Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione S-transferase A1

Gene

GSTA1

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

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei9Glutathione2 Publications1
Binding sitei45Glutathione2 Publications1

GO - Molecular functioni

  • glutathione peroxidase activity Source: BHF-UCL
  • glutathione transferase activity Source: UniProtKB

GO - Biological processi

  • epithelial cell differentiation Source: UniProtKB
  • glutathione derivative biosynthetic process Source: Reactome
  • glutathione metabolic process Source: UniProtKB
  • linoleic acid metabolic process Source: BHF-UCL
  • metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:G66-32542-MONOMER.
ZFISH:G66-32542-MONOMER.
BRENDAi2.5.1.18. 2681.
ReactomeiR-HSA-156590. Glutathione conjugation.
SABIO-RKP08263.

Chemistry databases

SwissLipidsiSLP:000001476.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase A1 (EC:2.5.1.18)
Alternative name(s):
GST HA subunit 1
GST class-alpha member 1
GST-epsilon
GSTA1-1
GTH1
Cleaved into the following chain:
Gene namesi
Name:GSTA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4626. GSTA1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi71I → A or V: No significant effect on enzyme activity. Reduces protein stability. 1 Publication1
Mutagenesisi216A → H: Confers ability to hydrolyze S-glutathionyl benzoate to glutathione and benzoic acid. 1 Publication1

Organism-specific databases

DisGeNETi2938.
OpenTargetsiENSG00000243955.
PharmGKBiPA29016.

Chemistry databases

ChEMBLiCHEMBL3409.
DrugBankiDB00993. Azathioprine.
DB01008. Busulfan.
DB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGSTA1.
DMDMi121730.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004232031 – 222Glutathione S-transferase A1Add BLAST222
Initiator methionineiRemoved; alternateBy similarity1 Publication
ChainiPRO_00001857832 – 222Glutathione S-transferase A1, N-terminally processedAdd BLAST221

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylalanine; in Glutathione S-transferase A1, N-terminally processedBy similarity1
Modified residuei4N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP08263.
PaxDbiP08263.
PeptideAtlasiP08263.
PRIDEiP08263.

2D gel databases

REPRODUCTION-2DPAGEIPI00657682.

PTM databases

iPTMnetiP08263.
PhosphoSitePlusiP08263.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSG00000243955.
CleanExiHS_GSTA1.
ExpressionAtlasiP08263. baseline and differential.
GenevisibleiP08263. HS.

Organism-specific databases

HPAiHPA004342.
HPA048934.
HPA053817.

Interactioni

Subunit structurei

Homodimer or heterodimer of GSTA1 and GSTA2.8 Publications

Protein-protein interaction databases

BioGridi109193. 15 interactors.
IntActiP08263. 6 interactors.
MINTiMINT-5000131.
STRINGi9606.ENSP00000335620.

Chemistry databases

BindingDBiP08263.

Structurei

Secondary structure

1222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 13Combined sources8
Turni14 – 16Combined sources3
Helixi17 – 26Combined sources10
Beta strandi31 – 35Combined sources5
Helixi38 – 46Combined sources9
Beta strandi57 – 60Combined sources4
Beta strandi63 – 67Combined sources5
Helixi68 – 78Combined sources11
Helixi86 – 108Combined sources23
Helixi109 – 111Combined sources3
Helixi114 – 130Combined sources17
Helixi132 – 143Combined sources12
Beta strandi146 – 149Combined sources4
Helixi155 – 170Combined sources16
Turni172 – 177Combined sources6
Helixi179 – 190Combined sources12
Helixi192 – 198Combined sources7
Helixi210 – 220Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GSDX-ray2.50A/B/C/D2-222[»]
1GSEX-ray2.00A/B2-222[»]
1GSFX-ray2.70A/B/C/D2-222[»]
1GUHX-ray2.60A/B/C/D2-222[»]
1K3LX-ray1.50A/B2-222[»]
1K3OX-ray1.80A/B2-222[»]
1K3YX-ray1.30A/B2-222[»]
1LBKX-ray1.86A/B208-213[»]
1PKWX-ray2.00A/B1-222[»]
1PKZX-ray2.10A/B1-222[»]
1PL1X-ray1.75A/B1-222[»]
1PL2X-ray1.80A/B1-222[»]
1USBX-ray2.07A/B2-222[»]
1XWGX-ray1.85A/B2-222[»]
1YDKX-ray1.95A/B1-222[»]
2R3XX-ray1.80A/B1-222[»]
2R6KX-ray2.51A/B1-222[»]
3I69X-ray2.38A/B/C/D/E/F/G/H1-222[»]
3I6AX-ray1.98A/B/C/D/E/F/G/H1-222[»]
3IK9X-ray2.20A/B/C/D/E/F/G/H1-222[»]
3KTLX-ray1.75A/B2-222[»]
3L0HX-ray2.13A/B1-222[»]
3Q74X-ray1.79A/B2-222[»]
3U6VX-ray2.20A/B1-222[»]
3ZFBX-ray1.86A/B1-222[»]
3ZFLX-ray1.88A/B1-222[»]
4HJ2X-ray2.10A/B4-220[»]
5JCUX-ray1.93A/B/C/D2-222[»]
5LCZX-ray2.33A/B1-100[»]
A/B201-222[»]
5LD0X-ray1.60A1-85[»]
A214-222[»]
ProteinModelPortaliP08263.
SMRiP08263.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08263.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 83GST N-terminalAdd BLAST81
Domaini85 – 207GST C-terminalAdd BLAST123

