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NANS | N-acetylneuraminic acid synthase; Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3- deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N- acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively (359 aa) | |||
LAP3 | leucine aminopeptidase 3; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (519 aa) | |||
CAT | catalase; Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells (527 aa) | |||
ERP44 | endoplasmic reticulum protein 44; Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum (406 aa) | |||
PRDX1 | peroxiredoxin 1; Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity) (199 aa) | |||
DNAJC10 | DnaJ (Hsp40) homolog, subfamily C, member 10 (793 aa) | |||
PRDX5 | peroxiredoxin 5; Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling (214 aa) | |||
SOD1 | superoxide dismutase 1, soluble; Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity) (154 aa) | |||
PDIA6 | protein disulfide isomerase family A, member 6; May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (440 aa) | |||
BAX | BCL2-associated X protein (218 aa) | |||
PRDX3 | peroxiredoxin 3; Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical- generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol (256 aa) | |||
GLOD4 | glyoxalase domain containing 4 (298 aa) | |||
PRDX2 | peroxiredoxin 2; Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (198 aa) | |||
PKM | pyruvate kinase, muscle (531 aa) | |||
PARK7 | parkinson protein 7; Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide [...] (189 aa) | |||
PRDX6 | peroxiredoxin 6; Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury (224 aa) | |||
GPX4 | glutathione peroxidase 4; Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage (By similarity) (197 aa) | |||
UBE2H | ubiquitin-conjugating enzyme E2H; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-linked polyubiquitination. Capable, in vitro, to ubiquitinate histone H2A (183 aa) | |||
UBA3 | ubiquitin-like modifier activating enzyme 3; Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression (463 aa) | |||
TIPRL | TIP41, TOR signaling pathway regulator-like (S. cerevisiae); May be a allosteric regulator of serine/threonine- protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C)-TIPRL complex does not show phosphatase activity. May play a role in the regulation of ATM/ATR signaling pathway controlling DNA replication and repair (272 aa) | |||
SEC23IP | SEC23 interacting protein; Plays a role in the organization of endoplasmic reticulum exit sites. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P) and phosphatidylinositol 5-phosphate (PI(5)P) (1000 aa) | |||
PGAM1 | phosphoglycerate mutase 1 (brain); Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity (254 aa) | |||
TXN | thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates A [...] (105 aa) | |||
SRXN1 | sulfiredoxin 1; Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase (137 aa) | |||
FSCN1 | fascin homolog 1, actin-bundling protein (Strongylocentrotus purpuratus); Organizes filamentous actin into bundles with a minimum of 4.1-1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (493 aa) | |||
URM1 | ubiquitin related modifier 1; Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. May also act as an ubiquitin-like protein that is covalently conjugated to other proteins; the relevance of such function is however unclear in vivo (146 aa) |