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Protein

Hepatocyte growth factor receptor

Gene

MET

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. May regulate cortical bone osteogenesis (By similarity).By similarity
Acts as a receptor for Listeria internalin inlB, mediating entry of the pathogen into cells.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1003Required for ligand-induced CBL-mediated ubiquitination1 Publication1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1110ATP1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1204Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1084 – 1092ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-416550 Sema4D mediated inhibition of cell attachment and migration
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6806942 MET Receptor Activation
R-HSA-6807004 Negative regulation of MET activity
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8851805 MET activates RAS signaling
R-HSA-8851907 MET activates PI3K/AKT signaling
R-HSA-8865999 MET activates PTPN11
R-HSA-8874081 MET activates PTK2 signaling
R-HSA-8875360 InlB-mediated entry of Listeria monocytogenes into host cell
R-HSA-8875513 MET interacts with TNS proteins
R-HSA-8875555 MET activates RAP1 and RAC1
R-HSA-8875656 MET receptor recycling
R-HSA-8875791 MET activates STAT3
R-HSA-9022699 MECP2 regulates neuronal receptors and channels

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P08581

SIGNOR Signaling Network Open Resource

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SIGNORi
P08581

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MET
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000105976.14

Human Gene Nomenclature Database

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HGNCi
HGNC:7029 MET

Online Mendelian Inheritance in Man (OMIM)

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MIMi
164860 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P08581

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini25 – 932ExtracellularSequence analysisAdd BLAST908
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei933 – 955HelicalSequence analysisAdd BLAST23
Topological domaini956 – 1390CytoplasmicSequence analysisAdd BLAST435

Keywords - Cellular componenti

Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:114550
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0324901173T → I in HCC. 1 PublicationCorresponds to variant dbSNP:rs121913675Ensembl.1
Natural variantiVAR_0324921244K → R in HCC. 1 PublicationCorresponds to variant dbSNP:rs121913677Ensembl.1
Natural variantiVAR_0324931250M → I in HCC. 1 PublicationCorresponds to variant dbSNP:rs121913676Ensembl.1
Renal cell carcinoma papillary (RCCP)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:605074
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0324851092V → I in RCCP; constitutive autophosphorylation. 3 PublicationsCorresponds to variant dbSNP:rs786202724Ensembl.1
Natural variantiVAR_0324861094H → L in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 1 Publication1
Natural variantiVAR_0324871094H → R in RCCP; causes malignant transformation in cell lines. 2 PublicationsCorresponds to variant dbSNP:rs121913243Ensembl.1
Natural variantiVAR_0324881094H → Y in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 1 PublicationCorresponds to variant dbSNP:rs121913244Ensembl.1
Natural variantiVAR_0324891106H → D in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 2 Publications1
Natural variantiVAR_0062861131M → T in RCCP; germline mutation. 2 PublicationsCorresponds to variant dbSNP:rs121913668Ensembl.1
Natural variantiVAR_0062871188V → L in RCCP; germline mutation. 2 PublicationsCorresponds to variant dbSNP:rs121913669Ensembl.1
Natural variantiVAR_0062881195L → V in RCCP; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913673Ensembl.1
Natural variantiVAR_0062891220V → I in RCCP; germline mutation. 1 PublicationCorresponds to variant dbSNP:rs121913670Ensembl.1
Natural variantiVAR_0062911228D → H in RCCP; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913671Ensembl.1
Natural variantiVAR_0062901228D → N in RCCP; germline mutation. 1 PublicationCorresponds to variant dbSNP:rs121913671Ensembl.1
Natural variantiVAR_0062921230Y → C in RCCP; germline mutation. 2 PublicationsCorresponds to variant dbSNP:rs121913246Ensembl.1
Natural variantiVAR_0324911230Y → D in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 2 Publications1
Natural variantiVAR_0062931230Y → H in RCCP; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913247Ensembl.1
Natural variantiVAR_0062941250M → T in RCCP; somatic mutation. 2 PublicationsCorresponds to variant dbSNP:rs121913245Ensembl.1
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.
Deafness, autosomal recessive, 97 (DFNB97)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic sensorineural hearing loss with prelingual onset. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
See also OMIM:616705
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075757841F → V in DFNB97. 1 PublicationCorresponds to variant dbSNP:rs794728016EnsemblClinVar.1
Osteofibrous dysplasia (OSFD)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry. Disease-associated variants identified in 4 families cause the deletion of exon 14. This results in the exclusion of an ubiquitination target site within the cytoplasmic domain, hence in protein stabilization. The persistent presence of MET at the cell surface in conditions of ligand-dependent activation retards osteoblastic differentiation.1 Publication
Disease descriptionA congenital disorder of osteogenesis characterized by non-neoplastic, radiolucent lesions that affect the cortical bone immediately under the periosteum. It usually manifests as a painless swelling or anterior bowing of the long bones, most commonly the tibia and fibula.
See also OMIM:607278
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076584964 – 1010Missing in OSFD; loss of CBL-mediated destabilization. 1 PublicationAdd BLAST47

