MET_HUMAN - dbPTM
MET_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MET_HUMAN
UniProt AC P08581
Protein Name Hepatocyte growth factor receptor
Gene Name MET
Organism Homo sapiens (Human).
Sequence Length 1390
Subcellular Localization Membrane
Single-pass type I membrane protein.
Isoform 3: Secreted.
Protein Description Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells. May regulate cortical bone osteogenesis (By similarity).; Acts as a receptor for Listeria internalin inlB, mediating entry of the pathogen into cells..
Protein Sequence MKAPAVLAPGILVLLFTLVQRSNGECKEALAKSEMNVNMKYQLPNFTAETPIQNVILHEHHIFLGATNYIYVLNEEDLQKVAEYKTGPVLEHPDCFPCQDCSSKANLSGGVWKDNINMALVVDTYYDDQLISCGSVNRGTCQRHVFPHNHTADIQSEVHCIFSPQIEEPSQCPDCVVSALGAKVLSSVKDRFINFFVGNTINSSYFPDHPLHSISVRRLKETKDGFMFLTDQSYIDVLPEFRDSYPIKYVHAFESNNFIYFLTVQRETLDAQTFHTRIIRFCSINSGLHSYMEMPLECILTEKRKKRSTKKEVFNILQAAYVSKPGAQLARQIGASLNDDILFGVFAQSKPDSAEPMDRSAMCAFPIKYVNDFFNKIVNKNNVRCLQHFYGPNHEHCFNRTLLRNSSGCEARRDEYRTEFTTALQRVDLFMGQFSEVLLTSISTFIKGDLTIANLGTSEGRFMQVVVSRSGPSTPHVNFLLDSHPVSPEVIVEHTLNQNGYTLVITGKKITKIPLNGLGCRHFQSCSQCLSAPPFVQCGWCHDKCVRSEECLSGTWTQQICLPAIYKVFPNSAPLEGGTRLTICGWDFGFRRNNKFDLKKTRVLLGNESCTLTLSESTMNTLKCTVGPAMNKHFNMSIIISNGHGTTQYSTFSYVDPVITSISPKYGPMAGGTLLTLTGNYLNSGNSRHISIGGKTCTLKSVSNSILECYTPAQTISTEFAVKLKIDLANRETSIFSYREDPIVYEIHPTKSFISGGSTITGVGKNLNSVSVPRMVINVHEAGRNFTVACQHRSNSEIICCTTPSLQQLNLQLPLKTKAFFMLDGILSKYFDLIYVHNPVFKPFEKPVMISMGNENVLEIKGNDIDPEAVKGEVLKVGNKSCENIHLHSEAVLCTVPNDLLKLNSELNIEWKQAISSTVLGKVIVQPDQNFTGLIAGVVSISTALLLLLGFFLWLKKRKQIKDLGSELVRYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGSCRQVQYPLTDMSPILTSGDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHYVHVNATYVNVKCVAPYPSLLSSEDNADDEVDTRPASFWETS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
17PhosphorylationGILVLLFTLVQRSNG
HHHHHHHHHHHCCCC
26.4522210691
22PhosphorylationLFTLVQRSNGECKEA
HHHHHHCCCCCHHHH
31.9022210691
45N-linked_GlycosylationNMKYQLPNFTAETPI
CCCEECCCCCCCCCC
56.33UniProtKB CARBOHYD
84PhosphorylationDLQKVAEYKTGPVLE
HHHHHHHHCCCCCCC
12.2429759185
85UbiquitinationLQKVAEYKTGPVLEH
HHHHHHHCCCCCCCC
38.21-
86PhosphorylationQKVAEYKTGPVLEHP
HHHHHHCCCCCCCCC
45.9029759185
106N-linked_GlycosylationQDCSSKANLSGGVWK
CCCCCCCCCCCCCCC
38.1819196183
149N-linked_GlycosylationQRHVFPHNHTADIQS
CCCCCCCCCCCCCCC
34.15UniProtKB CARBOHYD
189UbiquitinationAKVLSSVKDRFINFF
HHHHHHCHHHHHHHH
45.1721906983
189 (in isoform 1)Ubiquitination-45.1721890473
189 (in isoform 2)Ubiquitination-45.1721890473
202N-linked_GlycosylationFFVGNTINSSYFPDH
HHCCCCCCCCCCCCC
23.90UniProtKB CARBOHYD
223UbiquitinationVRRLKETKDGFMFLT
EEECEECCCCEEEEE
57.8721906983
223 (in isoform 1)Ubiquitination-57.8721890473
223 (in isoform 2)Ubiquitination-57.8721890473
263PhosphorylationNNFIYFLTVQRETLD
