Skip Header

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

P08263

- GSTA1_HUMAN

UniProt

P08263 - GSTA1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutathione S-transferase A1

Gene

GSTA1

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91Glutathione2 Publications
Binding sitei45 – 451Glutathione2 Publications

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. epithelial cell differentiation Source: UniProt
  2. glutathione derivative biosynthetic process Source: Reactome
  3. glutathione metabolic process Source: UniProtKB
  4. metabolic process Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
  6. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:G66-32542-MONOMER.
ReactomeiREACT_6926. Glutathione conjugation.
SABIO-RKP08263.

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
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4626. GSTA1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi71 – 711I → A or V: No significant effect on enzyme activity. Reduces protein stability. 1 Publication
Mutagenesisi216 – 2161A → H: Confers ability to hydrolyze S-glutathionyl benzoate to glutathione and benzoic acid. 1 Publication

Organism-specific databases

PharmGKBiPA29016.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Glutathione S-transferase A1PRO_0000423203Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 222221Glutathione S-transferase A1, N-terminally processedPRO_0000185783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP08263.
PaxDbiP08263.
PRIDEiP08263.

2D gel databases

REPRODUCTION-2DPAGEIPI00657682.

PTM databases

PhosphoSiteiP08263.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiP08263.
CleanExiHS_GSTA1.
GenevestigatoriP08263.

Organism-specific databases

HPAiHPA004342.
HPA053817.

Interactioni

Subunit structurei

Homodimer or heterodimer of GSTA1 and GSTA2.8 Publications

Protein-protein interaction databases

BioGridi109193. 13 interactions.
IntActiP08263. 6 interactions.
MINTiMINT-5000131.
STRINGi9606.ENSP00000335620.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 138
Turni14 – 163
Helixi17 – 2610
Beta strandi31 – 355
Helixi38 – 469
Beta strandi57 – 604
Beta strandi63 – 675
Helixi68 – 7811
Helixi86 – 10823
Helixi109 – 1113
Helixi114 – 13017
Helixi132 – 14312
Beta strandi146 – 1494
Helixi155 – 17016
Turni172 – 1776
Helixi179 – 19012
Helixi192 – 1987
Helixi210 – 22011

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP08263.
SMRiP08263. Positions 2-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08263.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8381GST N-terminalAdd
BLAST
Domaini85 – 207123GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 552Glutathione binding
Regioni67 – 682Glutathione binding

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

eggNOGiNOG266414.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiP08263.
KOiK00799.
OMAiDTNILAN.
OrthoDBiEOG79CZ0K.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181S → C in AAA36174. (PubMed:3678589)Curated
Sequence conflicti51 – 511M → T in AAT06769. 1 PublicationCurated
Sequence conflicti56 – 583PMV → AML in AAA36174. (PubMed:3678589)Curated
Sequence conflicti212 – 2121S → L AA sequence (PubMed:2604726)Curated
Sequence conflicti216 – 2161A → S AA sequence (PubMed:8431482)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191T → I.
Corresponds to variant rs1051578 [ dbSNP | Ensembl ].
VAR_033978
Natural varianti113 – 1131P → Q.
Corresponds to variant rs1051745 [ dbSNP | Ensembl ].
VAR_049482
Natural varianti117 – 1171K → Q.
Corresponds to variant rs1051757 [ dbSNP | Ensembl ].
VAR_049483

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_145740.3.
UniGeneiHs.446309.

Genome annotation databases

EnsembliENST00000334575; ENSP00000335620; ENSG00000243955.
GeneIDi2938.
KEGGihsa:2938.
UCSCiuc003paz.3. human.

Polymorphism databases

DMDMi121730.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4945.1.
PIRi A25909. A56666.
S29657.
RefSeqi NP_665683.1. NM_145740.3.
UniGenei Hs.446309.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GSD X-ray 2.50 A/B/C/D 2-222 [» ]
1GSE X-ray 2.00 A/B 2-222 [» ]
1GSF X-ray 2.70 A/B/C/D 2-222 [» ]
1GUH X-ray 2.60 A/B/C/D 2-222 [» ]
1K3L X-ray 1.50 A/B 2-222 [» ]
1K3O X-ray 1.80 A/B 2-222 [» ]
1K3Y X-ray 1.30 A/B 2-222 [» ]
1LBK X-ray 1.86 A/B 208-213 [» ]
1PKW X-ray 2.00 A/B 1-222 [» ]
1PKZ X-ray 2.10 A/B 1-222 [» ]
1PL1 X-ray 1.75 A/B 1-222 [» ]
1PL2 X-ray 1.80 A/B 1-222 [» ]
1USB X-ray 2.07 A/B 2-222 [» ]
1XWG X-ray 1.85 A/B 2-222 [» ]
1YDK X-ray 1.95 A/B 1-222 [» ]
2R3X X-ray 1.80 A/B 1-222 [» ]
2R6K X-ray 2.51 A/B 1-222 [» ]
3I69 X-ray 2.38 A/B/C/D/E/F/G/H 1-222 [» ]
3I6A X-ray 1.98 A/B/C/D/E/F/G/H 1-222 [» ]
3IK9 X-ray 2.20 A/B/C/D/E/F/G/H 1-222 [» ]
3KTL X-ray 1.75 A/B 2-222 [» ]
3L0H X-ray 2.13 A/B 1-222 [» ]
3Q74 X-ray 1.79 A/B 2-222 [» ]
3U6V X-ray 2.20 A/B 1-222 [» ]
3ZFB X-ray 1.86 A/B 1-222 [» ]
3ZFL X-ray 1.88 A/B 1-222 [» ]
4HJ2 X-ray 2.10 A/B 4-220 [» ]
ProteinModelPortali P08263.
SMRi P08263. Positions 2-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109193. 13 interactions.
IntActi P08263. 6 interactions.
MINTi MINT-5000131.
STRINGi 9606.ENSP00000335620.

Chemistry

BindingDBi P08263.
ChEMBLi CHEMBL3409.
DrugBanki DB00993. Azathioprine.
DB01008. Busulfan.
DB00143. Glutathione.

PTM databases

PhosphoSitei P08263.

Polymorphism databases

DMDMi 121730.

2D gel databases

REPRODUCTION-2DPAGE IPI00657682.

Proteomic databases

MaxQBi P08263.
PaxDbi P08263.
PRIDEi P08263.

Protocols and materials databases

DNASUi 2938.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334575 ; ENSP00000335620 ; ENSG00000243955 .
GeneIDi 2938.
KEGGi hsa:2938.
UCSCi uc003paz.3. human.

Organism-specific databases

CTDi 2938.
GeneCardsi GC06M052656.
HGNCi HGNC:4626. GSTA1.
HPAi HPA004342.
HPA053817.
MIMi 138359. gene.
neXtProti NX_P08263.
PharmGKBi PA29016.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266414.
GeneTreei ENSGT00670000097856.
HOGENOMi HOG000115734.
HOVERGENi HBG053749.
InParanoidi P08263.
KOi K00799.
OMAi DTNILAN.
OrthoDBi EOG79CZ0K.
PhylomeDBi P08263.
TreeFami TF105321.

Enzyme and pathway databases

BioCyci MetaCyc:G66-32542-MONOMER.
Reactomei REACT_6926. Glutathione conjugation.
SABIO-RK P08263.

Miscellaneous databases

EvolutionaryTracei P08263.
GeneWikii Glutathione_S-transferase_A1.
GenomeRNAii 2938.
NextBioi 11643.
PROi P08263.
SOURCEi Search...

