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Center for Computational Systems Medicine
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Protein Summary

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AS Summary

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Protein Functional Features

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Gene Isoform Structures and Expression Levels

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Protein Structures

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pLDDT Score Distribution

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Ramachandran Plot of Protein Structures

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Potential Active Site Information

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Protein Structure and Feature Comparision

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Protein-Protein Interaction

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Related Drugs

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Related Diseases

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Clinically Important Variants

Protein:MST1R

Protein Summary

check button Gene summary
Gene name: MST1R
ASpdb.0 ID: 4486
Gene
Gene symbol

MST1R

Gene ID

4486

Gene namemacrophage stimulating 1 receptor
SynonymsCD136|CDw136|NPCA3|PTK8|RON|SEA|p185-Ron
Cytomap

3p21.31

Type of geneprotein-coding
Descriptionmacrophage-stimulating protein receptorMSP receptorPTK8 protein tyrosine kinase 8S13 avian erythroblastosis oncogene homologS13 erythroblastosis oncogene homologc-met-related tyrosine kinase
Modification date20240411
UniProtAcc

Q04912


check button Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
GeneMST1R

GO:0009615

response to virus

12676986

GeneMST1R

GO:0043406

positive regulation of MAP kinase activity

12676986

GeneMST1R

GO:0051897

positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction

12676986



AS Summary

check button Information of the canonical protein with experimentally identified structure from PDB (2023).
UniProt AccFile namePDB IDMethodResolutionChainStartEnd
Q04912-1Q04912-1_4qt8_A.pdb4QT8X-ray3.0A28683

check button ASpdb's canonical and alternatively spliced isoform information.
accession_idgene_namecanonical_idalternative_idcanonical_lengthalternative_lengthcanonical_startcanonical_endtypeoriginalSEQvariationSEQalternative_startalternative_end
Q04912MST1RQ04912-1Q04912-31400495475495SubstitutionELVRSLNYLLYVSNFSLGDSGGPHPHSPLALGPCLHPHFAHI475495
Q04912MST1RQ04912-1Q04912-314004954961400Deletionnonenone495495
Q04912MST1RQ04912-1Q04912-41400541411516Deletionnonenone410410
Q04912MST1RQ04912-1Q04912-41400541628647SubstitutionPVPRKDFVEEFECELEPLGTYNLVPPLPFPEGGNQAAPSP522541
Q04912MST1RQ04912-1Q04912-414005416481400Deletionnonenone541541
Q04912MST1RQ04912-1Q04912-51400907884907SubstitutionYIGLGAVADCVGINVTVGGESCQHVSVRDRGRDSWGSESRGQPTGWSS884907
Q04912MST1RQ04912-1Q04912-514009079081400Deletionnonenone907907
Q04912MST1RQ04912-1Q04912-61400647628647SubstitutionPVPRKDFVEEFECELEPLGTYNLVPPLPFPEGGNQAAPSP628647
Q04912MST1RQ04912-1Q04912-614006476481400Deletionnonenone647647

check buttonMultiple sequence alignment of our canonical and alternatively spliced MST1R

check button Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of MST1R
UniProt-idENSGENSTENSP
Q04912-1ENSG00000164078.14ENST00000296474.8ENSP00000296474.3

