Glutathione reductase, mitochondrial
Details
- Name
- Glutathione reductase, mitochondrial
- Synonyms
- 1.8.1.7
- GLUR
- GR
- GRD1
- Gene Name
- GSR
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0001292|Glutathione reductase, mitochondrial MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAG AVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHS EFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDP KPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAG YIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKK TLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVD EFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPP IGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQ GLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR
- Number of residues
- 522
- Molecular Weight
- 56256.565
- Theoretical pI
- 8.66
- GO Classification
- Functionselectron carrier activity / flavin adenine dinucleotide binding / glutathione-disulfide reductase activity / NADP bindingProcessescell redox homeostasis / gene expression / glutathione metabolic process / nucleobase-containing small molecule interconversion / nucleobase-containing small molecule metabolic process / response to reactive oxygen species / small molecule metabolic process / transcription initiation from RNA polymerase II promoterComponentscytosol / external side of plasma membrane / extracellular exosome / mitochondrial matrix
- General Function
- Nadp binding
- Specific Function
- Maintains high levels of reduced glutathione in the cytosol.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Mitochondrion
- Gene sequence
>lcl|BSEQ0016164|Glutathione reductase, mitochondrial (GSR) ATGGCCCTGCTGCCCCGAGCCCTGAGCGCCGGCGCGGGACCGAGCTGGCGGCGGGCGGCG CGCGCCTTCCGAGGCTTCCTGCTGCTTCTGCCCGAGCCCGCGGCCCTCACGCGCGCCCTC TCCCGTGCCATGGCCTGCAGGCAGGAGCCGCAGCCGCAGGGCCCGCCGCCCGCTGCTGGC GCCGTGGCCTCCTATGACTACCTGGTGATCGGGGGCGGCTCGGGCGGGCTGGCCAGCGCG CGCAGGGCGGCCGAGCTGGGTGCCAGGGCCGCCGTGGTGGAGAGCCACAAGCTGGGTGGC ACTTGCGTGAATGTTGGATGTGTACCCAAAAAGGTAATGTGGAACACAGCTGTCCACTCT GAATTCATGCATGATCATGCTGATTATGGCTTTCCAAGTTGTGAGGGTAAATTCAATTGG CGTGTTATTAAGGAAAAGCGGGATGCCTATGTGAGCCGCCTGAATGCCATCTATCAAAAC AATCTCACCAAGTCCCATATAGAAATCATCCGTGGCCATGCAGCCTTCACGAGTGATCCC AAGCCCACAATAGAGGTCAGTGGGAAAAAGTACACCGCCCCACACATCCTGATCGCCACA GGTGGTATGCCCTCCACCCCTCATGAGAGCCAGATCCCCGGTGCCAGCTTAGGAATAACC AGCGATGGATTTTTTCAGCTGGAAGAATTGCCCGGCCGCAGCGTCATTGTTGGTGCAGGT TACATTGCTGTGGAGATGGCAGGGATCCTGTCAGCCCTGGGTTCTAAGACATCACTGATG ATACGGCATGATAAGGTACTTAGAAGTTTTGATTCAATGATCAGCACCAACTGCACGGAG GAGCTGGAGAACGCTGGCGTGGAGGTGCTGAAGTTCTCCCAGGTCAAGGAGGTTAAAAAG ACTTTGTCGGGCTTGGAAGTCAGCATGGTTACTGCAGTTCCCGGTAGGCTACCAGTCATG ACCATGATTCCAGATGTTGACTGCCTGCTCTGGGCCATTGGGCGGGTCCCGAATACCAAG GACCTGAGTTTAAACAAACTGGGGATTCAAACCGATGACAAGGGTCATATCATCGTAGAC GAATTCCAGAATACCAACGTCAAAGGCATCTATGCAGTTGGGGATGTATGTGGAAAAGCT CTTCTTACTCCAGTTGCAATAGCTGCTGGCCGAAAACTTGCCCATCGACTTTTTGAATAT AAGGAAGATTCCAAATTAGATTATAACAACATCCCAACTGTGGTCTTCAGCCACCCCCCT ATTGGGACAGTGGGACTCACGGAAGATGAAGCCATTCATAAATATGGAATAGAAAATGTG AAGACCTATTCAACGAGCTTTACCCCGATGTATCACGCAGTTACCAAAAGGAAAACAAAA TGTGTGATGAAAATGGTCTGTGCTAACAAGGAAGAAAAGGTGGTTGGGATCCATATGCAG GGACTTGGGTGTGATGAAATGCTGCAGGGTTTTGCTGTTGCAGTGAAGATGGGAGCAACG AAGGCAGACTTTGACAACACAGTCGCCATTCACCCTACCTCTTCAGAAGAGCTGGTCACA CTTCGTTGA
- Chromosome Location
- 8
- Locus
- 8p21.1
- External Identifiers