CCEEEEEEEEHHHCC
12.5124719451
283PhosphorylationTRIIRFCSINSGLHS
HHHHHHHCCCCCHHH
23.3029759185
286PhosphorylationIRFCSINSGLHSYME
HHHHCCCCCHHHHHH
40.8529759185
290PhosphorylationSINSGLHSYMEMPLE
CCCCCHHHHHHCCHH
31.0829759185
291PhosphorylationINSGLHSYMEMPLEC
CCCCHHHHHHCCHHH
6.0729759185
324UbiquitinationLQAAYVSKPGAQLAR
HHHHHCCCHHHHHHH
37.1121906983
324 (in isoform 1)Ubiquitination-37.1121890473
324 (in isoform 2)Ubiquitination-37.1121890473
376UbiquitinationYVNDFFNKIVNKNNV
HHHHHHHHHHCCCCC
42.76-
399N-linked_GlycosylationPNHEHCFNRTLLRNS
CCHHHHHCHHHHHCC
41.23UniProtKB CARBOHYD
405N-linked_GlycosylationFNRTLLRNSSGCEAR
HCHHHHHCCCCCHHC
40.26UniProtKB CARBOHYD
435PhosphorylationDLFMGQFSEVLLTSI
HHHCCCHHHHHHHHH
20.9327174698
440PhosphorylationQFSEVLLTSISTFIK
CHHHHHHHHHHHHHC
21.6127174698
441PhosphorylationFSEVLLTSISTFIKG
HHHHHHHHHHHHHCC
17.9527174698
443PhosphorylationEVLLTSISTFIKGDL
HHHHHHHHHHHCCCE
19.6227174698
444PhosphorylationVLLTSISTFIKGDLT
HHHHHHHHHHCCCEE
27.9227174698
468PhosphorylationRFMQVVVSRSGPSTP
EEEEEEEECCCCCCC
14.7720860994
553PhosphorylationVRSEECLSGTWTQQI
CCCHHHHCCCCCHHH
45.9228985074
555PhosphorylationSEECLSGTWTQQICL
CHHHHCCCCCHHHHH
23.2028985074
557PhosphorylationECLSGTWTQQICLPA
HHHCCCCCHHHHHHH
15.5028985074
607N-linked_GlycosylationKTRVLLGNESCTLTL
CCEEEECCCEEEEEE
37.67UniProtKB CARBOHYD
624S-palmitoylationSTMNTLKCTVGPAMN
HHCHHEEEEECHHHH
4.1327081699
635N-linked_GlycosylationPAMNKHFNMSIIISN
HHHHCCCCEEEEEEC
24.02UniProtKB CARBOHYD
637PhosphorylationMNKHFNMSIIISNGH
HHCCCCEEEEEECCC
16.25-
641PhosphorylationFNMSIIISNGHGTTQ
CCEEEEEECCCCCCC
26.76-
725UbiquitinationTEFAVKLKIDLANRE
HHHHEEEEEECCCCC
28.58-
745PhosphorylationYREDPIVYEIHPTKS
ECCCCCEEEEECCCC
15.1920071362
750PhosphorylationIVYEIHPTKSFISGG
CEEEEECCCCEECCC
25.7620071362
751UbiquitinationVYEIHPTKSFISGGS
EEEEECCCCEECCCC
48.06-
752PhosphorylationYEIHPTKSFISGGST
EEEECCCCEECCCCE
30.2323403867
755PhosphorylationHPTKSFISGGSTITG
ECCCCEECCCCEEEE
34.7823403867
758PhosphorylationKSFISGGSTITGVGK
CCEECCCCEEEECCC
21.8423403867
759PhosphorylationSFISGGSTITGVGKN
CEECCCCEEEECCCC
26.3223403867
761PhosphorylationISGGSTITGVGKNLN
ECCCCEEEECCCCCC
26.3823403867
765UbiquitinationSTITGVGKNLNSVSV
CEEEECCCCCCCCCC
56.7221906983
765 (in isoform 1)Ubiquitination-56.7221890473
771PhosphorylationGKNLNSVSVPRMVIN
CCCCCCCCCCEEEEE
26.6530576142
785N-linked_GlycosylationNVHEAGRNFTVACQH
EEEHHCCCEEEEEEC
35.70UniProtKB CARBOHYD
828PhosphorylationFMLDGILSKYFDLIY
HHHHHHHHHHCEEEE
24.3220068231
830PhosphorylationLDGILSKYFDLIYVH
HHHHHHHHCEEEEEC
10.0323663014
835PhosphorylationSKYFDLIYVHNPVFK
HHHCEEEEECCCCCC
11.7123663014
876UbiquitinationAVKGEVLKVGNKSCE
HHCCCEEEECCCCCC
53.95-
879N-linked_GlycosylationGEVLKVGNKSCENIH
