 4225
    Beta strandi424 – 4274
    Turni429 – 4368
    Beta strandi439 – 4479
    Beta strandi450 – 4578
    Beta strandi462 – 4665
    Beta strandi469 – 4713
    Beta strandi476 – 4805
    Beta strandi490 – 4934
    Turni496 – 4983
    Beta strandi501 – 5066
    Beta strandi509 – 5146
    Helixi518 – 5214
    Helixi526 – 5316
    Helixi534 – 5363
    Beta strandi538 – 5403
    Beta strandi545 – 5484
    Beta strandi552 – 5543
    Beta strandi557 – 5593
    Beta strandi564 – 5729
    Beta strandi580 – 5867
    Beta strandi590 – 5923
    Beta strandi595 – 5984
    Beta strandi602 – 6054
    Helixi614 – 6163
    Beta strandi619 – 6257
    Beta strandi637 – 6415
    Beta strandi646 – 6505
    Helixi1048 – 10503
    Helixi1055 – 10573
    Helixi1060 – 10667
    Helixi1067 – 10693
    Helixi1073 – 10753
    Beta strandi1076 – 108712
    Beta strandi1090 – 10978
    Beta strandi1100 – 11023
    Beta strandi1105 – 11128
    Helixi1118 – 113215
    Beta strandi1144 – 11463
    Beta strandi1149 – 11513
    Beta strandi1154 – 11585
    Helixi1165 – 11706
    Turni1172 – 11743
    Helixi1178 – 119720
    Helixi1207 – 12093
    Beta strandi1210 – 12123
    Beta strandi1218 – 12203
    Helixi1224 – 12263
    Helixi1232 – 12343
    Helixi1237 – 12393
    Beta strandi1241 – 12455
    Helixi1247 – 12493
    Helixi1252 – 12576
    Helixi1262 – 127716
    Beta strandi1283 – 12875
    Turni1289 – 12913
    Helixi1292 – 12976
    Helixi1310 – 131910
    Helixi1324 – 13263
    Helixi1330 – 134213
    Turni1354 – 13585

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FYRX-ray2.40I/J/K/L1356-1359[»]
    1R0PX-ray1.80A1049-1360[»]
    1R1WX-ray1.80A1049-1360[»]
    1SHYX-ray3.22B25-567[»]
    1SSLNMR-A519-562[»]
    1UX3model-A25-656[»]
    2G15X-ray2.15A1038-1346[»]
    2RFNX-ray2.50A/B1048-1351[»]
    2RFSX-ray2.20A1048-1351[»]
    2UZXX-ray2.80B/D25-740[»]
    2UZYX-ray4.00B/D25-740[»]
    2WD1X-ray2.00A1055-1346[»]
    2WGJX-ray2.00A1051-1348[»]
    2WKMX-ray2.20A1051-1348[»]
    3A4PX-ray2.54A1049-1360[»]
    3BUXX-ray1.35A/C997-1009[»]
    3C1XX-ray2.17A1049-1360[»]
    3CCNX-ray1.90A1048-1350[»]
    3CD8X-ray2.00A1048-1350[»]
    3CE3X-ray2.40A1049-1360[»]
    3CTHX-ray2.30A1049-1360[»]
    3CTJX-ray2.50A1049-1360[»]
    3DKCX-ray1.52A1049-1360[»]
    3DKFX-ray1.80A1049-1360[»]
    3DKGX-ray1.91A1049-1360[»]
    3EFJX-ray2.60A/B1048-1351[»]
    3EFKX-ray2.20A/B1048-1351[»]
    3F66X-ray1.40A/B1052-1349[»]
    3F82X-ray2.50A1049-1360[»]
    3I5NX-ray2.00A1048-1350[»]
    3L8VX-ray2.40A1049-1360[»]
    3LQ8X-ray2.02A1051-1348[»]
    3Q6UX-ray1.60A1048-1348[»]
    3Q6WX-ray1.75A1048-1348[»]
    3QTIX-ray2.00A/B1050-1360[»]
    3R7OX-ray2.30A1048-1348[»]
    3RHKX-ray1.94A/B1038-1346[»]
    3U6HX-ray2.00A1048-1351[»]
    3U6IX-ray2.10A1048-1351[»]
    3VW8X-ray2.10A1024-1352[»]
    3ZBXX-ray2.20A1051-1348[»]
    3ZC5X-ray2.20A1051-1348[»]
    3ZCLX-ray1.40A1051-1348[»]
    3ZXZX-ray1.80A1051-1348[»]
    3ZZEX-ray1.87A1051-1348[»]
    4AOIX-ray1.90A1051-1348[»]
    4AP7X-ray1.80A1051-1348[»]
    4DEGX-ray2.00A1048-1351[»]
    4DEHX-ray2.00A1048-1351[»]
    4DEIX-ray2.05A1048-1351[»]
    4EEVX-ray1.80A1038-1346[»]
    4GG5X-ray2.42A1038-1346[»]
    4GG7X-ray2.27A1038-1346[»]
    4IWDX-ray1.99A1048-1348[»]
    4K3JX-ray2.80B39-564[»]
    4KNBX-ray2.40A/B/C/D1060-1346[»]
    4O3TX-ray2.99B25-567[»]
    4O3UX-ray3.04B25-567[»]
    DisProtiDP00317.
    ProteinModelPortaliP08581.
    SMRiP08581. Positions 40-741, 1024-1352.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08581.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 932908ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini956 – 1390435CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei933 – 95523HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 515489SemaPROSITE-ProRule annotationAdd
    BLAST
    Domaini563 – 65593IPT/TIG 1Add
    BLAST
    Domaini657 – 73983IPT/TIG 2Add
    BLAST
    Domaini742 – 83695IPT/TIG 3Add
    BLAST
    Domaini1078 – 1345268Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1212 – 1390179Interaction with RANBP9Add
    BLAST
    Regioni1320 – 135940Interaction with MUC20Add
    BLAST

