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(pro)renin receptor + H2O
soluble (pro)renin receptor + ?
-
-
-
-
?
2-aminobenzoic acid-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu-Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala + H2O
2-aminobenzoic acid-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu + Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala
-
cleaves between Leu and Gly
-
?
2-aminobenzoic acid-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu-Gly-Thr-Phe-Thr-3-nitrotyrosyl-Ala-CONH2 + H2O
2-aminobenzoic acid-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu + Gly-Thr-Phe-Thr-3-nitrotyrosyl-Ala-CONH2
-
-
-
-
?
2-aminobenzoic acid-SSGSRRLLSEESY(NO2)-Ala-NH2 + H2O
?
-
-
-
-
?
2-aminobenzoyl-ALVLRKPLFLDSY(NO2)-Ala + H2O
?
-
cleaves between Leu and Phe
-
?
2-aminobenzoyl-Arg-Asn-Thr-Pro-Arg-Arg-Glu-Arg-Arg-Arg-Lys-Lys-Arg-Gly-Leu-(3-nitro)Tyr-Ala + H2O
2-aminobenzoyl-Arg-Asn-Thr-Pro-Arg-Arg-Glu-Arg-Arg-Arg-Lys-Lys-Arg-Gly-Leu + (3-nitro)Tyr-Ala
-
cleaves between Leu and 3-nitrotyrosine
-
?
2-aminobenzoyl-Arg-His-Ser-Ser-Arg-Arg-Leu-Leu-Arg-Ala-Ile-(3-nitro)Tyr-Ala + H2O
2-aminobenzoyl-Arg-His-Ser-Ser-Arg-Arg-Leu-Leu + Arg-Ala-Ile-(3-nitro)Tyr-Ala
-
cleaves between Leu and Arg
-
?
2-aminobenzoyl-Arg-Ser-Leu-Lys-Tyr-Ala-Glu-Ser-Asp-(3-nitro)-Tyr-Ala + H2O
2-aminobenzoyl-Arg-Ser-Leu-Lys + Tyr-Ala-Glu-Ser-Asp-(3-nitro)-Tyr-Ala
-
cleaves between Lys and Tyr
-
?
2-aminobenzoyl-Ser-Arg-Arg-Leu-Leu-Arg-Ala-Leu-Glu-(3-nitro)Tyr-Ala + H2O
2-aminobenzoyl-Ser-Arg-Arg-Leu-Leu + Arg-Ala-Leu-Glu-(3-nitro)Tyr-Ala
-
cleaves between Leu and Arg
-
?
2-aminobenzoyl-SSGSRRLLSEESY(NO2)-Ala + H2O
?
-
cleaves between Leu and Ser
-
?
2-aminobenzoyl-Val-Phe-Arg-Ser-Leu-Lys-Tyr-Ala-Glu-Ser-Asp-(3-nitro)Tyr-Ala + H2O
2-aminobenzoyl-Val-Phe-Arg-Ser-Leu-Lys + Tyr-Ala-Glu-Ser-Asp-(3-nitro)Tyr-Ala
-
cleaves between Lys and Tyr
-
?
Abz-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu-Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala-CONH2 + H2O
Abz-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu + Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala-CONH2
-
i.e. QPC251-263
-
-
?
Abz-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu-Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala-NH2 + H2O
?
-
favored quenched fluorogenic substrate
-
-
?
Abz-DIYISRRLL-GTFT-Tyx-A + H2O
Abz-DIYISRRLL + GTFT-Tyx-A
-
-
-
-
?
Abz-DIYISRRLLGTFTY(NO2)A + H2O
?
-
S1P displays pronounced positive cooperativity with this substrate derived from the viral coat glycoprotein of the lassa virus
-
-
?
Ac-AISRRLL-7-amido-4-methylcoumarin + H2O
Ac-AISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-Arg-Arg-Leu-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
Ac-Arg-Ser-Leu-Lys-p-nitroanilide + H2O
?
-
-
-
-
?
Ac-FISRRLL-7-amido-4-methylcoumarin + H2O
Ac-FISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-IAVGRTLK-7-amido-4-methylcoumarin + H2O
Ac-IAVGRTLK + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-IYISRRLL-7-amido-4-methylcoumarin + H2O
Ac-IYISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-Leu-4-methyl-coumaryl-7-amide + H2O
?
-
-
-
-
?
Ac-QKSIAVGRTLK-7-amido-4-methylcoumarin + H2O
Ac-QKSIAVGRTLK + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-RKLL-7-amido-4-methylcoumarin + H2O
Ac-RKLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-RRLL-7-amido-4-methylcoumarin + H2O
Ac-RRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-RRLQ-7-amido-4-methylcoumarin + H2O
Ac-RRLQ + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-RTLK-7-amido-4-methylcoumarin + H2O
Ac-RTLK + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-SFITRRLQ-7-amido-4-methylcoumarin + H2O
Ac-SFITRRLQ + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-VFRSLK-4-methyl-coumaryl-7-amide + H2O
?
Ac-VFRSLK-4-methylcoumarin 7-amide
?
-
-
-
?
Ac-VFRSLK-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
Ac-YISRRLL-7-amido-4-methylcoumarin + H2O
Ac-YISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-YSSVSRKLL-7-amido-4-methylcoumarin + H2O
Ac-YSSVSRKLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
arenavirus envelope glycoprotein precursor + H2O
?
ATF6 precursor + H2O
nuclear ATF6
-
rSt-1 and rSt-2 seem to affect the processing of ATF6 by SKI-1
-
-
?
brain-derived neurotrophic factor precursor + H2O
?
-
cleaves at an RGLTLS site between Thr and Ser
-
?
CREB4 + H2O
?
-
i.e. androgen-induced leucine zipper protein, C-terminal domain of CREB4 somehow confers resistance to cleavage by S1P, which can be released either by removal of the region or physiologically by some regulatory signal
-
-
?
Crimean Congo hemorrhagic fever virus glycoprotein + H2O
?
Crimean Congo hemorrhagic fever virus glycoprotein + H2O
glycoprotein precursor Gn + glycoprotein precursor Gc
-
-
-
-
?
Dabcyl-Arg-His-Ser-Ser-Arg-Arg-Leu-Leu-Arg-Ala-Leu-Glu-Gly-Gly-Lys(tetramethylrhodamine)-OH + H2O
?
-
-
-
?
Dabcyl-Ser-Gly-Ser-Gly-Arg-Ser-Val-Leu-Ser-Phe-Glu-Ser-Gly-Ser-Lys(tetramethylrhodamine)-Arg-OH + H2O
?
-
-
-
?
glycoprotein + H2O
?
-
S1P is involved in the processing of the glycoproteins of the genetically more-distant South American hemorrhagic fever viruses Guanarito, Machupo, and Junin
-
-
?
glycoprotein precursor Gc + H2O
?
glycoprotein precursor Gn + H2O
?
