GSTA1

Protein identityUniProt · HPA

UniProt accession

P08263

Gene

GSTA1

Ensembl

ENSG00000243955

Chromosome

6

Canonical length

222 aa

Protein class

Enzymes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins

Subcellular location

Cytosol

Quaternary structure

Homodimer

OverviewNCBI Gene

This gene encodes a member of a family of enzymes that function to add glutathione to target electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. This action is an important step in detoxification of these compounds. This subfamily of enzymes has a particular role in protecting cells from reactive oxygen species and the products of peroxidation. Polymorphisms in this gene influence the ability of individuals to metabolize different drugs. This gene is located in a cluster of similar genes and pseudogenes on chromosome 6. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2016]

Canonical amino-acid sequenceUniProt

222 residues, UniProt reviewed canonical sequence.

>P08263|GSTA1
     1  MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI
    61  DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA DLGEMILLLP VCPPEEKDAK
   121  LALIKEKIKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL
   181  LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEEARKIF RF

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against GSTA1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.28

Highest tissue expression

2,439 nTPM

Expression across tissuesHPA

ReferencesPubMed · IEDB

Publications for GSTA1 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1.63

gnomAD pLI

0

gnomAD missense Z

-1.6

DepMap mean gene effect

-0.11

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• epithelial cell differentiation
• glutathione derivative biosynthetic process
• glutathione metabolic process
• linoleic acid metabolic process
• prostaglandin metabolic process
• xenobiotic metabolic process

Molecular functions

• fatty acid binding
• glutathione peroxidase activity
• glutathione transferase activity
• steroid Delta-isomerase activity

Cellular components

• cytosol
• extracellular exosome

Protein domainsUniProt · Pfam · InterPro

• Glutathione S-transferase, alpha class
• Glutathione S-transferase, N-terminal
• Glutathione S-transferase, C-terminal
• Glutathione S-transferase, C-terminal-like
• Thioredoxin-like superfamily
• Glutathione S-transferase, C-terminal domain superfamily
• Glutathione transferase family
• Glutathione S-transferase superfamily
• Glutathione S-transferase, C-terminal domain
• Glutathione S-transferase, N-terminal domain

KeywordsUniProt

• Acetylation
• Cytoplasm
• Isomerase
• Lipid metabolism
• Oxidoreductase
• Peroxidase
• Transferase