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P16056

- MET_MOUSE

UniProt

P16056 - MET_MOUSE

Protein

Hepatocyte growth factor receptor

Gene

Met

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei306 – 3072CleavageSequence Analysis
    Binding sitei1108 – 11081ATPPROSITE-ProRule annotation
    Active sitei1202 – 12021Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1082 – 10909ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hepatocyte growth factor-activated receptor activity Source: MGI
    3. protein binding Source: IntAct
    4. protein kinase activity Source: MGI

    GO - Biological processi

    1. activation of MAPK activity Source: MGI
    2. adult behavior Source: MGI
    3. brain development Source: MGI
    4. glucose homeostasis Source: MGI
    5. hepatocyte growth factor receptor signaling pathway Source: MGI
    6. liver development Source: MGI
    7. muscle cell migration Source: MGI
    8. muscle organ development Source: MGI
    9. myoblast proliferation Source: MGI
    10. myotube differentiation Source: MGI
    11. placenta development Source: MGI
    12. positive chemotaxis Source: UniProtKB
    13. positive regulation of endothelial cell chemotaxis Source: UniProtKB
    14. positive regulation of glucose transport Source: MGI
    15. protein autophosphorylation Source: MGI
    16. regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling Source: MGI
    17. regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
    18. regulation of synaptic transmission Source: BHF-UCL
    19. semaphorin-plexin signaling pathway Source: UniProtKB
    20. skeletal muscle tissue development Source: MGI

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.

    Names & Taxonomyi

    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
    Gene namesi
    Name:Met
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:96969. Met.

    Subcellular locationi

    GO - Cellular componenti

    1. basal plasma membrane Source: MGI
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Activation of Met after rearrangement with the TPR (translocated promoter) locus of chromosome 1 produces an oncogenic protein.

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 13791355Hepatocyte growth factor receptorPRO_0000024441Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi95 ↔ 101PROSITE-ProRule annotation
    Disulfide bondi98 ↔ 160PROSITE-ProRule annotation
    Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi133 ↔ 141PROSITE-ProRule annotation
    Disulfide bondi171 ↔ 174PROSITE-ProRule annotation
    Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi297 ↔ 362PROSITE-ProRule annotation
    Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi384 ↔ 396PROSITE-ProRule annotation
    Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi519 ↔ 537PROSITE-ProRule annotation
    Disulfide bondi525 ↔ 560PROSITE-ProRule annotation
    Disulfide bondi528 ↔ 544PROSITE-ProRule annotation
    Disulfide bondi540 ↔ 550PROSITE-ProRule annotation
    Glycosylationi606 – 6061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi634 – 6341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi784 – 7841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi878 – 8781N-linked (GlcNAc...)Sequence Analysis
    Modified residuei975 – 9751PhosphothreonineBy similarity
    Modified residuei988 – 9881PhosphoserineBy similarity
    Modified residuei995 – 9951PhosphoserineBy similarity
    Modified residuei998 – 9981PhosphoserineBy similarity
    Modified residuei1001 – 10011PhosphotyrosineBy similarity
    Modified residuei1228 – 12281PhosphotyrosineBy similarity
    Modified residuei1232 – 12321Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1233 – 12331Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1287 – 12871PhosphothreonineBy similarity
    Modified residuei1347 – 13471Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1354 – 13541Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1363 – 13631PhosphotyrosineBy similarity

    Post-translational modificationi

    Autophosphorylated in response to ligand binding on Tyr-1232 and Tyr-1233 in the kinase domain leading to further phosphorylation of Tyr-1347 and Tyr-1354 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1347 and Tyr-1363 By similarity. Dephosphorylated by PTPN1 and PTPN2 By similarity.By similarity
    Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP16056.
    PaxDbiP16056.
    PRIDEiP16056.

    PTM databases

    PhosphoSiteiP16056.

    Miscellaneous databases

    PMAP-CutDBP16056.

    Expressioni

    Gene expression databases

    CleanExiMM_MET.
    GenevestigatoriP16056.

    Interactioni

    Subunit structurei

    Heterodimer made of an alpha chain (50 kDa) and a beta chain (145 kDa) which are disulfide linked By similarity. Binds PLXNB1 By similarity. Interacts when phosphorylated with downstream effectors including STAT3, PIK3R1, SRC, PCLG1, GRB2 and GAB1 By similarity. When phosphorylated at Tyr-1354, interacts with INPPL1/SHIP2 By similarity. Interacts with RANBP9 and RANBP10 By similarity. Interacts with INPP5D/SHIP1. Interacts with SPSB1, SPSB2, SPSB4 and probably SPSB3. 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 By similarity. Interacts with PTPN1 and PTPN2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CblP226822EBI-1798780,EBI-640919
    HGFP142102EBI-1798780,EBI-1039104From a different organism.
    KdrP359183EBI-1798780,EBI-1555005

    Protein-protein interaction databases

    IntActiP16056. 4 interactions.
    MINTiMINT-137318.

