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P97523

- MET_RAT

UniProt

P97523 - MET_RAT

Protein

Hepatocyte growth factor receptor

Gene

Met

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      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
    Sitei308 – 3092CleavageSequence Analysis
    Binding sitei1111 – 11111ATPPROSITE-ProRule annotation
    Active sitei1205 – 12051Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1085 – 10939ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. beta-catenin binding Source: RGD
    3. hepatocyte growth factor-activated receptor activity Source: RGD
    4. phosphatidylinositol 3-kinase binding Source: RGD
    5. phospholipase binding Source: RGD
    6. protein complex binding Source: RGD
    7. protein heterodimerization activity Source: RGD
    8. protein tyrosine kinase activity Source: RGD

    GO - Biological processi

    1. brain development Source: RGD
    2. cell aging Source: RGD
    3. cellular response to arsenic-containing substance Source: RGD
    4. cellular response to glucose stimulus Source: RGD
    5. cellular response to growth factor stimulus Source: RGD
    6. cellular response to inorganic substance Source: RGD
    7. cellular response to interleukin-6 Source: RGD
    8. cellular response to peptide hormone stimulus Source: RGD
    9. central nervous system neuron differentiation Source: RGD
    10. hepatocyte growth factor receptor signaling pathway Source: GOC
    11. lactation Source: RGD
    12. liver development Source: RGD
    13. male gonad development Source: RGD
    14. negative regulation of peptidyl-threonine phosphorylation Source: RGD
    15. negative regulation of transcription from RNA polymerase II promoter Source: RGD
    16. neuron migration Source: RGD
    17. oligodendrocyte development Source: RGD
    18. pancreas development Source: RGD
    19. peptidyl-tyrosine phosphorylation Source: GOC
    20. positive chemotaxis Source: UniProtKB
    21. positive regulation of dendrite morphogenesis Source: RGD
    22. positive regulation of DNA replication Source: RGD
    23. positive regulation of endothelial cell chemotaxis Source: UniProtKB
    24. positive regulation of gene expression Source: RGD
    25. positive regulation of mitosis Source: RGD
    26. positive regulation of neuron projection development Source: RGD
    27. positive regulation of peptidyl-serine phosphorylation Source: RGD
    28. positive regulation of peptidyl-threonine phosphorylation Source: RGD
    29. positive regulation of transcription from RNA polymerase II promoter Source: RGD
    30. protein autophosphorylation Source: RGD
    31. response to acid chemical Source: RGD
    32. response to drug Source: RGD
    33. response to organic cyclic compound Source: RGD
    34. response to peptide hormone Source: RGD
    35. response to wounding Source: RGD
    36. semaphorin-plexin signaling pathway Source: UniProtKB
    37. sperm motility Source: RGD

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 5301.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3082. Met.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. dendrite Source: RGD
    3. excitatory synapse Source: RGD
    4. extracellular space Source: RGD
    5. integral component of membrane Source: RGD
    6. neuronal cell body Source: RGD
    7. neuron projection Source: RGD
    8. plasma membrane Source: RGD
    9. postsynaptic density Source: RGD
    10. postsynaptic membrane Source: RGD
    11. sperm flagellum Source: RGD

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 13821358Hepatocyte growth factor receptorPRO_0000024442Add
    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 bondi173 ↔ 176PROSITE-ProRule annotation
    Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi299 ↔ 364PROSITE-ProRule annotation
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi386 ↔ 398PROSITE-ProRule annotation
    Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi521 ↔ 539PROSITE-ProRule annotation
    Disulfide bondi527 ↔ 562PROSITE-ProRule annotation
    Disulfide bondi530 ↔ 546PROSITE-ProRule annotation
    Disulfide bondi542 ↔ 552PROSITE-ProRule annotation
    Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi636 – 6361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi786 – 7861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi880 – 8801N-linked (GlcNAc...)Sequence Analysis
    Modified residuei978 – 9781PhosphothreonineBy similarity
    Modified residuei991 – 9911PhosphoserineBy similarity
    Modified residuei998 – 9981PhosphoserineBy similarity
    Modified residuei1001 – 10011PhosphoserineBy similarity
    Modified residuei1004 – 10041PhosphotyrosineBy similarity
    Modified residuei1231 – 12311PhosphotyrosineBy similarity
    Modified residuei1235 – 12351Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1236 – 12361Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1290 – 12901PhosphothreonineBy similarity
    Modified residuei1350 – 13501Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1357 – 13571Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1366 – 13661PhosphotyrosineBy similarity

    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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP97523.
    PRIDEiP97523.

