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MST1 (macrophage stimulating 1 (hepatocyte growth factor-like))

Written2013-05Makiko Kawaguchi, Hiroaki Kataoka
Section of Oncopathology, Regenerative Biology, Department of Pathology, Faculty of Medicine, University of Miyazaki, Japan

(Note : for Links provided by Atlas : click)


Alias (NCBI)D3F15S2
HGNC (Hugo) MST1
HGNC Alias symbMSP
HGNC Previous nameD3F15S2
HGNC Previous namehepatocyte growth factor-like
LocusID (NCBI) 4485
Atlas_Id 44411
Location 3p21.31  [Link to chromosome band 3p21]
Location_base_pair Starts at 49683947 and ends at 49688763 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping MST1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
MST1 (3p21.31)::SRRD (22q12.1)MST1L (1p36.13)::MST1 (3p21.31)


  Structure of the human MST1 gene.
Description Total length: 4817 bp; mRNA product length: 2348 bp.
Transcription The human MST1 gene structure consists of 18 exons and 17 introns spanning 4817 bp. One transcript of 2348 bps mRNA encode for 711 amino acid.
Pseudogene There are no known pseudogenes.


Note MSP was originally identified by E.J. Leonard as a serum protein that activates murine resident peritoneal macrophages (Skeel et al., 1991). The specific receptor for MSP is recepteur d'origine nantais (RON) tyrosine kinase, a member of the MET proto-oncogene family (Wang et al., 2002).
  Schematic representations of the domain structures of pro-MSP and mature MSP proteins. After proteolytic cleavage at the Arg483-Val484 bond, pro-MSP is converted to mature MSP and acquires its biological activity. Mature MSP is composed of α-chain (53 kDa) and β-chain (30 kDa) linked by a disulfide bond. The α-chain contains PAN/APPLE-like domain, followed by four kringle domains, and the β-chain has a serine protease (peptidase S1)-like domain. SP, signal peptide; PAN, PAN/APPLE-like domain; K1-K4, Kringle domain1-4.
Description The human MSP has the highest amino acid sequence similarity (45%) to human hepatocyte growth factor (HGF), hence its name "hepatocyte growth factor-like protein (HGFL)". MSP is a glycoprotein belonging to a plasminogen-related growth factor family. It is secreted as a single-chain precursor protein (pro-MSP), which has no biological activity (Wang et al., 2002). Pro-MSP becomes active after cleavage at the Arg483-Val484 bond by specific trypsin-like serine proteases such as hepatocyte growth factor activator (HGFA), ST14 (matriptase), hepsin (transmembrane protease, serine 1; TMPRSS1), TMPRSS11D (Human airway trypsin-like protease; HAT), clotting factor XIIa, clotting factor XIa, and serum kallikrein (Wang et al., 2002; Kawaguchi et al., 2009; Bhatt et al., 2007; Ganesan et al., 2011; Orikawa et al., 2012). Among them, HGFA is a physiological serum activator of MSP at site of tissue injury, and ST14/matriptase likely has significant roles in activation of MSP/RON signaling on the cell surface as a cellular activator. In respiratory epithelial cells, TMPRSS11D/HAT serves as an efficient activator of MSP. In addition, hepsin may have a role in cancer cells. After cleavage of pro-MSP, MSP β-chain binds to its specific receptor tyrosine kinase RON, which results in autophosphorylation within its kinase catalytic domain, leading to the initiation of multiple signaling pathways including Ras/mitogen-activated protein kinase, phosphatidylinositol 3-kinase, c-Jun amino terminal kinase, β-catenin and nuclear factor-kappaB (NF-κB) (Wang et al., 2002; Kretschmann et al., 2010).
Expression MSP transcripts are present in the liver and, to a lesser amount, in adrenal glands, lungs, kidney, placenta and pancreas (Yoshimura et al., 1993; Ganesan et al., 2011).
Localisation MSP is synthesized and secreted mainly by hepatocytes as a biologically inactive single-chain precursor form and circulate as a plasma protein. The concentration of pro-MSP in the plasma is about 2-5 nM (Wang et al., 2002). Pro-MSP is activated by trypsin-like serum serine proteases such as HGFA, clotting factor XIIa, clotting factor XIa, serum kallikrein. On the cell surface, this activation can be processed by membrane-anchored serine proteases such as ST14/matriptase, hepsin and TMPRSS11D/HAT.
Function MSP was originally identified as a serum protein that activates resident macrophages, such as induction of shape change and motility, enhanced chemotaxis in response to complement factor C5a (Wang et al., 2002). However, its biological effects are not restricted to macrophages. MSP promotes proliferation and migration of various epithelial cells and microglia (Kretschmann et al., 2010; Suzuki et al., 2008), increases ciliary motility of nasal epithelial cells (Sakamoto et al., 1997), stimulates the bone resorbing activity of osteoclasts (Kurihara et al., 1996), and stimulates sperm motility (Ohshiro et al., 1996). To date, many studies have suggested that MSP/RON signaling pathway plays roles in various pathophysiological conditions such as inflammation, wound healing, and cancer. Gene knockout studies revealed that MSP is not essential for embryogenesis, fertility (Bezerra et al., 1998).

