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APPBP2 | Amyloid protein-binding protein 2; May play a role in intracellular protein transport. May be involved in the translocation of APP along microtubules toward the cell surface (585 aa) | |||
TIMP1 | Metalloproteinase inhibitor 1; Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it [...] (207 aa) | |||
TIMP2 | Metalloproteinase 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; Belongs to the protease inhibitor I35 (TIMP) family (220 aa) | |||
TIMP3 | Metalloproteinase inhibitor 3; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15 (211 aa) | |||
TIMP4 | Metalloproteinase inhibitor 4; 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 and MMP- 9; Tissue inhibitor of metallopeptidases (224 aa) | |||
TRIM68 | E3 ubiquitin-protein ligase TRIM68; Functions as a ubiquitin E3 ligase. Acts as a coactivator of androgen receptor (AR) depending on its ubiquitin ligase activity; Ring finger proteins (485 aa) | |||
PTGDR | Prostaglandin D2 receptor; Receptor for prostaglandin D2 (PGD2). The activity of this receptor is mainly mediated by G(s) proteins that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP. A mobilization of calcium is also observed, but without formation of inositol 1,4,5-trisphosphate (By similarity) (359 aa) | |||
SND1 | Staphylococcal nuclease domain-containing protein 1; Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2); Tudor domain containing (910 aa) | |||
YARS | Tyrosine--tRNA ligase, cytoplasmic; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family (528 aa) | |||
VPREB1 | Immunoglobulin iota chain; Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation; CD molecules (145 aa) | |||
PPP1R9A | Neurabin-1; Binds to actin filaments (F-actin) and shows cross- linking activity. Binds along the sides of the F-actin. May be involved in neurite formation. Inhibits protein phosphatase 1- alpha activity (By similarity); PDZ domain containing (1374 aa) | |||
IGLL5 | Immunoglobulin lambda like polypeptide 5; C1-set domain containing (214 aa) | |||
FBN3 | Fibrillin-3; Fibrillin-3- Fibrillins are structural components of 10- 12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-containing microfibrils provide long-term force bearing structural support; Belongs to the fibrillin family (2809 aa) | |||
MMP28 | Matrix metalloproteinase-28; Can degrade casein. Could play a role in tissues homeostasis and repair; Belongs to the peptidase M10A family (520 aa) |