-
-
-
-
?
Lassa virus envelope glycoprotein precursor + H2O
?
the enzyme recognition motif RRLL is critical for the processing of the Lassa virus envelope glycoprotein in the endoplasmic reticulum/cis-Golgi compartment
-
-
?
Lassa virus glycoprotein + H2O
?
-
cleavage at RRLL-sites
-
-
?
Lassa virus glycoprotein precursor GP-C + H2O
Lassa virus glycoprotein GP-2 + ?
-
cleavage at the C-terminal end of the recognition motif R-R-L-L
-
-
?
Lassa virus glycoprotein precursor protein + H2O
peripheral virion attachment protein GP1 + fusion-active transmembrane protein GP2
-
-
Arg-Arg-Leu-Leu + Gly-Thr-Phe
-
?
lymphocytic choriomeningitis virus glycoprotein precursor protein + H2O
peripheral virion attachment protein GP1 + fusion-active transmembrane protein GP2
-
-
Arg-Arg-Leu-Ala + Gly-Thr-Phe
-
?
membrane-associated transcription factor bZIP28 + H2O
?
sterol regulatory element-binding protein + H2O
?
sterol regulatory element-binding protein SREBP-2 + H2O
?
-
-
-
-
?
succinyl-YISRRLL-7-amido-4-methylcoumarin + H2O
succinyl-YISRRLL + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
Ac-VFRSLK-4-methyl-coumaryl-7-amide + H2O
?
-
-
-
-
?
Ac-VFRSLK-4-methyl-coumaryl-7-amide + H2O
?
-
-
-
-
?
arenavirus envelope glycoprotein precursor + H2O
?
-
-
-
?
arenavirus envelope glycoprotein precursor + H2O
?
activation, F259A replacement at P7 of the viral protein substrate impaires the reaction, while replacement of with F does not affect enzyme processing. The catalytic pocket of the enzyme may interact with additional substrate residues distal from the actual cleavage site. Residue Y285 of the enzyme, located distal from the catalytic triad, is implicated in the molecular recognition of the aromatic signature residue at P7 and is crucial for efficient processing of OW and clade C NW arenavirus glycoprotein precursor
-
-
?
arenavirus envelope glycoprotein precursor + H2O
?
activation/maturation
-
-
?
ATF6 + H2O
?
-
i.e. activating transcription factor 6
-
-
?
ATF6 + H2O
?
-
i.e. activating transcription factor 6
-
-
?
Crimean Congo hemorrhagic fever virus glycoprotein + H2O
?
-
cleavage at RRLL-sites
-
-
?
Crimean Congo hemorrhagic fever virus glycoprotein + H2O
?
-
posttranslational cleavage by furin/PC-mediated processing at its N-terminus at RSKR247 and by SKI-1 at its C-terminus at RRLL519
-
-
?
glycoprotein precursor Gc + H2O
?
-
-
-
?
glycoprotein precursor Gc + H2O
?
-
-
-
-
?
membrane-associated transcription factor bZIP28 + H2O
?
-
-
-
-
?
membrane-associated transcription factor bZIP28 + H2O
?
-
endoplasmic reticulum stress-induced activation, the RRIL573 site, but not the RVLM373 site, on the lumen-facing domain of bZIP28 is critical for the biological function of bZIP28 under endoplasmic reticulum stress condition
-
-
?
RsiW + H2O
?
-
PrsW is both necessary and sufficient for site-1 cleavage of the anti-sigmaW factor RsiW. Site-2 cleavage depends on the prior action of PrsW
-
-
?
RsiW + H2O
?
-
site-1 proteolysis of RsiW. Is converted to a C-terminally truncated form that remains membrane bound
-
-
?
RsiW + H2O
?
-
PrsW is both necessary and sufficient for site-1 cleavage of the anti-sigmaW factor RsiW. Site-2 cleavage depends on the prior action of PrsW
-
-
?
sterol regulatory element-binding protein + H2O
?
-
SREBP
-
?
sterol regulatory element-binding protein + H2O
?
-
SREBP, cleaves the luminal loop following the tetrapeptide sequence Arg-Xaa-Xaa-Leu
-
?
sterol regulatory element-binding protein + H2O
?
-
mutating the crucial Arg at position 486 to Ala blocks cleavage by dS1P
-
-
?
sterol regulatory element-binding protein + H2O
?
-
S1P cleaves in the luminal loop of the membrane-bound SREBP precursor, cutting it in two. The NH2- and COOH-terminal domains remain membrane bound owing to their single membrane-spanning helices
-
-
?
sterol regulatory element-binding protein + H2O
?
-
SREBP
-
?
sterol regulatory element-binding protein + H2O
?
-
-
-
-
?
additional information
?
-
-
initiates a process by which the transcriptionally active N-terminal fragments of SREBPs are released from membranes
-
?
additional information
?
-
-
initiates a process by which the active fragments of the SREBPs translocate to the nucleus and activate genes controlling the synthesis and uptake of cholersterol and unsaturated fatty acids in animal cells
-
?
additional information
?
-
-
peptides containing RSLK and RRLL are cleaved best
-
?
additional information
?
-
-
RRLL peptide representing the Gn processing site is efficiently cleaves but an RKPL peptide representing the GC processing site is cleaved at negligible levels
-
?
additional information
?
-
-
SKI-1 cleaves inactive proproteins at the motif R-X-(hydrophobic)-Z with Z being mostly Leu
-
-
?
additional information
?
-
the enzyme performs autocatalytic cleavage and activation. The cleavage of arenavirus glycoproteins, but not cellular substrates, critically depends on the autoprocessing of the enzyme, suggesting differences in the processing of cellular and viral substrates. The exogenous soluble enzyme is unable to process arenavirus lymphocytic choriomeningitis virus and pathogenic Lassa virus envelope glycoproteins displayed at the surface of enzyme-deficient cells, indicating that glycoprotein processing occurs in an intracellular compartment
-
-
?
additional information
?
-
zymogen activation of the enzyme involving sequential autocatalytic processing of its N-terminal prodomain at sites B'/B followed by the C'/C sites. Enzyme autoprocessing results in intermediates whose catalytic domain remains associated with prodomain fragments of different lengths. All incompletely matured intermediates of SKI-1/S1P show full catalytic activity toward cellular substrates, whereas optimal cleavage of viral glycoproteins depends on B'/B processing. Incompletely matured forms of SKI-1/S1P further process cellular and viral substrates in distinct subcellular compartments
-
-
?
additional information
?
-
substrate specificity and activity of wild-type enzyme and pro-domain mutants towards cellular and viral substrates, construction and evaluation of a cell-based chimeric protein molecular sensor, containing the LASVGPC cleavage site IYISRRLL-/-G, to monitor endogenous enzyme activity, overview
-
-
?
additional information
?