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1234Y → F: Complete loss of kinase activity and of ligand-induced ubiquitination. Alters interaction with PTPN1 and PTPN2. Loss of interaction with PTPN1 and PTPN2; when associated with F-1235. 2 Publications1
Mutagenesisi1235Y → F: Complete loss of kinase activity. Alters interaction with PTPN1 and PTPN2. Loss of interaction with PTPN1 and PTPN2; when associated with F-1234. 2 Publications1
Mutagenesisi1313Y → F: No effect on ligand-induced CBL-mediated ubiquitination; when associated with F-1349, F-1356 and F-1365. 1 Publication1
Mutagenesisi1349Y → F: No effect on ligand-induced CBL-mediated ubiquitination; when associated with F-1313, F-1356 and F-1365. 1 Publication1
Mutagenesisi1356Y → F: No effect on ligand-induced CBL-mediated ubiquitination; when associated with F-1313, F-1349 and F-1365. 1 Publication1
Mutagenesisi1365Y → F: No effect on ligand-induced CBL-mediated ubiquitination; when associated with F-1313, F-1349 and F-1356. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1009 – 1010Breakpoint for translocation to form TPR-MET oncogene2

Keywords - Diseasei

Deafness, Disease mutation, Non-syndromic deafness, Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
4233

MalaCards human disease database

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MalaCardsi
MET
MIMi114550 phenotype
605074 phenotype
607278 phenotype
616705 phenotype

Open Targets

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OpenTargetsi
ENSG00000105976

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
90636 Autosomal recessive non-syndromic sensorineural deafness type DFNB
47044 Hereditary papillary renal cell carcinoma
106 NON RARE IN EUROPE: Autism
488265 Osteofibrous dysplasia
319298 Papillary renal cell carcinoma
33402 Pediatric hepatocellular carcinoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30763

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3717

Drug and drug target database

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DrugBanki
DB07969 3-[3-(4-methylpiperazin-1-yl)-7-(trifluoromethyl)quinoxalin-5-yl]phenol
DB08875 Cabozantinib
DB08865 Crizotinib
DB02152 K-252a
DB05216 MP470
DB06995 N-({4-[(2-aminopyridin-4-yl)oxy]-3-fluorophenyl}carbamoyl)-2-(4-fluorophenyl)acetamide
DB05153 XL184

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1815

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
MET

Domain mapping of disease mutations (DMDM)

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DMDMi
251757497

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002444025 – 1390Hepatocyte growth factor receptorAdd BLAST1366

