EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.112 | glycoprotein |
- |
653621, 732162 |
| 3.4.21.112 | glycoprotein |
putative N-glycosylation at Asn148 |
652020 |
| 3.4.21.112 | glycoprotein |
six potential N-glycosylation sites |
651938 |
| 3.4.21.112 | proteolytic modification |
enzyme undergoes autocatalytic processing, generating an active form S1P-B, which is further cleaved after residue 186 to generate S1P-C |
651939 |
| 3.4.21.112 | proteolytic modification |
proSKI-1 is converted to active SKI-1 |
652020 |
| 3.4.21.112 | proteolytic modification |
proSKI-1 is processed into two membrane-bound forms of SKI-1: 120000 Da and 106000 Da |
653621 |
| 3.4.21.112 | proteolytic modification |
protein is inactive and undergoes autocatalytic processing, generating an active form S1P-B, which is further cleaved at an internal RRLL sequence to generate an active S1P-C |
651938 |
| 3.4.21.112 | proteolytic modification |
SP1-A is inactive and undergoes autocatalytic processing, generating an active form S1P-B, which is further cleaved after residue 186 to generate S1P-C |
650785 |
| 3.4.21.112 | proteolytic modification |
the enzyme performs autocatalytic cleavage and activation depending on the recognition site RRLL, present in the enzyme prodomain |
732412 |
| 3.4.21.112 | proteolytic modification |
zymogen activation of the enzyme involves sequential autocatalytic processing of its N-terminal prodomain at sites B'/B followed by the C'/C sites. Autocatalytic maturation by sequential cleavages of the N-terminal pro-domain first at sites B'/B (RKVF2RSLK1372), followed by site C (RRLL1862), with crucial roles for R and V/L residues at P4 and P2 (fourth and second residue upstream the scissile bond, respectively). Enzyme autoprocessing results in intermediates whose catalytic domain remains associated with prodomain fragments of different lengths. 9 Amino acid residues at the cleavage site (P1-P8) and P1' are necessary and sufficient to define the subcellular location of processing and to determine to what extent processing of a substrate depends on SKI-1/S1P maturation. Mature enzyme retains prodomain fragments of different lengths, overview. The post-translational modifications are crucial for the subcellular localization of autoprocessing intermediates of the enzyme |
732162 |