-
the SKI-1/S1P recognition site RRLL is present in the enzyme SKI-1/S1P prodomain and Lassa virus envelope glycoprotein precursor , but not in the lymphocytic choriomeningitis virus envelope glycoprotein precursor, it is crucial for the processing of the Lassa virus glycoprotein in the endoplasmic reticulum/cis-Golgi compartment
-
-
?
additional information
?
-
-
cleaves after lysine or leucine rather than arginine
-
?
additional information
?
-
-
functions to control lipid biosynthesis and uptake in animal cells
-
?
additional information
?
-
-
can cleave postsingle and possibly pairs of Thr residues in certain precursors
-
?
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Ac-AISRRLL-7-amido-4-methylcoumarin + H2O
Ac-AISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-FISRRLL-7-amido-4-methylcoumarin + H2O
Ac-FISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-IAVGRTLK-7-amido-4-methylcoumarin + H2O
Ac-IAVGRTLK + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-IYISRRLL-7-amido-4-methylcoumarin + H2O
Ac-IYISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-QKSIAVGRTLK-7-amido-4-methylcoumarin + H2O
Ac-QKSIAVGRTLK + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-RKLL-7-amido-4-methylcoumarin + H2O
Ac-RKLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-RRLL-7-amido-4-methylcoumarin + H2O
Ac-RRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-RRLQ-7-amido-4-methylcoumarin + H2O
Ac-RRLQ + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-RTLK-7-amido-4-methylcoumarin + H2O
Ac-RTLK + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-SFITRRLQ-7-amido-4-methylcoumarin + H2O
Ac-SFITRRLQ + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-YISRRLL-7-amido-4-methylcoumarin + H2O
Ac-YISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
Ac-YSSVSRKLL-7-amido-4-methylcoumarin + H2O
Ac-YSSVSRKLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
-
-
?
arenavirus envelope glycoprotein precursor + H2O
?
Lassa virus glycoprotein precursor protein + H2O
peripheral virion attachment protein GP1 + fusion-active transmembrane protein GP2
-
-
Arg-Arg-Leu-Leu + Gly-Thr-Phe
-
?
lymphocytic choriomeningitis virus glycoprotein precursor protein + H2O
peripheral virion attachment protein GP1 + fusion-active transmembrane protein GP2
-
-
Arg-Arg-Leu-Ala + Gly-Thr-Phe
-
?
membrane-associated transcription factor bZIP28 + H2O
?
-
endoplasmic reticulum stress-induced activation, the RRIL573 site, but not the RVLM373 site, on the lumen-facing domain of bZIP28 is critical for the biological function of bZIP28 under endoplasmic reticulum stress condition
-
-
?
succinyl-YISRRLL-7-amido-4-methylcoumarin + H2O
succinyl-YISRRLL + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
arenavirus envelope glycoprotein precursor + H2O
?
activation, F259A replacement at P7 of the viral protein substrate impaires the reaction, while replacement of with F does not affect enzyme processing. The catalytic pocket of the enzyme may interact with additional substrate residues distal from the actual cleavage site. Residue Y285 of the enzyme, located distal from the catalytic triad, is implicated in the molecular recognition of the aromatic signature residue at P7 and is crucial for efficient processing of OW and clade C NW arenavirus glycoprotein precursor
-
-
?
arenavirus envelope glycoprotein precursor + H2O
?
activation/maturation
-
-
?
additional information
?
-
-
initiates a process by which the active fragments of the SREBPs translocate to the nucleus and activate genes controlling the synthesis and uptake of cholersterol and unsaturated fatty acids in animal cells
-
?
additional information
?
-
the enzyme performs autocatalytic cleavage and activation. The cleavage of arenavirus glycoproteins, but not cellular substrates, critically depends on the autoprocessing of the enzyme, suggesting differences in the processing of cellular and viral substrates. The exogenous soluble enzyme is unable to process arenavirus lymphocytic choriomeningitis virus and pathogenic Lassa virus envelope glycoproteins displayed at the surface of enzyme-deficient cells, indicating that glycoprotein processing occurs in an intracellular compartment
-
-
?
additional information
?
-
zymogen activation of the enzyme involving sequential autocatalytic processing of its N-terminal prodomain at sites B'/B followed by the C'/C sites. Enzyme autoprocessing results in intermediates whose catalytic domain remains associated with prodomain fragments of different lengths. All incompletely matured intermediates of SKI-1/S1P show full catalytic activity toward cellular substrates, whereas optimal cleavage of viral glycoproteins depends on B'/B processing. Incompletely matured forms of SKI-1/S1P further process cellular and viral substrates in distinct subcellular compartments
-
-
?
additional information
?
-
-
functions to control lipid biosynthesis and uptake in animal cells
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R,2'R)-2,2'-[(E)-diazene-1,2-diylbis[benzene-2,1-diyloxy(1-oxoethane-2,1-diyl)imino[(2S)-1-oxo-4-phenylbutane-2,1-diyl]imino]]bis(3-phenylpropanoic acid)
-
-
(2S,2'S)-2,2'-[(E)-diazene-1,2-diylbis[benzene-2,1-diyloxy(1-oxoethane-2,1-diyl)imino]]bis(3-methylbutanoic acid)
-
-
(2S,2'S)-2,2'-[(E)-diazene-1,2-diylbis[benzene-2,1-diyloxy(1-oxoethane-2,1-diyl)imino]]bis(4-phenylbutanoic acid)
-
-
(3S,4S,5S,6R)-2-([(2R,3S,4S,5S,6S)-3,5-dihydroxy-2-(hydroxymethyl)-6-methoxytetrahydro-2H-pyran-4-yl]amino)-6-(hydroxymethyl)tetrahydro-2H-thiopyran-3,4,5-triol
-
i.e. BJ-12-26-1, greatly reduces SKI-1 zymogen processing, and abolishes the processing of substrate SREBP-2
(3S,4S,5S,6R)-2-([(2S,3S,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-2-methoxytetrahydro-2H-pyran-3-yl]amino)-6-(hydroxymethyl)tetrahydro-2H-thiopyran-3,4,5-triol
-
i.e. BJ-12-21-2, greatly reduces SKI-1 zymogen processing, and abolishes the processing of substrate SREBP-2
(R)-4-((diethylamino)methyl)-N-(2-methoxyphenethyl)-N-(pyrrolidin-3-yl)benzamide
inhibits endogenous SREBP processing in Chinese hamster ovary cells. Compound down-regulates the signal from an SRE-luciferase reporter gene in human embryonic kidney 293 cells and the expression of endogenous SREBP target genes in cultured HepG2 cells. In mice treated with the compound for 24 h, the expression of hepatic SREBP target genes is suppressed, and the hepatic rates of cholesterol and fatty acid synthesis are reduced
