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P08581

- MET_HUMAN

UniProt

P08581 - MET_HUMAN

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Protein

Hepatocyte growth factor receptor

Gene

MET

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 phosphatase binding Source: UniProtKB
  4. 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. endothelial cell morphogenesis Source: UniProtKB
  9. glucose homeostasis Source: Ensembl
  10. liver development Source: Ensembl
  11. muscle cell migration Source: Ensembl
  12. myoblast proliferation Source: Ensembl
  13. myotube differentiation Source: Ensembl
  14. negative regulation of hydrogen peroxide-mediated programmed cell death Source: BHF-UCL
  15. peptidyl-tyrosine phosphorylation Source: GOC
  16. placenta development Source: Ensembl
  17. positive chemotaxis Source: UniProtKB
  18. positive regulation of endothelial cell chemotaxis Source: UniProtKB
  19. positive regulation of glucose transport Source: Ensembl
  20. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  21. protein autophosphorylation Source: Ensembl
  22. regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling Source: Ensembl
  23. semaphorin-plexin signaling pathway Source: UniProtKB
  24. signal transduction Source: ProtInc
  25. skeletal muscle tissue development Source: Ensembl
Complete GO annotation...

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. cell surface Source: UniProtKB
  3. extracellular region Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB
  5. integral component of plasma membrane Source: ProtInc
  6. plasma membrane Source: Reactome
Complete GO annotation...

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.
88673. Hepatocellular carcinoma.
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 – 9771Phosphothreonine1 Publication
Modified residuei990 – 9901Phosphoserine1 Publication
Modified residuei997 – 9971Phosphoserine1 Publication
Modified residuei1000 – 10001Phosphoserine1 Publication
Modified residuei1003 – 10031Phosphotyrosine2 Publications
Modified residuei1230 – 12301Phosphotyrosine1 Publication
Modified residuei1234 – 12341Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1235 – 12351Phosphotyrosine; by autocatalysis2 Publications
Modified residuei1289 – 12891Phosphothreonine1 Publication
Modified residuei1349 – 13491Phosphotyrosine; by autocatalysis2 Publications
Modified residuei1356 – 13561Phosphotyrosine; by autocatalysis2 Publications
Modified residuei1365 – 13651Phosphotyrosine1 Publication

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

BgeeiP08581.
CleanExiHS_MET.
ExpressionAtlasiP08581. baseline and differential.
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. 37 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.
GeneTreeiENSGT00760000119065.
HOGENOMiHOG000220900.
HOVERGENiHBG006348.
InParanoidiP08581.
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

        10         20         30         40         50
MKAPAVLAPG ILVLLFTLVQ RSNGECKEAL AKSEMNVNMK YQLPNFTAET
60 70 80 90 100
PIQNVILHEH HIFLGATNYI YVLNEEDLQK VAEYKTGPVL EHPDCFPCQD
110 120 130 140 150
CSSKANLSGG VWKDNINMAL VVDTYYDDQL ISCGSVNRGT CQRHVFPHNH
160 170 180 190 200
TADIQSEVHC IFSPQIEEPS QCPDCVVSAL GAKVLSSVKD RFINFFVGNT
210 220 230 240 250
INSSYFPDHP LHSISVRRLK ETKDGFMFLT DQSYIDVLPE FRDSYPIKYV
260 270 280 290 300
HAFESNNFIY FLTVQRETLD AQTFHTRIIR FCSINSGLHS YMEMPLECIL
310 320 330 340 350
TEKRKKRSTK KEVFNILQAA YVSKPGAQLA RQIGASLNDD ILFGVFAQSK
360 370 380 390 400
PDSAEPMDRS AMCAFPIKYV NDFFNKIVNK NNVRCLQHFY GPNHEHCFNR
410 420 430 440 450
TLLRNSSGCE ARRDEYRTEF TTALQRVDLF MGQFSEVLLT SISTFIKGDL
460 470 480 490 500
TIANLGTSEG RFMQVVVSRS GPSTPHVNFL LDSHPVSPEV IVEHTLNQNG
510 520 530 540 550
YTLVITGKKI TKIPLNGLGC RHFQSCSQCL SAPPFVQCGW CHDKCVRSEE
560 570 580 590 600
CLSGTWTQQI CLPAIYKVFP NSAPLEGGTR LTICGWDFGF RRNNKFDLKK
610 620 630 640 650
TRVLLGNESC TLTLSESTMN TLKCTVGPAM NKHFNMSIII SNGHGTTQYS
660 670 680 690 700
TFSYVDPVIT SISPKYGPMA GGTLLTLTGN YLNSGNSRHI SIGGKTCTLK
710 720 730 740 750
SVSNSILECY TPAQTISTEF AVKLKIDLAN RETSIFSYRE DPIVYEIHPT
760 770 780 790 800
KSFISGGSTI TGVGKNLNSV SVPRMVINVH EAGRNFTVAC QHRSNSEIIC
810 820 830 840 850
CTTPSLQQLN LQLPLKTKAF FMLDGILSKY FDLIYVHNPV FKPFEKPVMI
860 870 880 890 900
SMGNENVLEI KGNDIDPEAV KGEVLKVGNK SCENIHLHSE AVLCTVPNDL
910 920 930 940 950
LKLNSELNIE WKQAISSTVL GKVIVQPDQN FTGLIAGVVS ISTALLLLLG
960 970 980 990 1000
FFLWLKKRKQ IKDLGSELVR YDARVHTPHL DRLVSARSVS PTTEMVSNES
1010 1020 1030 1040 1050
VDYRATFPED QFPNSSQNGS CRQVQYPLTD MSPILTSGDS DISSPLLQNT
1060 1070 1080 1090 1100
VHIDLSALNP ELVQAVQHVV IGPSSLIVHF NEVIGRGHFG CVYHGTLLDN
1110 1120 1130 1140 1150
DGKKIHCAVK SLNRITDIGE VSQFLTEGII MKDFSHPNVL SLLGICLRSE
1160 1170 1180 1190 1200
GSPLVVLPYM KHGDLRNFIR NETHNPTVKD LIGFGLQVAK GMKYLASKKF
1210 1220 1230 1240 1250
VHRDLAARNC MLDEKFTVKV ADFGLARDMY DKEYYSVHNK TGAKLPVKWM
1260 1270 1280 1290 1300
ALESLQTQKF TTKSDVWSFG VLLWELMTRG APPYPDVNTF DITVYLLQGR
1310 1320 1330 1340 1350
RLLQPEYCPD PLYEVMLKCW HPKAEMRPSF SELVSRISAI FSTFIGEHYV
1360 1370 1380 1390
HVNATYVNVK CVAPYPSLLS SEDNADDEVD TRPASFWETS
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. 37 interactions.
DIPi DIP-6023N.
IntActi P08581. 85 interactions.
MINTi MINT-4837114.
STRINGi 9606.ENSP00000317272.

Chemistry

BindingDBi P08581.
ChEMBLi CHEMBL3717.
DrugBanki DB08875. Cabozantinib.
DB08865. Crizotinib.
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.
88673. Hepatocellular carcinoma.
PharmGKBi PA30763.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119065.
HOGENOMi HOG000220900.
HOVERGENi HBG006348.
InParanoidi P08581.
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

Bgeei P08581.
CleanExi HS_MET.
ExpressionAtlasi P08581. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 200 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

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