Glutaredoxin-1

Details

Name
Glutaredoxin-1
Synonyms
  • GRX
  • Thioltransferase-1
  • TTase-1
Gene Name
GLRX
Organism
Humans
Amino acid sequence
>lcl|BSEQ0011645|Glutaredoxin-1
MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDY
LQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGELLTRLKQIGALQ
Number of residues
106
Molecular Weight
11775.665
Theoretical pI
8.21
GO Classification
Functions
electron carrier activity / glutathione disulfide oxidoreductase activity / glutathione oxidoreductase activity / protein N-terminus binding
Processes
cell redox homeostasis / nucleobase-containing small molecule interconversion / nucleobase-containing small molecule metabolic process / positive regulation of membrane potential / positive regulation of sodium ion transmembrane transporter activity / protein deglutathionylation / small molecule metabolic process
Components
cytosol / extracellular exosome / mitochondrion / nucleus
General Function
Protein n-terminus binding
Specific Function
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011646|Glutaredoxin-1 (GLRX)
ATGGCTCAAGAGTTTGTGAACTGCAAAATCCAGCCTGGGAAGGTGGTTGTGTTCATCAAG
CCCACCTGCCCGTACTGCAGGAGGGCCCAAGAGATCCTCAGTCAATTGCCCATCAAACAA
GGGCTTCTGGAATTTGTCGATATCACAGCCACCAACCACACTAACGAGATTCAAGATTAT
TTGCAACAGCTCACGGGAGCAAGAACGGTGCCTCGAGTCTTTATTGGTAAAGATTGTATA
GGCGGATGCAGTGATCTAGTCTCTTTGCAACAGAGTGGGGAACTGCTGACGCGGCTAAAG
CAGATTGGAGCTCTGCAGTAA
Chromosome Location
5
Locus
5q14
External Identifiers
ResourceLink
UniProtKB IDP35754
UniProtKB Entry NameGLRX1_HUMAN
GenBank Protein ID643695
GenBank Gene IDD21238
GenAtlas IDGLRX
HGNC IDHGNC:4330
General References
  1. Fernando MR, Sumimoto H, Nanri H, Kawabata S, Iwanaga S, Minakami S, Fukumaki Y, Takeshige K: Cloning and sequencing of the cDNA encoding human glutaredoxin. Biochim Biophys Acta. 1994 Jun 21;1218(2):229-31. [Article]
  2. Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A: Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin. Eur J Biochem. 1995 Jan 15;227(1-2):27-34. [Article]
  3. Park JB, Levine M: Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin. Biochem J. 1996 May 1;315 ( Pt 3):931-8. [Article]
  4. Park JB, Levine M: The human glutaredoxin gene: determination of its organization, transcription start point, and promoter analysis. Gene. 1997 Sep 15;197(1-2):189-93. [Article]
  5. Qiao F, Xing K, Liu A, Ehlers N, Raghavachari N, Lou MF: Human lens thioltransferase: cloning, purification, and function. Invest Ophthalmol Vis Sci. 2001 Mar;42(3):743-51. [Article]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  8. Papov VV, Gravina SA, Mieyal JJ, Biemann K: The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells. Protein Sci. 1994 Mar;3(3):428-34. [Article]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  10. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  11. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  12. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  13. Sun C, Berardi MJ, Bushweller JH: The NMR solution structure of human glutaredoxin in the fully reduced form. J Mol Biol. 1998 Jul 24;280(4):687-701. [Article]
  14. Yang Y, Jao Sc, Nanduri S, Starke DW, Mieyal JJ, Qin J: 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. 1998 Dec 8;37(49):17145-56. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00143Glutathioneapproved, investigational, nutraceuticalunknownDetails