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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-Experimental evidence at protein leveli

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

  • ATP binding Source: UniProtKB-KW
  • beta-catenin binding Source: RGD
  • hepatocyte growth factor-activated receptor activity Source: RGD
  • phosphatidylinositol 3-kinase binding Source: RGD
  • phospholipase binding Source: RGD
  • protein complex binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein tyrosine kinase activity Source: RGD

GO - Biological processi

  • brain development Source: RGD
  • cell aging Source: RGD
  • cellular response to arsenic-containing substance Source: RGD
  • cellular response to glucose stimulus Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to inorganic substance Source: RGD
  • cellular response to interleukin-6 Source: RGD
  • cellular response to peptide hormone stimulus Source: RGD
  • central nervous system neuron differentiation Source: RGD
  • hepatocyte growth factor receptor signaling pathway Source: GOC
  • lactation Source: RGD
  • liver development Source: RGD
  • male gonad development Source: RGD
  • negative regulation of peptidyl-threonine phosphorylation Source: RGD
  • negative regulation of transcription from RNA polymerase II promoter Source: RGD
  • neuron migration Source: RGD
  • oligodendrocyte development Source: RGD
  • pancreas development Source: RGD
  • peptidyl-tyrosine phosphorylation Source: GOC
  • positive chemotaxis Source: UniProtKB
  • positive regulation of dendrite morphogenesis Source: RGD
  • positive regulation of DNA replication Source: RGD
  • positive regulation of endothelial cell chemotaxis Source: UniProtKB
  • positive regulation of gene expression Source: RGD
  • positive regulation of mitotic nuclear division Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • positive regulation of peptidyl-serine phosphorylation Source: RGD
  • positive regulation of peptidyl-threonine phosphorylation Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: RGD
  • protein autophosphorylation Source: RGD
  • response to acidic pH Source: RGD
  • response to drug Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to peptide hormone Source: RGD
  • response to wounding Source: RGD
  • semaphorin-plexin signaling pathway Source: UniProtKB
  • sperm motility Source: RGD
Complete GO annotation...

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 Componenti: Unplaced

Organism-specific databases

RGDi3082. Met.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 935911ExtracellularSequence AnalysisAdd
BLAST
Transmembranei936 – 95621HelicalSequence AnalysisAdd
BLAST
Topological domaini957 – 1379423CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • excitatory synapse Source: RGD
  • extracellular space Source: RGD
  • integral component of membrane Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: RGD
  • sperm flagellum Source: RGD
Complete GO annotation...

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 residuei967 – 9671PhosphoserineBy similarity
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

GenevisibleiP97523. RN.

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009662.

Structurei

3D structure databases

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

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

        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
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 → A (Ref. 5) Curated
Sequence conflicti1331 – 13311V → F in AAB19189 (PubMed:8853431).Curated

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.
UniGeneiRn.10617.

Genome annotation databases

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

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.
UniGeneiRn.10617.

3D structure databases

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009662.

PTM databases

PhosphoSiteiP97523.

Proteomic databases

PaxDbiP97523.
PRIDEiP97523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4233.
RGDi3082. Met.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000220900.
HOVERGENiHBG006348.
InParanoidiP97523.
KOiK05099.
PhylomeDBiP97523.

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Miscellaneous databases

NextBioi603662.
PROiP97523.

Gene expression databases

GenevisibleiP97523. RN.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 148 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.