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P78417

- GSTO1_HUMAN

UniProt

P78417 - GSTO1_HUMAN

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Protein

Glutathione S-transferase omega-1

Gene

GSTO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Exhibits 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.5 Publications

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.
Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.

Enzyme regulationi

Monomethylarsonic acid reductase activity is competitively inhibited by 1-chloro 2,4-dinitrobenzene (CDNB) and by deoxycholate.

pH dependencei

Optimum pH is 8.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei32 – 321Nucleophile1 Publication
Binding sitei59 – 591Glutathione1 Publication
Binding sitei72 – 721Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

GO - Molecular functioni

  1. glutathione dehydrogenase (ascorbate) activity Source: UniProtKB
  2. glutathione transferase activity Source: UniProtKB
  3. methylarsonate reductase activity Source: UniProtKB-EC
  4. oxidoreductase activity Source: UniProtKB

GO - Biological processi

  1. cellular response to arsenic-containing substance Source: UniProtKB
  2. glutathione derivative biosynthetic process Source: Reactome
  3. L-ascorbic acid metabolic process Source: UniProtKB
  4. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  5. positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  6. positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion Source: BHF-UCL
  7. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  8. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  9. small molecule metabolic process Source: Reactome
  10. xenobiotic catabolic process Source: UniProtKB
  11. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS07564-MONOMER.
ReactomeiREACT_11202. Vitamin C (ascorbate) metabolism.
REACT_6926. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase omega-1 (EC:2.5.1.18)
Short name:
GSTO-1
Alternative name(s):
Glutathione S-transferase omega 1-1
Short name:
GSTO 1-1
Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
Monomethylarsonic acid reductase (EC:1.20.4.2)
Short name:
MMA(V) reductase
S-(Phenacyl)glutathione reductase
Short name:
SPG-R
Gene namesi
Name:GSTO1
Synonyms:GSTTLP28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:13312. GSTO1.

Subcellular locationi

Cytoplasmcytosol 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321C → A: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA133787054.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 241240Glutathione S-transferase omega-1PRO_0000185884Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei57 – 571N6-acetyllysine1 Publication
Modified residuei143 – 1431N6-acetyllysine1 Publication
Modified residuei148 – 1481N6-acetyllysine1 Publication
Modified residuei152 – 1521N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP78417.
PaxDbiP78417.
PeptideAtlasiP78417.
PRIDEiP78417.

2D gel databases

OGPiP78417.
UCD-2DPAGEP78417.

PTM databases

PhosphoSiteiP78417.

Expressioni

Tissue specificityi

Ubiquitous. Highest expression in liver, pancreas, skeletal muscle, spleen, thymus, colon, blood leukocyte and heart. Lowest expression in brain, placenta and lung.1 Publication

Gene expression databases

BgeeiP78417.
CleanExiHS_GSTO1.
ExpressionAtlasiP78417. baseline and differential.
GenevestigatoriP78417.

Organism-specific databases

HPAiHPA037603.
HPA037604.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi114836. 12 interactions.
IntActiP78417. 7 interactions.
MINTiMINT-1384709.
STRINGi9606.ENSP00000358727.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63
Beta strandi24 – 285
Helixi33 – 4513
Beta strandi49 – 546
Beta strandi56 – 583
Helixi63 – 664
Beta strandi74 – 763
Beta strandi82 – 854
Helixi86 – 9611
Helixi107 – 12014
Helixi123 – 1319
Helixi136 – 16025
Beta strandi162 – 1643
Beta strandi167 – 1693
Helixi172 – 18413
Turni185 – 1884
Helixi190 – 1923
Beta strandi193 – 1953
Helixi197 – 20711
Helixi210 – 2156
Helixi219 – 22911
Turni230 – 2323
Helixi236 – 2383

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EEMX-ray2.00A1-241[»]
3LFLX-ray2.10A/B/C1-241[»]
3VLNX-ray1.70A1-241[»]
4IS0X-ray1.72A1-241[»]
ProteinModelPortaliP78417.
SMRiP78417. Positions 3-241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78417.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 10180GST N-terminalAdd
BLAST
Domaini106 – 230125GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni85 – 862Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Omega family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00390000005479.
HOGENOMiHOG000006560.
HOVERGENiHBG051853.
InParanoidiP78417.
KOiK00799.
OMAiHKAYLDS.
OrthoDBiEOG71CFNG.
PhylomeDBiP78417.
TreeFamiTF105325.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
PRINTSiPR01625. GSTRNSFRASEO.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P78417) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGESARSLG KGSAPPGPVP EGSIRIYSMR FCPFAERTRL VLKAKGIRHE
60 70 80 90 100
VININLKNKP EWFFKKNPFG LVPVLENSQG QLIYESAITC EYLDEAYPGK
110 120 130 140 150
KLLPDDPYEK ACQKMILELF SKVPSLVGSF IRSQNKEDYA GLKEEFRKEF
160 170 180 190 200
TKLEEVLTNK KTTFFGGNSI SMIDYLIWPW FERLEAMKLN ECVDHTPKLK
210 220 230 240
LWMAAMKEDP TVSALLTSEK DWQGFLELYL QNSPEACDYG L
Length:241
Mass (Da):27,566
Last modified:January 1, 1998 - v2
Checksum:i9134ABA265F5C87E
GO
Isoform 2 (identifier: P78417-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-155: Missing.