    Structurei

    3D structure databases

    ProteinModelPortaliP16056.
    SMRiP16056. Positions 40-740, 1022-1376.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 931907ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini955 – 1379425CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei932 – 95423HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 514488SemaPROSITE-ProRule annotationAdd
    BLAST
    Domaini562 – 65493IPT/TIG 1Add
    BLAST
    Domaini656 – 73883IPT/TIG 2Add
    BLAST
    Domaini741 – 83595IPT/TIG 3Add
    BLAST
    Domaini1076 – 1343268Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1210 – 1379170Interaction with RANBP9By similarityAdd
    BLAST
    Regioni1318 – 135740Interaction with MUC20By similarityAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
    Contains 3 IPT/TIG domains.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 Sema domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000220900.
    HOVERGENiHBG006348.
    InParanoidiP16056.
    PhylomeDBiP16056.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    2.60.40.10. 3 hits.
    InterProiIPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    IPR011009. Kinase-like_dom.
    IPR016201. Plexin-like_fold.
    IPR002165. Plexin_repeat.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001627. Semap_dom.
    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.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF01437. PSI. 1 hit.
    PF01403. Sema. 1 hit.
    PF01833. TIG. 3 hits.
    [Graphical view]
    PIRSFiPIRSF000617. TyrPK_HGF-R. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00429. IPT. 4 hits.
    SM00423. PSI. 1 hit.
    SM00630. Sema. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF101912. SSF101912. 1 hit.
    SSF103575. SSF103575. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF81296. SSF81296. 3 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS51004. SEMA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16056-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAPTVLAPG ILVLLLSLVQ RSHGECKEAL VKSEMNVNMK YQLPNFTAET     50
    PIQNVVLHGH HIYLGATNYI YVLNDKDLQK VSEFKTGPVL EHPDCLPCRD 100
    CSSKANSSGG VWKDNINMAL LVDTYYDDQL ISCGSVNRGT CQRHVLPPDN 150
    SADIQSEVHC MFSPEEESGQ CPDCVVSALG AKVLLSEKDR FINFFVGNTI 200
    NSSYPPGYSL HSISVRRLKE TQDGFKFLTD QSYIDVLPEF LDSYPIKYIH 250
    AFESNHFIYF LTVQKETLDA QTFHTRIIRF CSVDSGLHSY MEMPLECILT 300
    EKRRKRSTRE EVFNILQAAY VSKPGANLAK QIGASPSDDI LFGVFAQSKP 350
    DSAEPVNRSA VCAFPIKYVN DFFNKIVNKN NVRCLQHFYG PNHEHCFNRT 400
    LLRNSSGCEA RSDEYRTEFT TALQRVDLFM GRLNQVLLTS ISTFIKGDLT 450
    IANLGTSEGR FMQVVLSRTA HLTPHVNFLL DSHPVSPEVI VEHPSNQNGY 500
    TLVVTGKKIT KIPLNGLGCG HFQSCSQCLS APYFIQCGWC HNQCVRFDEC 550
    PSGTWTQEIC LPAVYKVFPT SAPLEGGTVL TICGWDFGFR KNNKFDLRKT 600
    KVLLGNESCT LTLSESTTNT LKCTVGPAMS EHFNVSVIIS NSRETTQYSA 650
    FSYVDPVITS ISPRYGPQAG GTLLTLTGKY LNSGNSRHIS IGGKTCTLKS 700
    VSDSILECYT PAQTTSDEFP VKLKIDLANR ETSSFSYRED PVVYEIHPTK 750
    SFISGGSTIT GIGKTLNSVS LPKLVIDVHE VGVNYTVACQ HRSNSEIICC 800
    TTPSLKQLGL QLPLKTKAFF LLDGILSKHF DLTYVHNPVF EPFEKPVMIS 850
    MGNENVVEIK GNNIDPEAVK GEVLKVGNQS CESLHWHSGA VLCTVPSDLL 900
    KLNSELNIEW KQAVSSTVLG KVIVQPDQNF AGLIIGAVSI SVVVLLLSGL 950
    FLWMRKRKHK DLGSELVRYD ARVHTPHLDR LVSARSVSPT TEMVSNESVD 1000
    YRATFPEDQF PNSSQNGACR QVQYPLTDLS PILTSGDSDI SSPLLQNTVH 1050
    IDLSALNPEL VQAVQHVVIG PSSLIVHFNE VIGRGHFGCV YHGTLLDNDG 1100
    KKIHCAVKSL NRITDIEEVS QFLTEGIIMK DFSHPNVLSL LGICLRSEGS 1150
    PLVVLPYMKH GDLRNFIRNE THNPTVKDLI GFGLQVAKGM KYLASKKFVH 1200
    RDLAARNCML DEKFTVKVAD FGLARDMYDK EYYSVHNKTG AKLPVKWMAL 1250
    ESLQTQKFTT KSDVWSFGVL LWELMTRGAP PYPDVNTFDI TIYLLQGRRL 1300
    LQPEYCPDAL YEVMLKCWHP KAEMRPSFSE LVSRISSIFS TFIGEHYVHV 1350
    NATYVNVKCV APYPSLLPSQ DNIDGEGNT 1379
    Length:1,379
    Mass (Da):153,549
    Last modified:April 1, 1990 - v1
    Checksum:iFC5CC87FDD8ADED8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1199 – 11991V → I in AAA40015. (PubMed:2482828)Curated
    Sequence conflicti1255 – 12551T → R in AAA40015. (PubMed:2482828)Curated
    Sequence conflicti1261 – 12611K → T in AAA40015. (PubMed:2482828)Curated
    Sequence conflicti1269 – 12702VL → IP(PubMed:2482828)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00671 mRNA. Translation: CAA68680.1.
    M33424 mRNA. Translation: AAA40015.1.
    CCDSiCCDS19925.1.
    PIRiS01254.
    UniGeneiMm.86844.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00671 mRNA. Translation: CAA68680.1 .
    M33424 mRNA. Translation: AAA40015.1 .
    CCDSi CCDS19925.1.
    PIRi S01254.
    UniGenei Mm.86844.

