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(Top) 1 Interactions 2 References 3 Further reading

GLRX

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GLRX

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1B4Q, 1JHB, 4RQR

Identifiers

Aliases

GLRX, GRX, GRX1, glutaredoxin

External IDs

OMIM: 600443; MGI: 2135625; HomoloGene: 37566; GeneCards: GLRX; OMA:GLRX - orthologs

Gene location (Human)

Chr.	Chromosome 5 (human)^[1]

Band	5q15	Start	95,751,319 bp^[1]
Band	5q15	End	95,822,726 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 13 (mouse)^[2]

Band	13 C1\|13 40.95 cM	Start	75,987,987 bp^[2]
Band	13 C1\|13 40.95 cM	End	75,998,273 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

jejunal mucosa

decidua

stromal cell of endometrium

monocyte

skin of thigh

mucosa of ileum

duodenum

oocyte

gastrocnemius muscle

human kidney

Top expressed in

granulocyte

esophagus

primary oocyte

jejunum

ileum

lip

duodenum

zygote

blastocyst

epithelium of stomach

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein-disulfide reductase activity electron transfer activity glutathione oxidoreductase activity protein N-terminus binding glutathione disulfide oxidoreductase activity
Cellular component	cytoplasm cytosol extracellular exosome mitochondrion nucleus
Biological process	positive regulation of sodium ion transmembrane transporter activity nucleobase-containing small molecule interconversion positive regulation of membrane potential protein deglutathionylation cell redox homeostasis electron transport chain
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


2745


93692

Ensembl


ENSG00000173221


ENSMUSG00000021591

UniProt


P35754


Q9QUH0

RefSeq (mRNA)


NM_002064 NM_001118890 NM_001243658 NM_001243659


NM_053108 NM_001360151

RefSeq (protein)


NP_001112362 NP_001230587 NP_001230588 NP_002055


NP_444338 NP_001347080

Location (UCSC)

Chr 5: 95.75 – 95.82 Mb

Chr 13: 75.99 – 76 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Glutaredoxin-1 is a protein that in humans is encoded by the GLRX gene.^[5]^[6]

Interactions[edit]

GLRX has been shown to interact with Wilson disease protein^[7] and ATP7A.^[7]

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000173221 – Ensembl, May 2017

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021591 – Ensembl, May 2017

^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ Padilla CA, Bajalica S, Lagercrantz J, Holmgren A (Feb 1997). "The gene for human glutaredoxin (GLRX) is localized to human chromosome 5q14". Genomics. 32 (3): 455–7. doi:10.1006/geno.1996.0141. PMID 8838810.

^ "Entrez Gene: GLRX glutaredoxin (thioltransferase)".

^ ^a ^b Lim, Chris M; Cater Michael A; Mercer Julian F B; La Fontaine Sharon (Sep 2006). "Copper-dependent interaction of glutaredoxin with the N termini of the copper-ATPases (ATP7A and ATP7B) defective in Menkes and Wilson diseases". Biochem. Biophys. Res. Commun. 348 (2): 428–36. doi:10.1016/j.bbrc.2006.07.067. hdl:10536/DRO/DU:30003772. ISSN 0006-291X. PMID 16884690.

Further reading[edit]

Lou MF (2003). "Redox regulation in the lens". Progress in Retinal and Eye Research. 22 (5): 657–82. doi:10.1016/S1350-9462(03)00050-8. PMID 12892645. S2CID 40914153.

Sykes MC, Mowbray AL, Jo H (2007). "Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced cell death". Circ. Res. 100 (2): 152–4. doi:10.1161/01.RES.0000258171.08020.72. PMID 17272816.

Padilla CA, Martínez-Galisteo E, Bárcena JA, et al. (1995). "Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin". Eur. J. Biochem. 227 (1–2): 27–34. doi:10.1111/j.1432-1033.1995.tb20356.x. PMID 7851394.

Bandyopadhyay S, Gronostajski RM (1994). "Identification of a conserved oxidation-sensitive cysteine residue in the NFI family of DNA-binding proteins". J. Biol. Chem. 269 (47): 29949–55. doi:10.1016/S0021-9258(18)43973-7. PMID 7961993.