Show »
Length:208
Mass (Da):23,709
Checksum:iF00CDE200E2A1738
GO
Isoform 3 (identifier: P78417-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Show »
Length:213
Mass (Da):24,796
Checksum:iC3F8EBA348399628
GO

Sequence cautioni

The sequence CAD97673.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321C → Y.
Corresponds to variant rs45529437 [ dbSNP | Ensembl ].
VAR_061231
Natural varianti86 – 861S → C.
Corresponds to variant rs11509436 [ dbSNP | Ensembl ].
VAR_029269
Natural varianti140 – 1401A → D in allele GSTO1*C; no effect on protein stability. 2 Publications
Corresponds to variant rs4925 [ dbSNP | Ensembl ].
VAR_016811
Natural varianti155 – 1551Missing in allele GSTO1*B; decreased protein stability. 2 Publications
VAR_016813
Natural varianti208 – 2081E → K.1 Publication
Corresponds to variant rs11509438 [ dbSNP | Ensembl ].
VAR_024484
Natural varianti236 – 2361A → V.1 Publication
Corresponds to variant rs11509439 [ dbSNP | Ensembl ].
VAR_026583

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform 3. CuratedVSP_045819Add
BLAST
Alternative sequencei123 – 15533Missing in isoform 2. CuratedVSP_045820Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U90313 mRNA. Translation: AAB70109.1.
AF212303 mRNA. Translation: AAF73376.1.
AY817669 Genomic DNA. Translation: AAV68046.1.
BX537431 mRNA. Translation: CAD97673.1. Different initiation.
AL139341 Genomic DNA. Translation: CAI17224.1.
CH471066 Genomic DNA. Translation: EAW49601.1.
CH471066 Genomic DNA. Translation: EAW49602.1.
CH471066 Genomic DNA. Translation: EAW49603.1.
BC000127 mRNA. Translation: AAH00127.1.
CCDSiCCDS53572.1. [P78417-2]
CCDS53573.1. [P78417-3]
CCDS7555.1. [P78417-1]
RefSeqiNP_001177931.1. NM_001191002.1. [P78417-2]
NP_001177932.1. NM_001191003.1. [P78417-3]
NP_004823.1. NM_004832.2. [P78417-1]
UniGeneiHs.190028.

Genome annotation databases

EnsembliENST00000369710; ENSP00000358724; ENSG00000148834. [P78417-2]
ENST00000369713; ENSP00000358727; ENSG00000148834. [P78417-1]
ENST00000539281; ENSP00000441488; ENSG00000148834. [P78417-3]
GeneIDi9446.
KEGGihsa:9446.
UCSCiuc001kya.3. human. [P78417-1]

Polymorphism databases

DMDMi6016173.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U90313 mRNA. Translation: AAB70109.1 .
AF212303 mRNA. Translation: AAF73376.1 .
AY817669 Genomic DNA. Translation: AAV68046.1 .
BX537431 mRNA. Translation: CAD97673.1 . Different initiation.
AL139341 Genomic DNA. Translation: CAI17224.1 .
CH471066 Genomic DNA. Translation: EAW49601.1 .
CH471066 Genomic DNA. Translation: EAW49602.1 .
CH471066 Genomic DNA. Translation: EAW49603.1 .
BC000127 mRNA. Translation: AAH00127.1 .
CCDSi CCDS53572.1. [P78417-2 ]
CCDS53573.1. [P78417-3 ]
CCDS7555.1. [P78417-1 ]
RefSeqi NP_001177931.1. NM_001191002.1. [P78417-2 ]
NP_001177932.1. NM_001191003.1. [P78417-3 ]
NP_004823.1. NM_004832.2. [P78417-1 ]
UniGenei Hs.190028.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EEM X-ray 2.00 A 1-241 [» ]
3LFL X-ray 2.10 A/B/C 1-241 [» ]
3VLN X-ray 1.70 A 1-241 [» ]
4IS0 X-ray 1.72 A 1-241 [» ]
ProteinModelPortali P78417.
SMRi P78417. Positions 3-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114836. 12 interactions.
IntActi P78417. 7 interactions.
MINTi MINT-1384709.
STRINGi 9606.ENSP00000358727.

