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Wikipedia

GLRX

February 27, 2024

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

GLRX
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGLRX, GRX, GRX1, glutaredoxin
External IDsOMIM: 600443 MGI: 2135625 HomoloGene: 37566 GeneCards: GLRX
Orthologs
SpeciesHumanMouse
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 MbChr 13: 75.99 – 76 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Interactions edit

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

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000173221 - Ensembl, May 2017
  2. ^ a b c 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.
  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.
  6. ^ "Entrez Gene: GLRX glutaredoxin (thioltransferase)".
  7. ^ 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.
 

This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by expanding it.

February 27, 2024
glrx, glutaredoxin, protein, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes1b4q, 1jhb, 4rqridentifiersaliases, grx1, glutaredoxinexternal, idsomim, 600443, 2135625, homologene, 37566, genecards, gene, location, hum. Glutaredoxin 1 is a protein that in humans is encoded by the GLRX gene 5 6 GLRXAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes1B4Q 1JHB 4RQRIdentifiersAliasesGLRX GRX GRX1 glutaredoxinExternal IDsOMIM 600443 MGI 2135625 HomoloGene 37566 GeneCards GLRXGene location Human Chr Chromosome 5 human 1 Band5q15Start95 751 319 bp 1 End95 822 726 bp 1 Gene location Mouse Chr Chromosome 13 mouse 2 Band13 C1 13 40 95 cMStart75 987 987 bp 2 End75 998 273 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed injejunal mucosastromal cell of endometriummonocyteduodenumoocytegastrocnemius musclekidneyspongy bonebone marrowkidney tubuleTop expressed inesophagusjejunumileumlipduodenumepithelium of stomachsecondary oocyteblastocystintestinal villusmucous cell of stomachMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein disulfide reductase activity electron transfer activity glutathione oxidoreductase activity protein N terminus binding glutathione disulfide oxidoreductase activityCellular componentcytoplasm cytosol extracellular exosome mitochondrion nucleusBiological processpositive regulation of sodium ion transmembrane transporter activity nucleobase containing small molecule interconversion positive regulation of membrane potential protein deglutathionylation cell redox homeostasis electron transport chainSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez274593692EnsemblENSG00000173221ENSMUSG00000021591UniProtP35754Q9QUH0RefSeq mRNA NM 002064NM 001118890NM 001243658NM 001243659NM 053108NM 001360151RefSeq protein NP 001112362NP 001230587NP 001230588NP 002055NP 444338NP 001347080Location UCSC Chr 5 95 75 95 82 MbChr 13 75 99 76 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseInteractions editGLRX 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 editLou 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 Martinez Galisteo E Barcena 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 Konig 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 Garcia Pardo L Granados MD Gaytan 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 nbsp This article on a gene on human chromosome 5 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title GLRX amp oldid 1116588210, wikipedia, wiki, book, books, library,

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