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P09210

- GSTA2_HUMAN

UniProt

P09210 - GSTA2_HUMAN

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Protein

Glutathione S-transferase A2

Gene

GSTA2

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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91Glutathione1 Publication
Binding sitei45 – 451Glutathione1 Publication

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. small molecule metabolic process Source: Reactome
  5. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS01846-MONOMER.
ReactomeiREACT_6926. Glutathione conjugation.
SABIO-RKP09210.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase A2 (EC:2.5.1.18)
Alternative name(s):
GST HA subunit 2
GST class-alpha member 2
GST-gamma
GSTA2-2
GTH2
Gene namesi
Name:GSTA2
Synonyms:GST2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4627. GSTA2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29017.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 222221Glutathione S-transferase A2PRO_0000185784Add
BLAST

Proteomic databases

MaxQBiP09210.
PaxDbiP09210.
PRIDEiP09210.

2D gel databases

REPRODUCTION-2DPAGEIPI00745233.

PTM databases

PhosphoSiteiP09210.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiP09210.
CleanExiHS_GSTA2.
GenevestigatoriP09210.

Organism-specific databases

HPAiHPA004342.

Interactioni

Subunit structurei

Homodimer or heterodimer of GSTA1 and GSTA2.2 Publications

Protein-protein interaction databases

BioGridi109194. 4 interactions.
STRINGi9606.ENSP00000420168.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94
Beta strandi11 – 133
Turni14 – 163
Helixi17 – 259
Beta strandi31 – 344
Helixi38 – 469
Beta strandi57 – 604
Beta strandi63 – 675
Helixi68 – 7811
Helixi86 – 10823
Helixi109 – 1113
Turni114 – 1163
Helixi117 – 13014
Helixi132 – 14312
Beta strandi146 – 1494
Helixi155 – 17016
Turni172 – 1776
Helixi179 – 19012
Helixi192 – 1976
Helixi210 – 22011

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AGSX-ray2.50A/B2-222[»]
2VCTX-ray2.10A/B/C/D/E/F/G/H1-222[»]
2WJUX-ray2.30A/B/C/D/E/F/G/H1-222[»]
4ACSX-ray2.10A/B/C/D1-221[»]
ProteinModelPortaliP09210.
SMRiP09210. Positions 2-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09210.

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

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.
InParanoidiP09210.
KOiK00799.
OMAiNIRGRME.
OrthoDBiEOG79CZ0K.
PhylomeDBiP09210.
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.

P09210-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEKPKLHYS NIRGRMESIR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL
60 70 80 90 100
MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKEKA LIDMYIEGIA
110 120 130 140 150
DLGEMILLLP FSQPEEQDAK LALIQEKTKN RYFPAFEKVL KSHGQDYLVG
160 170 180 190 200
NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP
210 220
GSPRKPPMDE KSLEESRKIF RF
Length:222
Mass (Da):25,664
Last modified:February 20, 2007 - v4
Checksum:i2823565A693A30AC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 123SNI → FNA AA sequence (PubMed:8431482)Curated
Sequence conflicti12 – 121I → T in CAA46642. (PubMed:1497629)Curated
Sequence conflicti19 – 191I → T AA sequence (PubMed:8431482)Curated
Sequence conflicti89 – 891K → R AA sequence (PubMed:8431482)Curated
Sequence conflicti128 – 1281T → I AA sequence (PubMed:8431482)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti110 – 1101P → S.
Corresponds to variant rs2234951 [ dbSNP | Ensembl ].
VAR_014495
Natural varianti112 – 1121S → T.3 Publications
Corresponds to variant rs2180314 [ dbSNP | Ensembl ].
VAR_012205
Natural varianti149 – 1491V → A.
Corresponds to variant rs2266631 [ dbSNP | Ensembl ].
VAR_014496
Natural varianti210 – 2101E → A.3 Publications
Corresponds to variant rs6577 [ dbSNP | Ensembl ].
VAR_012206

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16594 mRNA. Translation: AAA52616.1.
S45640
, S45627, S45629, S45636, S45637, S45639 Genomic DNA. Translation: AAB23672.1.
X65727
, X65728, X65729, X65730, X65731, X65732 Genomic DNA. Translation: CAA46642.1.
AL109918 Genomic DNA. Translation: CAB92770.1.
BC002895 mRNA. Translation: AAH02895.1.
CCDSiCCDS4944.1.
PIRiS24330.
S29658.
RefSeqiNP_000837.3. NM_000846.4.
UniGeneiHs.94107.