Chemistry

BindingDBi P78417.
ChEMBLi CHEMBL3174.
DrugBanki DB00143. Glutathione.
DB00163. Vitamin E.

PTM databases

PhosphoSitei P78417.

Polymorphism databases

DMDMi 6016173.

2D gel databases

OGPi P78417.
UCD-2DPAGE P78417.

Proteomic databases

MaxQBi P78417.
PaxDbi P78417.
PeptideAtlasi P78417.
PRIDEi P78417.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369710 ; ENSP00000358724 ; ENSG00000148834 . [P78417-2 ]
ENST00000369713 ; ENSP00000358727 ; ENSG00000148834 . [P78417-1 ]
ENST00000539281 ; ENSP00000441488 ; ENSG00000148834 . [P78417-3 ]
GeneIDi 9446.
KEGGi hsa:9446.
UCSCi uc001kya.3. human. [P78417-1 ]

Organism-specific databases

CTDi 9446.
GeneCardsi GC10P106004.
HGNCi HGNC:13312. GSTO1.
HPAi HPA037603.
HPA037604.
MIMi 605482. gene.
neXtProti NX_P78417.
PharmGKBi PA133787054.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0625.
GeneTreei ENSGT00390000005479.
HOGENOMi HOG000006560.
HOVERGENi HBG051853.
InParanoidi P78417.
KOi K00799.
OMAi HKAYLDS.
OrthoDBi EOG71CFNG.
PhylomeDBi P78417.
TreeFami TF105325.

Enzyme and pathway databases

BioCyci MetaCyc:HS07564-MONOMER.
Reactomei REACT_11202. Vitamin C (ascorbate) metabolism.
REACT_6926. Glutathione conjugation.

Miscellaneous databases

ChiTaRSi GSTO1. human.
EvolutionaryTracei P78417.
GeneWikii GSTO1.
GenomeRNAii 9446.
NextBioi 35384.
PROi P78417.
SOURCEi Search...

Gene expression databases

Bgeei P78417.
CleanExi HS_GSTO1.
ExpressionAtlasi P78417. baseline and differential.
Genevestigatori P78417.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view ]
PRINTSi PR01625. GSTRNSFRASEO.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the human homolog to a mouse protein, differentially expressed in lymphoma cells with different susceptibility to radiation induced apoptosis."
    Kodym R., Story M.D.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, TISSUE SPECIFICITY.
    Tissue: Fetus.
  3. "Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans."
    Yu L., Kalla K., Guthrie E., Vidrine A., Klimecki W.T.
    Environ. Health Perspect. 111:1421-1427(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-140; GLU-155 DEL; LYS-208 AND VAL-236.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye.
  8. "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping."
    Hubbard M.J., McHugh N.J.
    Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 12-21; 58-65; 133-139 AND 149-156, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Liver.
  9. "Human monomethylarsonic acid (MMA(V)) reductase is a member of the glutathione-S-transferase superfamily."
    Zakharyan R.A., Sampayo-Reyes A., Healy S.M., Tsaprailis G., Board P.G., Liebler D.C., Aposhian H.V.
    Chem. Res. Toxicol. 14:1051-1057(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Liver.
  10. "Glutathione transferase omega 1 catalyzes the reduction of S-(phenacyl)glutathiones to acetophenones."
    Board P.G., Anders M.W.
    Chem. Res. Toxicol. 20:149-154(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-32, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
  11. "S-(4-Nitrophenacyl)glutathione is a specific substrate for glutathione transferase omega 1-1."
    Board P.G., Coggan M., Cappello J., Zhou H., Oakley A.J., Anders M.W.
    Anal. Biochem. 374:25-30(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-143; LYS-148 AND LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Novel folding and stability defects cause a deficiency of human glutathione transferase omega 1."
    Zhou H., Brock J., Casarotto M.G., Oakley A.J., Board P.G.
    J. Biol. Chem. 286:4271-4279(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANT GLU-155 DEL, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, CHARACTERIZATION OF VARIANTS ASP-140 AND GLU-155 DEL.
  16. "Characterization of the human Omega class glutathione transferase genes and associated polymorphisms."
    Whitbread A.K., Tetlow N., Eyre H.J., Sutherland G.R., Board P.G.
    Pharmacogenetics 13:131-144(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ASP-140 AND GLU-155 DEL.

Entry informationi

Entry nameiGSTO1_HUMAN
AccessioniPrimary (citable) accession number: P78417
Secondary accession number(s): D3DRA3
, F5H7H0, Q5TA03, Q7Z3T2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3