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Proteinase 3, also known as PRTN3, is an enzyme that in humans is encoded by the PRTN3 gene.
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Cathepsin G is a protein that in humans is encoded by the CTSG gene. It is one of the three serine proteases of the chymotrypsin family that are stored in the azurophil granules, and also a member of the peptidase S1 protein family. Cathepsin G plays an important role in eliminating intracellular pathogens and breaking down tissues at inflammatory sites, as well as in anti-inflammatory response.
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LIFR also known as CD118, is a subunit of a receptor for leukemia inhibitory factor.
Protein-glutamine gamma-glutamyltransferase K is a transglutaminase enzyme that in humans is encoded by the TGM1 gene.
Nuclear bodies are membraneless structures found in the cell nuclei of eukaryotic cells. Nuclear bodies include Cajal bodies, the nucleolus, and promyelocytic leukemia protein (PML) nuclear bodies. Nuclear bodies also include ND10s. ND stands for nuclear domain, and 10 refers to the number of dots seen.
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Serine/threonine-protein kinase PAK 2 is an enzyme that in humans is encoded by the PAK2 gene.
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Azurocidin also known as cationic antimicrobial protein CAP37 or heparin-binding protein (HBP) is a protein that in humans is encoded by the AZU1 gene.
G/T mismatch-specific thymine DNA glycosylase is an enzyme that in humans is encoded by the TDG gene. Several bacterial proteins have strong sequence homology with this protein.
Serglycin, also known as hematopoietic proteoglycan core protein or secretory granule proteoglycan core protein, is a protein that in humans is encoded by the SRGN gene. It is primarily expressed in hematopoietic cells and endothelial cells, and is the only known intracellular proteoglycan.
The sedolisin family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.
References
- ↑ Martin KR, Witko-Sarsat V (September 2017). "Proteinase 3: the odd one out that became an autoantigen". Journal of Leukocyte Biology. 102 (3): 689–698. doi: 10.1189/jlb.3MR0217-069R . PMID 28546501.
- ↑ Brubaker MJ, Groutas WC, Hoidal JR, Rao NV (November 1992). "Human neutrophil proteinase 3: mapping of the substrate binding site using peptidyl thiobenzyl esters". Biochemical and Biophysical Research Communications. 188 (3): 1318–24. doi:10.1016/0006-291x(92)91375-z. PMID 1445363.
- ↑ Kam CM, Kerrigan JE, Dolman KM, Goldschmeding R, Von dem Borne AE, Powers JC (February 1992). "Substrate and inhibitor studies on proteinase 3". FEBS Letters. 297 (1–2): 119–23. doi: 10.1016/0014-5793(92)80340-m . PMID 1551417.
- ↑ Bories D, Raynal MC, Solomon DH, Darzynkiewicz Z, Cayre YE (December 1989). "Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells". Cell. 59 (6): 959–68. doi: 10.1016/0092-8674(89)90752-6 . PMID 2598267.