During inflammation, MSP exerts a dual function, both stimulatory and inhibitory, on macrophages. Stimulatory functions include its ability to induce macrophage spreading, migration, phagocytosis and the production of cytokines. However, MSP inhibits lipopolysaccharide-induced production of inflammatory mediators, such as inducible NO synthase, cyclooxygenase-2, and prostaglandin E2. These suppressive effects are mediated by RON-transduced signals that block LPS-induced activation of NF-κB pathways (Wang et al., 2002; Kretschmann et al., 2010).

Wound healing
MSP/RON signaling is involved at various steps of wound healing process. MSP promotes keratinocyte migration in mouse wound models and in wound healing assays in vitro. In experimental excisional wounds in rats, expression levels of MSP and RON within the wound were highest between 7 and 21 days. In a lung injury model, the function of MSP/RON appears to be necessary to suppress NF-κB activation and RON deficient mice exhibited increased lung injury and significantly decreased survival times (Kretschmann et al., 2010). However, MSP deficient mice do not show any defects in a skin wound healing model, suggesting that functional redundancies exist in the wound healing process (Bezerra et al., 1998). In a gentamicin(GM)-induced nephropathy model, MSP attenuates GM-induced inflammation and apoptosis by inhibition of the MAPKs/NF-κB signaling pathways (Lee et al., 2013).

Homology The human MSP has 45% amino acid sequence identity to hepatocyte growth factor, 43% to plasminogen and 36% to prothrombin, and 79% identity with murine and rat orthologue.


Note Non-synonymous SNP (rs3197999, R689C) in the human MST-1 gene has been linked to inflammatory bowel disease (IBD) (Goyette et al., 2008; Latiano et al., 2010). This R689C variant impairs MSP function by reducing its affinity to RON. Recent study suggests that the rs3197999 variant in MST1 gene is also associated with primary sclerosing cholangitis (PSC) and extrahepatic cholangiocarcinoma (Melum et al., 2011; Srivastava et al., 2012; Krawczyk et al., 2013).