    Domaini

    The kinase domain is involved in SPSB1 binding.
    The beta-propeller Sema domain mediates binding to HGF.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
    Contains 3 IPT/TIG domains.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 Sema domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000220900.
    HOVERGENiHBG006348.
    KOiK05099.
    OMAiQRVDLFM.
    OrthoDBiEOG7J70DR.
    PhylomeDBiP08581.
    TreeFamiTF317402.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    2.60.40.10. 3 hits.
    InterProiIPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    IPR011009. Kinase-like_dom.
    IPR016201. Plexin-like_fold.
    IPR002165. Plexin_repeat.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001627. Semap_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016244. Tyr_kinase_HGF/MSP_rcpt.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF01437. PSI. 1 hit.
    PF01403. Sema. 1 hit.
    PF01833. TIG. 3 hits.
    [Graphical view]
    PIRSFiPIRSF000617. TyrPK_HGF-R. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00429. IPT. 4 hits.
    SM00423. PSI. 1 hit.
    SM00630. Sema. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF101912. SSF101912. 1 hit.
    SSF103575. SSF103575. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF81296. SSF81296. 3 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS51004. SEMA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional soluble isoforms seem to exist.

    Isoform 1 (identifier: P08581-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKAPAVLAPG ILVLLFTLVQ RSNGECKEAL AKSEMNVNMK YQLPNFTAET     50
    PIQNVILHEH HIFLGATNYI YVLNEEDLQK VAEYKTGPVL EHPDCFPCQD 100
    CSSKANLSGG VWKDNINMAL VVDTYYDDQL ISCGSVNRGT CQRHVFPHNH 150
    TADIQSEVHC IFSPQIEEPS QCPDCVVSAL GAKVLSSVKD RFINFFVGNT 200
    INSSYFPDHP LHSISVRRLK ETKDGFMFLT DQSYIDVLPE FRDSYPIKYV 250
    HAFESNNFIY FLTVQRETLD AQTFHTRIIR FCSINSGLHS YMEMPLECIL 300
    TEKRKKRSTK KEVFNILQAA YVSKPGAQLA RQIGASLNDD ILFGVFAQSK 350
    PDSAEPMDRS AMCAFPIKYV NDFFNKIVNK NNVRCLQHFY GPNHEHCFNR 400
    TLLRNSSGCE ARRDEYRTEF TTALQRVDLF MGQFSEVLLT SISTFIKGDL 450
    TIANLGTSEG RFMQVVVSRS GPSTPHVNFL LDSHPVSPEV IVEHTLNQNG 500
    YTLVITGKKI TKIPLNGLGC RHFQSCSQCL SAPPFVQCGW CHDKCVRSEE 550
    CLSGTWTQQI CLPAIYKVFP NSAPLEGGTR LTICGWDFGF RRNNKFDLKK 600
    TRVLLGNESC TLTLSESTMN TLKCTVGPAM NKHFNMSIII SNGHGTTQYS 650
    TFSYVDPVIT SISPKYGPMA GGTLLTLTGN YLNSGNSRHI SIGGKTCTLK 700
    SVSNSILECY TPAQTISTEF AVKLKIDLAN RETSIFSYRE DPIVYEIHPT 750
    KSFISGGSTI TGVGKNLNSV SVPRMVINVH EAGRNFTVAC QHRSNSEIIC 800
    CTTPSLQQLN LQLPLKTKAF FMLDGILSKY FDLIYVHNPV FKPFEKPVMI 850
    SMGNENVLEI KGNDIDPEAV KGEVLKVGNK SCENIHLHSE AVLCTVPNDL 900
    LKLNSELNIE WKQAISSTVL GKVIVQPDQN FTGLIAGVVS ISTALLLLLG 950
    FFLWLKKRKQ IKDLGSELVR YDARVHTPHL DRLVSARSVS PTTEMVSNES 1000
    VDYRATFPED QFPNSSQNGS CRQVQYPLTD MSPILTSGDS DISSPLLQNT 1050
    VHIDLSALNP ELVQAVQHVV IGPSSLIVHF NEVIGRGHFG CVYHGTLLDN 1100
    DGKKIHCAVK SLNRITDIGE VSQFLTEGII MKDFSHPNVL SLLGICLRSE 1150
    GSPLVVLPYM KHGDLRNFIR NETHNPTVKD LIGFGLQVAK GMKYLASKKF 1200
    VHRDLAARNC MLDEKFTVKV ADFGLARDMY DKEYYSVHNK TGAKLPVKWM 1250
    ALESLQTQKF TTKSDVWSFG VLLWELMTRG APPYPDVNTF DITVYLLQGR 1300
    RLLQPEYCPD PLYEVMLKCW HPKAEMRPSF SELVSRISAI FSTFIGEHYV 1350
    HVNATYVNVK CVAPYPSLLS SEDNADDEVD TRPASFWETS 1390
    Length:1,390
    Mass (Da):155,541
    Last modified:July 7, 2009 - v4
    Checksum:i9CF896D1273905C3
    GO
    Isoform 2 (identifier: P08581-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         755-755: S → STWWKEPLNIVSFLFCFAS

    Note: No experimental confirmation available.

    Show »
    Length:1,408
    Mass (Da):157,712
    Checksum:iC5F64DCBBC13CC88
    GO
    Isoform 3 (identifier: P08581-3) [UniParc]FASTAAdd to Basket

    Also known as: Soluble MET variant 4

    The sequence of this isoform differs from the canonical sequence as follows:
         755-764: SGGSTITGVG → RHVNIALIQR
         765-1390: Missing.

    Show »
    Length:764
    Mass (Da):85,745
    Checksum:iBBCBC4197C9C18DE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 2371V → A in ACF47606. (PubMed:18593464)Curated
    Sequence conflicti508 – 5081K → R in ACF47606. (PubMed:18593464)Curated
    Sequence conflicti720 – 7201F → S in ACF47606. (PubMed:18593464)Curated
    Sequence conflicti1191 – 11911G → A in AAA59591. (PubMed:2819873)Curated
    Sequence conflicti1272 – 12721L → V in AAA59591. (PubMed:2819873)Curated
    Sequence conflicti1272 – 12721L → V in CAB56793. 1 PublicationCurated
    Sequence conflicti1272 – 12721L → V in AAA59590. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti143 – 1431R → Q.1 Publication
    Corresponds to variant rs35469582 [ dbSNP | Ensembl ].
    VAR_041738
    Natural varianti150 – 1501H → 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. 1 Publication
    VAR_064855
    Natural varianti156 – 1561S → L.1 Publication
    Corresponds to variant rs56311081 [ dbSNP | Ensembl ].
    VAR_041739
    Natural varianti168 – 1681E → 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. 2 Publications
    Corresponds to variant rs55985569 [ dbSNP | Ensembl ].
    VAR_041740
    Natural varianti238 – 2381L → S.
    Corresponds to variant rs34349517 [ dbSNP | Ensembl ].
    VAR_032478
    Natural varianti316 – 3161I → M.
    Corresponds to variant rs35225896 [ dbSNP | Ensembl ].
    VAR_032479
    Natural varianti320 – 3201A → V.1 Publication
    Corresponds to variant rs35776110 [ dbSNP | Ensembl ].
    VAR_006285
    Natural varianti375 – 3751N → S.1 Publication
    Corresponds to variant rs33917957 [ dbSNP | Ensembl ].
    VAR_032480
    Natural varianti385 – 3851C → 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. 1 Publication
    VAR_064856
    Natural varianti773 – 7731P → L in gastric cancer. 1 Publication
    VAR_032481
    Natural varianti970 – 9701R → C.2 Publications
    Corresponds to variant rs34589476 [ dbSNP | Ensembl ].
    VAR_032482
    Natural varianti991 – 9911P → S in gastric cancer; prolonged tyrosine phosphorylation in response to HGF/SF; transforming activity in athymic nude mice. 1 Publication
    VAR_032483
    Natural varianti992 – 9921T → 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. 4 Publications
    Corresponds to variant rs56391007 [ dbSNP | Ensembl ].
    VAR_032484
    Natural varianti1092 – 10921V → I in RCCP; constitutive autophosphorylation. 3 Publications
    VAR_032485
    Natural varianti1094 – 10941H → L in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 1 Publication
    VAR_032486
    Natural varianti1094 – 10941H → R in RCCP; causes malignant transformation in cell lines. 2 Publications
    VAR_032487
    Natural varianti1094 – 10941H → Y in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 1 Publication
    VAR_032488
    Natural varianti1106 – 11061H → D in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 2 Publications
    VAR_032489
    Natural varianti1131 – 11311M → T in RCCP; germline mutation. 2 Publications
    VAR_006286
    Natural varianti1173 – 11731T → I in HCC. 1 Publication
    VAR_032490
    Natural varianti1188 – 11881V → L in RCCP; germline mutation. 2 Publications
    VAR_006287
    Natural varianti1195 – 11951L → V in RCCP; somatic mutation. 1 Publication
    VAR_006288
    Natural varianti1220 – 12201V → I in RCCP; germline mutation. 1 Publication
    VAR_006289
    Natural varianti1228 – 12281D → H in RCCP; somatic mutation. 1 Publication
    VAR_006291
    Natural varianti1228 – 12281D → N in RCCP; germline mutation. 1 Publication
    VAR_006290
    Natural varianti1230 – 12301Y → C in RCCP; germline mutation. 2 Publications
    VAR_006292
    Natural varianti1230 – 12301Y → D in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 2 Publications
    VAR_032491
    Natural varianti1230 – 12301Y → H in RCCP; somatic mutation. 1 Publication
    VAR_006293
    Natural varianti1244 – 12441K → R in HCC. 1 Publication
    VAR_032492
    Natural varianti1250 – 12501M → I in HCC. 1 Publication
    VAR_032493
    Natural varianti1250 – 12501M → T in RCCP; somatic mutation. 2 Publications
    VAR_006294
    Natural varianti1294 – 12941V → 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. 1 Publication
    VAR_064857