UniProt-idNM IDNP ID
Q04912-1NM_002447.3NP_002438.2

check buttonAmino acid sequences of our canonical and alternatively spliced MST1R
accession_idProtein sequence
Q04912-1MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQS
LATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS
PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVT
DDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV
GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTA
LYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAW
HFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRPVP
RKDFVEEFECELEPLGTQAVGPTNVSLTVTNMPPGKHFRVDGTSVLRGFSFMEPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVN
GTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWTFQYREDPVVLSISPNCGYINSHITICGQHLTSAWHLVLSFHDGLRAV
ESRCERQLPEQQLCRLPEYVVRDPQGWVAGNLSARGDGAAGFTLPGFRFLPPPHPPSANLVPLKPEEHAIKFEYIGLGAVADCVGINVTV
GGESCQHEFRGDMVVCPLPPSLQLGQDGAPLQVCVDGECHILGRVVRPGPDGVPQSTLLGILLPLLLLVAALATALVFSYWWRRKQLVLP
PNLNDLASLDQTAGATPLPILYSGSDYRSGLALPAIDGLDSTTCVHGASFSDSEDESCVPLLRKESIQLRDLDSALLAEVKDVLIPHERV
VTHSDRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCHGDLL
QFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRHARLPVKWMALESLQ
TYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSALLG
Q04912-3MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQS
LATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS
PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVT
DDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV
GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTA
Q04912-4MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQS
LATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS
PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVT
DDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV
GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPVFQVPIQGPGCRHFLTCGRCLRAWHFMGCGWCGNMCGQQK
ECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRYNLVPPLPFPEGGNQAAPS
Q04912-5MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQS
LATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS
PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVT
DDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV
GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTA
LYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAW
HFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRPVP
RKDFVEEFECELEPLGTQAVGPTNVSLTVTNMPPGKHFRVDGTSVLRGFSFMEPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVN
GTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWTFQYREDPVVLSISPNCGYINSHITICGQHLTSAWHLVLSFHDGLRAV
ESRCERQLPEQQLCRLPEYVVRDPQGWVAGNLSARGDGAAGFTLPGFRFLPPPHPPSANLVPLKPEEHAIKFEVSVRDRGRDSWGSESRG
Q04912-6MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQS
LATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS
PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVT
DDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV
GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTA
LYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAW
HFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRYNL

Protein Functional Features

check buttonMain function of this protein. (from UniProt)
MST1R (go to UniProt):Q04912

check buttonRetention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at

download page

* Minus value of BPloci means that the break pointn is located before the CDS.
- Retained protein feature among the 13 regional features.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
Q04912Topological domain25957Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=475;End=495
Q04912Topological domain25957Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=496;End=1400
Q04912Topological domain25957Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=411;End=516
Q04912Topological domain25957Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=628;End=647
Q04912Topological domain25957Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=648;End=1400
Q04912Topological domain25957Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=884;End=907
Q04912Topological domain25957Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=908;End=1400
Q04912Topological domain25957Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=628;End=647
Q04912Topological domain25957Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=648;End=1400
Q04912Transmembrane958978Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=496;End=1400
Q04912Transmembrane958978Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=648;End=1400
Q04912Transmembrane958978Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=908;End=1400
Q04912Transmembrane958978Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=648;End=1400
Q04912Topological domain9791400Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=496;End=1400
Q04912Topological domain9791400Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=648;End=1400
Q04912Topological domain9791400Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=908;End=1400
Q04912Topological domain9791400Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=648;End=1400
Q04912Domain31522Note=Sema;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352Type=Substitution;Start=475;End=495
Q04912Domain31522Note=Sema;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352Type=Deletion;Start=496;End=1400
Q04912Domain31522Note=Sema;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352Type=Deletion;Start=411;End=516
Q04912Domain569671Note=IPT/TIG 1Type=Deletion;Start=496;End=1400
Q04912Domain569671Note=IPT/TIG 1Type=Substitution;Start=628;End=647
Q04912Domain569671Note=IPT/TIG 1Type=Deletion;Start=648;End=1400
Q04912Domain569671Note=IPT/TIG 1Type=Substitution;Start=628;End=647
Q04912Domain569671Note=IPT/TIG 1Type=Deletion;Start=648;End=1400
Q04912Domain684767Note=IPT/TIG 2Type=Deletion;Start=496;End=1400
Q04912Domain684767Note=IPT/TIG 2Type=Deletion;Start=648;End=1400
Q04912Domain684767Note=IPT/TIG 2Type=Deletion;Start=648;End=1400
Q04912Domain770860Note=IPT/TIG 3Type=Deletion;Start=496;End=1400
Q04912Domain770860Note=IPT/TIG 3Type=Deletion;Start=648;End=1400
Q04912Domain770860Note=IPT/TIG 3Type=Deletion;Start=648;End=1400
Q04912Domain10821345Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159Type=Deletion;Start=496;End=1400
Q04912Domain10821345Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159Type=Deletion;Start=648;End=1400
Q04912Domain10821345Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159Type=Deletion;Start=908;End=1400
Q04912Domain10821345Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159Type=Deletion;Start=648;End=1400
Q04912Region13671400Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=496;End=1400
Q04912Region13671400Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=648;End=1400
Q04912Region13671400Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=908;End=1400
Q04912Region13671400Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=648;End=1400


Gene Isoform Structures and Expression Levels for MST1R

check buttonGene structures of our canonical and alternative spliced genes of MST1R
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
gene isoform structure of MST1R

check button Expression levels of gene isoforms across GTEx.
gtex expression

check button Expression levels of gene isoforms across TCGA.
tcga expression


Protein Structures

check button PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.
3D view using mol* of Q04912-1
3D view using mol* of Q04912-3
3D view using mol* of Q04912-4
3D view using mol* of Q04912-5
3D view using mol* of Q04912-6


pLDDT Score Distribution

check button pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.
pLDDT distribution across the protein length of Q04912-1
all structure
pLDDT distribution across the protein length of Q04912-3
all structure
pLDDT distribution across the protein length of Q04912-4
all structure
pLDDT distribution across the protein length of Q04912-6
all structure


Ramachandran Plot of Protein Structures


check button Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.
Ramachandran plot of Q04912-1
all structure
Ramachandran plot of Q04912-3
all structure
Ramachandran plot of Q04912-6
all structure

Potential Active Site Information


check button The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.
UniProt-idSite scoreSizeD scoreVolumeExposureEnclosureContactPhobicPhilicBalanceDon/AccResidues
Q04912-11.0443360.9951053.3530.4940.7650.9970.4291.2380.3460.53927,28,29,30,31,32,34,37,38,482,484,485,486,530,532
,533,534,535,538,539,540,547,568,570,572,575,586,5
88,591,592,593,595,596,597,598,619,620,621,622,625
,626,627,628,629,630,631,633,634,635,636,637,639,6
65,666,667,668,670,1121
Q04912-31.0361671.092485.0020.5910.6770.8760.9160.781.1751.21238,39,40,41,42,43,44,46,47,60,61,62,66,68,69,70,83
,85,463,470,471,472,473,482,483,484,485,486,488,48
9,490,491,492,493,494
Q04912-41.0441221.092453.1030.6410.6990.8210.8520.821.0390.591235,245,267,268,269,270,279,290,291,293,294,295,29
6,378,381,382,384,385,386,394,395,396,397,398,399,
400,401,402,408,409
Q04912-61.0382031.039730.590.6470.7550.8790.2941.0870.2710.81854,55,56,57,58,59,60,119,120,121,122,123,124,125,1
27,182,183,184,185,186,187,188,202,248,249,250,251
,252,253,254,322,323,324,325,326,449,451,452,496,4
97,498,499,500,501,502,503,504,512,514

Protein Structure and Feature Comparision


check button Protein Structure Comparision Using Template Modeling Scores (TM-score).
all structure

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)
3D view using mol* of Q04912-1_Q04912-1_4qt8_A.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of Q04912-1_4qt8_A_Q04912-3.pdb
3D view using mol* of Q04912-1_4qt8_A_Q04912-4.pdb
3D view using mol* of Q04912-1_4qt8_A_Q04912-5.pdb
3D view using mol* of Q04912-1_4qt8_A_Q04912-6.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of Q04912-1_Q04912-3.pdb
3D view using mol* of Q04912-1_Q04912-4.pdb
3D view using mol* of Q04912-1_Q04912-5.pdb
3D view using mol* of Q04912-1_Q04912-6.pdb

check button Protein Feature Comparison of the protein sequendary structures among the protiens.
./stats/secondary_structure/figure/Q04912-1_vs_Q04912-3.png
all structure<
./stats/secondary_structure/figure/Q04912-1_vs_Q04912-4.png
all structure<
./stats/secondary_structure/figure/Q04912-1_vs_Q04912-5.png
all structure<
./stats/secondary_structure/figure/Q04912-1_vs_Q04912-6.png
all structure<

check button Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.
./stats/relative_asa/Q04912-1_vs_Q04912-3.png
all structure<
./stats/relative_asa/Q04912-1_vs_Q04912-4.png
all structure<
./stats/relative_asa/Q04912-1_vs_Q04912-5.png
all structure<
./stats/relative_asa/Q04912-1_vs_Q04912-6.png
all structure<