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 55Glutathione binding2 Publications2
Regioni67 – 68Glutathione binding2 Publications2

Domaini

The C-terminal domain may form a component of the hydrophobic substrate-binding site, but in contrast appears not to be directly involved in GSH binding and is not absolutely essential for catalytic activity.

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiKOG1695. Eukaryota.
ENOG4111VAU. LUCA.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiP08263.
KOiK00799.
OMAiFIEQPED.
OrthoDBiEOG091G0O3D.
PhylomeDBiP08263.
TreeFamiTF105321.

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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08263-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL
60 70 80 90 100
MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA
110 120 130 140 150
DLGEMILLLP VCPPEEKDAK LALIKEKIKN RYFPAFEKVL KSHGQDYLVG
160 170 180 190 200
NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP
210 220
GSPRKPPMDE KSLEEARKIF RF
Length:222
Mass (Da):25,631
Last modified:January 23, 2007 - v3
Checksum:iC8B6786DCD761350
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18S → C in AAA36174 (PubMed:3678589).Curated1
Sequence conflicti51M → T in AAT06769 (Ref. 7) Curated1
Sequence conflicti56 – 58PMV → AML in AAA36174 (PubMed:3678589).Curated3
Sequence conflicti212S → L AA sequence (PubMed:2604726).Curated1
Sequence conflicti216A → S AA sequence (PubMed:8431482).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03397819T → I.Corresponds to variant rs1051578dbSNPEnsembl.1
Natural variantiVAR_049482113P → Q.Corresponds to variant rs1051745dbSNPEnsembl.1
Natural variantiVAR_049483117K → Q.Corresponds to variant rs1051757dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15872 mRNA. Translation: AAA70226.1.
M21758 mRNA. Translation: AAA52615.1.
M25627 mRNA. Translation: AAA36174.1.
M14777 mRNA. Translation: AAA52618.1.
S76235
, S76221, S76223, S76225, S76228, S76232 Genomic DNA. Translation: AAB20973.1.
S49975 mRNA. Translation: AAB24012.1.
AY532928 mRNA. Translation: AAT06769.1.
CR407656 mRNA. Translation: CAG28584.1.
AL590363 Genomic DNA. Translation: CAI13812.1.
CH471081 Genomic DNA. Translation: EAX04385.1.
BC053578 mRNA. Translation: AAH53578.1.
BC110891 mRNA. Translation: AAI10892.1.
CCDSiCCDS4945.1.
PIRiA25909. A56666.
S29657.
RefSeqiNP_665683.1. NM_145740.4.
UniGeneiHs.446309.

