Q9H4Y5 · GSTO2_HUMAN
- ProteinGlutathione S-transferase omega-2
- GeneGSTO2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids243 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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).
Catalytic activity
- glutathione + RX = a halide anion + an S-substituted glutathione + H+
pH Dependence
Optimum pH is 7.5.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Molecular Function | glutathione dehydrogenase (ascorbate) activity | |
Molecular Function | glutathione transferase activity | |
Molecular Function | identical protein binding | |
Molecular Function | methylarsonate reductase activity | |
Molecular Function | oxidoreductase activity | |
Biological Process | cellular response to arsenic-containing substance | |
Biological Process | glutathione metabolic process | |
Biological Process | L-ascorbic acid metabolic process | |
Biological Process | xenobiotic metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione S-transferase omega-2
- EC number
- Short namesGSTO-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H4Y5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 34 | Abolishes DHAR activity. | ||||
Sequence: Y → A | ||||||
Natural variant | VAR_049492 | 130 | in dbSNP:rs45582439 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_016812 | 142 | in dbSNP:rs156697 | |||
Sequence: N → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 281 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000185888 | 1-243 | Glutathione S-transferase omega-2 | |||
Sequence: MSGDATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRKLFPYDPYERARQKMLLELFCKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWPWFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYFQNNPNAFDFGLC |
Proteomic databases
PTM databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H4Y5 | GCA P28676 | 3 | EBI-10194609, EBI-947242 | |
BINARY | Q9H4Y5 | GSTO2 Q9H4Y5 | 8 | EBI-10194609, EBI-10194609 | |
BINARY | Q9H4Y5 | HOXC8 P31273 | 3 | EBI-10194609, EBI-1752118 | |
BINARY | Q9H4Y5 | INCA1 Q0VD86 | 3 | EBI-10194609, EBI-6509505 | |
BINARY | Q9H4Y5 | KLHL10 Q6JEL2 | 3 | EBI-10194609, EBI-6426253 | |
BINARY | Q9H4Y5 | MUM1 Q9H6H2 | 3 | EBI-10194609, EBI-10307610 | |
BINARY | Q9H4Y5 | NTAQ1 Q96HA8 | 3 | EBI-10194609, EBI-741158 | |
BINARY | Q9H4Y5 | PFDN5 Q99471 | 3 | EBI-10194609, EBI-357275 | |
BINARY | Q9H4Y5 | POLR1C O15160 | 3 | EBI-10194609, EBI-1055079 | |
BINARY | Q9H4Y5 | SMARCC1 Q92922 | 3 | EBI-10194609, EBI-355653 | |
BINARY | Q9H4Y5 | TFAP2A P05549 | 4 | EBI-10194609, EBI-347351 | |
BINARY | Q9H4Y5 | TFAP2A P05549-5 | 6 | EBI-10194609, EBI-12194905 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-101 | GST N-terminal | ||||
Sequence: GLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRK | ||||||
Domain | 106-231 | GST C-terminal | ||||
Sequence: DPYERARQKMLLELFCKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWPWFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYF |
Sequence similarities
Belongs to the GST superfamily. Omega family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
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.
- Name1
- Length243
- Mass (Da)28,254
- Last updated2001-03-01 v1
- Checksum45A959432BCF490A
Q9H4Y5-2
- Name2
- Differences from canonical
- 123-156: Missing
Q9H4Y5-3
- Name3
- Differences from canonical
- 1-28: Missing
Features
Showing features for alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY350731 EMBL· GenBank· DDBJ | AAR02452.1 EMBL· GenBank· DDBJ | mRNA | ||
AY209189 EMBL· GenBank· DDBJ | AAP47743.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291886 EMBL· GenBank· DDBJ | BAF84575.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296266 EMBL· GenBank· DDBJ | BAG58978.1 EMBL· GenBank· DDBJ | mRNA | ||
AL139341 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL162742 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471066 EMBL· GenBank· DDBJ | EAW49600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC046194 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC056918 EMBL· GenBank· DDBJ | AAH56918.1 EMBL· GenBank· DDBJ | mRNA | ||
AY191318 EMBL· GenBank· DDBJ | AAO23573.1 EMBL· GenBank· DDBJ | mRNA |