Implicated in

Entity Cancer
Note Activation of RON by MSP can initiate signaling through many pathways implicated in tumor progression and metastasis. MSP activating serine proteases, such as HGFA, ST14/matriptase and hepsin are upregulated in various cancers. In addition, RON is overexpressed in many types of epithelial cancer. When MSP was activated at sites of tumors it would not only lead to activation of RON on tumor-associated macrophages, but also on the tumor cells, where RON has been shown to induce proliferation, survival, cell migration, epithelial-mesenchymal transition (EMT), invasion and metastasis. Furthermore, MSP/RON regulates M2 macrophage polarization leading to secretion of immunosuppressive cytokines as well as growth and angiogenic factors that promote the tumor progression. (Kretschmann et al., 2010).
Entity Lung cancer
Note MSP promoted liver metastasis of small cell lung cancer cells in a mouse model. Moreover, immunohistochemical analyses of liver metastases revealed that microvessel density and tumor-associated macrophages are significantly increased in lesions produced by MSP transfected cells (Sato et al., 2013).
Entity Breast cancer
Note In the MMTV-PyMT mouse breast cancer model, MSP promoted tumor growth and increased metastatic frequency. The most prominent effect of MSP expression in tumors was osteolytic metastasis to bone (Welm et al., 2007). Immunohistochemical analysis revealed that the proportion of malignant tumors (invasive ductal carcinoma) positive for MSP expression was significantly higher than that of benign tumor (Ren et al., 2012). However, there was no relationship between MSP expression and histopathological grade of the carcinoma cells.
Prognosis Breast cancer patients whose tumor overexpressed MSP/ST14/RON had significantly shorter metastasis-free survival and overall survival compared with patients whose tumors did not overexpress MSP/ST14/RON genes. Furthermore, overexpression of MSP/ST14/RON increased incidence of bone, lung, liver and brain metastases (Welm et al., 2007).
Entity Pancreatic cancer
Note MSP-induced activation of RON leads to enhanced L3.6pl pancreatic cancer cell migration and invasion. RON activation also induced morphological spindle-shape change and altered expression of E-cadherin (Camp et al., 2007). MSP strongly induced phosphorylation and nuclear translocation of , a downstream signaling protein of the Ras-Erk1/2 pathway. RSK-2 expressing L3.6pl pancreatic cancer cell shows EMT-like phenotypic changes after MSP stimulation (Ma et al., 2011).
Entity Merkel cell carcinoma
Note Tissue samples from 14 cases of Merkel cell carcinoma were used for immunohistochemical analysis. Nine cases out of 14 were positive for MSP and 9 cases out of 14 cases were positive for RON. Normal Merkel cells were negative for MSP and RON, suggesting MSP/RON signaling could play a role in tumorigenesis of MCC (Nagahama et al., 2011).
Entity Knee osteoarthritis (OA)
Note By using glycoproteomic approach, MSP was found as a prognostic factor for knee OA (Fukuda et al., 2012). In situ hybridization confirmed that abundant MSP mRNA expression was observed in the synovial tissues from OA knee.
Prognosis Higher plasma MSP level was associated with the progression of knee OA.


