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NME1 | NME/NM23 nucleoside diphosphate kinase 1; Major role in the synthesis of nucleoside triphosphates other than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3’-5’ exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination (177 aa) | |||
NME8 | NME/NM23 family member 8; Probably required during the final stages of sperm tail maturation in the testis and/or epididymis, where extensive disulfide bonding of fibrous sheath (FS) proteins occurs. May be involved in the reduction of disulfide bonds within the sperm FS components. In vitro, it has neither NDP kinase nor reducing activity on disulfide bonds (588 aa) | |||
PDIA2 | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins (525 aa) | |||
SPR | sepiapterin reductase (7,8-dihydrobiopterin-NADP+ oxidoreductase); Catalyzes the final one or two reductions in tetra- hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin (261 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) | |||
DSTN | destrin (actin depolymerizing factor); Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (G-actin). Acts in a pH- independent manner (165 aa) | |||
TRAP1 | TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity (704 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) | |||
TXNDC9 | thioredoxin domain containing 9; Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin (226 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) | |||
ERP27 | endoplasmic reticulum protein 27 (273 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) | |||
TMX3 | thioredoxin-related transmembrane protein 3; Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase (454 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) | |||
TXNDC2 | thioredoxin domain containing 2 (spermatozoa); Probably plays a regulatory role in sperm development. May participate in regulation of fibrous sheath (FS) assembly by supporting the formation of disulfide bonds during sperm tail morphogenesis. May also be required to rectify incorrect disulfide pairing and generate suitable pairs between the FS constituents. Can reduce disulfide bonds in vitro in the presence of NADP and thioredoxin reductase (553 aa) | |||
PDIA5 | protein disulfide isomerase family A, member 5 (519 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) | |||
PSRC1 | proline/serine-rich coiled-coil 1; Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate, and for normal rate of chromosomal segregation during anaphase. Plays a role in the regulation of mitotic spindle dynamics. Increases the rate of turnover of microtubules on metaphase spindles, and contributes to the generation of normal tension across sister kinetochores. Recruits KIF2A to the mitotic spindle and spindle poles. May participate in p53/TP53-regulated growth suppression (333 aa) | |||
TXNDC8 | thioredoxin domain containing 8 (spermatozoa); May be required for post-translational modifications of proteins required for acrosomal biogenesis. May act by reducing disulfide bonds within the sperm (115 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) | |||
SUMO1 | SMT3 suppressor of mif two 3 homolog 1 (S. cerevisiae); Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. [...] (101 aa) | |||
NIT2 | nitrilase family, member 2; Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting alpha- ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively. Overexpression decreases the colony-forming capacity of cultured cells by arresting cells in the G2 phase of the cell cycle (276 aa) |