ST14

Suppression of tumorigenicity 14 (colon carcinoma)
File:PBB Protein ST14 image.jpg PDB rendering based on 1eaw.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1eaw​, 1eax​, 2gv6​, 2gv7​
Identifiers
Symbols	ST14 ; HAI; MT-SP1; MTSP-1; MTSP1; PRSS14; SNC19; TADG-15
External IDs	Template:OMIM5 Template:MGI HomoloGene: 7906
Gene ontology Molecular function Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
File:PBB GE ST14 202005 at tn.png
File:PBB GE ST14 216905 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Suppression of tumorigenicity 14 (colon carcinoma), also known as ST14, is a human gene.

The protein encoded by this gene is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-phosphate. This protease has been shown to cleave and activate hepatocyte growth factor/scattering factor, and urokinase plasminogen activator, which suggest the function of this protease as an epithelial membrane activator for other proteases and latent growth factors. The expression of this protease has been associated with breast, colon, prostate, and ovarian tumors, which implicates its role in cancer invasion, and metastasis.

Further reading

• Uhland K (2007). "Matriptase and its putative role in cancer". Cell. Mol. Life Sci. 63 (24): 2968–78. doi:10.1007/s00018-006-6298-x. PMID 17131055.
• Zhang Y, Cai X, Schlegelberger B, Zheng S (1999). "Assignment1 of human putative tumor suppressor genes ST13 (alias SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and 11q24-->q25 by in situ hybridization". Cytogenet. Cell Genet. 83 (1–2): 56–7. PMID 9925927.CS1 maint: Multiple names: authors list (link)
• Lin CY, Anders J, Johnson M; et al. (1999). "Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity". J. Biol. Chem. 274 (26): 18231–6. PMID 10373424.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lin CY, Anders J, Johnson M, Dickson RB (1999). "Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk". J. Biol. Chem. 274 (26): 18237–42. PMID 10373425.CS1 maint: Multiple names: authors list (link)
• Takeuchi T, Shuman MA, Craik CS (1999). "Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue". Proc. Natl. Acad. Sci. U.S.A. 96 (20): 11054–61. PMID 10500122.CS1 maint: Multiple names: authors list (link)
• Takeuchi T, Harris JL, Huang W; et al. (2000). "Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates". J. Biol. Chem. 275 (34): 26333–42. doi:10.1074/jbc.M002941200. PMID 10831593.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lee SL, Dickson RB, Lin CY (2001). "Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease". J. Biol. Chem. 275 (47): 36720–5. doi:10.1074/jbc.M007802200. PMID 10962009.CS1 maint: Multiple names: authors list (link)
• Tanimoto H, Underwood LJ, Wang Y; et al. (2001). "Ovarian tumor cells express a transmembrane serine protease: a potential candidate for early diagnosis and therapeutic intervention". Tumour Biol. 22 (2): 104–14. PMID 11125283.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Oberst M, Anders J, Xie B; et al. (2001). "Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo". Am. J. Pathol. 158 (4): 1301–11. PMID 11290548.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Benaud C, Oberst M, Hobson JP; et al. (2002). "Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase". J. Biol. Chem. 277 (12): 10539–46. doi:10.1074/jbc.M109064200. PMID 11792696.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ihara S, Miyoshi E, Ko JH; et al. (2002). "Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching". J. Biol. Chem. 277 (19): 16960–7. doi:10.1074/jbc.M200673200. PMID 11864986.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Peek M, Moran P, Mendoza N; et al. (2003). "Unusual proteolytic activation of pro-hepatocyte growth factor by plasma kallikrein and coagulation factor XIa". J. Biol. Chem. 277 (49): 47804–9. doi:10.1074/jbc.M209778200. PMID 12372819.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Benaud CM, Oberst M, Dickson RB, Lin CY (2003). "Deregulated activation of matriptase in breast cancer cells". Clin. Exp. Metastasis. 19 (7): 639–49. PMID 12498394.CS1 maint: Multiple names: authors list (link)
• Oberst MD, Williams CA, Dickson RB; et al. (2003). "The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor". J. Biol. Chem. 278 (29): 26773–9. doi:10.1074/jbc.M304282200. PMID 12738778.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Santin AD, Cane' S, Bellone S; et al. (2003). "The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma". Cancer. 98 (9): 1898–904. doi:10.1002/cncr.11753. PMID 14584072.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Suzuki M, Kobayashi H, Kanayama N; et al. (2004). "Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase". J. Biol. Chem. 279 (15): 14899–908. doi:10.1074/jbc.M313130200. PMID 14747469.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hung RJ, Hsu IaW, Dreiling JL; et al. (2004). "Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts". Am. J. Physiol., Cell Physiol. 286 (5): C1159–69. doi:10.1152/ajpcell.00400.2003. PMID 15075215.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Sun LF, Zheng S, Shi Y; et al. (2004). "[SNC19/ST14 gene transfection and expression influence the biological behavior of colorectal cancer cells]". Zhonghua Yi Xue Za Zhi. 84 (10): 843–8. PMID 15200890.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)