Biological effects of targeted inactivation of hepatocyte growth factor-like protein in mice.
Bezerra JA, Carrick TL, Degen JL, Witte D, Degen SJ.
J Clin Invest. 1998 Mar 1;101(5):1175-83.
PMID 9486989
Coordinate expression and functional profiling identify an extracellular proteolytic signaling pathway.
Bhatt AS, Welm A, Farady CJ, Vasquez M, Wilson K, Craik CS.
Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5771-6. Epub 2007 Mar 27.
PMID 17389401
Tyrosine kinase receptor RON in human pancreatic cancer: expression, function, and validation as a target.
Camp ER, Yang A, Gray MJ, Fan F, Hamilton SR, Evans DB, Hooper AT, Pereira DS, Hicklin DJ, Ellis LM.
Cancer. 2007 Mar 15;109(6):1030-9.
PMID 17311308
Genetic evidence supporting the association of protease and protease inhibitor genes with inflammatory bowel disease: a systematic review.
Cleynen I, Juni P, Bekkering GE, Nuesch E, Mendes CT, Schmied S, Wyder S, Kellen E, Villiger PM, Rutgeerts P, Vermeire S, Lottaz D.
PLoS One. 2011;6(9):e24106. doi: 10.1371/journal.pone.0024106. Epub 2011 Sep 8. (REVIEW)
PMID 21931648
Potential plasma biomarkers for progression of knee osteoarthritis using glycoproteomic analysis coupled with a 2D-LC-MALDI system.
Fukuda I, Ishihara T, Ohmachi S, Sakikawa I, Morita A, Ikeda M, Yamane S, Toyosaki-Maeda T, Takinami Y, Okamoto H, Numata Y, Fukui N.
Proteome Sci. 2012 Jun 6;10(1):36. doi: 10.1186/1477-5956-10-36.
PMID 22672759
Proteolytic activation of pro-macrophage-stimulating protein by hepsin.
Ganesan R, Kolumam GA, Lin SJ, Xie MH, Santell L, Wu TD, Lazarus RA, Chaudhuri A, Kirchhofer D.
Mol Cancer Res. 2011 Sep;9(9):1175-86. doi: 10.1158/1541-7786.MCR-11-0004. Epub 2011 Aug 29.
PMID 21875933
Gene-centric association mapping of chromosome 3p implicates MST1 in IBD pathogenesis.
Goyette P, Lefebvre C, Ng A, Brant SR, Cho JH, Duerr RH, Silverberg MS, Taylor KD, Latiano A, Aumais G, Deslandres C, Jobin G, Annese V, Daly MJ, Xavier RJ, Rioux JD.
Mucosal Immunol. 2008 Mar;1(2):131-8. doi: 10.1038/mi.2007.15. Epub 2008 Jan 16.
PMID 19079170
Hepatocyte growth factor activator is a serum activator of single-chain precursor macrophage-stimulating protein.
Kawaguchi M, Orikawa H, Baba T, Fukushima T, Kataoka H.
FEBS J. 2009 Jul;276(13):3481-90. doi: 10.1111/j.1742-4658.2009.07070.x. Epub 2009 May 18.
PMID 19456860
Macrophage stimulating protein variation enhances the risk of sporadic extrahepatic cholangiocarcinoma.
Krawczyk M, Hoblinger A, Mihalache F, Grunhage F, Acalovschi M, Lammert F, Zimmer V.
Dig Liver Dis. 2013 Jul;45(7):612-5. doi: 10.1016/j.dld.2012.12.017. Epub 2013 Feb 16.
PMID 23422030
The macrophage stimulating protein/Ron pathway as a potential therapeutic target to impede multiple mechanisms involved in breast cancer progression.
Kretschmann KL, Eyob H, Buys SS, Welm AL.
Curr Drug Targets. 2010 Sep;11(9):1157-68. (REVIEW)
PMID 20545605