(S)-4-((diethylamino)methyl)-N-(2-methoxyphenethyl)-N-(pyrrolidin-3-yl)benzamide
purified S-enantiomer
1-(4-[[2-(2-methoxyphenyl)ethyl](pyrrolidin-3-yl)carbamoyl]benzyl)piperidine-3-carboxamide
-
-
2,2'-[(E)-diazene-1,2-diylbis[benzene-2,1-diyloxy(1-oxoethane-2,1-diyl)imino]]diacetic acid
-
-
3,4-dichloroisocoumarin
-
potent slow binding inhibitor, 100% inhibition by 0.05 mM
4-(2-aminoethyl benzene)sulfonyl fluoride
-
i.e. AEBSF, competitive
4-(2-aminoethyl)-benzenesulfonyl fluoride
-
-
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
4-(2-azabicyclo[2.2.1]hept-2-ylmethyl)-N-[2-(2-methoxyphenyl)ethyl]-N-pyrrolidin-3-ylbenzamide
-
-
4-(6-azabicyclo[3.2.1]oct-6-ylmethyl)-N-[2-(2-methoxyphenyl)ethyl]-N-pyrrolidin-3-ylbenzamide
-
-
4-(benzyloxy)-N-[2-(2-chlorophenyl)ethyl]-N-pyrrolidin-3-ylbenzamide
-
-
4-(benzyloxy)-N-[2-(2-methoxyphenyl)ethyl]-N-pyrrolidin-3-ylbenzamide
-
-
4-(benzyloxy)-N-[2-(3-chlorophenyl)ethyl]-N-pyrrolidin-3-ylbenzamide
-
-
4-([[(1S,2S)-2-hydroxycyclohexyl]amino]methyl)-N-[2-(2-methoxyphenyl)ethyl]-N-pyrrolidin-3-ylbenzamide
-
-
4-[(diethylamino)methyl]-N-[2-(2-ethoxyphenyl)ethyl]-N-pyrrolidin-3-ylbenzamide
-
-
4-[(diethylamino)methyl]-N-[2-(2-methoxyphenyl)ethyl]-N-pyrrolidin-3-ylbenzamide
-
-
4-[(diethylamino)methyl]-N-[2-(2-methoxyphenyl)ethyl]-N-[(3R)-pyrrolidin-3-yl]benzamide
-
-
4-[(diethylamino)methyl]-N-[2-(2-methylphenyl)ethyl]-N-pyrrolidin-3-ylbenzamide
-
-
4-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]methyl]-N-[2-(2-methoxyphenyl)ethyl]-N-pyrrolidin-3-ylbenzamide
-
-
Ac-VFRSLK-4-(2-aminoethyl benzene)sulfonyl fluoride
-
-
benzyl N-[(2-[(E)-[2-(2-oxo-2-[[(1S)-2-oxo-2-phenoxy-1-phenylethyl]amino]ethoxy)phenyl]diazenyl]phenoxy)acetyl]-L-phenylalaninate
-
competitive. E-isomer is thermally stable
benzyl N-[(2-[(E)-[2-(2-[[(2S)-3-methyl-1-oxo-1-phenoxybutan-2-yl]amino]-2-oxoethoxy)phenyl]diazenyl]phenoxy)acetyl]-L-leucinate
-
competitive. E-isomer is thermally stable
brefeldin A
-
abrogates St-2 production
Ca2+
-
inhibition above 3 mM
CuSO4
-
complete inactivation at 1 mM
decanoyl-RRLL-chloromethylketone
the selective and cell-permeable small-peptide inhibitor inhibits the enzyme and leads to suppression of proliferation and metabolic activity of melanoma cells in vitro. The inhibitor induces classical apoptosis of melanoma cells in vitro and affects expression of several SKI-1 target genes including activating transcription factor 6. The compound induces cell death in an ATF6-independent manner
decanoyl-RVKR-chlorometylketone
-
66% inhibition at 0.05 mM
dibenzyl (2R,2'S)-2,2'-[(E)-diazene-1,2-diylbis[benzene-2,1-diyloxy(1-oxoethane-2,1-diyl)imino]]bis(3-methylbutanoate)
-
-
dibenzyl (2R,2'S)-2,2'-[(E)-diazene-1,2-diylbis[benzene-2,1-diyloxy(1-oxoethane-2,1-diyl)imino]]bis(3-phenylpropanoate)
-
-
dithiothreitol
-
partial inhibition at very high concentrations
ethanolamine
-
supresses cleavage by dS1P
gabexate mesylate
-
8% inhibition at 0.05 mM
N-(2-chlorobenzyl)-4-(1-methylethoxy)-N-pyrrolidin-3-ylbenzamide
-
-
N-[(2-[(E)-[2-(2-[[(1S)-1-carboxy-2-methylpropyl]amino]-2-oxoethoxy)phenyl]diazenyl]phenoxy)acetyl]-L-leucine
-
competitive. E-isomer is thermally stable
N-[2-(2,6-dichlorophenyl)ethyl]-4-[(diethylamino)methyl]-N-pyrrolidin-3-ylbenzamide
-
-
N-[2-(2-chlorophenyl)ethyl]-4-(1-methylethoxy)-N-pyrrolidin-3-ylbenzamide
-
-
N-[2-(2-chlorophenyl)ethyl]-4-[(diethylamino)methyl]-N-pyrrolidin-3-ylbenzamide
-
-
N-[2-(2-chlorophenyl)ethyl]-4-[[3-(2-methylphenyl)piperidin-1-yl]methyl]-N-pyrrolidin-3-ylbenzamide
-
-
N-[2-(2-fluorophenyl)ethyl]-4-(1-methylethoxy)-N-pyrrolidin-3-ylbenzamide
-
-
N-[2-(2-methoxyphenyl)ethyl]-4-(piperidin-1-ylmethyl)-N-pyrrolidin-3-ylbenzamide
-
-
N-[2-(2-methoxyphenyl)ethyl]-4-[[3-(2-methylphenyl)piperidin-1-yl]methyl]-N-pyrrolidin-3-ylbenzamide
-
-
N-[2-(3-chlorophenyl)ethyl]-4-(1-methylethoxy)-N-pyrrolidin-3-ylbenzamide
-
-
N-[2-(4-chlorophenyl)ethyl]-4-[(diethylamino)methyl]-N-pyrrolidin-3-ylbenzamide
-
-
palmitate
-
supresses cleavage by dS1P
Pefabloc SC
-
at high concentrations
PF429242
-
inhibotor suppresses the formation of soluble (pro)renin receptor
PMSF
-
12% inhibition at 0.05 mM
prosegment of SKI-1
-
-
-
ZnSO4
-
complete inactivation at 1 mM
1,10-phenanthroline
-
complete inactivation at 5 mM
1,10-phenanthroline
-
partial inhibition at very high concentrations
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
-
inhibits SKI-1 and the autocatalytic generation of St-1
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
-
-
EDTA
-
complete inactivation at 10 mM
EDTA
-
partial inhibition at very high concentrations
EGTA
-
85% inactivation at 10 mM
EGTA
-
partial inhibition at very high concentrations
PF-429242
-
potent S1P inhibitor both in vitro and in cell-based assays, PF-429242 inhibits S1P-mediated processing of arenavirus arenavirus glycoprotein precursor protein
PF-429242
-
active-site-directed inhibitor
additional information
-
decanoyl-RVKR-chloromethylketone does not affect SKI-1-mediated processing; decanoyl-RVKR-chloromethylketone inhibition is selective to furin/PCs and does not affect SKI-1-mediated processing
-
additional information
-
SKI-1/S1P inhibition by overexpression of proSKI variants, results in reduced cholesterol synthesis and mRNA levels of the rate-limiting enzymes HMG-CoA reductase and squalene epoxidase in the cholesterol synthetic pathway. Inhibitory effect is maintained in the presence of homocysteine-induced endoplasmic reticulum stress. SKI-1/S1P inhibition also affects glycolysis and citric acid cycle
-
additional information
-
(Z-LL)2-chloromethylketone and PN1 have no effect on St-2 production. Overexpressed rSt-1 or rSt-2 impede ATF6 processing by SKI-1
-
additional information
-
not inhibited by Mn2+, 7B2 C-terminal peptide, ProSAAS235-244 peptide, ProSAAS235-246 peptide, trypsin inhibitor from bovine pancreas, trypsin inhibitor from soybean, Pefabloc SC (4-(2-aminoethyl) benzene sulphonyl fluoride), benzamidine, p-aminobenzamidine and chymostatin
-
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Alkalosis
Alkalosis monitored by 31P NMR in a human glioma cell line exposed to the anti-tumor drug 1,3-bis(2-chloroethyl)-1-nitrosourea.