    PTM databases

    PhosphoSiteiP97523.

    Expressioni

    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.

    Developmental stagei

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

    Inductioni

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

    Gene expression databases

    GenevestigatoriP97523.

    Interactioni

    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-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 By similarity. Interacts with PTPN1 and PTPN2 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP97523.
    SMRiP97523. Positions 40-742, 1047-1347.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 935911ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini957 – 1379423CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei936 – 95621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 516490SemaPROSITE-ProRule annotationAdd
    BLAST
    Domaini564 – 65693IPT/TIG 1Add
    BLAST
    Domaini658 – 74083IPT/TIG 2Add
    BLAST
    Domaini743 – 83795IPT/TIG 3Add
    BLAST
    Domaini1079 – 1346268Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1213 – 1382170Interaction with RANBP9By similarityAdd
    BLAST
    Regioni1321 – 136040Interaction 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.
    InParanoidiP97523.
    KOiK05099.
    PhylomeDBiP97523.

    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.

    P97523-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAPTALAPG ILLLLLTLAQ RSHGECKEAL VKSEMNVNMK YQLPNFTAET     50
    PIHNVVLPGH HIYLGATNYI YVLNDKDLQK VSEFKTGPVV EHPDCFPCQD 100
    CSSKANVSGG VWKDNVNMAL LVDTYYDDQL ISCGSVNRGT CQRHVLPPDN 150
    AADIQSEVHC MFSPLAEEES GQCPDCVVSA LGAKVLLSEK DRFINFFVGN 200
    TINSSYPPDY SLHSISVRRL KETQDGFKFL TDQSYIDVLP EFRDSYPIKY 250
    IHAFESNHFI YFLTVQKETL DAQTFHTRII RFCSVDSGLH SYMEMPLECI 300
    LTEKRRKRST REEVFNILQA AYVSKPGANL AKQIGASPYD DILYGVFAQS 350
    KPDSAEPMNR SAVCAFPIKY VNDFFNKIVN KNNVRCLQHF YGPNHEHCFN 400
    RTLLRNSSGC EVRSDEYRTE FTTALQRVDL FMGRLNHVLL TSISTFIKGD 450
    LTIANLGTSE GRFMQVVLSR TAHFTPHVNF LLDSYPVSPE VIVEHPSNQN 500
    GYTLVVTGKK ITKIPLNGLG CGHFQSCSQC LSPPYFIQCG WCHNRCVHSN 550
    ECPSGTWTQE ICLPAVYKVF PTSAPLEGGT MLTICGWDFG FKKNNKFDLR 600
    KTKVLLGNES CTLTLSESTT NTLKCTVGPA MSEHFNVSVI VSNSRETTQY 650
    SAFSYVDPVI TSISPRYGPH AGGTLLTLTG KYLNSGNSRH ISIGGKTCTL 700
    KSVSDSILEC YTPGHTVSAE FPVKLKIDLA DRVTSSFSYR EDPVVSEIHP 750
    TKSFISGGST ITGIGKNLNS VSTPKLVIEV HDVGVNYTVA CQHRSSSEII 800
    CCTTPSLRQL DLQLPLKTKA FFLLDGILSK HFDLTYVHDP MFKPFEKPVM 850
    ISMGNENVVE IKGDDIDPEA VKGEVLKVGN KSCENLHWHS EALLCTVPSD 900
    LLKLNGGELN IEWKQAVSST VLGKVIVQPD QNFAGLIIGA VSISVVVLLV 950
    SGLFLWLRKR KHKDLGSELV RYDARVHTPH LDRLVSARSV SPTTEMVSNE 1000
    SVDYRATFPE DQFPNSSQNG ACRQVQYLLT DLSPILTSGD SDISSPLLQN 1050
    TVHIDLSALN PELVQAVPHV VIGPSSLIVH FNEVIGRGHF GCVYHGTLLD 1100
    SDGKKIHCAV KSLNRITDIE EVSQFLTEGI IMKDFSHPNV LSLLGICLRS 1150
    EGSPLVVLPY MKHGDLRNFI RNETHNPTVK DLIGFGLQVA KGMKYLVSKK 1200
    FVHRDLAARN CMLDEKFTVK VADFGLARDM YDKEYYSVHN KTGAKLPVKW 1250
    MALESLQTQK FTTKSDVWSF GVLLWELMTR GAPPYPDVNT FDITIYLLQG 1300
    RRLLQPEYCP DALYEVMLKC WHPKAEMRPS VSELVSRISS IFSTFIGEHY 1350
    VHVNATYVNV KCVAPYPSLL PSQDNIDGEA NT 1382
    Length:1,382
    Mass (Da):153,941
    Last modified:May 1, 1997 - v1
    Checksum:i66B8F2C88FE34427
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531H → Q in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti58 – 581P → H in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti240 – 2401P → G in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti427 – 4271R → A in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti485 – 4851Y → H in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti490 – 4956EVIVEH → GAAGIR(PubMed:8166728)Curated
    Sequence conflicti533 – 5331P → A in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti740 – 7401R → G in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti744 – 7441V → F in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti808 – 8081R → Q in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti890 – 8934SEAL → TASV in CAA86508. (PubMed:7628535)Curated
    Sequence conflicti907 – 9071Missing in CAA86508. (PubMed:7628535)Curated
    Sequence conflicti924 – 9241K → E in CAA86508. (PubMed:7628535)Curated
    Sequence conflicti934 – 9341A → R in CAA86508. (PubMed:7628535)Curated
    Sequence conflicti1028 – 10281L → P in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti1068 – 10681P → Q in AAB19189. (PubMed:8853431)Curated
    Sequence conflicti1197 – 11971V → A(PubMed:8853431)Curated
    Sequence conflicti1197 – 11971V → A1 PublicationCurated
    Sequence conflicti1331 – 13311V → F in AAB19189. (PubMed:8853431)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UniGeneiRn.10617.