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei755 – 76410SGGSTITGVG → RHVNIALIQR in isoform 3. 1 PublicationVSP_042447
    Alternative sequencei755 – 7551S → STWWKEPLNIVSFLFCFAS in isoform 2. 1 PublicationVSP_005005
    Alternative sequencei765 – 1390626Missing in isoform 3. 1 PublicationVSP_042448Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02958 mRNA. Translation: AAA59591.1.
    X54559 mRNA. Translation: CAB56793.1.
    EU826570 mRNA. Translation: ACF47606.1.
    AC002080 Genomic DNA. Translation: AAB54047.1.
    AC002543 Genomic DNA. Translation: AAC60383.1.
    AC004416 Genomic DNA. Translation: AAF66137.2.
    CH236947 Genomic DNA. Translation: EAL24359.1.
    CH471070 Genomic DNA. Translation: EAW83509.1.
    BC130420 mRNA. Translation: AAI30421.1.
    U08818 mRNA. Translation: AAB60323.1. Sequence problems.
    M35074 mRNA. Translation: AAA59590.1.
    CCDSiCCDS43636.1. [P08581-1]
    CCDS47689.1. [P08581-2]
    PIRiA40175. TVHUME.
    RefSeqiNP_000236.2. NM_000245.2. [P08581-1]
    NP_001120972.1. NM_001127500.1. [P08581-2]
    UniGeneiHs.132966.

    Genome annotation databases

    EnsembliENST00000318493; ENSP00000317272; ENSG00000105976. [P08581-2]
    ENST00000397752; ENSP00000380860; ENSG00000105976. [P08581-1]
    ENST00000436117; ENSP00000410980; ENSG00000105976. [P08581-3]
    GeneIDi4233.
    KEGGihsa:4233.
    UCSCiuc003vij.3. human. [P08581-1]
    uc010lkh.3. human. [P08581-2]
    uc011knc.1. human. [P08581-3]

