MST1R
entrez
4486
canonical
uniprot
Q04912
canonical
ensembl
ENSG00000164078
resolver
ensp
ENSP00000296474
resolver
ensp
ENSP00000341325
resolver
ensp
ENSP00000393294
resolver
ensp
ENSP00000407926
resolver
ensp
ENSP00000482642
resolver
ensp
ENSP00000528966
resolver
ensp
ENSP00000528967
resolver
ensp
ENSP00000528969
resolver
ensp
ENSP00000528970
resolver
ensp
ENSP00000528971
resolver
ensp
ENSP00000528974
resolver
ensp
ENSP00000528978
resolver
ensp
ENSP00000528979
resolver
ensp
ENSP00000528980
resolver
ensp
ENSP00000528981
resolver
ensp
ENSP00000614909
resolver
enst
ENST00000434765
resolver
genesymbol
MST1R
resolver
genesymbol_syn
PTK8
resolver
genesymbol_syn
RON
resolver
hgnc
HGNC:7381
resolver
uniprot
A0A087WZG2
resolver
uniprot
B4E058
resolver
uniprot
B5A944
resolver
uniprot
B5A945
resolver
uniprot
B5A946
resolver
uniprot
B5A947
resolver
uniprot
G9JXB8
resolver
uniprot
H7C074
resolver
uniprot_entry
B4E058_HUMAN
resolver
uniprot_entry
G9JXB8_HUMAN
resolver
uniprot_entry
H7C074_HUMAN
resolver
uniprot_entry
RON_HUMAN
resolver
uniprot_sec
A0A087WZG2
resolver
uniprot_sec
B5A944
resolver
uniprot_sec
B5A945
resolver
uniprot_sec
B5A946
resolver
uniprot_sec
B5A947
resolver
activity_regulation
ACTIVITY REGULATION: 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. {ECO:0000269|PubMed:15632155}.
uniprot
proteins
amino_acid_sequence
MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVASPLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVTDDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGVGPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAWHFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRPVPRKDFVEEFECELEPLGTQAVGPTNVSLTVTNMPPGKHFRVDGTSVLRGFSFMEPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVNGTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWTFQYREDPVVLSISPNCGYINSHITICGQHLTSAWHLVLSFHDGLRAVESRCERQLPEQQLCRLPEYVVRDPQGWVAGNLSARGDGAAGFTLPGFRFLPPPHPPSANLVPLKPEEHAIKFEYIGLGAVADCVGINVTVGGESCQHEFRGDMVVCPLPPSLQLGQDGAPLQVCVDGECHILGRVVRPGPDGVPQSTLLGILLPLLLLVAALATALVFSYWWRRKQLVLPPNLNDLASLDQTAGATPLPILYSGSDYRSGLALPAIDGLDSTTCVHGASFSDSEDESCVPLLRKESIQLRDLDSALLAEVKDVLIPHERVVTHSDRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSALLGDHYVQLPATYMNLGPSTSHEMNVRPEQPQFSPMPGNVRRPRPLSEPPRPT
uniprot
proteins
disease_involvement
DISEASE: Nasopharyngeal carcinoma, 3 (NPCA3) [MIM:617075]: A form of nasopharyngeal carcinoma, a malignant neoplasm that originates in the nasopharyngeal epithelium and includes 4 subtypes: keratinizing squamous cell, non-keratinizing, basaloid squamous cell, and papillary adenocarcinoma. {ECO:0000269|PubMed:26951679}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Also plays a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand. {ECO:0000269|PubMed:18836480, ECO:0000269|PubMed:7939629, ECO:0000269|PubMed:9764835}.
uniprot
proteins
mass_dalton
152241
uniprot
proteins
post_translational_modification
PTM: Proteolytic processing yields the two subunits.; PTM: Autophosphorylated in response to ligand binding on Tyr-1238 and Tyr-1239 in the kinase domain leading to further phosphorylation of Tyr-1353 and Tyr-1360 in the C-terminal multifunctional docking site. {ECO:0000269|PubMed:15632155, ECO:0000269|PubMed:20726546}.; PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation. {ECO:0000269|PubMed:12802274}.; PTM: O-mannosylation of IPT/TIG domains on Thr or Ser residues by TMEM260 is required for protein maturation (PubMed:37186866). O-mannosylated residues are composed of single mannose glycans that are not elongated or modified (PubMed:37186866). {ECO:0000269|PubMed:37186866}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10222149
uniprot
proteins
pubmed
10514476
uniprot
proteins
pubmed
12472665
uniprot
proteins
pubmed
12676986
uniprot
proteins
pubmed
12802274
uniprot
proteins
pubmed
15184888
uniprot
proteins
pubmed
15632155
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18593464
uniprot
proteins
pubmed
18836480
uniprot
proteins
pubmed
20726546
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21784853
uniprot
proteins
pubmed
22848655
uniprot
proteins
pubmed
26951679
uniprot
proteins
pubmed
37186866
uniprot
proteins
pubmed
7687741
uniprot
proteins
pubmed
7939629
uniprot
proteins
pubmed
8062829
uniprot
proteins
pubmed
8386824
uniprot
proteins
pubmed
8816464
uniprot
proteins
pubmed
9764835
uniprot
proteins
sequence_length
1400
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 958..978; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins