MBTPS1 Antibody, FITC conjugated

1. rs11642644 associated with facial profile PMID: 29301965
2. In the absence of S1P, the catalytically inactive alpha/beta-subunit precursor of GlcNAc-1-phosphotransferase fails to be activated and results in missorting of newly synthesized lysosomal enzymes, and lysosomal accumulation of non-degraded material, which are biochemical features of defective GlcNAc-1-phosphotransferase subunits and the associated pediatric lysosomal diseases mucolipidosis type II and III. PMID: 28693924
3. Results suggest that (pro)renin receptor (s(P)RR) is generated by sequential processing by site-1 protease (S1P) and furin protein. PMID: 28013223
4. primordial SKI-1/S1P likely contained a simpler prodomain consisting of the highly conserved AB fragment that represents an independent folding unit PMID: 26645686
5. S1P substrate-dependent regulatory mechanisms for lipid synthesis and biogenesis of lysosomes are different PMID: 26108224
6. The interaction between S1P and C5a plays an important role in neutrophils for antineutrophil cytoplasmic antibody -mediated activation PMID: 25000985
7. Incompletely matured forms of SKI-1/S1P further process cellular and viral substrates in distinct subcellular compartments. PMID: 25378398
8. We show that SKI-1 is constitutively expressed in human pigment cells with higher SKI activity in seven out of eight melanoma cell lines compared with normal melanocytes. PMID: 23884247
9. Diabetic high-density lipoprotein carries higher levels of S1P compared with normal high-density lipoprotein. PMID: 23360427
10. Y285 of SKI-1 is crucial for the efficient processing of envelope glycoproteins from Old World and clade C New World arenavirus. PMID: 23536681
11. The role of MBTPS1 (SKI-1/S1P) peptides in cancer and approaches used to inhibit SKI-1/S1P were studied. PMID: 21568902
12. study found that the N-acetylglucosamine-1-phosphotransferase alpha/beta-subunit precursor is cleaved by S1P that activates sterol regulatory element-binding proteins in response to cholesterol deprivation; S1P functions in the biogenesis of lysosomes PMID: 21719679
13. S1P has a role in reducing the size of the luminal domain to prepare ATF6 to be an optimal S2P substrate PMID: 15299016
14. enzymatic activity of S1P is not calcium dependent, but can be modulated by a variety of mono- and divalent cations. S1P displayed pronounced positive cooperativity with a substrate derived from the viral coat glycoprotein of the lassa virus. PMID: 16973377
15. SKI-1/S1P inhibition resulted in reduced cholesterol synthesis and mRNA levels of the rate-limiting enzymes, HMG-CoA reductase and squalene epoxidase, in the cholesterol synthetic pathway. PMID: 17867930
16. Complementation of SKI-1/S1P-deficient cells with a SKI-1/S1P expression vector restored release of infectious Crimean-Congo hemorrhagic fever virus (>106 PFU/ml), confirming that SKI-1/S1P processing is required for incorporation of viral glycoproteins. PMID: 17898072
17. Site 1 protease is required for proteolytic processing of the glycoproteins of the South American hemorrhagic fever viruses Junin, Machupo, and Guanarito. PMID: 18400865

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HGNC: 15456

OMIM: 603355

KEGG: hsa:8720

STRING: 9606.ENSP00000344223

UniGene: Hs.75890