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Entry version 179 (26 Feb 2020)
Sequence version 1 (01 May 1997)
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Protein

Hepatocyte growth factor receptor

Gene

Met

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei1111ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei1205Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi1085 – 1093ATPPROSITE-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

More...
BRENDAi
2.7.10.1 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1257604 PIP3 activates AKT signaling
R-RNO-416550 Sema4D mediated inhibition of cell attachment and migration
R-RNO-5673001 RAF/MAP kinase cascade
R-RNO-6806942 MET Receptor Activation
R-RNO-6807004 Negative regulation of MET activity
R-RNO-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-RNO-8851805 MET activates RAS signaling
R-RNO-8851907 MET activates PI3K/AKT signaling
R-RNO-8865999 MET activates PTPN11
R-RNO-8874081 MET activates PTK2 signaling
R-RNO-8875513 MET interacts with TNS proteins
R-RNO-8875555 MET activates RAP1 and RAC1
R-RNO-8875656 MET receptor recycling
R-RNO-8875791 MET activates STAT3

<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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3082 Met

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 – 935ExtracellularSequence analysisAdd BLAST911
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei936 – 956HelicalSequence analysisAdd BLAST21
Topological domaini957 – 1379CytoplasmicSequence analysisAdd BLAST423

Keywords - Cellular componenti

Membrane

<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

Keywords - Diseasei

Proto-oncogene

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002444225 – 1382Hepatocyte growth factor receptorAdd BLAST1358

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 ↔ 101PROSITE-ProRule annotation
Disulfide bondi98 ↔ 160PROSITE-ProRule annotation
Glycosylationi106N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi133 ↔ 141PROSITE-ProRule annotation
Disulfide bondi173 ↔ 176PROSITE-ProRule annotation
Glycosylationi203N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi299 ↔ 364PROSITE-ProRule annotation
Glycosylationi359N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi386 ↔ 398PROSITE-ProRule annotation
Glycosylationi400N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi521 ↔ 539PROSITE-ProRule annotation
Disulfide bondi527 ↔ 562PROSITE-ProRule annotation
Disulfide bondi530 ↔ 546PROSITE-ProRule annotation
Disulfide bondi542 ↔ 552PROSITE-ProRule annotation
Glycosylationi608N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi636N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi786N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi880N-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 residuei967PhosphoserineBy similarity1
Modified residuei978PhosphothreonineBy similarity1
Modified residuei991PhosphoserineBy similarity1
Modified residuei998PhosphoserineBy similarity1
Modified residuei1001PhosphoserineBy similarity1
Modified residuei1004PhosphotyrosineBy similarity1
Modified residuei1231PhosphotyrosineBy similarity1
Modified residuei1235Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1236Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1290PhosphothreonineBy similarity1
Modified residuei1350Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1357Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1366PhosphotyrosineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-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).By similarity
Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation (By similarity).By similarity

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>Sitei308 – 309CleavageSequence analysis2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
P97523

PRoteomics IDEntifications database

More...
PRIDEi
P97523

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P97523

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

More...
PhosphoSitePlusi
P97523

<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 at highest levels in lung, liver and kidney, also expressed in stomach, intestine, spleen, testis and brain. Not expressed in heart or muscle.

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expression is down-regulated during pregnancy and is virtually undetectable during lactation. Expression progressively increases post-lactation.

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By interleukin-6 and acute acid-induced gastric injury. Inhibited by prolactin.

<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%5Fsection">'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%5Fsection">'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.

Interacts with INPP5D/SHIP1. When phosphorylated at Tyr-1357, 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 HSP90AA1 and HSP90AB1; the interaction suppresses MET kinase activity.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000009662

<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

3D structure databases

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

More...
SMRi
P97523

Database of comparative protein structure models

More...
ModBasei
Search...