CCEEEECCCCCCCEE
35.73UniProtKB CARBOHYD
894S-palmitoylationLHSEAVLCTVPNDLL
ECCCEEEEECCHHHH
2.6427081699
930N-linked_GlycosylationVIVQPDQNFTGLIAG
EEECCCCCCCHHHHH
43.77UniProtKB CARBOHYD
959UbiquitinationFLWLKKRKQIKDLGS
HHHHHHHHHHHHHHH
66.31-
962UbiquitinationLKKRKQIKDLGSELV
HHHHHHHHHHHHHHH
44.3921890473
962UbiquitinationLKKRKQIKDLGSELV
HHHHHHHHHHHHHHH
44.3921890473
962UbiquitinationLKKRKQIKDLGSELV
HHHHHHHHHHHHHHH
44.3921890473
962 (in isoform 1)Ubiquitination-44.3921890473
966PhosphorylationKQIKDLGSELVRYDA
HHHHHHHHHHHHHCC
34.7528355574
971PhosphorylationLGSELVRYDARVHTP
HHHHHHHHCCCCCCH
13.3828152594
977PhosphorylationRYDARVHTPHLDRLV
HHCCCCCCHHHHHHH
15.0022167270
977 (in isoform 2)Ubiquitination-15.00-
980 (in isoform 2)Ubiquitination-4.2821890473
985PhosphorylationPHLDRLVSARSVSPT
HHHHHHHHCCCCCCC
23.6627422710
988PhosphorylationDRLVSARSVSPTTEM
HHHHHCCCCCCCCCC
27.0222322096
990PhosphorylationLVSARSVSPTTEMVS
HHHCCCCCCCCCCCC
20.1322322096
992PhosphorylationSARSVSPTTEMVSNE
HCCCCCCCCCCCCCC
28.0722322096
993PhosphorylationARSVSPTTEMVSNES
CCCCCCCCCCCCCCC
26.0122322096
995 (in isoform 2)Phosphorylation-3.6327251275
997PhosphorylationSPTTEMVSNESVDYR
CCCCCCCCCCCCCHH
33.3028355574
1000PhosphorylationTEMVSNESVDYRATF
CCCCCCCCCCHHHCC
25.2523927012
1003PhosphorylationVSNESVDYRATFPED
CCCCCCCHHHCCCHH
10.4527273156
1006PhosphorylationESVDYRATFPEDQFP
CCCCHHHCCCHHHCC
30.6223090842
1006 (in isoform 2)Phosphorylation-30.6227251275
1008 (in isoform 2)Phosphorylation-39.6427642862
1015PhosphorylationPEDQFPNSSQNGSCR
CHHHCCCCCCCCCCC
33.2728555341
1016PhosphorylationEDQFPNSSQNGSCRQ
HHHCCCCCCCCCCCE
34.0127050516
1018 (in isoform 2)Phosphorylation-46.4227642862
1020PhosphorylationPNSSQNGSCRQVQYP
CCCCCCCCCCEEECC
17.4227050516
1021 (in isoform 2)Phosphorylation-3.6027642862
1026PhosphorylationGSCRQVQYPLTDMSP
CCCCEEECCCCCCCC
11.01-
1093PhosphorylationRGHFGCVYHGTLLDN
CCCCEEEEECEEECC
9.9020736484
1096PhosphorylationFGCVYHGTLLDNDGK
CEEEEECEEECCCCC
15.73-
1103UbiquitinationTLLDNDGKKIHCAVK
EEECCCCCEEEEEEE
51.96-
1104UbiquitinationLLDNDGKKIHCAVKS
EECCCCCEEEEEEEC
43.12-
1110AcetylationKKIHCAVKSLNRITD
CEEEEEEECCCCCCC
30.6027452117
1110UbiquitinationKKIHCAVKSLNRITD
CEEEEEEECCCCCCC
30.60-
1159PhosphorylationSPLVVLPYMKHGDLR
CCEEEEEECCCCCHH
18.03-
1161UbiquitinationLVVLPYMKHGDLRNF
EEEEEECCCCCHHHH
38.3021906983
1161 (in isoform 1)Ubiquitination-38.3021890473
1179UbiquitinationETHNPTVKDLIGFGL
CCCCCCHHHHHHHHH
49.66-
1179 (in isoform 2)Ubiquitination-49.6621890473
1190AcetylationGFGLQVAKGMKYLAS
HHHHHHHHHHHHHHC
61.767296701
1190UbiquitinationGFGLQVAKGMKYLAS
HHHHHHHHHHHHHHC
61.7621906983
1190 (in isoform 1)Ubiquitination-61.7621890473
1193UbiquitinationLQVAKGMKYLASKKF
HHHHHHHHHHHCCCC
45.86-
1194PhosphorylationQVAKGMKYLASKKFV
HHHHHHHHHHCCCCH
9.90-
1197 (in isoform 2)Ubiquitination-33.51-
1199UbiquitinationMKYLASKKFVHRDLA
HHHHHCCCCHHHHHH
50.56-
1208 (in isoform 2)Ubiquitination-31.1321890473
1211 (in isoform 2)Ubiquitination-6.37-
1215UbiquitinationRNCMLDEKFTVKVAD
HCCCCCCCEEEEEHH
46.10-
1219UbiquitinationLDEKFTVKVADFGLA
CCCCEEEEEHHHCCC
28.75-
1219 (in isoform 1)Ubiquitination-28.7521890473
1230PhosphorylationFGLARDMYDKEYYSV
HCCCCCCCCCCEEEE
28.3127273156
1232UbiquitinationLARDMYDKEYYSVHN
CCCCCCCCCEEEECC
30.0821906983
1232 (in isoform 1)Ubiquitination-30.0821890473
1233PhosphorylationARDMYDKEYYSVHNK
CCCCCCCCEEEECCC
46.9717016520
1234PhosphorylationRDMYDKEYYSVHNKT
CCCCCCCEEEECCCC
13.5421918175
1235PhosphorylationDMYDKEYYSVHNKTG
CCCCCCEEEECCCCC
12.8127273156
1236PhosphorylationMYDKEYYSVHNKTGA
CCCCCEEEECCCCCC
18.9227273156
1237 (in isoform 2)Ubiquitination-3.1421890473
1240UbiquitinationEYYSVHNKTGAKLPV
CEEEECCCCCCCCCC
33.202190698
1240 (in isoform 1)Ubiquitination-33.2021890473
1241PhosphorylationYYSVHNKTGAKLPVK
EEEECCCCCCCCCCE
47.92-
1244UbiquitinationVHNKTGAKLPVKWMA
ECCCCCCCCCCEEHH
55.45-
1248UbiquitinationTGAKLPVKWMALESL
CCCCCCCEEHHHHHH
29.34-
1248 (in isoform 2)Phosphorylation-29.3427642862
1250 (in isoform 2)Ubiquitination-2.2421890473
1252 (in isoform 2)Phosphorylation-2.3827642862
1253 (in isoform 2)Phosphorylation-39.6027642862
1254 (in isoform 2)Phosphorylation-26.9927642862
1257PhosphorylationMALESLQTQKFTTKS
HHHHHHCCCCCCCHH
38.7329083192
1258 (in isoform 2)Ubiquitination-26.3821890473
1259UbiquitinationLESLQTQKFTTKSDV
HHHHCCCCCCCHHHH
48.33-
1261PhosphorylationSLQTQKFTTKSDVWS
HHCCCCCCCHHHHHH
40.1129759185
1262PhosphorylationLQTQKFTTKSDVWSF
HCCCCCCCHHHHHHH
31.5129759185
1264PhosphorylationTQKFTTKSDVWSFGV
CCCCCCHHHHHHHHH
34.9929759185
1266 (in isoform 2)Ubiquitination-6.27-
1289PhosphorylationPPYPDVNTFDITVYL
CCCCCCCCCEEEEEE
23.6419369195
1295PhosphorylationNTFDITVYLLQGRRL
CCCEEEEEEECCCCC
7.9510069803
1307PhosphorylationRRLLQPEYCPDPLYE
CCCCCCCCCCCCHHH
18.9022461510
1313PhosphorylationEYCPDPLYEVMLKCW
CCCCCCHHHHHHHHH
16.3317062641
1318UbiquitinationPLYEVMLKCWHPKAE
CHHHHHHHHHCCCHH
19.72-
1331PhosphorylationAEMRPSFSELVSRIS
HHHCCCHHHHHHHHH
34.077513258
1338PhosphorylationSELVSRISAIFSTFI
HHHHHHHHHHHHHHC
17.757513258
1342PhosphorylationSRISAIFSTFIGEHY
HHHHHHHHHHCCCCE
19.1226356563
1343PhosphorylationRISAIFSTFIGEHYV
HHHHHHHHHCCCCEE
14.4426356563
1349DephosphorylationSTFIGEHYVHVNATY
HHHCCCCEEEEEEEE
6.4812370829
1349PhosphorylationSTFIGEHYVHVNATY
HHHCCCCEEEEEEEE
6.4822322096
1355PhosphorylationHYVHVNATYVNVKCV
CEEEEEEEEEEEEEE
23.8522322096
1356DephosphorylationYVHVNATYVNVKCVA
EEEEEEEEEEEEEEC
6.3912370829
1356PhosphorylationYVHVNATYVNVKCVA
EEEEEEEEEEEEEEC
6.3922322096
1365PhosphorylationNVKCVAPYPSLLSSE
EEEEECCCHHHCCCC
8.8410417759
1367PhosphorylationKCVAPYPSLLSSEDN
EEECCCHHHCCCCCC
35.7828442448
1367 (in isoform 2)Phosphorylation-35.7827642862
1370PhosphorylationAPYPSLLSSEDNADD
CCCHHHCCCCCCCCC
36.6519060867
1371PhosphorylationPYPSLLSSEDNADDE
CCHHHCCCCCCCCCC
49.2719060867
1373 (in isoform 2)Phosphorylation-58.5327642862
1374 (in isoform 2)Phosphorylation-41.0127642862

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
985SPhosphorylationKinasePKC_GROUP-PhosphoELM
985SPhosphorylationKinasePKC-FAMILY-GPS
985SPhosphorylationKinasePRKG2Q13237
GPS
985SPhosphorylationKinasePRKCAP17252
GPS
985SPhosphorylationKinasePRKCDQ05655
GPS
985SPhosphorylationKinasePRKCEQ02156
GPS
1230YPhosphorylationKinaseMETP08581
PSP
1234YPhosphorylationKinaseMST1RQ04912
GPS
1234YPhosphorylationKinaseMETP08581
PSP
1234YPhosphorylationKinaseMETP97523
PSP
1235YPhosphorylationKinaseBMXP51813
GPS
1235YPhosphorylationKinaseMST1RQ04912
GPS
1235YPhosphorylationKinaseMETP08581
PSP
1235YPhosphorylationKinaseMETP97523
PSP
1349YPhosphorylationKinaseABL1P00519
GPS
1349YPhosphorylationKinaseMST1RQ04912
GPS
1349YPhosphorylationKinaseMETP08581
PSP
1349YPhosphorylationKinaseFERP16591
PSP
1356YPhosphorylationKinaseMETP08581
PSP
1356YPhosphorylationKinaseMST1RQ04912
GPS
1356YPhosphorylationKinaseABL1P00519
GPS
1365YPhosphorylationKinaseMETP08581
PSP
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:17449471
-KUbiquitinationE3 ubiquitin ligaseRNF126Q9BV68
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseRNF115Q9Y4L5
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MET_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MET_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
11254878
CADH1_HUMANCDH1physical
11254878
HGF_HUMANHGFphysical
8380735
RANB9_HUMANRANBP9physical
12147692
GRB2_HUMANGRB2physical
8662889
SHC1_HUMANSHC1physical
9660480
SOS1_HUMANSOS1physical
9660480
GRB2_HUMANGRB2physical
9660480
CBL_HUMANCBLphysical
18273061
STAT3_HUMANSTAT3physical
9440692
CBL_HUMANCBLphysical
16397241
CBL_HUMANCBLphysical
19450681
PGS2_HUMANDCNphysical
19433454
HGF_HUMANHGFphysical
19433454
CBL_HUMANCBLphysical
19433454
GRB2_HUMANGRB2physical
19433454
SPSB1_HUMANSPSB1physical
15713673
SPSB2_HUMANSPSB2physical
15713673
SPSB3_HUMANSPSB3physical
15713673
SPSB4_HUMANSPSB4physical
15713673
CBLC_HUMANCBLCphysical
22888118
CHIP_HUMANSTUB1physical
21325980
HSP74_HUMANHSPA4physical
21325980
HS90A_HUMANHSP90AA1physical
21325980
GLMN_HUMANGLMNphysical
11571281
GGA3_HUMANGGA3physical
21664574
GAB1_HUMANGAB1physical
9242692
CBL_HUMANCBLphysical
21163258
LRIG1_HUMANLRIG1physical
24828152
CRK_HUMANCRKphysical
24828152
SOCS1_HUMANSOCS1physical
25728680
EGFR_HUMANEGFRphysical
24362532