Macrophage-stimulating protein activates STK receptor tyrosine kinase on osteoclasts and facilitates bone resorption by osteoclast-like cells.
Kurihara N, Iwama A, Tatsumi J, Ikeda K, Suda T.
Blood. 1996 May 1;87(9):3704-10.
PMID 8611695
Variants at the 3p21 locus influence susceptibility and phenotype both in adults and early-onset patients with inflammatory bowel disease.
Latiano A, Palmieri O, Corritore G, Valvano MR, Bossa F, Cucchiara S, Castro M, Riegler G, De Venuto D, D'Inca R, Andriulli A, Annese V.
Inflamm Bowel Dis. 2010 Jul;16(7):1108-17. doi: 10.1002/ibd.21176.
PMID 20024904
Macrophage-stimulating protein attenuates gentamicin-induced inflammation and apoptosis in human renal proximal tubular epithelial cells.
Lee KE, Kim EY, Kim CS, Choi JS, Bae EH, Ma SK, Kim KK, Lee JU, Kim SW.
Biochem Biophys Res Commun. 2013 May 10;434(3):527-33. doi: 10.1016/j.bbrc.2013.03.108. Epub 2013 Apr 10.
PMID 23583394
Ribosomal protein S6 kinase (RSK)-2 as a central effector molecule in RON receptor tyrosine kinase mediated epithelial to mesenchymal transition induced by macrophage-stimulating protein.
Ma Q, Guin S, Padhye SS, Zhou YQ, Zhang RW, Wang MH.
Mol Cancer. 2011 May 28;10:66. doi: 10.1186/1476-4598-10-66.
PMID 21619683
Genome-wide association analysis in primary sclerosing cholangitis identifies two non-HLA susceptibility loci.
Melum E, Franke A, Schramm C, Weismuller TJ, Gotthardt DN, Offner FA, Juran BD, Laerdahl JK, Labi V, Bjornsson E, Weersma RK, Henckaerts L, Teufel A, Rust C, Ellinghaus E, Balschun T, Boberg KM, Ellinghaus D, Bergquist A, Sauer P, Ryu E, Hov JR, Wedemeyer J, Lindkvist B, Wittig M, Porte RJ, Holm K, Gieger C, Wichmann HE, Stokkers P, Ponsioen CY, Runz H, Stiehl A, Wijmenga C, Sterneck M, Vermeire S, Beuers U, Villunger A, Schrumpf E, Lazaridis KN, Manns MP, Schreiber S, Karlsen TH.
Nat Genet. 2011 Jan;43(1):17-9. doi: 10.1038/ng.728. Epub 2010 Dec 12.
PMID 21151127
Tyrosine kinase receptor RON and its ligand MSP in Merkel cell carcinoma.
Nagahama J, Daa T, Yada N, Kashima K, Fujiwara S, Saikawa T, Yokoyama S.
Pathol Res Pract. 2011 Aug 15;207(8):463-7. doi: 10.1016/j.prp.2011.05.006. Epub 2011 Jun 30.
PMID 21723047
Molecular cloning of rat macrophage-stimulating protein and its involvement in the male reproductive system.
Ohshiro K, Iwama A, Matsuno K, Ezaki T, Sakamoto O, Hamaguchi I, Takasu N, Suda T.
Biochem Biophys Res Commun. 1996 Oct 3;227(1):273-80.
PMID 8858136
Activation of macrophage-stimulating protein by human airway trypsin-like protease.
Orikawa H, Kawaguchi M, Baba T, Yorita K, Sakoda S, Kataoka H.
FEBS Lett. 2012 Feb 3;586(3):217-21. doi: 10.1016/j.febslet.2012.01.009. Epub 2012 Jan 11.
PMID 22245154
Macrophage-stimulating protein is produced by tubular cells and activates mesangial cells.
Rampino T, Collesi C, Gregorini M, Maggio M, Soccio G, Guallini P, Dal Canton A.
J Am Soc Nephrol. 2002 Mar;13(3):649-57.