    Polymorphism databases

    DMDMi251757497.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    C-MET entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02958 mRNA. Translation: AAA59591.1 .
    X54559 mRNA. Translation: CAB56793.1 .
    EU826570 mRNA. Translation: ACF47606.1 .
    AC002080 Genomic DNA. Translation: AAB54047.1 .
    AC002543 Genomic DNA. Translation: AAC60383.1 .
    AC004416 Genomic DNA. Translation: AAF66137.2 .
    CH236947 Genomic DNA. Translation: EAL24359.1 .
    CH471070 Genomic DNA. Translation: EAW83509.1 .
    BC130420 mRNA. Translation: AAI30421.1 .
    U08818 mRNA. Translation: AAB60323.1 . Sequence problems.
    M35074 mRNA. Translation: AAA59590.1 .
    CCDSi CCDS43636.1. [P08581-1 ]
    CCDS47689.1. [P08581-2 ]
    PIRi A40175. TVHUME.
    RefSeqi NP_000236.2. NM_000245.2. [P08581-1 ]
    NP_001120972.1. NM_001127500.1. [P08581-2 ]
    UniGenei Hs.132966.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FYR X-ray 2.40 I/J/K/L 1356-1359 [» ]
    1R0P X-ray 1.80 A 1049-1360 [» ]
    1R1W X-ray 1.80 A 1049-1360 [» ]
    1SHY X-ray 3.22 B 25-567 [» ]
    1SSL NMR - A 519-562 [» ]
    1UX3 model - A 25-656 [» ]
    2G15 X-ray 2.15 A 1038-1346 [» ]
    2RFN X-ray 2.50 A/B 1048-1351 [» ]
    2RFS X-ray 2.20 A 1048-1351 [» ]
    2UZX X-ray 2.80 B/D 25-740 [» ]
    2UZY X-ray 4.00 B/D 25-740 [» ]
    2WD1 X-ray 2.00 A 1055-1346 [» ]
    2WGJ X-ray 2.00 A 1051-1348 [» ]
    2WKM X-ray 2.20 A 1051-1348 [» ]
    3A4P X-ray 2.54 A 1049-1360 [» ]
    3BUX X-ray 1.35 A/C 997-1009 [» ]
    3C1X X-ray 2.17 A 1049-1360 [» ]
    3CCN X-ray 1.90 A 1048-1350 [» ]
    3CD8 X-ray 2.00 A 1048-1350 [» ]
    3CE3 X-ray 2.40 A 1049-1360 [» ]
    3CTH X-ray 2.30 A 1049-1360 [» ]
    3CTJ X-ray 2.50 A 1049-1360 [» ]
    3DKC X-ray 1.52 A 1049-1360 [» ]
    3DKF X-ray 1.80 A 1049-1360 [» ]
    3DKG X-ray 1.91 A 1049-1360 [» ]
    3EFJ X-ray 2.60 A/B 1048-1351 [» ]
    3EFK X-ray 2.20 A/B 1048-1351 [» ]
    3F66 X-ray 1.40 A/B 1052-1349 [» ]
    3F82 X-ray 2.50 A 1049-1360 [» ]
    3I5N X-ray 2.00 A 1048-1350 [» ]
    3L8V X-ray 2.40 A 1049-1360 [» ]
    3LQ8 X-ray 2.02 A 1051-1348 [» ]
    3Q6U X-ray 1.60 A 1048-1348 [» ]
    3Q6W X-ray 1.75 A 1048-1348 [» ]
    3QTI X-ray 2.00 A/B 1050-1360 [» ]
    3R7O X-ray 2.30 A 1048-1348 [» ]
    3RHK X-ray 1.94 A/B 1038-1346 [» ]
    3U6H X-ray 2.00 A 1048-1351 [» ]
    3U6I X-ray 2.10 A 1048-1351 [» ]
    3VW8 X-ray 2.10 A 1024-1352 [» ]
    3ZBX X-ray 2.20 A 1051-1348 [» ]
    3ZC5 X-ray 2.20 A 1051-1348 [» ]
    3ZCL X-ray 1.40 A 1051-1348 [» ]
    3ZXZ X-ray 1.80 A 1051-1348 [» ]
    3ZZE X-ray 1.87 A 1051-1348 [» ]
    4AOI X-ray 1.90 A 1051-1348 [» ]
    4AP7 X-ray 1.80 A 1051-1348 [» ]
    4DEG X-ray 2.00 A 1048-1351 [» ]
    4DEH X-ray 2.00 A 1048-1351 [» ]
    4DEI X-ray 2.05 A 1048-1351 [» ]
    4EEV X-ray 1.80 A 1038-1346 [» ]
    4GG5 X-ray 2.42 A 1038-1346 [» ]
    4GG7 X-ray 2.27 A 1038-1346 [» ]
    4IWD X-ray 1.99 A 1048-1348 [» ]
    4K3J X-ray 2.80 B 39-564 [» ]
    4KNB X-ray 2.40 A/B/C/D 1060-1346 [» ]
    4O3T X-ray 2.99 B 25-567 [» ]
    4O3U X-ray 3.04 B 25-567 [» ]
    DisProti DP00317.
    ProteinModelPortali P08581.
    SMRi P08581. Positions 40-741, 1024-1352.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110391. 34 interactions.
    DIPi DIP-6023N.
    IntActi P08581. 85 interactions.
    MINTi MINT-4837114.
    STRINGi 9606.ENSP00000317272.

    Chemistry

    BindingDBi P08581.
    ChEMBLi CHEMBL3717.
    GuidetoPHARMACOLOGYi 1815.

    PTM databases

    PhosphoSitei P08581.

    Polymorphism databases

    DMDMi 251757497.

    2D gel databases

    OGPi P08581.

    Proteomic databases

    MaxQBi P08581.
    PaxDbi P08581.
    PRIDEi P08581.