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi45N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi95 ↔ 101
Disulfide bondi98 ↔ 160
Glycosylationi106N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi133 ↔ 141
Glycosylationi149N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi172 ↔ 175
Glycosylationi202N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi298 ↔ 363
Disulfide bondi385 ↔ 397
Glycosylationi399N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi405N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi520 ↔ 538
Disulfide bondi526 ↔ 561
Disulfide bondi529 ↔ 545
Disulfide bondi541 ↔ 551
Glycosylationi607N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi635N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi785N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi879N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi930N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei966PhosphoserineCombined sources1
Modified residuei977PhosphothreonineCombined sources1
Modified residuei990PhosphoserineCombined sources1
Modified residuei997PhosphoserineCombined sources1
Modified residuei1000PhosphoserineCombined sources1
Modified residuei1003PhosphotyrosineCombined sources1
Modified residuei1230Phosphotyrosine1 Publication1
Modified residuei1234Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1235Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei1289PhosphothreonineCombined sources1
Modified residuei1349Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei1356Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei1365Phosphotyrosine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 PTPN2.5 Publications
Ubiquitinated. Ubiquitination by CBL regulates MET endocytosis, resulting in decreasing plasma membrane receptor abundance, and in endosomal degradation and/or recycling of internalized receptors.1 Publication1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei307 – 308CleavageSequence analysis2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P08581

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P08581

MaxQB - The MaxQuant DataBase

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MaxQBi
P08581

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P08581

PeptideAtlas

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PeptideAtlasi
P08581

PRoteomics IDEntifications database

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PRIDEi
P08581

ProteomicsDB human proteome resource

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ProteomicsDBi
52128
52129 [P08581-2]
52130 [P08581-3]

2D gel databases

USC-OGP 2-DE database

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OGPi
P08581

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
680

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P08581

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P08581

SwissPalm database of S-palmitoylation events

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SwissPalmi
P08581

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
P08581

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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. Expressed in metaphyseal bone (at protein level) (PubMed:26637977).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000105976 Expressed in 207 organ(s), highest expression level in pigmented layer of retina

CleanEx database of gene expression profiles

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CleanExi
HS_MET

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P08581 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P08581 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB005282
CAB018577
HPA055607

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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. Interacts with LECT2; this interaction may have an antagonistic effect on receptor activation (PubMed:27334921). Interacts with HSP90AA1 and HSP90AB1; the interaction suppresses MET kinase activity (PubMed:26517842).By similarity18 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1039152,EBI-1039152
CBLP2268115EBI-1039152,EBI-518228
DNAJA3Q96EY1-22EBI-1039152,EBI-3952284
EGFRP005338EBI-1039152,EBI-297353
FGRP097692EBI-1039152,EBI-1383732
HGFP142107EBI-1039152,EBI-1039104
HGFP14210-63EBI-1039152,EBI-6280319
HgfQ080483EBI-1039152,EBI-15655650From Mus musculus.
inlBP251474EBI-1039152,EBI-1379295From Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
INPPL1O153572EBI-1039152,EBI-1384248
KDRP359683EBI-1039152,EBI-1005487
KdrP359183EBI-1039152,EBI-1555005From Mus musculus.
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 Gallus gallus.
PTPN1P180313EBI-1039152,EBI-968788
PTPN11Q0612413EBI-1039152,EBI-297779
PTPRBP234672EBI-1039152,EBI-1265766
PTPRJQ129135EBI-1039152,EBI-2264500
PTPROQ168272EBI-1039152,EBI-723739
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
TNS1Q9HBL02EBI-1039152,EBI-3389814
TNS2Q63HR22EBI-1039152,EBI-949753
TNS3Q68CZ23EBI-1039152,EBI-1220488
VAV3Q9UKW42EBI-1039152,EBI-297568
YES1P079473EBI-1039152,EBI-515331
ZAP70P434032EBI-1039152,EBI-1211276

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110391, 67 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P08581

Database of interacting proteins

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DIPi
DIP-6023N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P08581

Protein interaction database and analysis system

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IntActi
P08581, 91 interactors

Molecular INTeraction database

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MINTi
P08581

STRING: functional protein association networks

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STRINGi
9606.ENSP00000317272

