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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) | |||
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) | |||
YY1 | Transcriptional repressor protein YY1; Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5’-CCGCCATNTT-3’; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activa [...] (414 aa) | |||
LMF1 | Lipase maturation factor 1; Involved in the maturation of specific proteins in the endoplasmic reticulum. Required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway. Each LMF1 molecule chaperones 50 or more molecules of LPL (567 aa) | |||
CBL | E3 ubiquitin-protein ligase CBL; Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family [...] (906 aa) | |||
CBLB | E3 ubiquitin-protein ligase CBL-B; E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B- cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impair [...] (982 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) | |||
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) | |||
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) | |||
WDR37 | WD repeat-containing protein 37; WD repeat domain containing (494 aa) | |||
CBWD3 | COBW domain containing 3 (395 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) | |||
DNLZ | DNL-type zinc finger protein; May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation; Zinc fingers (178 aa) | |||
ITPA | Inosine triphosphate pyrophosphatase; Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2’-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5’-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (194 aa) | |||
SIL1 | Nucleotide exchange factor SIL1; Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5; Belongs to the SIL1 family (461 aa) | |||
CPE | Carboxypeptidase E; Removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing. Processes proinsulin; Belongs to the peptidase M14 family (476 aa) | |||
YY2 | Transcription factor YY2; Functions as a multifunctional transcription factor that may exhibit positive and negative control on a large number of genes. May antagonize YY1 and function in development and differentiation (372 aa) | |||
CTSO | Cathepsin O; Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover; Belongs to the peptidase C1 family (321 aa) | |||
SERPINB11 | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change; Serpin peptidase inhibitors (392 aa) | |||
CTSV | Cathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family (334 aa) |