    3D structure databases

    ProteinModelPortali P16056.
    SMRi P16056. Positions 40-740, 1022-1376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P16056. 4 interactions.
    MINTi MINT-137318.

    Chemistry

    ChEMBLi CHEMBL5585.

    PTM databases

    PhosphoSitei P16056.

    Proteomic databases

    MaxQBi P16056.
    PaxDbi P16056.
    PRIDEi P16056.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:96969. Met.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000220900.
    HOVERGENi HBG006348.
    InParanoidi P16056.
    PhylomeDBi P16056.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    ChiTaRSi MET. mouse.
    PMAP-CutDB P16056.
    PROi P16056.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_MET.
    Genevestigatori P16056.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    2.60.40.10. 3 hits.
    InterProi IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    IPR011009. Kinase-like_dom.
    IPR016201. Plexin-like_fold.
    IPR002165. Plexin_repeat.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001627. Semap_dom.
    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.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF01437. PSI. 1 hit.
    PF01403. Sema. 1 hit.
    PF01833. TIG. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF000617. TyrPK_HGF-R. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00429. IPT. 4 hits.
    SM00423. PSI. 1 hit.
    SM00630. Sema. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101912. SSF101912. 1 hit.
    SSF103575. SSF103575. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF81296. SSF81296. 3 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS51004. SEMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the mouse met proto-oncogene."
      Chan A.M.-L., King H.W.S., Deakin E.A., Tempest P.R., Hilkens J., Kroezen V., Edwards D.R., Wills A.J., Brookes P., Cooper C.S.
      Oncogene 2:593-599(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family."
      Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.
      Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1199-1270.
    3. "The Met receptor tyrosine kinase transduces motility, proliferation, and morphogenic signals of scatter factor/hepatocyte growth factor in epithelial cells."
      Weidner K.M., Sachs M., Birchmeier W.
      J. Cell Biol. 121:145-154(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 924-935.
    4. "Essential role for the c-met receptor in the migration of myogenic precursor cells into the limb bud."
      Bladt F., Riethmacher D., Isenmann S., Aguzzi A., Birchmeier C.
      Nature 376:768-771(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEVELOPMENT.
    5. "The SH2-containing inositol 5-phosphatase (SHIP)-1 is implicated in the control of cell-cell junction and induces dissociation and dispersion of MDCK cells."
      Mancini A., Koch A., Wilms R., Tamura T.
      Oncogene 21:1477-1484(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    6. "MUC20 suppresses the hepatocyte growth factor-induced Grb2-Ras pathway by binding to a multifunctional docking site of met."
      Higuchi T., Orita T., Katsuya K., Yamasaki Y., Akiyama K., Li H., Yamamoto T., Saito Y., Nakamura M.
      Mol. Cell. Biol. 24:7456-7468(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MUC20.
    7. "The SPRY domain of SSB-2 adopts a novel fold that presents conserved Par-4-binding residues."
      Masters S.L., Yao S., Willson T.A., Zhang J.-G., Palmer K.R., Smith B.J., Babon J.J., Nicola N.A., Norton R.S., Nicholson S.E.
      Nat. Struct. Mol. Biol. 13:77-84(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPSB1; SPSB2 AND SPSB4.

    Entry informationi

    Entry nameiMET_MOUSE
    AccessioniPrimary (citable) accession number: P16056
    Secondary accession number(s): Q62125
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3