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P08581

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
4MXCX-ray1.63A1038-1346[»]
4O3TX-ray2.99B25-567[»]
4O3UX-ray3.04B25-567[»]
4R1VX-ray1.20A1055-1345[»]
4R1YX-ray2.00A1055-1346[»]
4XMOX-ray1.75A1048-1350[»]
4XYFX-ray1.85A1048-1351[»]
5DG5X-ray2.60A/B1038-1346[»]
5EOBX-ray1.75A1038-1346[»]
5EYCX-ray1.80A1048-1351[»]
5EYDX-ray1.85A1048-1351[»]
5HLWX-ray1.97A1057-1355[»]
5HNIX-ray1.71X/Y1049-1360[»]
5HO6X-ray1.97A1049-1360[»]
5HOAX-ray2.14A1049-1360[»]
5HORX-ray2.20A1049-1360[»]
5HTIX-ray1.66A1038-1346[»]
5LSPX-ray2.60A/P519-743[»]
X/Y25-35[»]
5T3QX-ray2.00A1048-1350[»]
5UABX-ray1.90A1023-1360[»]
5UADX-ray2.25A1023-1360[»]
5UAFX-ray2.25A1023-1360[»]
5YA5X-ray1.89A1038-1346[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P08581

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P08581

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P08581

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini27 – 515SemaPROSITE-ProRule annotationAdd BLAST489
Domaini563 – 655IPT/TIG 1Add BLAST93
Domaini657 – 739IPT/TIG 2Add BLAST83
Domaini742 – 836IPT/TIG 3Add BLAST95
Domaini1078 – 1345Protein kinasePROSITE-ProRule annotationAdd BLAST268

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1212 – 1390Interaction with RANBP9Add BLAST179
Regioni1320 – 1359Interaction with MUC201 PublicationAdd BLAST40

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1095 Eukaryota
KOG3610 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158022

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000220900

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG006348

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P08581

KEGG Orthology (KO)

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KOi
K05099

Identification of Orthologs from Complete Genome Data

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OMAi
TNMLKCT

Database of Orthologous Groups

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OrthoDBi
1153238at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P08581

TreeFam database of animal gene trees

More...
TreeFami
TF317402

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.130.10.10, 1 hit
2.60.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
IPR011009 Kinase-like_dom_sf
IPR002165 Plexin_repeat
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR016201 PSI
IPR001627 Semap_dom
IPR036352 Semap_dom_sf
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_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF01437 PSI, 1 hit
PF01403 Sema, 1 hit
PF01833 TIG, 3 hits

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000617 TyrPK_HGF-R, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00429 IPT, 4 hits
SM00423 PSI, 1 hit
SM00630 Sema, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF101912 SSF101912, 1 hit
SSF56112 SSF56112, 1 hit
SSF81296 SSF81296, 3 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS51004 SEMA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional soluble isoforms seem to exist.

