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Q9H4Y5

- GSTO2_HUMAN

UniProt

Q9H4Y5 - GSTO2_HUMAN

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Protein

Glutathione S-transferase omega-2

Gene

GSTO2

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

Functioni

Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 7.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei32 – 321Nucleophile
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-EC
  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. oxidation-reduction process Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
  6. vitamin metabolic process Source: Reactome
  7. water-soluble vitamin metabolic process Source: Reactome
  8. xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 2681.
ReactomeiREACT_11202. Vitamin C (ascorbate) metabolism.
REACT_6926. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase omega-2 (EC:2.5.1.18)
Short name:
GSTO-2
Alternative name(s):
Glutathione S-transferase omega 2-2
Short name:
GSTO 2-2
Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
Monomethylarsonic acid reductase (EC:1.20.4.2)
Short name:
MMA(V) reductase
Gene namesi
Name:GSTO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:23064. GSTO2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341Y → A: Abolishes DHAR activity. 1 Publication

Organism-specific databases

PharmGKBiPA133787053.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 243243Glutathione S-transferase omega-2PRO_0000185888Add
BLAST

Proteomic databases

PaxDbiQ9H4Y5.
PRIDEiQ9H4Y5.

PTM databases

PhosphoSiteiQ9H4Y5.

Expressioni

Tissue specificityi

Expressed in a range of tissues, including the liver, kidney, skeletal muscle and prostate. Strongest expression in the testis.1 Publication

Gene expression databases

BgeeiQ9H4Y5.
CleanExiHS_GSTO2.
GenevestigatoriQ9H4Y5.

Organism-specific databases

HPAiHPA048141.

Interactioni

Protein-protein interaction databases

BioGridi125638. 1 interaction.
STRINGi9606.ENSP00000345023.

Structurei

Secondary structure

1
243
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 285Combined sources
Helixi33 – 4412Combined sources
Beta strandi49 – 546Combined sources
Beta strandi56 – 583Combined sources
Helixi61 – 655Combined sources
Beta strandi74 – 763Combined sources
Beta strandi82 – 854Combined sources
Helixi86 – 9611Combined sources
Helixi107 – 11913Combined sources
Turni120 – 1223Combined sources
Helixi123 – 13614Combined sources
Helixi141 – 16121Combined sources
Beta strandi168 – 1703Combined sources
Helixi173 – 18311Combined sources
Helixi185 – 1884Combined sources
Helixi191 – 1944Combined sources
Helixi198 – 20811Combined sources
Helixi211 – 2166Combined sources
Helixi220 – 23112Combined sources
Helixi235 – 2384Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q18X-ray1.70A/B1-239[»]
3Q19X-ray1.90A/B1-239[»]
3QAGX-ray2.00A1-239[»]
ProteinModelPortaliQ9H4Y5.
SMRiQ9H4Y5. Positions 4-239.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 10180GST N-terminalAdd
BLAST
Domaini106 – 231126GST 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.
InParanoidiQ9H4Y5.
KOiK00799.
OMAiFCNLEEI.
OrthoDBiEOG71CFNG.
PhylomeDBiQ9H4Y5.
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.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. 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.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H4Y5-1) [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
MSGDATRTLG KGSQPPGPVP EGLIRIYSMR FCPYSHRTRL VLKAKDIRHE
60 70 80 90 100
VVNINLRNKP EWYYTKHPFG HIPVLETSQC QLIYESVIAC EYLDDAYPGR
110 120 130 140 150
KLFPYDPYER ARQKMLLELF CKVPHLTKEC LVALRCGREC TNLKAALRQE
160 170 180 190 200
FSNLEEILEY QNTTFFGGTC ISMIDYLLWP WFERLDVYGI LDCVSHTPAL
210 220 230 240
RLWISAMKWD PTVCALLMDK SIFQGFLNLY FQNNPNAFDF GLC
Length:243
Mass (Da):28,254
Last modified:March 1, 2001 - v1
Checksum:i45A959432BCF490A
GO
Isoform 2 (identifier: Q9H4Y5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-156: Missing.

Note: No experimental confirmation available.

Show »
Length:209
Mass (Da):24,399
Checksum:i4FEFB66449685934
GO
Isoform 3 (identifier: Q9H4Y5-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:215
Mass (Da):25,387
Checksum:iA04CD756F6EB962F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2151A → V in AAP47743. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti130 – 1301C → Y.
Corresponds to variant rs45582439 [ dbSNP | Ensembl ].
VAR_049492
Natural varianti142 – 1421N → D.1 Publication
Corresponds to variant rs156697 [ dbSNP | Ensembl ].
VAR_016812

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform 3. 1 PublicationVSP_045267Add
BLAST
Alternative sequencei123 – 15634Missing in isoform 2. 1 PublicationVSP_042567Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY350731 mRNA. Translation: AAR02452.1.
AY209189 mRNA. Translation: AAP47743.1.
AK291886 mRNA. Translation: BAF84575.1.
AK296266 mRNA. Translation: BAG58978.1.
AL139341 Genomic DNA. No translation available.
AL162742 Genomic DNA. Translation: CAC16040.1.
AL162742 Genomic DNA. Translation: CAI12107.1.
CH471066 Genomic DNA. Translation: EAW49600.1.
BC046194 mRNA. No translation available.
BC056918 mRNA. Translation: AAH56918.1.
AY191318 mRNA. Translation: AAO23573.1.
CCDSiCCDS53574.1. [Q9H4Y5-2]
CCDS53575.1. [Q9H4Y5-3]
CCDS7556.1. [Q9H4Y5-1]
RefSeqiNP_001177942.1. NM_001191013.1. [Q9H4Y5-2]
NP_001177943.1. NM_001191014.1. [Q9H4Y5-3]
NP_001177944.1. NM_001191015.1.
NP_899062.1. NM_183239.1. [Q9H4Y5-1]
XP_006717686.1. XM_006717623.1. [Q9H4Y5-1]
UniGeneiHs.107384.
Hs.203634.