    Genome annotation databases

    GeneIDi24553.
    KEGGirno:24553.
    UCSCiRGD:3082. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi PC2131.
    RefSeqi NP_113705.1. NM_031517.2.
    UniGenei Rn.10617.

    3D structure databases

    ProteinModelPortali P97523.
    SMRi P97523. Positions 40-742, 1047-1347.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P97523.

    Proteomic databases

    PaxDbi P97523.
    PRIDEi P97523.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24553.
    KEGGi rno:24553.
    UCSCi RGD:3082. rat.

    Organism-specific databases

    CTDi 4233.
    RGDi 3082. Met.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000220900.
    HOVERGENi HBG006348.
    InParanoidi P97523.
    KOi K05099.
    PhylomeDBi P97523.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 5301.

    Miscellaneous databases

    NextBioi 603662.
    PROi P97523.

    Gene expression databases

    Genevestigatori P97523.

    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. "Chromosomal localization of rat hepatocyte growth factor (Hgf) and HGF receptor (Met) and characterization of HGF receptor cDNA."
      Wallenius V.R., Rawet H., Skrtic S., Helou K., Qiu Y., Levan G., Ekberg S., Carlsson B., Isaksson O.G.P., Nakamura T., Jansson J.-O.
      Mamm. Genome 8:661-667(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Liver.
    2. "Primary structure of rat HGF receptor and induced expression in glomerular mesangial cells."
      Liu Y., Tolbert E.M., Sun A.M., Dworkin L.D.
      Am. J. Physiol. 271:F679-F688(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
      Strain: Sprague-Dawley.
      Tissue: Kidney.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 364-495.
      Strain: Sprague-Dawley.
      Tissue: Gastric mucosa.
    4. "Modulation of hepatocyte growth factor and c-met in the rat mammary gland during pregnancy, lactation, and involution."
      Pepper M.S., Soriano J.V., Menoud P.-A., Sappino A.-P., Orci L., Montesano R.
      Exp. Cell Res. 219:204-210(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 851-1002.
      Tissue: Intestine.
    5. Kikuchi Y.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1129-1267.

    Entry informationi

    Entry nameiMET_RAT
    AccessioniPrimary (citable) accession number: P97523
    Secondary accession number(s): P97579, Q63119, Q63964
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 143 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3