    Protocols and materials databases

    DNASUi 4233.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318493 ; ENSP00000317272 ; ENSG00000105976 . [P08581-2 ]
    ENST00000397752 ; ENSP00000380860 ; ENSG00000105976 . [P08581-1 ]
    ENST00000436117 ; ENSP00000410980 ; ENSG00000105976 . [P08581-3 ]
    GeneIDi 4233.
    KEGGi hsa:4233.
    UCSCi uc003vij.3. human. [P08581-1 ]
    uc010lkh.3. human. [P08581-2 ]
    uc011knc.1. human. [P08581-3 ]

    Organism-specific databases

    CTDi 4233.
    GeneCardsi GC07P116312.
    HGNCi HGNC:7029. MET.
    HPAi CAB005282.
    CAB018577.
    HPA055607.
    MIMi 114550. phenotype.
    164860. gene.
    605074. phenotype.
    neXtProti NX_P08581.
    Orphaneti 106. Autism.
    47044. Familial papillary renal cell carcinoma.
    33402. Hepatocellular carcinoma, childhood-onset.
    PharmGKBi PA30763.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000220900.
    HOVERGENi HBG006348.
    KOi K05099.
    OMAi QRVDLFM.
    OrthoDBi EOG7J70DR.
    PhylomeDBi P08581.
    TreeFami TF317402.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
    SignaLinki P08581.

