Met
entrez
24553
canonical
uniprot
P97523
canonical
ensembl
ENSRNOG00000052745
resolver
ensp
ENSRNOP00000070486
resolver
ensp
ENSRNOP00000085968
resolver
ensp
ENSRNOP00000104256
resolver
enst
ENSRNOT00000086902
resolver
enst
ENSRNOT00000115453
resolver
genesymbol
Met
resolver
uniprot
A0A0G2JY19
resolver
uniprot
A0A8I6GEH2
resolver
uniprot
A0A9K3Y8B9
resolver
uniprot
P97579
resolver
uniprot
Q2IBC7
resolver
uniprot
Q63119
resolver
uniprot
Q63964
resolver
uniprot_entry
A0A8I6GEH2_RAT
resolver
uniprot_entry
A0A9K3Y8B9_RAT
resolver
uniprot_entry
MET_RAT
resolver
uniprot_entry
Q2IBC7_RAT
resolver
uniprot_sec
A0A0G2JY19
resolver
uniprot_sec
P97579
resolver
uniprot_sec
Q63119
resolver
uniprot_sec
Q63964
resolver
activity_regulation
ACTIVITY REGULATION: In its inactive state, the C-terminal tail interacts with the catalytic domain and inhibits the kinase activity. Upon ligand binding, the C-terminal tail is displaced and becomes phosphorylated, thus increasing the kinase activity (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MKAPTALAPGILLLLLTLAQRSHGECKEALVKSEMNVNMKYQLPNFTAETPIHNVVLPGHHIYLGATNYIYVLNDKDLQKVSEFKTGPVVEHPDCFPCQDCSSKANVSGGVWKDNVNMALLVDTYYDDQLISCGSVNRGTCQRHVLPPDNAADIQSEVHCMFSPLAEEESGQCPDCVVSALGAKVLLSEKDRFINFFVGNTINSSYPPDYSLHSISVRRLKETQDGFKFLTDQSYIDVLPEFRDSYPIKYIHAFESNHFIYFLTVQKETLDAQTFHTRIIRFCSVDSGLHSYMEMPLECILTEKRRKRSTREEVFNILQAAYVSKPGANLAKQIGASPYDDILYGVFAQSKPDSAEPMNRSAVCAFPIKYVNDFFNKIVNKNNVRCLQHFYGPNHEHCFNRTLLRNSSGCEVRSDEYRTEFTTALQRVDLFMGRLNHVLLTSISTFIKGDLTIANLGTSEGRFMQVVLSRTAHFTPHVNFLLDSYPVSPEVIVEHPSNQNGYTLVVTGKKITKIPLNGLGCGHFQSCSQCLSPPYFIQCGWCHNRCVHSNECPSGTWTQEICLPAVYKVFPTSAPLEGGTMLTICGWDFGFKKNNKFDLRKTKVLLGNESCTLTLSESTTNTLKCTVGPAMSEHFNVSVIVSNSRETTQYSAFSYVDPVITSISPRYGPHAGGTLLTLTGKYLNSGNSRHISIGGKTCTLKSVSDSILECYTPGHTVSAEFPVKLKIDLADRVTSSFSYREDPVVSEIHPTKSFISGGSTITGIGKNLNSVSTPKLVIEVHDVGVNYTVACQHRSSSEIICCTTPSLRQLDLQLPLKTKAFFLLDGILSKHFDLTYVHDPMFKPFEKPVMISMGNENVVEIKGDDIDPEAVKGEVLKVGNKSCENLHWHSEALLCTVPSDLLKLNGGELNIEWKQAVSSTVLGKVIVQPDQNFAGLIIGAVSISVVVLLVSGLFLWLRKRKHKDLGSELVRYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGACRQVQYLLTDLSPILTSGDSDISSPLLQNTVHIDLSALNPELVQAVPHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDSDGKKIHCAVKSLNRITDIEEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLVSKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITIYLLQGRRLLQPEYCPDALYEVMLKCWHPKAEMRPSVSELVSRISSIFSTFIGEHYVHVNATYVNVKCVAPYPSLLPSQDNIDGEANT
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Also promotes differentiation and proliferation of hematopoietic cells (By similarity). {ECO:0000250}.
uniprot
proteins
mass_dalton
153941
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated in response to ligand binding on Tyr-1235 and Tyr-1236 in the kinase domain leading to further phosphorylation of Tyr-1350 and Tyr-1357 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1350 and Tyr-1366. Dephosphorylated by PTPN1 and PTPN2 (By similarity). {ECO:0000250|UniProtKB:P08581}.; PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P08581}.; PTM: O-mannosylation of IPT/TIG domains by TMEM260 is required for protein maturation. O-mannosylated residues are composed of single mannose glycans that are not elongated or modified. {ECO:0000250|UniProtKB:P08581}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
7628535
uniprot
proteins
pubmed
8166728
uniprot
proteins
pubmed
8853431
uniprot
proteins
pubmed
9271668
uniprot
proteins
sequence_length
1382
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 936..956; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins