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Q9H4Y5 (GSTO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase omega-2

Short name=GSTO-2
EC=2.5.1.18
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
Short name=MMA(V) reductase
EC=1.20.4.2
Gene names
Name:GSTO2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.8

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.8 Ref.9

2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate. Ref.8 Ref.9

Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O. Ref.8 Ref.9

Tissue specificity

Expressed in a range of tissues, including the liver, kidney, skeletal muscle and prostate. Strongest expression in the testis. Ref.7

Sequence similarities

Belongs to the GST superfamily. Omega family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5. Ref.8

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H4Y5-1)

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.
Isoform 2 (identifier: Q9H4Y5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     123-156: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9H4Y5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 243243Glutathione S-transferase omega-2
PRO_0000185888

Regions

Domain22 – 10180GST N-terminal
Domain106 – 231126GST C-terminal
Region85 – 862Glutathione binding

Sites

Active site321Nucleophile
Binding site591Glutathione
Binding site721Glutathione; via amide nitrogen and carbonyl oxygen

Natural variations

Alternative sequence1 – 2828Missing in isoform 3.
VSP_045267
Alternative sequence123 – 15634Missing in isoform 2.
VSP_042567
Natural variant1301C → Y.
Corresponds to variant rs45582439 [ dbSNP | Ensembl ].
VAR_049492
Natural variant1421N → D. Ref.7
Corresponds to variant rs156697 [ dbSNP | Ensembl ].
VAR_016812

Experimental info

Mutagenesis341Y → A: Abolishes DHAR activity. Ref.9
Sequence conflict2151A → V in AAP47743. Ref.2

Secondary structure

...................................... 243
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 45A959432BCF490A

FASTA24328,254
        10         20         30         40         50         60 
MSGDATRTLG KGSQPPGPVP EGLIRIYSMR FCPYSHRTRL VLKAKDIRHE VVNINLRNKP 

        70         80         90        100        110        120 
EWYYTKHPFG HIPVLETSQC QLIYESVIAC EYLDDAYPGR KLFPYDPYER ARQKMLLELF 

       130        140        150        160        170        180 
CKVPHLTKEC LVALRCGREC TNLKAALRQE FSNLEEILEY QNTTFFGGTC ISMIDYLLWP 

       190        200        210        220        230        240 
WFERLDVYGI LDCVSHTPAL RLWISAMKWD PTVCALLMDK SIFQGFLNLY FQNNPNAFDF 


GLC 

« Hide

Isoform 2 [UniParc].

Checksum: 4FEFB66449685934
Show »

FASTA20924,399
Isoform 3 [UniParc].

Checksum: A04CD756F6EB962F
Show »

FASTA21525,387

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001177942.1. NM_001191013.1.
NP_001177943.1. NM_001191014.1.
NP_001177944.1. NM_001191015.1.
NP_899062.1. NM_183239.1.
UniGeneHs.203634.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q18X-ray1.70A/B1-239[»]
3Q19X-ray1.90A/B1-239[»]
3QAGX-ray2.00A1-239[»]
ProteinModelPortalQ9H4Y5.
SMRQ9H4Y5. Positions 4-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125638. 1 interaction.
STRING9606.ENSP00000345023.

Chemistry

ChEMBLCHEMBL2161.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteQ9H4Y5.

Polymorphism databases

DMDM34922124.

Proteomic databases

PaxDbQ9H4Y5.
PRIDEQ9H4Y5.

Protocols and materials databases

DNASU119391.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338595; ENSP00000345023; ENSG00000065621. [Q9H4Y5-1]
ENST00000369707; ENSP00000358721; ENSG00000065621. [Q9H4Y5-3]
ENST00000450629; ENSP00000390986; ENSG00000065621. [Q9H4Y5-2]
GeneID119391.
KEGGhsa:119391.
UCSCuc001kyb.3. human. [Q9H4Y5-1]
uc010qqx.2. human. [Q9H4Y5-2]

Organism-specific databases

CTD119391.
GeneCardsGC10P106018.
HGNCHGNC:23064. GSTO2.
HPAHPA048141.
MIM612314. gene.
neXtProtNX_Q9H4Y5.
PharmGKBPA133787053.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000006560.
HOVERGENHBG051853.
InParanoidQ9H4Y5.
KOK00799.
OMAFCNLEEI.
OrthoDBEOG71CFNG.
PhylomeDBQ9H4Y5.
TreeFamTF105325.

Enzyme and pathway databases

BRENDA2.5.1.18. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ9H4Y5.
BgeeQ9H4Y5.
CleanExHS_GSTO2.
GenevestigatorQ9H4Y5.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF13417. GST_N_3. 1 hit.
[Graphical view]
PRINTSPR01625. GSTRNSFRASEO.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGSTO2.
GenomeRNAi119391.
NextBio80409.
PROQ9H4Y5.
SOURCESearch...

Entry information

Entry nameGSTO2_HUMAN
AccessionPrimary (citable) accession number: Q9H4Y5
Secondary accession number(s): A8K771 expand/collapse secondary AC list , B4DJW6, E7ESD6, Q49TW5, Q5GM70, Q5JU15, Q86WP3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM