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Glutathione S-transferase omega-1

NameGlutathione S-transferase omega-1
Synonyms
  • 2.5.1.18
  • Glutathione S-transferase omega 1-1
  • Glutathione-dependent dehydroascorbate reductase
  • GSTO 1-1
  • GSTO-1
  • GSTTLP28
  • MMA(V) reductase
  • Monomethylarsonic acid reductase
  • S-(Phenacyl)glutathione reductase
  • SPG-R
Gene NameGSTO1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0001626|Glutathione S-transferase omega-1
MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKP
EWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELF
SKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPW
FERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYG
L
Number of residues241
Molecular Weight27565.6
Theoretical pI6.54
GO Classification
Functions
  • oxidoreductase activity
  • glutathione dehydrogenase (ascorbate) activity
  • glutathione transferase activity
  • methylarsonate reductase activity
Processes
  • positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
  • xenobiotic metabolic process
  • L-ascorbic acid metabolic process
  • glutathione metabolic process
  • glutathione derivative biosynthetic process
  • methylation
  • xenobiotic catabolic process
  • cellular response to arsenic-containing substance
  • small molecule metabolic process
  • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
  • L-ascorbic acid biosynthetic process
  • negative regulation of ryanodine-sensitive calcium-release channel activity
  • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
  • positive regulation of ryanodine-sensitive calcium-release channel activity
  • oxidation-reduction process
Components
  • cell body
  • axon
  • cytoplasm
  • basement membrane
  • cytosol
  • extracellular exosome
  • myelin sheath
  • nuclear membrane
General FunctionOxidoreductase activity
Specific FunctionExhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID2393722
UniProtKB IDP78417
UniProtKB Entry NameGSTO1_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0016215|Glutathione S-transferase omega-1 (GSTO1)
ATGTCCGGGGAGTCAGCCAGGAGCTTGGGGAAGGGAAGCGCGCCCCCGGGGCCGGTCCCG
GAGGGCTCGATCCGCATCTACAGCATGAGGTTCTGCCCGTTTGCTGAGAGGACGCGTCTA
GTCCTGAAGGCCAAGGGAATCAGGCATGAAGTCATCAATATCAACCTGAAAAATAAGCCT
GAGTGGTTCTTTAAGAAAAATCCCTTTGGTCTGGTGCCAGTTCTGGAAAACAGTCAGGGT
CAGCTGATCTACGAGTCTGCCATCACCTGTGAGTACCTGGATGAAGCATACCCAGGGAAG
AAGCTGTTGCCGGATGACCCCTATGAGAAAGCTTGCCAGAAGATGATCTTAGAGTTGTTT
TCTAAGGTTCTGACTAATAAGAAGACGACCTTCTTTGGTGGCAATTCTATCTCTATGATT
GATTACCTCATCTGGCCCTGGTTTGAACGGCTGGAAGCAATGAAGTTAAATGAGTGTGTA
GACCACACTCCAAAACTGAAACTGTGGATGGCAGCCATGAAGGAAGATCCCACAGTCTCA
GCCCTGCTTACTAGTGAGAAAGACTGGCAAGGTTTCCTAGAGCTCTACTTACAGAACAGC
CCTGAGGCCTGTGACTATGGGCTCTGA
GenBank Gene IDU90313
GeneCard IDNot Available
GenAtlas IDGSTO1
HGNC IDHGNC:13312
Chromosome Location10
Locus10q25.1
References
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  2. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. 12928150
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. 17974005
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  10. 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. 19413330
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  13. 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. 24275569
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