Gene expression databases

Bgeei P08263.
CleanExi HS_GSTA1.
Genevestigatori P08263.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01266. GSTRNSFRASEA.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA."
    Tu C.-P.D., Qian B.
    Biochem. Biophys. Res. Commun. 141:229-237(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The basic glutathione S-transferases from human livers are products of separate genes."
    Rhoads D.M., Zarlengo R.P., Tu C.-P.D.
    Biochem. Biophys. Res. Commun. 145:474-481(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA."
    Tu C.-P.D., Qian B.
    Biochem. Soc. Trans. 15:734-736(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. "Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12."
    Board P.G., Webb G.C.
    Proc. Natl. Acad. Sci. U.S.A. 84:2377-2381(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Isolation and characterization of a human glutathione S-transferase Ha1 subunit gene."
    Rozen F., Nguyen T., Pickett C.B.
    Arch. Biochem. Biophys. 292:589-593(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Heterologous expression of recombinant human glutathione transferase A1-1 from a hepatoma cell line."
    Stenberg G., Bjornestedt R., Mannervik B.
    Protein Expr. Purif. 3:80-84(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  7. Chen P., Zhang C., Xie D., Wu Y., Han L., Chen L.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  8. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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].
    Tissue: Brain.
  11. "Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities."
    Chow N.W., Whang-Peng J., Kao-Shan C.S., Tam M.F., Lai H.-C.J., Tu C.-P.D.
    J. Biol. Chem. 263:12797-12800(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-9.
  12. "Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver."
    Ahmad H., Singhal S.S., Saxena M., Awasthi Y.C.
    Biochim. Biophys. Acta 1161:333-336(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-170; 188-195 AND 209-222.
  13. "Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other alpha class glutathione S-transferases."
    Hayes J.D., Kerr L.A., Cronshaw A.D.
    Biochem. J. 264:437-445(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-36; 63-155 AND 208-212.
  14. "The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathione transferase."
    Board P.G., Mannervik B.
    Biochem. J. 275:171-174(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 200-222.
  15. "Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes."
    Sinning I., Kleywegt G.J., Cowan S.W., Reinemer P., Dirr H.W., Huber R., Gilliland G.L., Armstrong R.N., Ji X., Board P.G., Olin B., Mannervik B., Jones T.A.
    J. Mol. Biol. 232:192-212(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH S-BENZYL-GLUTATHIONE, SUBUNIT.
  16. "Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate."
    Cameron A.D., Sinning I., L'Hermite G., Olin B., Board P.G., Mannervik B., Jones T.A.
    Structure 3:717-727(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH ETHACRYNIC ACID AND GLUTATHIONE, SUBUNIT.
  17. "1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site."
    Le Trong I., Stenkamp R.E., Ibarra C., Atkins W.M., Adman E.T.
    Proteins 48:618-627(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH S-HEXYL GLUTATHIONE, SUBUNIT.
  18. "Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1."
    Hederos S., Broo K.S., Jakobsson E., Kleywegt G.J., Mannervik B., Baltzer L.
    Proc. Natl. Acad. Sci. U.S.A. 101:13163-13167(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH S-BENZYLGLUTATHIONE, MUTAGENESIS OF ALA-216.
  19. "Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study."
    Kuhnert D.C., Sayed Y., Mosebi S., Sayed M., Sewell T., Dirr H.W.
    J. Mol. Biol. 349:825-838(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANT ALA-219 IN COMPLEX WITH S-HEXYLGLUTATHIONE.
  20. "New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix."
    Grahn E., Novotny M., Jakobsson E., Gustafsson A., Grehn L., Olin B., Madsen D., Wahlberg M., Mannervik B., Kleywegt G.J.
    Acta Crystallogr. D 62:197-207(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.
  21. "Structural analysis of a glutathione transferase A1-1 mutant tailored for high catalytic efficiency with toxic alkenals."
    Balogh L.M., Le Trong I., Kripps K.A., Tars K., Stenkamp R.E., Mannervik B., Atkins W.M.
    Biochemistry 48:7698-7704(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1-210 IN COMPLEX WITH GLUTATHIONE.
  22. "The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function."
    Achilonu I., Gildenhuys S., Fisher L., Burke J., Fanucchi S., Sewell B.T., Fernandes M., Dirr H.W.
    Acta Crystallogr. F 66:776-780(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANTS ALA-71 AND VAL-71 IN COMPLEX WITH S-HEXYLGLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-71.

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: October 29, 2014
This is version 168 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

External Data

Dasty 3