<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%5Fand%5Fdomains%5Fsection">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 – 516SemaPROSITE-ProRule annotationAdd BLAST490
Domaini564 – 656IPT/TIG 1Add BLAST93
Domaini658 – 740IPT/TIG 2Add BLAST83
Domaini743 – 837IPT/TIG 3Add BLAST95
Domaini1079 – 1346Protein 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>Regioni1213 – 1382Interaction with RANBP9By similarityAdd BLAST170
Regioni1321 – 1360Interaction with MUC20By similarityAdd 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.By similarity
The beta-propeller Sema domain mediates binding to HGF.By similarity

<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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P97523

KEGG Orthology (KO)

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KOi
K05099

Database of Orthologous Groups

More...
OrthoDBi
408584at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P97523

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.130.10.10, 1 hit
2.60.40.10, 3 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
IPR031148 Plexin
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

The PANTHER Classification System

More...
PANTHERi
PTHR22625 PTHR22625, 1 hit

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000617 TyrPK_HGF-R, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
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

More...
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P97523-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKAPTALAPG ILLLLLTLAQ RSHGECKEAL VKSEMNVNMK YQLPNFTAET
60 70 80 90 100
PIHNVVLPGH HIYLGATNYI YVLNDKDLQK VSEFKTGPVV EHPDCFPCQD
110 120 130 140 150
CSSKANVSGG VWKDNVNMAL LVDTYYDDQL ISCGSVNRGT CQRHVLPPDN
160 170 180 190 200
AADIQSEVHC MFSPLAEEES GQCPDCVVSA LGAKVLLSEK DRFINFFVGN
210 220 230 240 250
TINSSYPPDY SLHSISVRRL KETQDGFKFL TDQSYIDVLP EFRDSYPIKY
260 270 280 290 300
IHAFESNHFI YFLTVQKETL DAQTFHTRII RFCSVDSGLH SYMEMPLECI
310 320 330 340 350
LTEKRRKRST REEVFNILQA AYVSKPGANL AKQIGASPYD DILYGVFAQS
360 370 380 390 400
KPDSAEPMNR SAVCAFPIKY VNDFFNKIVN KNNVRCLQHF YGPNHEHCFN
410 420 430 440 450
RTLLRNSSGC EVRSDEYRTE FTTALQRVDL FMGRLNHVLL TSISTFIKGD
460 470 480 490 500
LTIANLGTSE GRFMQVVLSR TAHFTPHVNF LLDSYPVSPE VIVEHPSNQN
510 520 530 540 550
GYTLVVTGKK ITKIPLNGLG CGHFQSCSQC LSPPYFIQCG WCHNRCVHSN
560 570 580 590 600
ECPSGTWTQE ICLPAVYKVF PTSAPLEGGT MLTICGWDFG FKKNNKFDLR
610 620 630 640 650
KTKVLLGNES CTLTLSESTT NTLKCTVGPA MSEHFNVSVI VSNSRETTQY
660 670 680 690 700
SAFSYVDPVI TSISPRYGPH AGGTLLTLTG KYLNSGNSRH ISIGGKTCTL
710 720 730 740 750
KSVSDSILEC YTPGHTVSAE FPVKLKIDLA DRVTSSFSYR EDPVVSEIHP
760 770 780 790 800
TKSFISGGST ITGIGKNLNS VSTPKLVIEV HDVGVNYTVA CQHRSSSEII
810 820 830 840 850
CCTTPSLRQL DLQLPLKTKA FFLLDGILSK HFDLTYVHDP MFKPFEKPVM
860 870 880 890 900
ISMGNENVVE IKGDDIDPEA VKGEVLKVGN KSCENLHWHS EALLCTVPSD
910 920 930 940 950
LLKLNGGELN IEWKQAVSST VLGKVIVQPD QNFAGLIIGA VSISVVVLLV
960 970 980 990 1000
SGLFLWLRKR KHKDLGSELV RYDARVHTPH LDRLVSARSV SPTTEMVSNE
1010 1020 1030 1040 1050
SVDYRATFPE DQFPNSSQNG ACRQVQYLLT DLSPILTSGD SDISSPLLQN
1060 1070 1080 1090 1100
TVHIDLSALN PELVQAVPHV VIGPSSLIVH FNEVIGRGHF GCVYHGTLLD
1110 1120 1130 1140 1150
SDGKKIHCAV KSLNRITDIE EVSQFLTEGI IMKDFSHPNV LSLLGICLRS
1160 1170 1180 1190 1200
EGSPLVVLPY MKHGDLRNFI RNETHNPTVK DLIGFGLQVA KGMKYLVSKK
1210 1220 1230 1240 1250
FVHRDLAARN CMLDEKFTVK VADFGLARDM YDKEYYSVHN KTGAKLPVKW
1260 1270 1280 1290 1300
MALESLQTQK FTTKSDVWSF GVLLWELMTR GAPPYPDVNT FDITIYLLQG
1310 1320 1330 1340 1350
RRLLQPEYCP DALYEVMLKC WHPKAEMRPS VSELVSRISS IFSTFIGEHY
1360 1370 1380
VHVNATYVNV KCVAPYPSLL PSQDNIDGEA NT
Length:1,382
Mass (Da):153,941
Last modified:May 1, 1997 - v1
<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:i66B8F2C88FE34427
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JY19A0A0G2JY19_RAT
Hepatocyte growth factor receptor
Met
1,409Annotation score:

