DOSEN PROFIL LENGKAP

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)
End	95,822,726 bp
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)
End	75,998,273 bp
RNA expression pattern
	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
	; ;
	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
	2745
	93692
	ENSG00000173221
	ENSMUSG00000021591
	P35754
	Q9QUH0
	NM_002064; NM_001118890; NM_001243658; NM_001243659
	NM_053108; NM_001360151
	NP_001112362; NP_001230587; NP_001230588; NP_002055
	NP_444338; NP_001347080
	Wikidata
View/Edit Human	View/Edit Mouse

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

Interactions

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

References

^ ^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.

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.

This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000173221 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021591 – Ensembl, May 2017

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

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

[pmid8838810-5] 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-6] "Entrez Gene: GLRX glutaredoxin (thioltransferase)".

[pmid16884690-7] 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.

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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 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 Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

DOSEN PROFIL LENGKAP

GLRX

Interactions

References

Further reading

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