Protein-Protein Interaction


check button Interactors from UniProt.
Accession_idSubsectionStartEndFuncitonal featureSplicing information


check button Interactors from STRING.
Gene nameInteractors


Related Drugs to MST1R


check button Drugs targeting this gene/protein.
(DrugBank)
UniProt accessionGene nameDrugBank IDDrug nameDrug groupActions
Q04912MST1RDB12010Fostamatinibapproved, investigationalinhibitor
Q04912MST1RDB08865Crizotinibapproved, investigationalinhibitor

Related Diseases to MST1R


check button Previous studies relating to the alternative splicing of MST1R and disease information from the MeSH term (PubMed)
GenePMIDTitleAbstractMeSH IDMeSH term
MST1R18593464Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis.Despite the advent of biological therapies for the treatment of rheumatoid arthritis, there is a compelling need to develop alternative therapeutic targets for nonresponders to existing treatments. Soluble receptors occur naturally in vivo, such as the splice variant of the cell surface receptor for vascular endothelial growth factor (VEGF)--a key regulator of angiogenesis in rheumatoid arthritis. Bioinformatics analyses predict that the majority of human genes undergo alternative splicing, generating proteins--many of which may have regulatory functions. The objective of the present study was to identify alternative splice variants (ASV) from cell surface receptor genes, and to determine whether the novel proteins encoded exert therapeutic activity in an in vivo model of arthritis.D001172Arthritis, Rheumatoid
MST1R18593464Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis.Despite the advent of biological therapies for the treatment of rheumatoid arthritis, there is a compelling need to develop alternative therapeutic targets for nonresponders to existing treatments. Soluble receptors occur naturally in vivo, such as the splice variant of the cell surface receptor for vascular endothelial growth factor (VEGF)--a key regulator of angiogenesis in rheumatoid arthritis. Bioinformatics analyses predict that the majority of human genes undergo alternative splicing, generating proteins--many of which may have regulatory functions. The objective of the present study was to identify alternative splice variants (ASV) from cell surface receptor genes, and to determine whether the novel proteins encoded exert therapeutic activity in an in vivo model of arthritis.D004195Disease Models, Animal
MST1R25997828RON alternative splicing regulation in primary ovarian cancer.The proto-oncogene recepteur d'origine nantais (RON, MST1R) and its alternatively spliced variants are involved in various tumor biological processes, such as cell motility, adhesion, proliferation, apoptosis and epithelial-to-mesenchymal transition (EMT). RON overexpression and the occurrence of specific alternatively spliced RON isoforms have been detected in ovarian cancer. In the present study, we evaluated the role and regulation of cancer-related RON splicing isoforms in primary ovarian cancer. Expression of RON variants (RONΔ165, RONΔ160) was determined in 45 primary ovarian cancer and 4 physiological ovarian tissue specimens by RT-PCR and western blot analysis. The results were correlated to clinicopathological parameters. Additionally, expression of splicing factors with known involvement in RON alternative splicing regulation was examined. Increased RON levels were detected in all tumor samples (p=0.001) without differences between the primary tumors and metastases. Alternative RON variants were present in the majority of tumor samples (39 of 45; 86.67%). Potential RONΔ165 occurred more often (82.22%) than potential RONΔ160 or RONΔ155 (24.40%). Several significant correlations of RON and splicing factor expression [e.g. ASF/SFRS1 (p=0.035)] were detected. Correlations of RON expression to clinicopathological parameters were not observed. Significant splicing factor interactions (e.g. SRp55/SRp75: p<0.001) were observed in tumor samples with alternative RON splicing. Our data demonstrated upregulated RON isoform expression and significant changes in splicing factor expression in primary ovarian cancer. These findings account for an essential regulatory interplay of splicing factor-driven alterations in the RON alternative splicing pattern with subsequent tumor biological consequences in ovarian cancer.D010051Ovarian Neoplasms


Clinically important variants in MST1R


check button (ClinVar, 04/20/2024)
accession_iduniprot_idgene_nameTypeVariantClinical_significance