Resource Link UniProtKB ID P00390 UniProtKB Entry Name GSHR_HUMAN GenBank Protein ID 31825 GenBank Gene ID X15722 GenAtlas ID GSR HGNC ID HGNC:4623 - General References
- Tutic M, Lu XA, Schirmer RH, Werner D: Cloning and sequencing of mammalian glutathione reductase cDNA. Eur J Biochem. 1990 Mar 30;188(3):523-8. [Article]
- Kelner MJ, Montoya MA: Structural organization of the human glutathione reductase gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence. Biochem Biophys Res Commun. 2000 Mar 16;269(2):366-8. [Article]
- Satoh N, Watanabe N, Kanda A, Sugaya-Fukasawa M, Hisatomi H: Expression of glutathione reductase splice variants in human tissues. Biochem Genet. 2010 Oct;48(9-10):816-21. doi: 10.1007/s10528-010-9362-z. Epub 2010 Jul 14. [Article]
- Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [Article]
- 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]
- Krauth-Siegel RL, Blatterspiel R, Saleh M, Schiltz E, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. Eur J Biochem. 1982 Jan;121(2):259-67. [Article]
- Krohne-Ehrich G, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide. Eur J Biochem. 1977 Oct 17;80(1):65-71. [Article]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [Article]
- 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]
- 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]
- 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]
- Thieme R, Pai EF, Schirmer RH, Schulz GE: Three-dimensional structure of glutathione reductase at 2 A resolution. J Mol Biol. 1981 Nov 15;152(4):763-82. [Article]
- Karplus PA, Schulz GE: Refined structure of glutathione reductase at 1.54 A resolution. J Mol Biol. 1987 Jun 5;195(3):701-29. [Article]
- Savvides SN, Karplus PA: Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J Biol Chem. 1996 Apr 5;271(14):8101-7. [Article]
- Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF: Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997 May 27;36(21):6437-47. [Article]
- Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA: Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. Nat Struct Biol. 1998 Apr;5(4):267-71. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00262 Carmustine approved, investigational yes inhibitor Details DB00157 NADH approved, nutraceutical unknown Details DB00143 Glutathione approved, investigational, nutraceutical unknown Details DB01644 3,6-dihydroxy-xanthene-9-propionic acid experimental unknown Details DB02153 3-sulfino-L-alanine experimental unknown Details DB02553 Glutathionylspermidine disulfide experimental unknown Details DB02895 3-(Prop-2-Ene-1-Sulfinyl)-Propene-1-Thiol experimental unknown Details DB03147 Flavin adenine dinucleotide approved unknown Details DB03310 Glutathione disulfide approved, experimental, investigational unknown substrate Details DB03867 3-nitro-L-tyrosine experimental unknown Details DB07393 2-(2-PHENYL-3-PYRIDIN-2-YL-4,5,6,7-TETRAHYDRO-2H-ISOPHOSPHINDOL-1-YL)PYRIDINE experimental unknown Details DB07714 6-(3-METHYL-1,4-DIOXO-1,4-DIHYDRONAPHTHALEN-2-YL)HEXANOIC ACID experimental unknown Details DB11135 Selenium approved, investigational, vet_approved no substrate Details DB09130 Copper approved, investigational unknown Details DB11590 Thimerosal approved unknown inducer Details DB09061 Cannabidiol approved, investigational unknown stimulator Details DB14011 Nabiximols investigational unknown stimulator Details DB14009 Medical Cannabis experimental, investigational unknown inducer Details