PMID 11856768
Expression and mutational status of RON in neoplastic lesions of the breast: analysis of MSP/RON signaling in ductal carcinoma in situ and invasive ductal carcinoma.
Ren X, Daa T, Yada N, Kashima K, Fujitomi Y, Yokoyama S.
APMIS. 2012 May;120(5):358-67. doi: 10.1111/j.1600-0463.2011.02841.x. Epub 2011 Nov 28.
PMID 22515290
Role of macrophage-stimulating protein and its receptor, RON tyrosine kinase, in ciliary motility.
Sakamoto O, Iwama A, Amitani R, Takehara T, Yamaguchi N, Yamamoto T, Masuyama K, Yamanaka T, Ando M, Suda T.
J Clin Invest. 1997 Feb 15;99(4):701-9.
PMID 9045873
Macrophage stimulating protein promotes liver metastases of small cell lung cancer cells by affecting the organ microenvironment.
Sato S, Hanibuchi M, Kuramoto T, Yamamori N, Goto H, Ogawa H, Mitsuhashi A, Van TT, Kakiuchi S, Akiyama S, Nishioka Y, Sone S.
Clin Exp Metastasis. 2013 Mar;30(3):333-44. doi: 10.1007/s10585-012-9540-y. Epub 2012 Sep 26.
PMID 23011677
Regulation of macrophage arginase expression and tumor growth by the Ron receptor tyrosine kinase.
Sharda DR, Yu S, Ray M, Squadrito ML, De Palma M, Wynn TA, Morris SM Jr, Hankey PA.
J Immunol. 2011 Sep 1;187(5):2181-92. doi: 10.4049/jimmunol.1003460. Epub 2011 Aug 1.
PMID 21810604
Macrophage stimulating protein: purification, partial amino acid sequence, and cellular activity.
Skeel A, Yoshimura T, Showalter SD, Tanaka S, Appella E, Leonard EJ.
J Exp Med. 1991 May 1;173(5):1227-34.
PMID 1827141
Fine mapping and replication of genetic risk loci in primary sclerosing cholangitis.
Srivastava B, Mells GF, Cordell HJ, Muriithi A, Brown M, Ellinghaus E, Franke A, Consortium UP, Karlsen TH, Sandford RN, Alexander GJ, Chapman RW, Rushbrook SM, Melum E.
Scand J Gastroenterol. 2012 Jul;47(7):820-6. doi: 10.3109/00365521.2012.682090. Epub 2012 May 4.
PMID 22554193
Regulation of cell migration and cytokine production by HGF-like protein (HLP) / macrophage stimulating protein (MSP) in primary microglia.
Suzuki Y, Funakoshi H, Machide M, Matsumoto K, Nakamura T.
Biomed Res. 2008 Apr;29(2):77-84.
PMID 18480548
Macrophage-stimulating protein and RON receptor tyrosine kinase: potential regulators of macrophage inflammatory activities.
Wang MH, Zhou YQ, Chen YQ.
Scand J Immunol. 2002 Dec;56(6):545-53. (REVIEW)
PMID 12472665
The macrophage-stimulating protein pathway promotes metastasis in a mouse model for breast cancer and predicts poor prognosis in humans.
Welm AL, Sneddon JB, Taylor C, Nuyten DS, van de Vijver MJ, Hasegawa BH, Bishop JM.
Proc Natl Acad Sci U S A. 2007 May 1;104(18):7570-5. Epub 2007 Apr 24.
PMID 17456594
Cloning, sequencing, and expression of human macrophage stimulating protein (MSP, MST1) confirms MSP as a member of the family of kringle proteins and locates the MSP gene on chromosome 3.
Yoshimura T, Yuhki N, Wang MH, Skeel A, Leonard EJ.
J Biol Chem. 1993 Jul 25;268(21):15461-8.
PMID 8393443


