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Protein

Glutathione S-transferase omega-2

Gene

GSTO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 Publications
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.2 Publications
Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei32Nucleophile1
Binding sitei59Glutathione1 Publication1
Binding sitei72Glutathione; via amide nitrogen and carbonyl oxygen1 Publication1

GO - Molecular functioni

  • glutathione dehydrogenase (ascorbate) activity Source: UniProtKB
  • glutathione transferase activity Source: GO_Central
  • methylarsonate reductase activity Source: UniProtKB-EC
  • oxidoreductase activity Source: UniProtKB

GO - Biological processi

  • cellular response to arsenic-containing substance Source: UniProtKB
  • glutathione derivative biosynthetic process Source: Reactome
  • glutathione metabolic process Source: GO_Central
  • L-ascorbic acid metabolic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Enzyme and pathway databases

BioCyciZFISH:HS00851-MONOMER.
BRENDAi1.8.5.1. 2681.
2.5.1.18. 2681.
ReactomeiR-HSA-156590. Glutathione conjugation.
R-HSA-196836. Vitamin C (ascorbate) metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase omega-2 (EC:2.5.1.182 Publications)
Short name:
GSTO-2
Alternative name(s):
Glutathione S-transferase omega 2-2
Short name:
GSTO 2-2
Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.12 Publications)
Monomethylarsonic acid reductase (EC:1.20.4.21 Publication)
Short name:
MMA(V) reductase
Gene namesi
Name:GSTO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:23064. GSTO2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi34Y → A: Abolishes DHAR activity. 1 Publication1

Organism-specific databases

DisGeNETi119391.
OpenTargetsiENSG00000065621.
PharmGKBiPA133787053.

Chemistry databases

ChEMBLiCHEMBL2161.
DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGSTO2.
DMDMi34922124.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001858881 – 243Glutathione S-transferase omega-2Add BLAST243

Proteomic databases

PaxDbiQ9H4Y5.
PeptideAtlasiQ9H4Y5.
PRIDEiQ9H4Y5.

PTM databases

iPTMnetiQ9H4Y5.
PhosphoSitePlusiQ9H4Y5.

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

BgeeiENSG00000065621.
CleanExiHS_GSTO2.
GenevisibleiQ9H4Y5. HS.

Organism-specific databases

HPAiHPA048141.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-10194609,EBI-10194609
MUM1Q9H6H23EBI-10194609,EBI-10307610
TFAP2AP055493EBI-10194609,EBI-347351

Protein-protein interaction databases

BioGridi125638. 13 interactors.
IntActiQ9H4Y5. 3 interactors.
STRINGi9606.ENSP00000345023.

Structurei

Secondary structure

1243
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 28Combined sources5
Helixi33 – 44Combined sources12
Beta strandi49 – 54Combined sources6
Beta strandi56 – 58Combined sources3
Helixi61 – 65Combined sources5
Beta strandi74 – 76Combined sources3
Beta strandi82 – 85Combined sources4
Helixi86 – 96Combined sources11
Helixi107 – 119Combined sources13
Turni120 – 122Combined sources3
Helixi123 – 136Combined sources14
Helixi141 – 161Combined sources21
Beta strandi168 – 170Combined sources3
Helixi173 – 183Combined sources11
Helixi185 – 188Combined sources4
Helixi191 – 194Combined sources4
Helixi198 – 208Combined sources11
Helixi211 – 216Combined sources6
Helixi220 – 231Combined sources12
Helixi235 – 238Combined sources4

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 101GST N-terminalAdd BLAST80
Domaini106 – 231GST C-terminalAdd BLAST126

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni85 – 86Glutathione binding1 Publication2

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

eggNOGiKOG0406. Eukaryota.
ENOG410XSIX. LUCA.
GeneTreeiENSGT00390000005479.
HOGENOMiHOG000006560.
HOVERGENiHBG051853.
InParanoidiQ9H4Y5.
KOiK00799.
OMAiYFQNNPN.
OrthoDBiEOG091G0IEA.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti215A → V in AAP47743 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049492130C → Y.Corresponds to variant rs45582439dbSNPEnsembl.1
Natural variantiVAR_016812142N → D.1 PublicationCorresponds to variant rs156697dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0452671 – 28Missing in isoform 3. 1 PublicationAdd BLAST28
Alternative sequenceiVSP_042567123 – 156Missing in isoform 2. 1 PublicationAdd BLAST34

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_011537572.1. XM_011539270.2. [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.4. human. [Q9H4Y5-1]

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.
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_011537572.1. XM_011539270.2. [Q9H4Y5-1]
UniGeneiHs.107384.
Hs.203634.

3D structure databases

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

Protein-protein interaction databases

BioGridi125638. 13 interactors.
IntActiQ9H4Y5. 3 interactors.
STRINGi9606.ENSP00000345023.

Chemistry databases

ChEMBLiCHEMBL2161.
DrugBankiDB00143. Glutathione.

PTM databases

iPTMnetiQ9H4Y5.
PhosphoSitePlusiQ9H4Y5.

Polymorphism and mutation databases

BioMutaiGSTO2.
DMDMi34922124.

Proteomic databases

PaxDbiQ9H4Y5.
PeptideAtlasiQ9H4Y5.
PRIDEiQ9H4Y5.

Protocols and materials databases

DNASUi119391.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338595; ENSP00000345023; ENSG00000065621. [Q9H4Y5-1]
ENST00000369707; ENSP00000358721; ENSG00000065621. [Q9H4Y5-3]
ENST00000450629; ENSP00000390986; ENSG00000065621. [Q9H4Y5-2]
GeneIDi119391.
KEGGihsa:119391.
UCSCiuc001kyb.4. human. [Q9H4Y5-1]

Organism-specific databases

CTDi119391.
DisGeNETi119391.
GeneCardsiGSTO2.
HGNCiHGNC:23064. GSTO2.
HPAiHPA048141.
MIMi612314. gene.
neXtProtiNX_Q9H4Y5.
OpenTargetsiENSG00000065621.
PharmGKBiPA133787053.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0406. Eukaryota.
ENOG410XSIX. LUCA.
GeneTreeiENSGT00390000005479.
HOGENOMiHOG000006560.
HOVERGENiHBG051853.
InParanoidiQ9H4Y5.
KOiK00799.
OMAiYFQNNPN.
OrthoDBiEOG091G0IEA.
PhylomeDBiQ9H4Y5.
TreeFamiTF105325.

Enzyme and pathway databases

BioCyciZFISH:HS00851-MONOMER.
BRENDAi1.8.5.1. 2681.
2.5.1.18. 2681.
ReactomeiR-HSA-156590. Glutathione conjugation.
R-HSA-196836. Vitamin C (ascorbate) metabolism.

Miscellaneous databases

ChiTaRSiGSTO2. human.
GeneWikiiGSTO2.
GenomeRNAii119391.
PROiQ9H4Y5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000065621.
CleanExiHS_GSTO2.
GenevisibleiQ9H4Y5. HS.

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]
ProtoNetiSearch...

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 30, 2016
This is version 139 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.