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C130H7C130_HUMAN
Hepatocyte growth factor receptor
MET
158Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JKM5C9JKM5_HUMAN
Hepatocyte growth factor receptor
MET
190Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C174H7C174_HUMAN
Hepatocyte growth factor receptor
MET
214Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti237V → A in ACF47606 (PubMed:18593464).Curated1
Sequence conflicti508K → R in ACF47606 (PubMed:18593464).Curated1
Sequence conflicti720F → S in ACF47606 (PubMed:18593464).Curated1
Sequence conflicti1191G → A in AAA59591 (PubMed:2819873).Curated1
Sequence conflicti1272L → V in AAA59591 (PubMed:2819873).Curated1
Sequence conflicti1272L → V in CAB56793 (Ref. 2) Curated1
Sequence conflicti1272L → V in AAA59590 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041738143R → Q1 PublicationCorresponds to variant dbSNP:rs35469582EnsemblClinVar.1
Natural variantiVAR_064855150H → 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 PublicationCorresponds to variant dbSNP:rs1436957498Ensembl.1
Natural variantiVAR_041739156S → L1 PublicationCorresponds to variant dbSNP:rs56311081EnsemblClinVar.1
Natural variantiVAR_041740168E → 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 PublicationsCorresponds to variant dbSNP:rs55985569EnsemblClinVar.1
Natural variantiVAR_032478238L → S. Corresponds to variant dbSNP:rs34349517EnsemblClinVar.1
Natural variantiVAR_032479316I → M. Corresponds to variant dbSNP:rs35225896EnsemblClinVar.1
Natural variantiVAR_006285320A → V1 PublicationCorresponds to variant dbSNP:rs35776110EnsemblClinVar.1
Natural variantiVAR_079370375N → K Found in lung cancer also including cases carrying EGFR mutations; unknown pathological significance; decreased hepatocyte growth factor-activated receptor activity; decreased interaction with HGF. 1 PublicationCorresponds to variant dbSNP:rs776693512EnsemblClinVar.1
Natural variantiVAR_032480375N → S1 PublicationCorresponds to variant dbSNP:rs33917957EnsemblClinVar.1
Natural variantiVAR_064856385C → 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 PublicationCorresponds to variant dbSNP:rs752055485Ensembl.1
Natural variantiVAR_032481773P → L in gastric cancer. 1 PublicationCorresponds to variant dbSNP:rs771333219Ensembl.1
Natural variantiVAR_075757841F → V in DFNB97. 1 PublicationCorresponds to variant dbSNP:rs794728016EnsemblClinVar.1
Natural variantiVAR_076584964 – 1010Missing in OSFD; loss of CBL-mediated destabilization. 1 PublicationAdd BLAST47
Natural variantiVAR_032482970R → C2 PublicationsCorresponds to variant dbSNP:rs34589476EnsemblClinVar.1
Natural variantiVAR_032483991P → S in gastric cancer; prolonged tyrosine phosphorylation in response to HGF/SF; transforming activity in athymic nude mice. 1 PublicationCorresponds to variant dbSNP:rs768678989Ensembl.1
Natural variantiVAR_032484992T → 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 PublicationsCorresponds to variant dbSNP:rs56391007EnsemblClinVar.1
Natural variantiVAR_0765851003Y → S Probable disease-associated mutation found in lesional sample from a patient with sporadically occurring, unilateral osteofibrous dysplasia; somatic mutation; complete loss of ligand-induced CBL-mediated ubiquitination, resulting in protein stabilization. 1 Publication1
Natural variantiVAR_0324851092V → I in RCCP; constitutive autophosphorylation. 3 PublicationsCorresponds to variant dbSNP:rs786202724Ensembl.1
Natural variantiVAR_0324861094H → L in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 1 Publication1
Natural variantiVAR_0324871094H → R in RCCP; causes malignant transformation in cell lines. 2 PublicationsCorresponds to variant dbSNP:rs121913243Ensembl.1
Natural variantiVAR_0324881094H → Y in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 1 PublicationCorresponds to variant dbSNP:rs121913244Ensembl.1
Natural variantiVAR_0324891106H → D in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 2 Publications1
Natural variantiVAR_0062861131M → T in RCCP; germline mutation. 2 PublicationsCorresponds to variant dbSNP:rs121913668Ensembl.1
Natural variantiVAR_0324901173T → I in HCC. 1 PublicationCorresponds to variant dbSNP:rs121913675Ensembl.1
Natural variantiVAR_0062871188V → L in RCCP; germline mutation. 2 PublicationsCorresponds to variant dbSNP:rs121913669Ensembl.1
Natural variantiVAR_0062881195L → V in RCCP; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913673Ensembl.1
Natural variantiVAR_0062891220V → I in RCCP; germline mutation. 1 PublicationCorresponds to variant dbSNP:rs121913670Ensembl.1
Natural variantiVAR_0062911228D → H in RCCP; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913671Ensembl.1
Natural variantiVAR_0062901228D → N in RCCP; germline mutation. 1 PublicationCorresponds to variant dbSNP:rs121913671Ensembl.1
Natural variantiVAR_0062921230Y → C in RCCP; germline mutation. 2 PublicationsCorresponds to variant dbSNP:rs121913246Ensembl.1
Natural variantiVAR_0324911230Y → D in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines. 2 Publications1
Natural variantiVAR_0062931230Y → H in RCCP; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913247Ensembl.1
Natural variantiVAR_0324921244K → R in HCC. 1 PublicationCorresponds to variant dbSNP:rs121913677Ensembl.1
Natural variantiVAR_0324931250M → I in HCC. 1 PublicationCorresponds to variant dbSNP:rs121913676Ensembl.1
Natural variantiVAR_0062941250M → T in RCCP; somatic mutation. 2 PublicationsCorresponds to variant dbSNP:rs121913245Ensembl.1
Natural variantiVAR_0648571294V → 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 PublicationCorresponds to variant dbSNP:rs1263785859Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_042447755 – 764SGGSTITGVG → RHVNIALIQR in isoform 3. 1 Publication10
Alternative sequenceiVSP_005005755S → STWWKEPLNIVSFLFCFAS in isoform 2. 1 Publication1
Alternative sequenceiVSP_042448765 – 1390Missing in isoform 3. 1 PublicationAdd BLAST626