    Miscellaneous databases

    ChiTaRSi MET. human.
    EvolutionaryTracei P08581.
    GeneWikii C-Met.
    GenomeRNAii 4233.
    NextBioi 16689.
    PROi P08581.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08581.
    Bgeei P08581.
    CleanExi HS_MET.
    Genevestigatori P08581.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    2.60.40.10. 3 hits.
    InterProi IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    IPR011009. Kinase-like_dom.
    IPR016201. Plexin-like_fold.
    IPR002165. Plexin_repeat.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001627. Semap_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016244. Tyr_kinase_HGF/MSP_rcpt.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF01437. PSI. 1 hit.
    PF01403. Sema. 1 hit.
    PF01833. TIG. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF000617. TyrPK_HGF-R. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00429. IPT. 4 hits.
    SM00423. PSI. 1 hit.
    SM00630. Sema. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101912. SSF101912. 1 hit.
    SSF103575. SSF103575. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF81296. SSF81296. 3 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS51004. SEMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of MET protooncogene cDNA has features characteristic of the tyrosine kinase family of growth-factor receptors."
      Park M., Dean M., Kaul K., Braun M.J., Gonda M.A., Vande Woude G.
      Proc. Natl. Acad. Sci. U.S.A. 84:6379-6383(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. Giordano S.
      Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
      Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
      Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING.
    4. "The DNA sequence of human chromosome 7."
      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.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      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.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    8. "Primary structure of the met protein tyrosine kinase domain."
      Chan A.M.-L., King H.W.S., Tempest P.R., Deakin E.A., Cooper C.S., Brookes P.
      Oncogene 1:229-233(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1010-1390.
    9. "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
      Lee S.-T., Strunk K.M., Spritz R.A.
      Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1206-1264.
    10. "The human met oncogene is related to the tyrosine kinase oncogenes."
      Dean M., Park M., le Beau M.M., Robins T.S., Diaz M.O., Rowley J.D., Blair D.G., Vande Woude G.F.
      Nature 318:385-388(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1267-1390.
    11. "The receptor encoded by the human c-MET oncogene is expressed in hepatocytes, epithelial cells and solid tumors."
      Prat M., Narsimhan R.P., Crepaldi T., Nicotra M.R., Natali P.G., Comoglio P.M.
      Int. J. Cancer 49:323-328(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "The tyrosine-phosphorylated hepatocyte growth factor/scatter factor receptor associates with phosphatidylinositol 3-kinase."
      Graziani A., Gramaglia D., Cantley L.C., Comoglio P.M.
      J. Biol. Chem. 266:22087-22090(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIK3R1.
    13. "Expression of the Met/HGF receptor in normal and neoplastic human tissues."
      Di Renzo M.F., Narsimhan R.P., Olivero M., Bretti S., Giordano S., Medico E., Gaglia P., Zara P., Comoglio P.M.
      Oncogene 6:1997-2003(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. "Identification of the hepatocyte growth factor receptor as the c-met proto-oncogene product."
      Bottaro D.P., Rubin J.S., Faletto D.L., Chan A.M.-L., Kmiecik T.E., Vande Woude G.F., Aaronson S.A.
      Science 251:802-804(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Identification of the major autophosphorylation site of the Met/hepatocyte growth factor receptor tyrosine kinase."
      Ferracini R., Longati P., Naldini L., Vigna E., Comoglio P.M.
      J. Biol. Chem. 266:19558-19564(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-1235, ATP-BINDING SITE LYS-1110.
    16. "A multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor/scatter factor receptor family."
      Ponzetto C., Bardelli A., Zhen Z., Maina F., dalla Zonca P., Giordano S., Graziani A., Panayotou G., Comoglio P.M.
      Cell 77:261-271(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-1349 AND TYR-1356, INTERACTION WITH SRC; PLCG1 AND GRB2.
    17. "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."
      Nusrat A., Parkos C.A., Bacarra A.E., Godowski P.J., Delp-Archer C., Rosen E.M., Madara J.L.
      J. Clin. Invest. 93:2056-2065(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN WOUND HEALING.
    18. "Induction of epithelial tubules by growth factor HGF depends on the STAT pathway."
      Boccaccio C., Ando M., Tamagnone L., Bardelli A., Michieli P., Battistini C., Comoglio P.M.
      Nature 391:285-288(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STAT3.
    19. "Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis."
      Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A., Swamy O.R., Leone M.E., Riedel H.
      Mol. Cell. Biol. 19:6217-6228(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB10.
    20. "Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM."
      Wang D., Li Z., Messing E.M., Wu G.
      J. Biol. Chem. 277:36216-36222(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RANBP9.
    21. "c-Cbl is involved in Met signaling in B cells and mediates hepatocyte growth factor-induced receptor ubiquitination."
      Taher T.E., Tjin E.P., Beuling E.A., Borst J., Spaargaren M., Pals S.T.
      J. Immunol. 169:3793-3800(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    22. "The semaphorin 4D receptor controls invasive growth by coupling with Met."
      Giordano S., Corso S., Conrotto P., Artigiani S., Gilestro G., Barberis D., Tamagnone L., Comoglio P.M.
      Nat. Cell Biol. 4:720-724(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLXNB1.
    23. "Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1."
      Palka H.L., Park M., Tonks N.K.
      J. Biol. Chem. 278:5728-5735(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-1230; TYR-1234; TYR-1235; TYR-1349 AND TYR-1365, DEPHOSPHORYLATION AT TYR-1349 AND TYR-1365 BY PTPRJ.
    24. "A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling."
      Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.
      Biochem. Biophys. Res. Commun. 313:320-326(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RANBP9 AND RANBP10.
    25. "MUC20 suppresses the hepatocyte growth factor-induced Grb2-Ras pathway by binding to a multifunctional docking site of met."
      Higuchi T., Orita T., Katsuya K., Yamasaki Y., Akiyama K., Li H., Yamamoto T., Saito Y., Nakamura M.
      Mol. Cell. Biol. 24:7456-7468(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MUC20.
    26. "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."
      Koch A., Mancini A., El Bounkari O., Tamura T.