Fernando MR, Sumimoto H, Nanri H, et al. (1994). "Cloning and sequencing of the cDNA encoding human glutaredoxin". Biochim. Biophys. Acta. 1218 (2): 229–31. doi:10.1016/0167-4781(94)90019-1. PMID 8018729.

Papov VV, Gravina SA, Mieyal JJ, Biemann K (1994). "The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells". Protein Sci. 3 (3): 428–34. doi:10.1002/pro.5560030307. PMC 2142694. PMID 8019414.

Padilla CA, Spyrou G, Holmgren A (1996). "High-level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys7 to Ser mutant protein". FEBS Lett. 378 (1): 69–73. doi:10.1016/0014-5793(95)01413-6. PMID 8549805. S2CID 37604224.

Park JB, Levine M (1996). "Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin". Biochem. J. 315. ( Pt 3) (3): 931–8. doi:10.1042/bj3150931. PMC 1217296. PMID 8645179.

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.

Park JB, Levine M (1997). "The human glutaredoxin gene: determination of its organization, transcription start point, and promoter analysis". Gene. 197 (1–2): 189–93. doi:10.1016/S0378-1119(97)00262-X. PMID 9332366.

Bandyopadhyay S, Starke DW, Mieyal JJ, Gronostajski RM (1998). "Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I." J. Biol. Chem. 273 (1): 392–7. doi:10.1074/jbc.273.1.392. PMID 9417094.

Sun C, Berardi MJ, Bushweller JH (1998). "The NMR solution structure of human glutaredoxin in the fully reduced form". J. Mol. Biol. 280 (4): 687–701. CiteSeerX 10.1.1.156.1182. doi:10.1006/jmbi.1998.1913. PMID 9677297.

Yang Y, Jao S, Nanduri S, et al. (1999). "Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity". Biochemistry. 37 (49): 17145–56. doi:10.1021/bi9806504. PMID 9860827.

Balijepalli S, Tirumalai PS, Swamy KV, et al. (1999). "Rat brain thioltransferase: regional distribution, immunological characterization, and localization by fluorescent in situ hybridization". J. Neurochem. 72 (3): 1170–8. doi:10.1046/j.1471-4159.1999.0721170.x. PMID 10037490. S2CID 13507470.

Barrett WC, DeGnore JP, König S, et al. (1999). "Regulation of PTP1B via glutathionylation of the active site cysteine 215". Biochemistry. 38 (20): 6699–705. doi:10.1021/bi990240v. PMID 10350489.

García-Pardo L, Granados MD, Gaytán F, et al. (1999). "Immunolocalization of glutaredoxin in the human corpus luteum". Mol. Hum. Reprod. 5 (10): 914–9. doi:10.1093/molehr/5.10.914. PMID 10508218.

Mallis RJ, Poland BW, Chatterjee TK, et al. (2000). "Crystal structure of S-glutathiolated carbonic anhydrase III". FEBS Lett. 482 (3): 237–41. doi:10.1016/S0014-5793(00)02022-6. PMID 11024467. S2CID 8235342.

Balijepalli S, Boyd MR, Ravindranath V (2001). "Human brain thioltransferase: constitutive expression and localization by fluorescence in situ hybridization". Brain Res. Mol. Brain Res. 85 (1–2): 123–32. doi:10.1016/S0169-328X(00)00206-0. PMID 11146114.

Qiao F, Xing K, Liu A, et al. (2001). "Human lens thioltransferase: cloning, purification, and function". Invest. Ophthalmol. Vis. Sci. 42 (3): 743–51. PMID 11222536.

v t e PDB gallery
1b4q: SOLUTION STRUCTURE OF HUMAN THIOLTRANSFERASE COMPLEX WITH GLUTATHIONE 1jhb: HUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURES

v t e 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 (Methionine synthase) reductase
1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase 7-Hydroxymethyl chlorophyll a 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 phosphorusorarsenic 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 Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

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