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS43636.1 [P08581-1]
CCDS47689.1 [P08581-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A40175 TVHUME

NCBI Reference Sequences

More...
RefSeqi
NP_000236.2, NM_000245.3 [P08581-1]
NP_001120972.1, NM_001127500.2 [P08581-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.132966

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000318493; ENSP00000317272; ENSG00000105976 [P08581-2]
ENST00000397752; ENSP00000380860; ENSG00000105976 [P08581-1]
ENST00000436117; ENSP00000410980; ENSG00000105976 [P08581-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4233

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4233

UCSC genome browser

More...
UCSCi
uc003vij.4 human [P08581-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

C-MET entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_000245.3 [P08581-1]
NP_001120972.1, NM_001127500.2 [P08581-2]
UniGeneiHs.132966

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4MXCX-ray1.63A1038-1346[»]
4O3TX-ray2.99B25-567[»]
4O3UX-ray3.04B25-567[»]
4R1VX-ray1.20A1055-1345[»]
4R1YX-ray2.00A1055-1346[»]
4XMOX-ray1.75A1048-1350[»]
4XYFX-ray1.85A1048-1351[»]
5DG5X-ray2.60A/B1038-1346[»]
5EOBX-ray1.75A1038-1346[»]
5EYCX-ray1.80A1048-1351[»]
5EYDX-ray1.85A1048-1351[»]
5HLWX-ray1.97A1057-1355[»]
5HNIX-ray1.71X/Y1049-1360[»]
5HO6X-ray1.97A1049-1360[»]
5HOAX-ray2.14A1049-1360[»]
5HORX-ray2.20A1049-1360[»]
5HTIX-ray1.66A1038-1346[»]
5LSPX-ray2.60A/P519-743[»]
X/Y25-35[»]
5T3QX-ray2.00A1048-1350[»]
5UABX-ray1.90A1023-1360[»]
5UADX-ray2.25A1023-1360[»]
5UAFX-ray2.25A1023-1360[»]
5YA5X-ray1.89A1038-1346[»]
ProteinModelPortaliP08581
SMRiP08581
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110391, 67 interactors
CORUMiP08581
DIPiDIP-6023N
ELMiP08581
IntActiP08581, 91 interactors
MINTiP08581
STRINGi9606.ENSP00000317272

Chemistry databases

BindingDBiP08581
ChEMBLiCHEMBL3717
DrugBankiDB07969 3-[3-(4-methylpiperazin-1-yl)-7-(trifluoromethyl)quinoxalin-5-yl]phenol
DB08875 Cabozantinib
DB08865 Crizotinib
DB02152 K-252a
DB05216 MP470
DB06995 N-({4-[(2-aminopyridin-4-yl)oxy]-3-fluorophenyl}carbamoyl)-2-(4-fluorophenyl)acetamide
DB05153 XL184
GuidetoPHARMACOLOGYi1815

