GLRX2

Glutaredoxin 2

PDB rendering based on 2cq9.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2CQ9, 2FLS, 2HT9

Identifiers

Symbols

GLRX2 ; CGI-133; GRX2

External IDs

OMIM: 606820 MGI: 1916617 HomoloGene: 41098 GeneCards: GLRX2 Gene

Gene ontology
Molecular function	• protein disulfide isomerase activity • arsenate reductase (glutaredoxin) activity • electron carrier activity • protein disulfide oxidoreductase activity • glutathione disulfide oxidoreductase activity • metal ion binding • 2 iron, 2 sulfur cluster binding
Cellular component	• nucleus • nucleoplasm • mitochondrion • mitochondrial matrix • dendrite • neuronal cell body • intracellular membrane-bounded organelle
Biological process	• regulation of transcription, DNA-templated • protein folding • glutathione metabolic process • apoptotic process • aging • response to temperature stimulus • regulation of signal transduction • response to organic substance • cell differentiation • DNA protection • response to hydrogen peroxide • cell redox homeostasis • response to redox state • oxidation-reduction process • cellular response to superoxide
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
193.1 – 193.11 Mb

Chr 1:
143.72 – 143.75 Mb

PubMed search

Glutaredoxin-2, mitochondrial is a protein that in humans is encoded by the GLRX2 gene.^[1]^[2]

Glutaredoxins (e.g., GLRX; MIM 600443) are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions.[supplied by OMIM]^[2]

References

↑ Lundberg M, Johansson C, Chandra J, Enoksson M, Jacobsson G, Ljung J, Johansson M, Holmgren A (Jul 2001). "Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms". J Biol Chem 276 (28): 26269–75. doi:10.1074/jbc.M011605200. PMID 11297543.
1 2 "Entrez Gene: GLRX2 glutaredoxin 2".

Davis DA, Newcomb FM, Starke DW; et al. (1997). "Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro.". J. Biol. Chem. 272 (41): 25935–40. doi:10.1074/jbc.272.41.25935. PMID 9325327.
Lai CH, Chou CY, Ch'ang LY; et al. (2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics.". Genome Res. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
Gladyshev VN, Liu A, Novoselov SV; et al. (2001). "Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2.". J. Biol. Chem. 276 (32): 30374–80. doi:10.1074/jbc.M100020200. PMID 11397793.
Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Johansson C, Lillig CH, Holmgren A (2004). "Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase.". J. Biol. Chem. 279 (9): 7537–43. doi:10.1074/jbc.M312719200. PMID 14676218.
Lundberg M, Fernandes AP, Kumar S, Holmgren A (2004). "Cellular and plasma levels of human glutaredoxin 1 and 2 detected by sensitive ELISA systems.". Biochem. Biophys. Res. Commun. 319 (3): 801–9. doi:10.1016/j.bbrc.2004.04.199. PMID 15184054.
Peltoniemi M, Kaarteenaho-Wiik R, Säily M; et al. (2004). "Expression of glutaredoxin is highly cell specific in human lung and is decreased by transforming growth factor-beta in vitro and in interstitial lung diseases in vivo.". Hum. Pathol. 35 (8): 1000–7. doi:10.1016/j.humpath.2004.04.009. PMID 15297967.
Lillig CH, Lönn ME, Enoksson M; et al. (2004). "Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide.". Proc. Natl. Acad. Sci. U.S.A. 101 (36): 13227–32. doi:10.1073/pnas.0401896101. PMC 516552. PMID 15328416.
Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Enoksson M, Fernandes AP, Prast S; et al. (2005). "Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release.". Biochem. Biophys. Res. Commun. 327 (3): 774–9. doi:10.1016/j.bbrc.2004.12.067. PMID 15649413.
Lillig CH, Berndt C, Vergnolle O; et al. (2005). "Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor.". Proc. Natl. Acad. Sci. U.S.A. 102 (23): 8168–73. doi:10.1073/pnas.0500735102. PMC 1149418. PMID 15917333.
Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
Fernando MR, Lechner JM, Löfgren S; et al. (2007). "Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cells.". FASEB J. 20 (14): 2645–7. doi:10.1096/fj.06-5919fje. PMID 17065220.
Berndt C, Hudemann C, Hanschmann EM; et al. (2007). "How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?". Antioxid. Redox Signal. 9 (1): 151–7. doi:10.1089/ars.2007.9.151. PMID 17115894.
Johansson C, Kavanagh KL, Gileadi O, Oppermann U (2007). "Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria.". J. Biol. Chem. 282 (5): 3077–82. doi:10.1074/jbc.M608179200. PMID 17121859.
Sagemark J, Elgán TH, Bürglin TR; et al. (2007). "Redox properties and evolution of human glutaredoxins.". Proteins 68 (4): 879–92. doi:10.1002/prot.21416. PMID 17546662.

PDB gallery

2cq9: Solution structure of RSGI RUH-044, an N-terminal domain of Glutaredoxin 2 from human cDNA

2fls: Crystal structure of Human Glutaredoxin 2 complexed with glutathione

2ht9: The structure of dimeric human glutaredoxin 2

Other oxidoreductases (EC 1.15-1.21)

1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3

1.16: Oxidizing metal ions	Ceruloplasmin

1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase

1.18: Acting on iron-sulfur proteins as donors	Nitrogenase

1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase

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GLRX2

References

Further reading