Genome annotation databases

EnsembliENST00000493422; ENSP00000420168; ENSG00000244067.
GeneIDi2939.
KEGGihsa:2939.
UCSCiuc003pay.3. human.

Polymorphism databases

DMDMi126302551.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16594 mRNA. Translation: AAA52616.1 .
S45640
, S45627 , S45629 , S45636 , S45637 , S45639 Genomic DNA. Translation: AAB23672.1 .
X65727
, X65728 , X65729 , X65730 , X65731 , X65732 Genomic DNA. Translation: CAA46642.1 .
AL109918 Genomic DNA. Translation: CAB92770.1 .
BC002895 mRNA. Translation: AAH02895.1 .
CCDSi CCDS4944.1.
PIRi S24330.
S29658.
RefSeqi NP_000837.3. NM_000846.4.
UniGenei Hs.94107.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AGS X-ray 2.50 A/B 2-222 [» ]
2VCT X-ray 2.10 A/B/C/D/E/F/G/H 1-222 [» ]
2WJU X-ray 2.30 A/B/C/D/E/F/G/H 1-222 [» ]
4ACS X-ray 2.10 A/B/C/D 1-221 [» ]
ProteinModelPortali P09210.
SMRi P09210. Positions 2-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109194. 4 interactions.
STRINGi 9606.ENSP00000420168.

Chemistry

BindingDBi P09210.
ChEMBLi CHEMBL2241.
DrugBanki DB00993. Azathioprine.
DB01008. Busulfan.
DB00608. Chloroquine.
DB00636. Clofibrate.
DB00903. Ethacrynic acid.
DB00143. Glutathione.
DB00163. Vitamin E.

PTM databases

PhosphoSitei P09210.

Polymorphism databases

DMDMi 126302551.

2D gel databases

REPRODUCTION-2DPAGE IPI00745233.

Proteomic databases

MaxQBi P09210.
PaxDbi P09210.
PRIDEi P09210.

Protocols and materials databases

DNASUi 2939.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000493422 ; ENSP00000420168 ; ENSG00000244067 .
GeneIDi 2939.
KEGGi hsa:2939.
UCSCi uc003pay.3. human.

Organism-specific databases

CTDi 2939.
GeneCardsi GC06M052614.
H-InvDB HIX0200871.
HGNCi HGNC:4627. GSTA2.
HPAi HPA004342.
MIMi 138360. gene.
neXtProti NX_P09210.
PharmGKBi PA29017.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266414.
GeneTreei ENSGT00670000097856.
HOGENOMi HOG000115734.
HOVERGENi HBG053749.
InParanoidi P09210.
KOi K00799.
OMAi NIRGRME.
OrthoDBi EOG79CZ0K.
PhylomeDBi P09210.
TreeFami TF105321.

Enzyme and pathway databases

BioCyci MetaCyc:HS01846-MONOMER.
Reactomei REACT_6926. Glutathione conjugation.
SABIO-RK P09210.

Miscellaneous databases

EvolutionaryTracei P09210.
GeneWikii GSTA2.
GenomeRNAii 2939.
NextBioi 11647.
PROi P09210.
SOURCEi Search...

Gene expression databases

Bgeei P09210.
CleanExi HS_GSTA2.
Genevestigatori P09210.

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. "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], VARIANT THR-112.
  2. "Isolation and characterization of the human glutathione S-transferase A2 subunit gene."
    Rohrdanz E., Nguyen T., Pickett C.B.
    Arch. Biochem. Biophys. 298:747-752(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-210.
    Tissue: Liver.
  3. "Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2."
    Klone A., Hussnatter R., Sies H.
    Biochem. J. 285:925-928(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-210.
    Tissue: Blood.
  4. "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].
  5. "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], VARIANT THR-112.
    Tissue: Lung.
  6. "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.
  7. "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 63-155 AND 208-222.
  8. "A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal."
    Zeng K., Rose J.P., Chen H.C., Strickland C.L., Tu C.P., Wang B.C.
    Proteins 20:259-263(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
  9. "Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases."
    Tars K., Olin B., Mannervik B.
    J. Mol. Biol. 397:332-340(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND DELTA5-ANDROSTENE-3-17-DIONE, SUBUNIT.
  10. "Polymorphism of human alpha class glutathione transferases."
    Tetlow N., Liu D., Board P.
    Pharmacogenetics 11:609-617(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-112 AND ALA-210.

Entry informationi

Entry nameiGSTA2_HUMAN
AccessioniPrimary (citable) accession number: P09210
Secondary accession number(s): Q12759, Q16491, Q9NTY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 20, 2007
Last modified: October 29, 2014
This is version 164 of the entry and version 4 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