Genome annotation databases

EnsembliENST00000338595; ENSP00000345023; ENSG00000065621. [Q9H4Y5-1]
ENST00000369707; ENSP00000358721; ENSG00000065621. [Q9H4Y5-3]
ENST00000450629; ENSP00000390986; ENSG00000065621. [Q9H4Y5-2]
GeneIDi119391.
KEGGihsa:119391.
UCSCiuc001kyb.3. human. [Q9H4Y5-1]
uc010qqx.2. human. [Q9H4Y5-2]

Polymorphism databases

DMDMi34922124.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY350731 mRNA. Translation: AAR02452.1 .
AY209189 mRNA. Translation: AAP47743.1 .
AK291886 mRNA. Translation: BAF84575.1 .
AK296266 mRNA. Translation: BAG58978.1 .
AL139341 Genomic DNA. No translation available.
AL162742 Genomic DNA. Translation: CAC16040.1 .
AL162742 Genomic DNA. Translation: CAI12107.1 .
CH471066 Genomic DNA. Translation: EAW49600.1 .
BC046194 mRNA. No translation available.
BC056918 mRNA. Translation: AAH56918.1 .
AY191318 mRNA. Translation: AAO23573.1 .
CCDSi CCDS53574.1. [Q9H4Y5-2 ]
CCDS53575.1. [Q9H4Y5-3 ]
CCDS7556.1. [Q9H4Y5-1 ]
RefSeqi NP_001177942.1. NM_001191013.1. [Q9H4Y5-2 ]
NP_001177943.1. NM_001191014.1. [Q9H4Y5-3 ]
NP_001177944.1. NM_001191015.1.
NP_899062.1. NM_183239.1. [Q9H4Y5-1 ]
XP_006717686.1. XM_006717623.1. [Q9H4Y5-1 ]
UniGenei Hs.107384.
Hs.203634.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3Q18 X-ray 1.70 A/B 1-239 [» ]
3Q19 X-ray 1.90 A/B 1-239 [» ]
3QAG X-ray 2.00 A 1-239 [» ]
ProteinModelPortali Q9H4Y5.
SMRi Q9H4Y5. Positions 4-239.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125638. 1 interaction.
STRINGi 9606.ENSP00000345023.

Chemistry

ChEMBLi CHEMBL2161.
DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei Q9H4Y5.

Polymorphism databases

DMDMi 34922124.

Proteomic databases

PaxDbi Q9H4Y5.
PRIDEi Q9H4Y5.

Protocols and materials databases

DNASUi 119391.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338595 ; ENSP00000345023 ; ENSG00000065621 . [Q9H4Y5-1 ]
ENST00000369707 ; ENSP00000358721 ; ENSG00000065621 . [Q9H4Y5-3 ]
ENST00000450629 ; ENSP00000390986 ; ENSG00000065621 . [Q9H4Y5-2 ]
GeneIDi 119391.
KEGGi hsa:119391.
UCSCi uc001kyb.3. human. [Q9H4Y5-1 ]
uc010qqx.2. human. [Q9H4Y5-2 ]

Organism-specific databases

CTDi 119391.
GeneCardsi GC10P106018.
HGNCi HGNC:23064. GSTO2.
HPAi HPA048141.
MIMi 612314. gene.
neXtProti NX_Q9H4Y5.
PharmGKBi PA133787053.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0625.
GeneTreei ENSGT00390000005479.
HOGENOMi HOG000006560.
HOVERGENi HBG051853.
InParanoidi Q9H4Y5.
KOi K00799.
OMAi FCNLEEI.
OrthoDBi EOG71CFNG.
PhylomeDBi Q9H4Y5.
TreeFami TF105325.

Enzyme and pathway databases

BRENDAi 2.5.1.18. 2681.
Reactomei REACT_11202. Vitamin C (ascorbate) metabolism.
REACT_6926. Glutathione conjugation.

Miscellaneous databases

ChiTaRSi GSTO2. human.
GeneWikii GSTO2.
GenomeRNAii 119391.
NextBioi 80409.
PROi Q9H4Y5.
SOURCEi Search...

Gene expression databases

Bgeei Q9H4Y5.
CleanExi HS_GSTO2.
Genevestigatori Q9H4Y5.

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.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami 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 and characterization of human GSTO-2 gene."
    Wang L., Xie Y., Mao Y.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Xu J., Xie Y., Mao Y.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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 T.-O., 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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Skeletal muscle and Thalamus.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 3).
    Tissue: Brain and Pancreatic carcinoma.
  7. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 3-243 (ISOFORM 1), VARIANT ASP-142, TISSUE SPECIFICITY.
    Tissue: Testis.
  8. "Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: implications for arsenic metabolism and the age-at-onset of Alzheimer's and Parkinson's diseases."
    Schmuck E.M., Board P.G., Whitbread A.K., Tetlow N., Cavanaugh J.A., Blackburn A.C., Masoumi A.
    Pharmacogenet. Genomics 15:493-501(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
  9. "Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases."
    Zhou H., Brock J., Liu D., Board P.G., Oakley A.J.
    J. Mol. Biol. 420:190-203(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-239 ALONE AND IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-34.

Entry informationi

Entry nameiGSTO2_HUMAN
AccessioniPrimary (citable) accession number: Q9H4Y5
Secondary accession number(s): A8K771
, B4DJW6, E7ESD6, Q49TW5, Q5GM70, Q5JU15, Q86WP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 119 of the entry and version 1 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, 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