PTM databases

GlyConnecti680
iPTMnetiP08581
PhosphoSitePlusiP08581
SwissPalmiP08581
UniCarbKBiP08581

Polymorphism and mutation databases

BioMutaiMET
DMDMi251757497

2D gel databases

OGPiP08581

Proteomic databases

EPDiP08581
jPOSTiP08581
MaxQBiP08581
PaxDbiP08581
PeptideAtlasiP08581
PRIDEiP08581
ProteomicsDBi52128
52129 [P08581-2]
52130 [P08581-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4233
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318493; ENSP00000317272; ENSG00000105976 [P08581-2]
ENST00000397752; ENSP00000380860; ENSG00000105976 [P08581-1]
ENST00000436117; ENSP00000410980; ENSG00000105976 [P08581-3]
GeneIDi4233
KEGGihsa:4233
UCSCiuc003vij.4 human [P08581-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4233
DisGeNETi4233
EuPathDBiHostDB:ENSG00000105976.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MET
HGNCiHGNC:7029 MET
HPAiCAB005282
CAB018577
HPA055607
MalaCardsiMET
MIMi114550 phenotype
164860 gene
605074 phenotype
607278 phenotype
616705 phenotype
neXtProtiNX_P08581
OpenTargetsiENSG00000105976
Orphaneti90636 Autosomal recessive non-syndromic sensorineural deafness type DFNB
47044 Hereditary papillary renal cell carcinoma
106 NON RARE IN EUROPE: Autism
488265 Osteofibrous dysplasia
319298 Papillary renal cell carcinoma
33402 Pediatric hepatocellular carcinoma
PharmGKBiPA30763

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1095 Eukaryota
KOG3610 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000158022
HOGENOMiHOG000220900
HOVERGENiHBG006348
InParanoidiP08581
KOiK05099
OMAiTNMLKCT
OrthoDBi1153238at2759
PhylomeDBiP08581
TreeFamiTF317402

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-1257604 PIP3 activates AKT signaling
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-416550 Sema4D mediated inhibition of cell attachment and migration
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6806942 MET Receptor Activation
R-HSA-6807004 Negative regulation of MET activity
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8851805 MET activates RAS signaling
R-HSA-8851907 MET activates PI3K/AKT signaling
R-HSA-8865999 MET activates PTPN11
R-HSA-8874081 MET activates PTK2 signaling
R-HSA-8875360 InlB-mediated entry of Listeria monocytogenes into host cell
R-HSA-8875513 MET interacts with TNS proteins
R-HSA-8875555 MET activates RAP1 and RAC1
R-HSA-8875656 MET receptor recycling
R-HSA-8875791 MET activates STAT3
R-HSA-9022699 MECP2 regulates neuronal receptors and channels
SignaLinkiP08581
SIGNORiP08581

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
MET human
EvolutionaryTraceiP08581

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
C-Met

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
4233

Protein Ontology

More...
PROi
PR:P08581

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000105976 Expressed in 207 organ(s), highest expression level in pigmented layer of retina
CleanExiHS_MET
ExpressionAtlasiP08581 baseline and differential
GenevisibleiP08581 HS

Family and domain databases

Gene3Di2.130.10.10, 1 hit
2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
IPR011009 Kinase-like_dom_sf
IPR002165 Plexin_repeat
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR016201 PSI
IPR001627 Semap_dom
IPR036352 Semap_dom_sf
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_sf
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF01437 PSI, 1 hit
PF01403 Sema, 1 hit
PF01833 TIG, 3 hits
PIRSFiPIRSF000617 TyrPK_HGF-R, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00429 IPT, 4 hits
SM00423 PSI, 1 hit
SM00630 Sema, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF101912 SSF101912, 1 hit
SSF56112 SSF56112, 1 hit
SSF81296 SSF81296, 3 hits
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS51004 SEMA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMET_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08581
Secondary accession number(s): A1L467
, B5A932, E7EQ94, O60366, Q12875, Q9UDX7, Q9UPL8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 7, 2009
Last modified: January 16, 2019
This is version 245 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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