This paper should be referenced as such :
Kawaguchi, M ; Kataoka, H
MST1 (macrophage stimulating 1 (hepatocyte growth factor-like))
Atlas Genet Cytogenet Oncol Haematol. 2013;17(12):828-832.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)MST1   7380
Atlas Explorer : (Salamanque)MST1
Entrez_Gene (NCBI)MST1    macrophage stimulating 1
AliasesD3F15S2; DNF15S2; HGFL; MSP; 
GeneCards (Weizmann)MST1
Ensembl hg19 (Hinxton)ENSG00000173531 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000173531 [Gene_View]  ENSG00000173531 [Sequence]  chr3:49683947-49688763 [Contig_View]  MST1 [Vega]
ICGC DataPortalENSG00000173531
TCGA cBioPortalMST1
AceView (NCBI)MST1
Genatlas (Paris)MST1
SOURCE (Princeton)MST1
Genetics Home Reference (NIH)MST1
Genomic and cartography
GoldenPath hg38 (UCSC)MST1  -     chr3:49683947-49688763 -  3p21.31   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)MST1  -     3p21.31   [Description]    (hg19-Feb_2009)
GoldenPathMST1 - 3p21.31 [CytoView hg19]  MST1 - 3p21.31 [CytoView hg38]
Genome Data Viewer NCBIMST1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AK222893 AK294324 AK296192 AK298396 AK298452
RefSeq transcript (Entrez)NM_001393581 NM_001393582 NM_001393583 NM_001393584 NM_001393585 NM_020998
Consensus coding sequences : CCDS (NCBI)MST1
Gene ExpressionMST1 [ NCBI-GEO ]   MST1 [ EBI - ARRAY_EXPRESS ]   MST1 [ SEEK ]   MST1 [ MEM ]
Gene Expression Viewer (FireBrowse)MST1 [ Firebrowse - Broad ]
GenevisibleExpression of MST1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)4485
GTEX Portal (Tissue expression)MST1
Human Protein AtlasENSG00000173531-MST1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP26927   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP26927  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP26927
Domaine pattern : Prosite (Expaxy)KRINGLE_1 (PS00021)    KRINGLE_2 (PS50070)    PAN (PS50948)    TRYPSIN_DOM (PS50240)   
Domains : Interpro (EBI)HGF/MST1    Kringle    Kringle-like    Kringle_CS    Kringle_sf    MSP_HGFL    Pan_app    Peptidase_S1_PA    Peptidase_S1_PA_chymotrypsin    Peptidase_S1A    Trypsin_dom   
Domain families : Pfam (Sanger)Kringle (PF00051)    PAN_1 (PF00024)    Trypsin (PF00089)   
Domain families : Pfam (NCBI)pfam00051    pfam00024    pfam00089   
Domain families : Smart (EMBL)KR (SM00130)  PAN_AP (SM00473)  Tryp_SPc (SM00020)  
Conserved Domain (NCBI)MST1
PDB (RSDB)2ASU    4QT8   
PDB Europe2ASU    4QT8   
PDB (PDBSum)2ASU    4QT8   
PDB (IMB)2ASU    4QT8   
Structural Biology KnowledgeBase2ASU    4QT8   
SCOP (Structural Classification of Proteins)2ASU    4QT8   
CATH (Classification of proteins structures)2ASU    4QT8   
AlphaFold pdb e-kbP26927   
Human Protein Atlas [tissue]ENSG00000173531-MST1 [tissue]
Protein Interaction databases
IntAct (EBI)P26927
Ontologies - Pathways
Ontology : AmiGOendopeptidase activity  signaling receptor binding  protein binding  extracellular region  extracellular space  extracellular space  proteolysis  receptor tyrosine kinase binding  receptor tyrosine kinase binding  histone H2A-S139 phosphorylation  negative regulation of gluconeogenesis  regulation of receptor signaling pathway via JAK-STAT  collagen-containing extracellular matrix  regulation of cAMP-dependent protein kinase activity  
Ontology : EGO-EBIendopeptidase activity  signaling receptor binding  protein binding  extracellular region  extracellular space  extracellular space  proteolysis  receptor tyrosine kinase binding  receptor tyrosine kinase binding  histone H2A-S139 phosphorylation  negative regulation of gluconeogenesis  regulation of receptor signaling pathway via JAK-STAT  collagen-containing extracellular matrix  regulation of cAMP-dependent protein kinase activity  
REACTOMEP26927 [protein]
REACTOME PathwaysR-HSA-8852405 [pathway]   
NDEx NetworkMST1
Atlas of Cancer Signalling NetworkMST1
Wikipedia pathwaysMST1
Orthology - Evolution
GeneTree (enSembl)ENSG00000173531
Phylogenetic Trees/Animal Genes : TreeFamMST1
Homologs : HomoloGeneMST1
Homology/Alignments : Family Browser (UCSC)MST1
Gene fusions - Rearrangements
Fusion : MitelmanMST1::SRRD [3p21.31/22q12.1]  
Fusion Cancer (Beijing)MST1P9 [MST1]  -  3p21.31 [FUSC002005]
Fusion : FusionHubAC099668.5--MST1    MST1--MST1P2    MST1--OSBPL6    MST1--SRRD    MST1P2--MST1    MST1P9--MST1    RAPL--MST1   
Fusion : QuiverMST1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerMST1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)MST1
Exome Variant ServerMST1
GNOMAD BrowserENSG00000173531
Varsome BrowserMST1
ACMGMST1 variants
Genomic Variants (DGV)MST1 [DGVbeta]
DECIPHERMST1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisMST1 
ICGC Data PortalMST1 
TCGA Data PortalMST1 
Broad Tumor PortalMST1
OASIS PortalMST1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICMST1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DMST1
Mutations and Diseases : HGMDMST1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)MST1
DoCM (Curated mutations)MST1
CIViC (Clinical Interpretations of Variants in Cancer)MST1
NCG (London)MST1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry MST1
NextProtP26927 [Medical]
Target ValidationMST1
Huge Navigator MST1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDMST1
Pharm GKB GenePA31185
Clinical trialMST1
DataMed IndexMST1
PubMed94 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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