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MMP11 | matrix metallopeptidase 11 (stromelysin 3); May play an important role in the progression of epithelial malignancies (488 aa) | |||
MMP2 | matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative s [...] (660 aa) | |||
MMP15 | matrix metallopeptidase 15 (membrane-inserted); Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A (669 aa) | |||
CCL2 | chemokine (C-C motif) ligand 2; Chemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis (99 aa) | |||
TFPI | tissue factor pathway inhibitor (lipoprotein-associated coagulation inhibitor); Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma (304 aa) | |||
MMP8 | matrix metallopeptidase 8 (neutrophil collagenase); Can degrade fibrillar type I, II, and III collagens (467 aa) | |||
MMP7 | matrix metallopeptidase 7 (matrilysin, uterine); Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase (267 aa) | |||
TIMP2 | TIMP metallopeptidase inhibitor 2; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19 (220 aa) | |||
ELANE | elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (267 aa) | |||
MMP10 | matrix metallopeptidase 10 (stromelysin 2); Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase (476 aa) | |||
COL14A1 | collagen, type XIV, alpha 1 (1796 aa) | |||
UMOD | uromodulin; Uromodulin- Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle’s loop (TALH), where it promotes formation of complex filamentous gel-like structure providing the water barrier permeability. May serve as a receptor for binding and endocytosis for cytokines (IL-1, IL-2) and TNF. Facilitates neutrophil migration across renal epithelial (640 aa) | |||
MMP14 | matrix metallopeptidase 14 (membrane-inserted); Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 (582 aa) | |||
PRSS1 | protease, serine, 1 (trypsin 1) (247 aa) | |||
MMP19 | matrix metallopeptidase 19; Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin (508 aa) | |||
KLK2 | kallikrein-related peptidase 2; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin (261 aa) | |||
MMP1 | matrix metallopeptidase 1 (interstitial collagenase); Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat’s mediated neurotoxicity (469 aa) | |||
COL12A1 | collagen, type XII, alpha 1; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix (By similarity) (3063 aa) | |||
BCAN | brevican; May play a role in the terminally differentiating and the adult nervous system during postnatal development. Could stabilize interactions between hyaluronan (HA) and brain proteoglycans (911 aa) | |||
COL9A3 | collagen, type IX, alpha 3; Structural component of hyaline cartilage and vitreous of the eye (684 aa) | |||
UBC | ubiquitin C (685 aa) | |||
COL9A1 | collagen, type IX, alpha 1 (921 aa) | |||
MMP9 | matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (707 aa) | |||
COL9A2 | collagen, type IX, alpha 2; Structural component of hyaline cartilage and vitreous of the eye (689 aa) | |||
COL16A1 | collagen, type XVI, alpha 1; Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology (1604 aa) | |||
ACAN | aggrecan; This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region (2530 aa) |