GLRX2
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Official Full Name
glutaredoxin 2 -
Overview
The protein encoded by this gene is a member of the glutaredoxin family of proteins, which maintain cellular thiol homeostasis. These proteins are thiol-disulfide oxidoreductases that use a glutathione-binding site and one or two active cysteines in their active site. This gene undergoes alternative splicing to produce multiple isoforms, one of which is ubiquitously expressed and localizes to mitochondria, where it functions in mitochondrial redox homeostasis and is important for the protection against and recovery from oxidative stress. Other isoforms, which have more restrictive expression patterns, show cytosolic and nuclear localization, and are thought to function in cellular differentiation and transformation, possibly with a role in tumor progression. GRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. -
Synonyms
GLRX2;glutaredoxin 2;bA101E13.1;bA101E13.1 (GRX2 glutaredoxin (thioltransferase) 2);GRX2;mitochondrial;CGI133;GLRX2_HUMAN;Glutaredoxin-2;OTTHUMP00000033766;OTTHUMP00000033767;CGI-133;TTR1;YDR513W
Recombinant Proteins
- Human
- Rhesus macaque
- Rat
- Zebrafish
- Cynomolgus
- Yeast
- Mouse
- E.coli
- Mammalian Cell
- HEK293
- HEK293T
- Wheat Germ
- In Vitro Cell Free System
- GST
- Non
- His
- His&Fc&Avi
- Myc&DDK
Involved Pathway
GLRX2 involved in several pathways and played different roles in them. We selected most pathways GLRX2 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with GLRX2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Protein Function
GLRX2 has several biochemical functions, for example, 2 iron, 2 sulfur cluster binding,arsenate reductase (glutaredoxin) activity,electron carrier activity. Some of the functions are cooperated with other proteins, some of the functions could acted by GLRX2 itself. We selected most functions GLRX2 had, and list some proteins which have the same functions with GLRX2. You can find most of the proteins on our site.
Function | Related Protein |
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protein disulfide isomerase activity | PDIA5,ZNF169,QSOX2,PDIA2,ITGB3,TMX3,PDIA3,QSOX1,TMX4,TXNDC11 |
protein disulfide oxidoreductase activity | CHCHD4,PTGES2,CCS,TXNL1,ERO1LB,ERO1L,PTGESL,TXN,ENOX2,GLRX5 |
glutathione disulfide oxidoreductase activity | GLRX |
metal ion binding | ZFP536,ITGA3,PPM1L,GALNT14,ZFP143,PLA2G3,ATP2A2B,ZCCHC16,VAV3,ZNF165 |
electron carrier activity | HSD17B6,LOXL2,ASPH,COX11,NQO2,COX7A3,IDH3B,DHDH,ACOX3,AKR1A1 |
2 iron, 2 sulfur cluster binding | FXN,FDX1,FECH,AOX3L1,AOX3,CMAH,FDX1L,NDUFV2,AIFM3,CISD3 |
Interacting Protein
GLRX2 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with GLRX2 here. Most of them are supplied by our site. Hope this information will be useful for your research of GLRX2.
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References
- Upadhyaya, B; Tian, XL; et al. Expression and distribution of thiol-regulating enzyme glutaredoxin 2 (GRX2) in porcine ocular tissues. EXPERIMENTAL EYE RESEARCH 130:58-65(2015).
- Zhang, J; Yan, H; et al. Ultraviolet Radiation-Induced Cataract in Mice: The Effect of Age and the Potential Biochemical Mechanism. INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE 53:7276-7285(2012).