GLRX2

Glutaredoxin 2

PDB rendering based on 2cq9.

Available structures
PDB	2CQ9, 2FLS, 2HT9

Identifiers

Symbols

GLRX2; GRX2; bA101E13.1

External IDs

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

Gene Ontology
Molecular function	• 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 • nucleolus • mitochondrion
Biological process	• regulation of transcription, DNA-dependent • protein thiol-disulfide exchange • glutathione metabolic process • transport • apoptosis • response to temperature stimulus • regulation of signal transduction • response to organic substance • electron transport chain • cell differentiation • DNA protection • response to hydrogen peroxide • cell redox homeostasis • response to redox state
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
193.07 – 193.08 Mb

Chr 1:
145.59 – 145.6 Mb

PubMed search

[1]

[2]

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.
^ ^a ^b "Entrez Gene: GLRX2 glutaredoxin 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51022.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310876.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=516552.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1149418.
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

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

GLRX2

References

Further reading