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PYCRL | pyrroline-5-carboxylate reductase-like (286 aa) | |||
MTRR | 5-methyltetrahydrofolate-homocysteine methyltransferase reductase; Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state (725 aa) | |||
GFOD2 | glucose-fructose oxidoreductase domain containing 2; Promotes matrix assembly (By similarity) (385 aa) | |||
ALDH4A1 | aldehyde dehydrogenase 4 family, member A1 (563 aa) | |||
NOS3 | nitric oxide synthase 3 (endothelial cell); Produces nitric oxide (NO) (By similarity) (1203 aa) | |||
PDIA3 | protein disulfide isomerase family A, member 3 (505 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) | |||
UQCRFS1 | ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (274 aa) | |||
BCAT2 | branched chain amino-acid transaminase 2, mitochondrial; Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids (392 aa) | |||
NOS2 | nitric oxide synthase 2, inducible (1153 aa) | |||
P4HB | prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] (508 aa) | |||
PYCR1 | pyrroline-5-carboxylate reductase 1; Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress (319 aa) | |||
NOS1 | nitric oxide synthase 1 (neuronal); Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR (1468 aa) | |||
PYCR2 | pyrroline-5-carboxylate reductase family, member 2; Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+). Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH (320 aa) | |||
PRODH | proline dehydrogenase (oxidase) 1 (600 aa) | |||
MT-CO1 | mitochondrially encoded cytochrome c oxidase I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B (By similarity) (513 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) | |||
GFOD1 | glucose-fructose oxidoreductase domain containing 1 (390 aa) | |||
TXNDC5 | thioredoxin domain containing 5 (endoplasmic reticulum); Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide- isomerase deficiency in yeast (By similarity) (432 aa) | |||
NOXRED1 | NADP-dependent oxidoreductase domain containing 1; Probable oxidoreductase (By similarity) (359 aa) | |||
IFFO2 | intermediate filament family orphan 2 (517 aa) | |||
P5CR2 | Uncharacterized protein (359 aa) | |||
POR | P450 (cytochrome) oxidoreductase; This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5 (680 aa) | |||
BCAT1 | branched chain amino-acid transaminase 1, cytosolic; Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine (398 aa) | |||
ENSG00000255275 | annotation not available (296 aa) |