Carcinogenesis
Inhibition of the Prohormone Convertase Subtilisin-Kexin Isoenzyme-1 Induces Apoptosis in Human Melanoma Cells.
Carcinoma
SREBP1 site 1 protease inhibitor PF-429242 suppresses renal cell carcinoma cell growth.
Carcinoma, Hepatocellular
Baicalin promoted site-2 protease and not site-1 protease in endoplasmic reticulum stress-induced apoptosis of human hepatocellular carcinoma cells.
Carcinoma, Hepatocellular
Human subtilase SKI-1/S1P is a master regulator of the HCV Lifecycle and a potential host cell target for developing indirect-acting antiviral agents.
Carcinoma, Hepatocellular
Human Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P) regulates cytoplasmic lipid droplet abundance: A potential target for indirect-acting anti-dengue virus agents.
Carcinoma, Renal Cell
SREBP1 site 1 protease inhibitor PF-429242 suppresses renal cell carcinoma cell growth.
Choriocarcinoma
The (pro)renin receptor and soluble (pro)renin receptor in choriocarcinoma.
Congenital Abnormalities
Patient with an autosomal-recessive MBTPS1-linked phenotype and clinical features of Silver-Russell syndrome.
Dengue
Suppressive Effects of the Site 1 Protease (S1P) Inhibitor, PF-429242, on Dengue Virus Propagation.
Fatty Liver
Human subtilase SKI-1/S1P is a master regulator of the HCV Lifecycle and a potential host cell target for developing indirect-acting antiviral agents.
Glioblastoma
Site-1 protease, a novel metabolic target for glioblastoma.
Glioma
Alkalosis monitored by 31P NMR in a human glioma cell line exposed to the anti-tumor drug 1,3-bis(2-chloroethyl)-1-nitrosourea.
Glioma
Altered cytotoxicity of (2-chloroethyl)-3-sarcosinamide-1-nitrosourea in human glioma cell lines SK-MG-1 and SKI-1 correlates with differential transport kinetics.
Glioma
Characterization of the catecholamine extraneuronal uptake2 carrier in human glioma cell lines SK-MG-1 and SKI-1 in relation to (2-chloroethyl)-3-sarcosinamide-1-nitrosourea (SarCNU) selective cytotoxicity.
Glioma
Identification of a 116 kDa protein able to bind 1,3-bis(2-chloroethyl)-1-nitrosourea-damaged DNA as poly(ADP-ribose) polymerase.
Glioma
Mechanisms of resistance to (2-chloroethyl)-3-sarcosinamide-1-nitrosourea (SarCNU) in sensitive and resistant human glioma cells.
Hemorrhagic Fever, American
Site 1 protease is required for proteolytic processing of the glycoproteins of the South American hemorrhagic fever viruses Junin, Machupo, and Guanarito.
Hemorrhagic Fever, Crimean
Crimean-congo hemorrhagic fever virus glycoprotein precursor is cleaved by Furin-like and SKI-1 proteases to generate a novel 38-kilodalton glycoprotein.
Hemorrhagic Fever, Crimean
Crimean-Congo hemorrhagic fever virus glycoprotein processing by the endoprotease SKI-1/S1P is critical for virus infectivity.
Hemorrhagic Fever, Crimean
Crimean-Congo hemorrhagic fever virus glycoprotein proteolytic processing by subtilase SKI-1.
Hepatitis C
SKI-1/S1P inhibition: a promising surrogate to statins to block hepatitis C virus replication.
Infections
Human subtilase SKI-1/S1P is a master regulator of the HCV Lifecycle and a potential host cell target for developing indirect-acting antiviral agents.
Infections
Human Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P) regulates cytoplasmic lipid droplet abundance: A potential target for indirect-acting anti-dengue virus agents.
Infections
Novel circular, cyclic and acyclic ?(CH(2)O) containing peptide inhibitors of SKI-1/S1P: synthesis, kinetic and biochemical evaluations.
Infections
SKI-1/S1P inhibitor PF-429242 impairs the onset of HCV infection.
Infections
Targeting the proteolytic processing of the viral glycoprotein precursor is a promising novel anti-viral strategy against arenaviruses.
Infections
Therapeutic effect of post-exposure treatment with antiserum on severe fever with thrombocytopenia syndrome (SFTS) in a mouse model of SFTS virus infection.
Lymphocytic Choriomeningitis
Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P.
Lymphocytic Choriomeningitis
Molecular characterization of the processing of arenavirus envelope glycoprotein precursors by subtilisin kexin isozyme-1/site-1 protease.
Lymphocytic Choriomeningitis
The role of proteolytic processing and the stable signal peptide in expression of the Old World arenavirus envelope glycoprotein ectodomain.
Lymphocytic Choriomeningitis
Tropism of CPMV to Professional Antigen Presenting Cells Enables a Platform to Eliminate Chronic Infections.
Melanoma
Inhibition of the Prohormone Convertase Subtilisin-Kexin Isoenzyme-1 Induces Apoptosis in Human Melanoma Cells.
Neoplasm Metastasis
Inhibition of the Prohormone Convertase Subtilisin-Kexin Isoenzyme-1 Induces Apoptosis in Human Melanoma Cells.
Neoplasms
Inhibition of the Prohormone Convertase Subtilisin-Kexin Isoenzyme-1 Induces Apoptosis in Human Melanoma Cells.
Neoplasms
SRC promotes survival and invasion of lung cancers with epidermal growth factor receptor abnormalities and is a potential candidate for molecular-targeted therapy.
Non-alcoholic Fatty Liver Disease
Regulation of SREBP-2 intracellular trafficking improves impaired autophagic flux and alleviates endoplasmic reticulum stress in NAFLD.
Prostatic Neoplasms
Nelfinavir inhibits regulated intramembrane proteolysis of sterol regulatory element binding protein-1 and activating transcription factor 6 in castration-resistant prostate cancer.
Severe Fever with Thrombocytopenia Syndrome
The cholesterol, fatty acid and triglyceride synthesis pathways regulated by site 1 protease (S1P) are required for efficient replication of severe fever with thrombocytopenia syndrome virus.
Silver-Russell Syndrome
Patient with an autosomal-recessive MBTPS1-linked phenotype and clinical features of Silver-Russell syndrome.
site-1 protease deficiency
Site-1 protease deficiency causes human skeletal dysplasia due to defective inter-organelle protein trafficking.
Thrombocytopenia
The cholesterol, fatty acid and triglyceride synthesis pathways regulated by site 1 protease (S1P) are required for efficient replication of severe fever with thrombocytopenia syndrome virus.
Vaccinia
Prosomatostatin is proteolytically processed at the amino terminal segment by subtilase SKI-1.
Virus Diseases
C(2)-Symmetric azobenzene-amino acid conjugates and their inhibition of Subtilisin Kexin Isozyme-1.
Virus Diseases
Hypomorphic mutation in the site-1 protease mbtps1 endows resistance to persistent viral infection in a cell-specific manner.
Virus Diseases
Tropism of CPMV to Professional Antigen Presenting Cells Enables a Platform to Eliminate Chronic Infections.
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0.0051
2-aminobenzoic acid-SSGSRRLLSEESY(NO2)-Ala-NH2
-
pH 7.4
0.028
2-aminobenzoyl-Arg-Asn-Thr-Pro-Arg-Arg-Glu-Arg-Arg-Arg-Lys-Lys-Arg-Gly-Leu-(3-nitro)Tyr-Ala
-
pH 7.4, 37°C
0.02
2-aminobenzoyl-Arg-His-Ser-Ser-Arg-Arg-Leu-Leu-Arg-Ala-Ile-(3-nitro)Tyr-Ala
-
pH 7.4, 37°C
0.00096
2-aminobenzoyl-Arg-Ser-Leu-Lys-Tyr-Ala-Glu-Ser-Asp-(3-nitro)Tyr-Ala
-
pH 7.4, 37°C
0.0044
2-aminobenzoyl-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu-Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala
-
pH 7.4, 37°C
0.023
2-aminobenzoyl-Ser-Arg-Arg-Leu-Leu-Arg-Ala-Leu-Glu-(3-nitro)Tyr-Ala
-
pH 7.4, 37°C
0.00428
2-aminobenzoyl-Val-Phe-Arg-Ser-Leu-Lys-Tyr-Ala-Glu-Ser-Asp-(3-nitro)Tyr-Ala
-
pH 7.4, 37°C
0.0031
Abz-DIYISRRLLGTFTY(NO2)A
-
-
0.0504 - 0.067
Ac-AISRRLL-7-amido-4-methylcoumarin
0.0255
Ac-Arg-Arg-Leu-Leu-p-nitroanilide
-
-
0.1335
Ac-Arg-Ser-Leu-Lys-p-nitroanilide
-
-
0.0123 - 0.015
Ac-FISRRLL-7-amido-4-methylcoumarin
0.0226 - 0.0846
Ac-IAVGRTLK-7-amido-4-methylcoumarin
0.0047 - 0.0074
Ac-IYISRRLL-7-amido-4-methylcoumarin
0.0025 - 0.0156
Ac-QKSIAVGRTLK-7-amido-4-methylcoumarin
0.0274 - 0.0564
Ac-RKLL-7-amido-4-methylcoumarin
0.0153 - 0.0228
Ac-RRLL-7-amido-4-methylcoumarin
0.0971 - 0.2263
Ac-RRLQ-7-amido-4-methylcoumarin
0.0967 - 0.2167
Ac-RTLK-7-amido-4-methylcoumarin
0.0443 - 0.0784
Ac-SFITRRLQ-7-amido-4-methylcoumarin
0.1
Ac-VFRSLK-4-methyl-coumaryl-7-amide
-
pH 8, 37°C
0.0028 - 0.0057
Ac-YISRRLL-7-amido-4-methylcoumarin
0.0212 - 0.0281
Ac-YSSVSRKLL-7-amido-4-methylcoumarin
0.0504
Ac-AISRRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.067
Ac-AISRRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0123
Ac-FISRRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.015
Ac-FISRRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0226
Ac-IAVGRTLK-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.0846
Ac-IAVGRTLK-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0047
Ac-IYISRRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.0074
Ac-IYISRRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0025
Ac-QKSIAVGRTLK-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.0156
Ac-QKSIAVGRTLK-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0274
Ac-RKLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.0564
Ac-RKLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0153
Ac-RRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.0228
Ac-RRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0971
Ac-RRLQ-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.2263
Ac-RRLQ-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0967
Ac-RTLK-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.2167
Ac-RTLK-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0443
Ac-SFITRRLQ-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.0784
Ac-SFITRRLQ-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0028
Ac-YISRRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.005
Ac-YISRRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.0056
Ac-YISRRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0057
Ac-YISRRLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
0.0212
Ac-YSSVSRKLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.0281
Ac-YSSVSRKLL-7-amido-4-methylcoumarin
pH and temperature not specified in the publication, recombinant mutant Y285A
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E75A/E76A
-
is catalytically inactive and traps RsiW in a complex in which the anti-sigma factor is protected from undergoing proteolysis
E95K
-
missense mutant with a a dominant (gain-of-function) mutation. Exhibits heightened resistance to the SdpC toxin in cells lacking the SdpI immunity protein. Is locked in a state that causes constitutive activation of sigmaW
H175A
-
is catalytically inactive and traps RsiW in a complex in which the anti-sigma factor is protected from undergoing proteolysis
E75A/E76A
-
is catalytically inactive and traps RsiW in a complex in which the anti-sigma factor is protected from undergoing proteolysis
-
E95K
-
missense mutant with a a dominant (gain-of-function) mutation. Exhibits heightened resistance to the SdpC toxin in cells lacking the SdpI immunity protein. Is locked in a state that causes constitutive activation of sigmaW
-
H175A
-
is catalytically inactive and traps RsiW in a complex in which the anti-sigma factor is protected from undergoing proteolysis
-
S414A
-
inactive mutant, no autocatalytic processing to generate S1P-C
I985A
-
has no effect on generation of St-2
I989L
-
results in more than 90% reduction in the generation of St-2
K948A
-
shedding site mutant
L952A
-
shedding site mutant
M990A
-
fails to generate St-2
M990I
-
fails to generate St-2
M990L
-
fails to generate St-2
N995A
-
has no effect on generation of St-2
P1003S
-
natural mutation identified in a female patient. The mutant protein is able to complement lipid and cholesterol biosynthetic capacities in cells that lack S1P and is abundant in both the ER and the Golgi
R130A/K131A
-
proSKI variant that exhibits no basic residue at the P4 position, has no effect on HMG-CoA reductase mRNA levels
R130E/R134E
site-directed mutagenesis, the double mutations at the B'/B site prevents autoprocessing
R160E
site-directed mutagenesis
R163E/R164E
site-directed mutagenesis
Y285A
site-directed mutagenesis, molecular modeling
Y994A
-
has no effect on generation of St-2
Y994A/N995A
-
has no effect on generation of St-2
H249A
site-directed mutagenesis, catalytically inactive mutant
H249A
-
active site mutant, autocatalytic generation of St-1 is abrogated, St-2 fragment is generated at a level of ca. 15%
H249A
site-directed mutagenesis, catalytically inactive mutant showing no autoprocessing
R134E
-
proSKI variant that lacks autocatalytic primary cleavage site RSLK, most efficient inhibitor of HMG-CoA reductase expression
R134E
site-directed mutagenesis, the single prodomain mutant, at the B autoprocessing site, allows maturation comparably with the wild-type enzyme
additional information
-
in a ypdC null mutant, induction of sigmaW-controlled genes is abolished and site-1 proteolysis of RsiW is completely blocked. Defect of sigmaW induction is complemented by ectopically integrated ypdC under xylose control in a heterologous Escherichia coli system
additional information
-
prsW insertion/deletion mutant prsW::erm exacerbates the growth defect of an sdpI mutant
additional information
-
prsW insertion/deletion mutant prsW::erm exacerbates the growth defect of an sdpI mutant
-
additional information
-
S1P-deficient cells, ATF6 processing partially blocked
additional information
stable cell lines inducibly expressing S1P-adapted alpha1-antitrypsin variants inhibit the proteolytic maturation of glycoprotein GP-C. Introduction of the S1P recognition motifs RRIL and RRLL into the reactive center loop of alpha1-antitrypsin results in abrogation of glycoprotein GP-C processing by endogenous S1P to a similar level observed in S1P-deficient cells. Moreover, S1P-specific alpha1-antitrypsins significantly inhibit replication and spread of a replication-competent recombinant vesicular stomatitis virus expressing the Lassa virus glycoprotein GP as well as authentic Lassa virus
additional information
-
Crimean Congo hemorrhagic fever virus-infected cells deficient in SKI-1/S1P produce no infectious virus, although precursor Gn and precursor Gc accumulate normally in the Golgi apparatus, the site of virus assembly. Complementation of SKI-1/S1P-deficient cells with a SKI-1/S1P expression vector restores release of infectious virus
additional information
-
in the triple shedding site mutant KLL/A autocatalytic generation of St-1 is abrogated, St-2 fragment is generated at a level of ca. 15%
additional information
-
using SRD12B mutant cells lacking the S1P gene, it is shown that lack of glycoprotein processing of Junin virus dramatically reduces production of infectious virus and prevents cell-to-cell propagation. Infection of S1P-deficient cells results in viral persistence over several weeks without the emergence of escape variants able to use other cellular proteases for GP processing
additional information
the soluble form of the enzyme is truncated before the transmembrane domain and comprised the ectodomain, followed by a C-terminal V5 tag, i.e. DELTA AC SKI-1/S1P BTMD. Extended mutagenesis performed on a region proximal to the C site results in normal SKI-1/S1P maturation at the B'/B intermediate state, suggesting that processing at B'/B either precedes or occurs independently of C site cleavage. The combined mutation at the C and C' sites results in marked reduction of the mature C form indicating that, similar to B'/B, mutation of both C and C' processing sites is required to prevent maturation
additional information
-
complete silencing of SKI-1/SP1 results in an embryonic lethal phenotype, elimination of about 70-90% of SKI-1/SP1 protein expression in liver results in a drop of ca. 50% in the level of circulating cholesterol and triglycerides, cholesterol and fatty acid biosynthesis in hepatocytes declines by 75%, low density lipoprotein receptor mRNA declines by 50%
additional information
-
cartilage-specific S1P knockout mice, exhibit chondrodysplasia and a complete lack of endochondral ossification even though Runx2 expression, Indian hedgehog signaling, and osteoblastogenesis is intact. Substantial increase in chondrocyte apoptosis. Collagen network is disorganized and collagen becomes entrapped in chondrocytes. Endoplasmic reticulum in chondrocytes is engorged and fragmented in a manner characteristic of severe endoplasmic reticulum stress
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Seidah, N.G.; Benjannet, S.; Hamelin, J.; Mamarbachi, A.M.; Basak, A.; Marcinkiewicz, J.; Mbikay, M.; Chretien, M.; Marcinkiewicz, M.
The subtilisin/kexin family of precursor convertases. Emphasis on PC1, PC2/7B2, POMC and the novel enzyme SKI-1
Ann. N. Y. Acad. Sci.
885
57-74
1999
Rattus norvegicus
brenda
DeBose-Boyd, R.A.; Brown, M.S.; Li, W.P.; Nohturfft, A.; Goldstein, J.L.; Espenshade, P.J.
Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi
Cell
99
703-712
1999
Cricetulus griseus
brenda
Basak, A.; Chretien, M.; Seidah, N.G.
A rapid fluorometric assay for the proteolytic activity of SKI-1/S1P based on the surface glycoprotein of the hemorrhagic fever Lassa virus
FEBS Lett.
514
333-339
2002
Homo sapiens
brenda
Espenshade, P.J.; Cheng, D.; Goldstein, J.L.; Brown, M.S.
Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins
J. Biol. Chem.
274
22795-22804
1999
Cricetulus griseus
brenda
Cheng, D.; Espenshade, P.J.; Slaughter, C.A.; Jaen, J.C.; Brown, M.S.; Goldstein, J.L.
Secreted site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins
J. Biol. Chem.
274
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Homo sapiens, Rattus norvegicus (Q9WTZ3)
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Homo sapiens
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Homo sapiens
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Proprotein convertase SKI-1/SIP
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Homo sapiens
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CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P
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Homo sapiens
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Ye, J.; Rawson, R.B.; Komuro, R.; Chen, X.; Dave, U.P.; Prywes, R.; Brown, M.S.; Goldstein, J.L.
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Cricetulus griseus
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Lenz, O.; Ter Meulen, J.; Klenk, H.D.; Seidah, N.G.; Garten, W.
The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P
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Homo sapiens
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Hay, B.A.; Abrams, B.; Zumbrunn, A.Y.; Valentine, J.J.; Warren, L.C.; Petras, S.F.; Shelly, L.D.; Xia, A.; Varghese, A.H.; Hawkins, J.L.; Van Camp, J.A.; Robbins, M.D.; Landschulz, K.; Harwood, H.J.
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Homo sapiens
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Gene Set Enrichment Analysis Reveals Several Globally Affected Pathways due to SKI-1/S1P Inhibition in HepG2 Cells
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Homo sapiens
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Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis
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Bacillus subtilis, Bacillus subtilis PY79
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Site-1 protease is essential for endochondral bone formation in mice
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Mus musculus
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Crimean-Congo hemorrhagic fever virus glycoprotein processing by the endoprotease SKI-1/S1P is critical for virus infectivity
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Homo sapiens
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YpdC determines site-1 degradation in regulated intramembrane proteolysis of the RsiW anti-sigma factor of Bacillus subtilis
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Homo sapiens
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Buraczewska, I.; Berne, B.; Lindberg, M.; Loden, M.; Toermae, H.
Long-term treatment with moisturizers affects the mRNA levels of genes involved in keratinocyte differentiation and desquamation
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Rattus norvegicus
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Pharmacologic inhibition of site 1 protease activity inhibits sterol regulatory element-binding protein processing and reduces lipogenic enzyme gene expression and lipid synthesis in cultured cells and experimental animals
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Homo sapiens (Q14703), Homo sapiens
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Site 1 protease is required for proteolytic processing of the glycoproteins of the South American hemorrhagic fever viruses Junin, Machupo, and Guanarito
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Homo sapiens
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Alternative processing of sterol regulatory element binding protein during larval development in Drosophila melanogaster
Genetics
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Drosophila melanogaster
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Yellaturu, C.; Deng, X.; Park, E.; Raghow, R.; Elam, M.
Insulin enhances the biogenesis of nuclear sterol regulatory element-binding protein (SREBP)-1c by posttranscriptionaldown-regulation of insig-2A and its dissociation from SREBP cleavage-activating protein (SCAP)SREBP-1c complex
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Drosophila melanogaster
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Inhibition of Lassa virus glycoprotein cleavage and multicycle replication by site 1 protease-adapted alpha(1)-antitrypsin variants
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Cricetulus griseus (Q9Z2A8)
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C2-Symmetric azobenzene-amino acid conjugates and their inhibition of Subtilisin Kexin Isozyme-1
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Homo sapiens
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Zandberg, W.F.; Benjannet, S.; Hamelin, J.; Pinto, B.M.; Seidah, N.G.
N-glycosylation controls trafficking, zymogen activation and substrate processing of proprotein convertases PC1/3 and subtilisin kexin isozyme-1
Glycobiology
21
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Homo sapiens
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Patra, D.; DeLassus, E.; Hayashi, S.; Sandell, L.J.
Site-1 protease is essential to growth plate maintenance and is a critical regulator of chondrocyte hypertrophic differentiation in postnatal mice
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286
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Mus musculus
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Urata, S.; Yun, N.; Pasquato, A.; Paessler, S.; Kunz, S.; de la Torre, J.C.
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Homo sapiens
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Zymogen activation and subcellular activity of subtilisin kexin isozyme 1/site 1 protease
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Homo sapiens (Q14703)
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Weiss, N.; Stegemann, A.; Elsayed, M.A.; Schallreuter, K.U.; Luger, T.A.; Loser, K.; Metze, D.; Weishaupt, C.; Boehm, M.
Inhibition of the prohormone convertase subtilisin-kexin isoenzyme-1 induces apoptosis in human melanoma cells
J. Invest. Dermatol.
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2014
Homo sapiens (Q14703), Homo sapiens
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Burri, D.; Pasqual, G.; Rochat, C.; Seidah, N.; Pasquato, A.; Kunz, S.
Molecular characterization of the processing of arenavirus envelope glycoprotein precursors by subtilisin kexin isozyme-1/site-1 protease
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Homo sapiens (Q14703)
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Burri, D.; da Palma, J.; Seidah, N.; Zanotti, G.; Cendron, L.; Pasquato, A.; Kunz, S.
Differential recognition of old world and new world arenavirus envelope glycoproteins by subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P)
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87
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2013
Homo sapiens (Q14703), Homo sapiens
brenda
Sun, L.; Zhang, S.S.; Lu, S.J.; Liu, J.X.
Site-1 protease cleavage site is important for the ER stress-induced activation of membrane-associated transcription factor bZIP28 in Arabidopsis
Sci. China Life Sci.
58
270-275
2015
Arabidopsis thaliana
brenda
Patra, D.; DeLassus, E.; Mueller, J.; Abou-Ezzi, G.; Sandell, L.J.
Site-1 protease regulates skeletal stem cell population and osteogenic differentiation in mice
Biol. Open
7
bio032094
2018
Mus musculus
brenda
Nakagawa, T.; Suzuki-Nakagawa, C.; Watanabe, A.; Asami, E.; Matsumoto, M.; Nakano, M.; Ebihara, A.; Uddin, M.N.; Suzuki, F.
Site-1 protease is required for the generation of soluble (pro)renin receptor
J. Biochem.
161
369-379
2017
Cricetulus griseus
brenda
Kluender, S.; Heeren, J.; Markmann, S.; Santer, R.; Braulke, T.; Pohl, S.
Site-1 protease-activated formation of lysosomal targeting motifs is independent of the lipogenic transcription control
J. Lipid Res.
56
1625-1632
2015
Homo sapiens, Mus musculus
brenda
Schweitzer, G.; Gan, C.; Bucelli, R.; Wegner, D.; Schmidt, R.; Shinawi, M.; Finck, B.; Brookheart, R.
A mutation in Site-1 Protease is associated with a complex phenotype that includes episodic hyperCKemia and focal myoedema
Mol. Genet. Genomic Med.
2019
e733
2019
Homo sapiens
brenda
Hyrina, A.; Meng, F.; McArthur, S.J.; Eivemark, S.; Nabi, I.R.; Jean, F.
Human subtilisin kexin isozyme-1 (SKI-1)/Site-1 Protease (S1P) regulates cytoplasmic lipid droplet abundance A potential target for indirect-acting anti-dengue virus agents
PLoS ONE
12
e0174483
2017
Homo sapiens
brenda
Al-Maskari, M.; Care, M.A.; Robinson, E.; Cocco, M.; Tooze, R.M.; Doody, G.M.
Site-1 protease function is essential for the generation of antibody secreting cells and reprogramming for secretory activity
Sci. Rep.
8
14338
2018
Homo sapiens
brenda