      Oncogene 24:3436-3447(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-1356, INTERACTION WITH INPPL1.
    27. "Invasive growth: a MET-driven genetic programme for cancer and stem cells."
      Boccaccio C., Comoglio P.M.
      Nat. Rev. Cancer 6:637-645(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN ANGIOGENESIS.
    28. "Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine phosphatase 1B and T-cell phosphatase."
      Sangwan V., Paliouras G.N., Abella J.V., Dube N., Monast A., Tremblay M.L., Park M.
      J. Biol. Chem. 283:34374-34383(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN1 AND PTPN2, INTERACTION WITH PTPN1 AND PTPN2, MUTAGENESIS OF TYR-1234 AND TYR-1235.
    29. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-977 AND TYR-1003, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    30. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-990; SER-997 AND SER-1000, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. "Identification of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells with a complementary proteomics approach."
      Cao J., Shen C., Wang H., Shen H., Chen Y., Nie A., Yan G., Lu H., Liu Y., Yang P.
      J. Proteome Res. 8:662-672(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106.
      Tissue: Hepatoma.
    32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1003 AND THR-1289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "The HGF/MET pathway as target for the treatment of multiple myeloma and B-cell lymphomas."
      Mahtouk K., Tjin E.P., Spaargaren M., Pals S.T.
      Biochim. Biophys. Acta 1806:208-219(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "Distinct involvement of the Gab1 and Grb2 adaptor proteins in signal transduction by the related receptor tyrosine kinases RON and MET."
      Chaudhuri A., Xie M.H., Yang B., Mahapatra K., Liu J., Marsters S., Bodepudi S., Ashkenazi A.
      J. Biol. Chem. 286:32762-32774(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAB1.
    36. "Dimer formation through domain swapping in the crystal structure of the Grb2-SH2-Ac-pYVNV complex."
      Schiering N., Casale E., Caccia P., Giordano P., Battistini C.
      Biochemistry 39:13376-13382(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1356-1359 IN COMPLEX WITH GRB2.
    37. "Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor c-Met and its complex with the microbial alkaloid K-252a."
      Schiering N., Knapp S., Marconi M., Flocco M.M., Cui J., Perego R., Rusconi L., Cristiani C.
      Proc. Natl. Acad. Sci. U.S.A. 100:12654-12659(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1049-1360 IN COMPLEX WITH INHIBITOR.
    38. "Insights into function of PSI domains from structure of the Met receptor PSI domain."
      Kozlov G., Perreault A., Schrag J.D., Park M., Cygler M., Gehring K., Ekiel I.
      Biochem. Biophys. Res. Commun. 321:234-240(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 519-562, DISULFIDE BONDS.
    39. "Crystal structure of the HGF beta-chain in complex with the Sema domain of the Met receptor."
      Stamos J., Lazarus R.A., Yao X., Kirchhofer D., Wiesmann C.
      EMBO J. 23:2325-2335(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.22 ANGSTROMS) OF 25-567 IN COMPLEX WITH HGF, DISULFIDE BONDS.
    40. "Structure of the human receptor tyrosine kinase met in complex with the Listeria invasion protein InlB."
      Niemann H.H., Jager V., Butler P.J., van den Heuvel J., Schmidt S., Ferraris D., Gherardi E., Heinz D.W.
      Cell 130:235-246(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-740 IN COMPLEX WITH L.MONOCYTOGENES INLB, DISULFIDE BONDS.
    41. Cited for: VARIANTS RCCP THR-1131; LEU-1188; VAL-1195; ILE-1220; HIS-1228; ASN-1228; CYS-1230; HIS-1230 AND THR-1250, VARIANT VAL-320.
    42. "Two North American families with hereditary papillary renal carcinoma and identical novel mutations in the MET proto-oncogene."
      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.
      Cancer Res. 58:1719-1722(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RCCP ARG-1094, CHARACTERIZATION OF VARIANT RCCP ARG-1094.
    43. "Hereditary and sporadic papillary renal carcinomas with c-met mutations share a distinct morphological phenotype."
      Lubensky I.A., Schmidt L., Zhuang Z., Weirich G., Pack S., Zambrano N., Walther M.M., Choyke P., Linehan W.M., Zbar B.
      Am. J. Pathol. 155:517-526(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RCCP ILE-1092; ARG-1094; ASP-1106; THR-1131; LEU-1188; ASP-1230; CYS-1230 AND THR-1250.
    44. "Somatic mutations in the kinase domain of the Met/hepatocyte growth factor receptor gene in childhood hepatocellular carcinomas."
      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.
      Cancer Res. 59:307-310(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HCC ILE-1173; ARG-1244 AND ILE-1250.
    45. "Novel mutation in the ATP-binding site of the MET oncogene tyrosine kinase in a HPRCC family."
      Olivero M., Valente G., Bardelli A., Longati P., Ferrero N., Cracco C., Terrone C., Rocca-Rossetti S., Comoglio P.M., Di Renzo M.F.
      Int. J. Cancer 82:640-643(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RCCP ILE-1092, CHARACTERIZATION OF VARIANT RCCP ILE-1092.
    46. Cited for: VARIANTS RCCP ILE-1092; LEU-1094; TYR-1094; ASP-1106 AND ASP-1230, CHARACTERIZATION OF VARIANTS RCCP ILE-1092; LEU-1094; TYR-1094; ASP-1106 AND ASP-1230.
    47. "A novel germ line juxtamembrane Met mutation in human gastric cancer."
      Lee J.-H., Han S.-U., Cho H., Jennings B., Gerrard B., Dean M., Schmidt L., Zbar B., Vande Woude G.F.V.
      Oncogene 19:4947-4953(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GASTRIC CANCER SER-991, VARIANT ILE-992, CHARACTERIZATION OF VARIANT GASTRIC CANCER SER-991, CHARACTERIZATION OF VARIANT ILE-992.
    48. "A novel germline mutation in the MET extracellular domain in a Korean patient with the diffuse type of familial gastric cancer."
      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.
      J. Med. Genet. 40:E97-E97(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GASTRIC CANCER LEU-773.
    49. "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."
      Wang D., Li Z., Messing E.M., Wu G.
      J. Biol. Chem. 280:16393-16401(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPSB1; SPSB2; SPSB3 AND SPSB4.
    50. Cited for: POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO AUTS9, VARIANTS CYS-970 AND ILE-992.
    51. "Patterns of somatic mutation in human cancer genomes."
      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.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-143; LEU-156; ASP-168; SER-375; CYS-970 AND ILE-992.
    52. Cited for: 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, POSSIBLE INVOLVEMENT IN CUP.

    Entry informationi

    Entry nameiMET_HUMAN
    AccessioniPrimary (citable) accession number: P08581
    Secondary accession number(s): A1L467
    , B5A932, E7EQ94, O60366, Q12875, Q9UDX7, Q9UPL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 199 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3