Protein:MST1R |
Protein Summary |
Gene summary |
| Gene name: MST1R | ASpdb.0 ID: 4486 | Gene | Gene symbol | MST1R | Gene ID | 4486 |
| Gene name | macrophage stimulating 1 receptor |
| Synonyms | CD136|CDw136|NPCA3|PTK8|RON|SEA|p185-Ron |
| Cytomap | 3p21.31 |
| Type of gene | protein-coding |
| Description | macrophage-stimulating protein receptorMSP receptorPTK8 protein tyrosine kinase 8S13 avian erythroblastosis oncogene homologS13 erythroblastosis oncogene homologc-met-related tyrosine kinase |
| Modification date | 20240411 |
| UniProtAcc | Q04912 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | MST1R | GO:0009615 | response to virus | 12676986 |
| Gene | MST1R | GO:0043406 | positive regulation of MAP kinase activity | 12676986 |
| Gene | MST1R | GO:0051897 | positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | 12676986 |
AS Summary |
Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q04912-1 | Q04912-1_4qt8_A.pdb | 4QT8 | X-ray | 3.0 | A | 28 | 683 |
ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q04912 | MST1R | Q04912-1 | Q04912-3 | 1400 | 495 | 475 | 495 | Substitution | ELVRSLNYLLYVSNFSLGDSG | GPHPHSPLALGPCLHPHFAHI | 475 | 495 |
| Q04912 | MST1R | Q04912-1 | Q04912-3 | 1400 | 495 | 496 | 1400 | Deletion | none | none | 495 | 495 |
| Q04912 | MST1R | Q04912-1 | Q04912-4 | 1400 | 541 | 411 | 516 | Deletion | none | none | 410 | 410 |
| Q04912 | MST1R | Q04912-1 | Q04912-4 | 1400 | 541 | 628 | 647 | Substitution | PVPRKDFVEEFECELEPLGT | YNLVPPLPFPEGGNQAAPSP | 522 | 541 |
| Q04912 | MST1R | Q04912-1 | Q04912-4 | 1400 | 541 | 648 | 1400 | Deletion | none | none | 541 | 541 |
| Q04912 | MST1R | Q04912-1 | Q04912-5 | 1400 | 907 | 884 | 907 | Substitution | YIGLGAVADCVGINVTVGGESCQH | VSVRDRGRDSWGSESRGQPTGWSS | 884 | 907 |
| Q04912 | MST1R | Q04912-1 | Q04912-5 | 1400 | 907 | 908 | 1400 | Deletion | none | none | 907 | 907 |
| Q04912 | MST1R | Q04912-1 | Q04912-6 | 1400 | 647 | 628 | 647 | Substitution | PVPRKDFVEEFECELEPLGT | YNLVPPLPFPEGGNQAAPSP | 628 | 647 |
| Q04912 | MST1R | Q04912-1 | Q04912-6 | 1400 | 647 | 648 | 1400 | Deletion | none | none | 647 | 647 |
Multiple sequence alignment of our canonical and alternatively spliced MST1R |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of MST1R |
| UniProt-id | ENSG | ENST | ENSP |
| Q04912-1 | ENSG00000164078.14 | ENST00000296474.8 | ENSP00000296474.3 |
| UniProt-id | NM ID | NP ID |
| Q04912-1 | NM_002447.3 | NP_002438.2 |
Amino acid sequences of our canonical and alternatively spliced MST1R |
| accession_id | Protein sequence |
| Q04912-1 | MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQS LATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVT DDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTA LYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAW HFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRPVP RKDFVEEFECELEPLGTQAVGPTNVSLTVTNMPPGKHFRVDGTSVLRGFSFMEPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVN GTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWTFQYREDPVVLSISPNCGYINSHITICGQHLTSAWHLVLSFHDGLRAV ESRCERQLPEQQLCRLPEYVVRDPQGWVAGNLSARGDGAAGFTLPGFRFLPPPHPPSANLVPLKPEEHAIKFEYIGLGAVADCVGINVTV GGESCQHEFRGDMVVCPLPPSLQLGQDGAPLQVCVDGECHILGRVVRPGPDGVPQSTLLGILLPLLLLVAALATALVFSYWWRRKQLVLP PNLNDLASLDQTAGATPLPILYSGSDYRSGLALPAIDGLDSTTCVHGASFSDSEDESCVPLLRKESIQLRDLDSALLAEVKDVLIPHERV VTHSDRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCHGDLL QFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRHARLPVKWMALESLQ TYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSALLG |
| Q04912-3 | MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQS LATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVT DDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTA |
| Q04912-4 | MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQS LATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVT DDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPVFQVPIQGPGCRHFLTCGRCLRAWHFMGCGWCGNMCGQQK ECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRYNLVPPLPFPEGGNQAAPS |
| Q04912-5 | MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQS LATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVT DDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTA LYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAW HFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRPVP RKDFVEEFECELEPLGTQAVGPTNVSLTVTNMPPGKHFRVDGTSVLRGFSFMEPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVN GTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWTFQYREDPVVLSISPNCGYINSHITICGQHLTSAWHLVLSFHDGLRAV ESRCERQLPEQQLCRLPEYVVRDPQGWVAGNLSARGDGAAGFTLPGFRFLPPPHPPSANLVPLKPEEHAIKFEVSVRDRGRDSWGSESRG |
| Q04912-6 | MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQS LATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVT DDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTA LYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAW HFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRYNL |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| MST1R (go to UniProt):Q04912 |
Retention 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 * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q04912 | Topological domain | 25 | 957 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=475;End=495 |
| Q04912 | Topological domain | 25 | 957 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=496;End=1400 |
| Q04912 | Topological domain | 25 | 957 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=411;End=516 |
| Q04912 | Topological domain | 25 | 957 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=628;End=647 |
| Q04912 | Topological domain | 25 | 957 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Topological domain | 25 | 957 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=884;End=907 |
| Q04912 | Topological domain | 25 | 957 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=908;End=1400 |
| Q04912 | Topological domain | 25 | 957 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=628;End=647 |
| Q04912 | Topological domain | 25 | 957 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Transmembrane | 958 | 978 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=496;End=1400 |
| Q04912 | Transmembrane | 958 | 978 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Transmembrane | 958 | 978 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=908;End=1400 |
| Q04912 | Transmembrane | 958 | 978 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Topological domain | 979 | 1400 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=496;End=1400 |
| Q04912 | Topological domain | 979 | 1400 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Topological domain | 979 | 1400 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=908;End=1400 |
| Q04912 | Topological domain | 979 | 1400 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Domain | 31 | 522 | Note=Sema;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 | Type=Substitution;Start=475;End=495 |
| Q04912 | Domain | 31 | 522 | Note=Sema;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 | Type=Deletion;Start=496;End=1400 |
| Q04912 | Domain | 31 | 522 | Note=Sema;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352 | Type=Deletion;Start=411;End=516 |
| Q04912 | Domain | 569 | 671 | Note=IPT/TIG 1 | Type=Deletion;Start=496;End=1400 |
| Q04912 | Domain | 569 | 671 | Note=IPT/TIG 1 | Type=Substitution;Start=628;End=647 |
| Q04912 | Domain | 569 | 671 | Note=IPT/TIG 1 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Domain | 569 | 671 | Note=IPT/TIG 1 | Type=Substitution;Start=628;End=647 |
| Q04912 | Domain | 569 | 671 | Note=IPT/TIG 1 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Domain | 684 | 767 | Note=IPT/TIG 2 | Type=Deletion;Start=496;End=1400 |
| Q04912 | Domain | 684 | 767 | Note=IPT/TIG 2 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Domain | 684 | 767 | Note=IPT/TIG 2 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Domain | 770 | 860 | Note=IPT/TIG 3 | Type=Deletion;Start=496;End=1400 |
| Q04912 | Domain | 770 | 860 | Note=IPT/TIG 3 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Domain | 770 | 860 | Note=IPT/TIG 3 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Domain | 1082 | 1345 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=496;End=1400 |
| Q04912 | Domain | 1082 | 1345 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Domain | 1082 | 1345 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=908;End=1400 |
| Q04912 | Domain | 1082 | 1345 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=648;End=1400 |
| Q04912 | Region | 1367 | 1400 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=496;End=1400 |
| Q04912 | Region | 1367 | 1400 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=648;End=1400 |
| Q04912 | Region | 1367 | 1400 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=908;End=1400 |
| Q04912 | Region | 1367 | 1400 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=648;End=1400 |
Gene Isoform Structures and Expression Levels for MST1R |
Gene 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. |
Expression levels of gene isoforms across GTEx. |
Expression levels of gene isoforms across TCGA. |
Protein Structures |
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 |
pLDDT score distribution of the predicted protein structures from AlphaFold2* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
Ramachandran Plot of Protein Structures |
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 |
![]() |
| Ramachandran plot of Q04912-3 |
![]() |
| Ramachandran plot of Q04912-6 |
![]() |
Potential Active Site Information |
The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q04912-1 | 1.044 | 336 | 0.995 | 1053.353 | 0.494 | 0.765 | 0.997 | 0.429 | 1.238 | 0.346 | 0.539 | 27,28,29,30,31,32,34,37,38,482,484,485,486,530,532 ,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 |
| Q04912-3 | 1.036 | 167 | 1.092 | 485.002 | 0.591 | 0.677 | 0.876 | 0.916 | 0.78 | 1.175 | 1.212 | 38,39,40,41,42,43,44,46,47,60,61,62,66,68,69,70,83 ,85,463,470,471,472,473,482,483,484,485,486,488,48 9,490,491,492,493,494 |
| Q04912-4 | 1.044 | 122 | 1.092 | 453.103 | 0.641 | 0.699 | 0.821 | 0.852 | 0.82 | 1.039 | 0.591 | 235,245,267,268,269,270,279,290,291,293,294,295,29 6,378,381,382,384,385,386,394,395,396,397,398,399, 400,401,402,408,409 |
| Q04912-6 | 1.038 | 203 | 1.039 | 730.59 | 0.647 | 0.755 | 0.879 | 0.294 | 1.087 | 0.271 | 0.818 | 54,55,56,57,58,59,60,119,120,121,122,123,124,125,1 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 |
Protein Structure Comparision Using Template Modeling Scores (TM-score). |
![]() |
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 |
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 |
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 |
Protein Feature Comparison of the protein sequendary structures among the protiens. |
Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q04912-1_vs_Q04912-3.png |
< |
| ./stats/relative_asa/Q04912-1_vs_Q04912-4.png |
< |
| ./stats/relative_asa/Q04912-1_vs_Q04912-5.png |
< |
| ./stats/relative_asa/Q04912-1_vs_Q04912-6.png |
< |
Protein-Protein Interaction |
Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to MST1R |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q04912 | MST1R | DB12010 | Fostamatinib | approved, investigational | inhibitor |
| Q04912 | MST1R | DB08865 | Crizotinib | approved, investigational | inhibitor |
Related Diseases to MST1R |
Previous studies relating to the alternative splicing of MST1R and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| MST1R | 18593464 | Novel 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. | D001172 | Arthritis, Rheumatoid |
| MST1R | 18593464 | Novel 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. | D004195 | Disease Models, Animal |
| MST1R | 25997828 | RON 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. | D010051 | Ovarian Neoplasms |
Clinically important variants in MST1R |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
|
|