ERBB3_HUMANERBB3physical
21918175
EGFR_HUMANEGFRphysical
21918175
MET_HUMANMETphysical
23794705
PTEN_HUMANPTENgenetic
28319113
MET_HUMANMETphysical
26285778

Drug and Disease Associations
Kegg Disease
H00018 Gastric cancer
H00021 Renal cell carcinoma
H00046 Cholangiocarcinoma
OMIM Disease
Note=Activation of MET after rearrangement with the TPR gene produces an oncogenic protein.
114550
605074Renal cell carcinoma papillary (RCCP)
Kegg Drug
D09618 Foretinib (USAN/INN)
D09941 Onartuzumab (USAN/INN)
D10173 Tivantinib (USAN/INN)
D10224 Golvatinib (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MET_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-glycosylation sites on secreted proteins of humanhepatocellular carcinoma cells with a complementary proteomicsapproach.";
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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-966; THR-977; SER-988;SER-990; SER-997; SER-1000; TYR-1003; TYR-1234 AND THR-1289, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-990; SER-997 ANDSER-1000, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-966; THR-977; SER-988;SER-990; SER-997; SER-1000 AND TYR-1003, AND MASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-977; SER-988; SER-990AND TYR-1003, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1234, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1003; TYR-1230; TYR-1234AND TYR-1235, AND MASS SPECTROMETRY.
"The SH2-domian-containing inositol 5-phosphatase (SHIP)-2 binds to c-Met directly via tyrosine residue 1356 and involves hepatocyte growthfactor (HGF)-induced lamellipodium formation, cell scattering and cellspreading.";
Koch A., Mancini A., El Bounkari O., Tamura T.;
Oncogene 24:3436-3447(2005).
Cited for: PHOSPHORYLATION AT TYR-1356, AND INTERACTION WITH INPPL1.
"Hepatocyte growth factor receptor tyrosine kinase met is a substrateof the receptor protein-tyrosine phosphatase DEP-1.";
Palka H.L., Park M., Tonks N.K.;
J. Biol. Chem. 278:5728-5735(2003).
Cited for: PHOSPHORYLATION AT TYR-1230; TYR-1234; TYR-1235; TYR-1349 ANDTYR-1365, AND DEPHOSPHORYLATION BY PTPRJ AT TYR-1349 AND TYR-1365.
"A multifunctional docking site mediates signaling and transformationby 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).
Cited for: AUTOPHOSPHORYLATION AT TYR-1349 AND TYR-1356, AND INTERACTION WITHSRC; PLCG1 AND GRB2.
"Identification of the major autophosphorylation site of theMet/hepatocyte growth factor receptor tyrosine kinase.";
Ferracini R., Longati P., Naldini L., Vigna E., Comoglio P.M.;
J. Biol. Chem. 266:19558-19564(1991).
Cited for: PHOSPHORYLATION AT TYR-1235, AND ATP-BINDING SITE LYS-1110.

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