Annotation score:4 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 conflicti53H → Q in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti58P → H in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti240P → G in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti427R → A in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti485Y → H in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti490 – 495EVIVEH → GAAGIR (PubMed:8166728).Curated6
Sequence conflicti533P → A in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti740R → G in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti744V → F in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti808R → Q in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti890 – 893SEAL → TASV in CAA86508 (PubMed:7628535).Curated4
Sequence conflicti907Missing in CAA86508 (PubMed:7628535).Curated1
Sequence conflicti924K → E in CAA86508 (PubMed:7628535).Curated1
Sequence conflicti934A → R in CAA86508 (PubMed:7628535).Curated1
Sequence conflicti1028L → P in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti1068P → Q in AAB19189 (PubMed:8853431).Curated1
Sequence conflicti1197V → A (PubMed:8853431).Curated1
Sequence conflicti1197V → A (Ref. 5) Curated1
Sequence conflicti1331V → F in AAB19189 (PubMed:8853431).Curated1

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
X96786 mRNA Translation: CAA65582.1
U65007 mRNA Translation: AAB19189.1
S69881 mRNA Translation: AAB30575.1
Z46374 mRNA Translation: CAA86508.1
AB012281 Genomic DNA Translation: BAA28171.1

Protein sequence database of the Protein Information Resource

More...
PIRi
PC2131

NCBI Reference Sequences

More...
RefSeqi
NP_113705.1, NM_031517.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24553

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24553

UCSC genome browser

More...
UCSCi
RGD:3082 rat

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96786 mRNA Translation: CAA65582.1
U65007 mRNA Translation: AAB19189.1
S69881 mRNA Translation: AAB30575.1
Z46374 mRNA Translation: CAA86508.1
AB012281 Genomic DNA Translation: BAA28171.1
PIRiPC2131
RefSeqiNP_113705.1, NM_031517.2

3D structure databases

SMRiP97523
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009662

PTM databases

iPTMnetiP97523
PhosphoSitePlusiP97523

Proteomic databases

PaxDbiP97523
PRIDEiP97523

Genome annotation databases

GeneIDi24553
KEGGirno:24553
UCSCiRGD:3082 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4233
RGDi3082 Met

Phylogenomic databases

eggNOGiKOG1095 Eukaryota
KOG3610 Eukaryota
COG0515 LUCA
InParanoidiP97523
KOiK05099
OrthoDBi408584at2759
PhylomeDBiP97523

Enzyme and pathway databases

BRENDAi2.7.10.1 5301
ReactomeiR-RNO-1257604 PIP3 activates AKT signaling
R-RNO-416550 Sema4D mediated inhibition of cell attachment and migration
R-RNO-5673001 RAF/MAP kinase cascade
R-RNO-6806942 MET Receptor Activation
R-RNO-6807004 Negative regulation of MET activity
R-RNO-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-RNO-8851805 MET activates RAS signaling
R-RNO-8851907 MET activates PI3K/AKT signaling
R-RNO-8865999 MET activates PTPN11
R-RNO-8874081 MET activates PTK2 signaling
R-RNO-8875513 MET interacts with TNS proteins
R-RNO-8875555 MET activates RAP1 and RAC1
R-RNO-8875656 MET receptor recycling
R-RNO-8875791 MET activates STAT3

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P97523

Family and domain databases

Gene3Di2.130.10.10, 1 hit
2.60.40.10, 3 hits
InterProiView protein in InterPro
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
IPR011009 Kinase-like_dom_sf
IPR031148 Plexin
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
PANTHERiPTHR22625 PTHR22625, 1 hit
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_RAT
<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: P97523
Secondary accession number(s): P97579, Q63119, Q63964
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1997
Last modified: February 26, 2020
This is version 179 of the entry and version 1 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

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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