Genome annotation databases

EnsembliENST00000334575; ENSP00000335620; ENSG00000243955.
GeneIDi2938.
KEGGihsa:2938.
UCSCiuc003paz.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15872 mRNA. Translation: AAA70226.1.
M21758 mRNA. Translation: AAA52615.1.
M25627 mRNA. Translation: AAA36174.1.
M14777 mRNA. Translation: AAA52618.1.
S76235
, S76221, S76223, S76225, S76228, S76232 Genomic DNA. Translation: AAB20973.1.
S49975 mRNA. Translation: AAB24012.1.
AY532928 mRNA. Translation: AAT06769.1.
CR407656 mRNA. Translation: CAG28584.1.
AL590363 Genomic DNA. Translation: CAI13812.1.
CH471081 Genomic DNA. Translation: EAX04385.1.
BC053578 mRNA. Translation: AAH53578.1.
BC110891 mRNA. Translation: AAI10892.1.
CCDSiCCDS4945.1.
PIRiA25909. A56666.
S29657.
RefSeqiNP_665683.1. NM_145740.4.
UniGeneiHs.446309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GSDX-ray2.50A/B/C/D2-222[»]
1GSEX-ray2.00A/B2-222[»]
1GSFX-ray2.70A/B/C/D2-222[»]
1GUHX-ray2.60A/B/C/D2-222[»]
1K3LX-ray1.50A/B2-222[»]
1K3OX-ray1.80A/B2-222[»]
1K3YX-ray1.30A/B2-222[»]
1LBKX-ray1.86A/B208-213[»]
1PKWX-ray2.00A/B1-222[»]
1PKZX-ray2.10A/B1-222[»]
1PL1X-ray1.75A/B1-222[»]
1PL2X-ray1.80A/B1-222[»]
1USBX-ray2.07A/B2-222[»]
1XWGX-ray1.85A/B2-222[»]
1YDKX-ray1.95A/B1-222[»]
2R3XX-ray1.80A/B1-222[»]
2R6KX-ray2.51A/B1-222[»]
3I69X-ray2.38A/B/C/D/E/F/G/H1-222[»]
3I6AX-ray1.98A/B/C/D/E/F/G/H1-222[»]
3IK9X-ray2.20A/B/C/D/E/F/G/H1-222[»]
3KTLX-ray1.75A/B2-222[»]
3L0HX-ray2.13A/B1-222[»]
3Q74X-ray1.79A/B2-222[»]
3U6VX-ray2.20A/B1-222[»]
3ZFBX-ray1.86A/B1-222[»]
3ZFLX-ray1.88A/B1-222[»]
4HJ2X-ray2.10A/B4-220[»]
5JCUX-ray1.93A/B/C/D2-222[»]
5LCZX-ray2.33A/B1-100[»]
A/B201-222[»]
5LD0X-ray1.60A1-85[»]
A214-222[»]
ProteinModelPortaliP08263.
SMRiP08263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109193. 15 interactors.
IntActiP08263. 6 interactors.
MINTiMINT-5000131.
STRINGi9606.ENSP00000335620.

Chemistry databases

BindingDBiP08263.
ChEMBLiCHEMBL3409.
DrugBankiDB00993. Azathioprine.
DB01008. Busulfan.
DB00143. Glutathione.
SwissLipidsiSLP:000001476.

PTM databases

iPTMnetiP08263.
PhosphoSitePlusiP08263.

Polymorphism and mutation databases

BioMutaiGSTA1.
DMDMi121730.

2D gel databases

REPRODUCTION-2DPAGEIPI00657682.

Proteomic databases

MaxQBiP08263.
PaxDbiP08263.
PeptideAtlasiP08263.
PRIDEiP08263.

Protocols and materials databases

DNASUi2938.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334575; ENSP00000335620; ENSG00000243955.
GeneIDi2938.
KEGGihsa:2938.
UCSCiuc003paz.4. human.

Organism-specific databases

CTDi2938.
DisGeNETi2938.
GeneCardsiGSTA1.
HGNCiHGNC:4626. GSTA1.
HPAiHPA004342.
HPA048934.
HPA053817.
MIMi138359. gene.
neXtProtiNX_P08263.
OpenTargetsiENSG00000243955.
PharmGKBiPA29016.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1695. Eukaryota.
ENOG4111VAU. LUCA.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiP08263.
KOiK00799.
OMAiFIEQPED.
OrthoDBiEOG091G0O3D.
PhylomeDBiP08263.
TreeFamiTF105321.

Enzyme and pathway databases

BioCyciMetaCyc:G66-32542-MONOMER.
ZFISH:G66-32542-MONOMER.
BRENDAi2.5.1.18. 2681.
ReactomeiR-HSA-156590. Glutathione conjugation.
SABIO-RKP08263.

Miscellaneous databases

ChiTaRSiGSTA1. human.
EvolutionaryTraceiP08263.
GeneWikiiGlutathione_S-transferase_A1.
GenomeRNAii2938.
PROiP08263.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000243955.
CleanExiHS_GSTA1.
ExpressionAtlasiP08263. baseline and differential.
GenevisibleiP08263. 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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSTA1_HUMAN
AccessioniPrimary (citable) accession number: P08263
Secondary accession number(s): Q14750, Q5GHF8, Q5SZC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 188 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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.