P16056
uniprot
P16056
canonical
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
MKAPTVLAPGILVLLLSLVQRSHGECKEALVKSEMNVNMKYQLPNFTAETPIQNVVLHGHHIYLGATNYIYVLNDKDLQKVSEFKTGPVLEHPDCLPCRDCSSKANSSGGVWKDNINMALLVDTYYDDQLISCGSVNRGTCQRHVLPPDNSADIQSEVHCMFSPEEESGQCPDCVVSALGAKVLLSEKDRFINFFVGNTINSSYPPGYSLHSISVRRLKETQDGFKFLTDQSYIDVLPEFLDSYPIKYIHAFESNHFIYFLTVQKETLDAQTFHTRIIRFCSVDSGLHSYMEMPLECILTEKRRKRSTREEVFNILQAAYVSKPGANLAKQIGASPSDDILFGVFAQSKPDSAEPVNRSAVCAFPIKYVNDFFNKIVNKNNVRCLQHFYGPNHEHCFNRTLLRNSSGCEARSDEYRTEFTTALQRVDLFMGRLNQVLLTSISTFIKGDLTIANLGTSEGRFMQVVLSRTAHLTPHVNFLLDSHPVSPEVIVEHPSNQNGYTLVVTGKKITKIPLNGLGCGHFQSCSQCLSAPYFIQCGWCHNQCVRFDECPSGTWTQEICLPAVYKVFPTSAPLEGGTVLTICGWDFGFRKNNKFDLRKTKVLLGNESCTLTLSESTTNTLKCTVGPAMSEHFNVSVIISNSRETTQYSAFSYVDPVITSISPRYGPQAGGTLLTLTGKYLNSGNSRHISIGGKTCTLKSVSDSILECYTPAQTTSDEFPVKLKIDLANRETSSFSYREDPVVYEIHPTKSFISGGSTITGIGKTLNSVSLPKLVIDVHEVGVNYTVACQHRSNSEIICCTTPSLKQLGLQLPLKTKAFFLLDGILSKHFDLTYVHNPVFEPFEKPVMISMGNENVVEIKGNNIDPEAVKGEVLKVGNQSCESLHWHSGAVLCTVPSDLLKLNSELNIEWKQAVSSTVLGKVIVQPDQNFAGLIIGAVSISVVVLLLSGLFLWMRKRKHKDLGSELVRYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGACRQVQYPLTDLSPILTSGDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIEEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITIYLLQGRRLLQPEYCPDALYEVMLKCWHPKAEMRPSFSELVSRISSIFSTFIGEHYVHVNATYVNVKCVAPYPSLLPSQDNIDGEGNT
uniprot
proteins
disease_involvement
DISEASE: Note=Activation of Met after rearrangement with the TPR (translocated promoter) locus of chromosome 1 produces an oncogenic protein.
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 neuronal precursors, angiogenesis and kidney formation. During skeletal muscle development, it is crucial for the migration of muscle progenitor cells and for the proliferation of secondary myoblasts (PubMed:30777867). In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Also promotes differentiation and proliferation of hematopoietic cells (By similarity). May regulate cortical bone osteogenesis (PubMed:26637977). {ECO:0000250, ECO:0000269|PubMed:26637977, ECO:0000269|PubMed:30777867, ECO:0000269|PubMed:7651534}.; FUNCTION: (Microbial infection) Acts as a receptor for Listeria monocytogenes internalin InlB, mediating entry of the pathogen into cells. {ECO:0000305|PubMed:11081636}.
uniprot
proteins
mass_dalton
153549
uniprot
proteins
mutagenesis
MUTAGEN 1232; /note="Y->C: Mice heterozygous for the mutation show reduced number of myofibers in appendicular and axial muscles, defective migration of muscle progenitor cells and impaired proliferation of secondary myoblasts."; /evidence="ECO:0000269|PubMed:30777867
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated in response to ligand binding on Tyr-1232 and Tyr-1233 in the kinase domain leading to further phosphorylation of Tyr-1347 and Tyr-1354 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1347 and Tyr-1363 (By similarity). Dephosphorylated by PTPN1 and PTPN2 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Ubiquitination by CBL regulates MET endocytosis, resulting in decreasing plasma membrane receptor abundance, and in endosomal degradation and/or recycling of internalized receptors. {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}.; PTM: (Microbial infection) Tyrosine phosphorylation is stimulated by L.monocytogenes InlB. {ECO:0000269|PubMed:11081636}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
11081636
uniprot
proteins
pubmed
11896575
uniprot
proteins
pubmed
15314156
uniprot
proteins
pubmed
16369487
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2482828
uniprot
proteins
pubmed
26637977
uniprot
proteins
pubmed
2838789
uniprot
proteins
pubmed
30777867
uniprot
proteins
pubmed
7651534
uniprot
proteins
pubmed
8384622
uniprot
proteins
sequence_length
1379
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 932..954; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins