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PRSS21 | Testisin; Could regulate proteolytic events associated with testicular germ cell maturation; Serine proteases (314 aa) | |||
GRN | Granulins; Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling (593 aa) | |||
PRSS22 | Brain-specific serine protease 4; Preferentially cleaves the synthetic substrate H-D-Leu- Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA; Serine proteases (317 aa) | |||
CTSZ | Cathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity; Cathepsins (303 aa) | |||
CTSH | Pro-cathepsin H; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family (335 aa) | |||
FBL | rRNA 2’-O-methyltransferase fibrillarin; S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2’-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of ’Gln-105’ of histone H2A (H2AQ104me), a modification [...] (321 aa) | |||
CTSC | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII (463 aa) | |||
SERPINF1 | Pigment epithelium-derived factor; Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity; Serpin peptidase inhibitors (418 aa) | |||
CTSK | Cathepsin K; Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation; Cathepsins (329 aa) | |||
PAM | Peptidyl-glycine alpha-amidating monooxygenase; Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity (974 aa) | |||
TMPRSS11E | Transmembrane protease serine 11E; Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position (423 aa) | |||
CTSF | Cathepsin F; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins (484 aa) | |||
CTSW | Cathepsin W; May have a specific function in the mechanism or regulation of T-cell cytolytic activity; Cathepsins (376 aa) | |||
TENC1 | Tensin-2; Regulates cell motility and proliferation. May have phosphatase activity. Reduces AKT1 phosphorylation. Lowers AKT1 kinase activity and interferes with AKT1 signaling (1419 aa) | |||
SERPINA6 | Corticosteroid-binding globulin; Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species; Serpin peptidase inhibitors (405 aa) | |||
CTSL | Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins (333 aa) | |||
CTSB | Cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins (339 aa) | |||
FN1 | Fibronectin type III domain containing; Endogenous ligands (2477 aa) | |||
LEPREL4 | Endoplasmic reticulum protein SC65; Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils. Required for normal bone density and normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly; Belongs to the leprecan family (437 aa) | |||
WDR37 | WD repeat-containing protein 37; WD repeat domain containing (494 aa) | |||
COL4A2 | Collagen alpha-2(IV) chain; Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a ’chicken-wire’ meshwork together with laminins, proteoglycans and entactin/nidogen (1712 aa) | |||
CTSS | Cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N; Cathepsins (331 aa) | |||
DHFRL1 | Dihydrofolate reductase 2, mitochondrial; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Binds its own mRNA and that of DHFR (187 aa) | |||
COCH | Cochlin; Plays a role in the control of cell shape and motility in the trabecular meshwork; Deafness associated genes (550 aa) | |||
CTSO | Cathepsin O; Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover; Belongs to the peptidase C1 family (321 aa) | |||
CTSV | Cathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family (334 aa) |