STRINGSTRING
MSRB1 MSRB1 SECISBP2 SECISBP2 MSRB2 MSRB2 SEPHS1 SEPHS1 GLRX GLRX CYS1 CYS1 SEPSECS SEPSECS GPX3 GPX3 GPX2 GPX2 TXNRD2 TXNRD2 FUT2 FUT2 GPX5 GPX5 GPX8 GPX8 SELENOW SELENOW GNLY GNLY TXNRD1 TXNRD1 SELENOP SELENOP GSR GSR PXDN PXDN EEFSEC EEFSEC GPX4 GPX4 PXDNL PXDNL GPX6 GPX6 GPX7 GPX7 TXN TXN
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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MSRB1Methionine-R-sulfoxide reductase B1; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to a [...] (116 aa)
SECISBP2Selenocysteine insertion sequence-binding protein 2; Binds to the SECIS element in the 3'-UTR of some mRNAs encoding selenoproteins. Binding is stimulated by SELB. (854 aa)
MSRB2Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] (182 aa)
SEPHS1Selenide, water dikinase 1; Synthesizes selenophosphate from selenide and ATP. (392 aa)
GLRXGlutaredoxin-1; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins; Belongs to the glutaredoxin family. (106 aa)
CYS1Cystin-1; Cystin 1. (158 aa)
SEPSECSO-phosphoseryl-tRNA(Sec) selenium transferase; Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl- tRNA(Sec) required for selenoprotein biosynthesis. Belongs to the SepSecS family. (501 aa)
GPX3Glutathione peroxidase 3; Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. (226 aa)
GPX2Glutathione peroxidase 2; Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors. (190 aa)
TXNRD2Thioredoxin reductase 2, mitochondrial; Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis. Maintains thioredoxin in a reduced state. May play a role in redox- regulated cell signaling. (524 aa)
FUT2Galactoside 2-alpha-L-fucosyltransferase 2; Mediates the transfer of fucose to the terminal galactose on glycan chains of cell surface glycoproteins and glycolipids. The resulting epitope plays a role in cell-cell interaction including host-microbe interaction. Mediates interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway. (343 aa)
GPX5Epididymal secretory glutathione peroxidase; Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids. (221 aa)
GPX8Glutathione peroxidase 8; Belongs to the glutathione peroxidase family. (209 aa)
SELENOWSelenoprotein W; Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency (By similarity); Belongs to the SelWTH family. Selenoprotein W subfamily. (87 aa)
GNLYGranulysin; Antimicrobial protein that kills intracellular pathogens. Active against a broad range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis. (172 aa)
TXNRD1Thioredoxin reductase 1, cytoplasmic; Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid. (649 aa)
SELENOPSelenoprotein P; Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis. (381 aa)
GSRGlutathione reductase, mitochondrial; Maintains high levels of reduced glutathione in the cytosol. (522 aa)
PXDNPeroxidasin homolog; Displays low peroxidase activity and is likely to participate in H(2)O(2) metabolism and peroxidative reactions in the cardiovascular system. Plays a role in extracellular matrix formation. (1479 aa)
EEFSECSelenocysteine-specific elongation factor; Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP. (596 aa)
GPX4Phospholipid hydroperoxide glutathione peroxidase; Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins (By similarity). Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (By similarity). Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species. Th [...] (197 aa)
PXDNLPeroxidasin-like protein; [Isoform PMR1]: Endonuclease selectively degrading some target mRNAs while they are engaged by translating ribosomes, among which albumin and beta-globin mRNAs. (1463 aa)
GPX6Glutathione peroxidase 6. (221 aa)
GPX7Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family. (187 aa)
TXNThioredoxin; 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 [...] (105 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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