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P09210 (GSTA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GSTA2
Synonyms:GST2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Homodimer or heterodimer of GSTA1 and GSTA2. Ref.8 Ref.9

Subcellular location

Cytoplasm.

Tissue specificity

Liver.

Sequence similarities

Belongs to the GST superfamily. Alpha family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 222221Glutathione S-transferase A2
PRO_0000185784

Regions

Domain3 – 8381GST N-terminal
Domain85 – 207123GST C-terminal
Region54 – 552Glutathione binding
Region67 – 682Glutathione binding

Sites

Binding site91Glutathione
Binding site451Glutathione

Natural variations

Natural variant1101P → S.
Corresponds to variant rs2234951 [ dbSNP | Ensembl ].
VAR_014495
Natural variant1121S → T. Ref.1 Ref.5 Ref.10
Corresponds to variant rs2180314 [ dbSNP | Ensembl ].
VAR_012205
Natural variant1491V → A.
Corresponds to variant rs2266631 [ dbSNP | Ensembl ].
VAR_014496
Natural variant2101E → A. Ref.2 Ref.3 Ref.10
Corresponds to variant rs6577 [ dbSNP | Ensembl ].
VAR_012206

Experimental info

Sequence conflict10 – 123SNI → FNA AA sequence Ref.6
Sequence conflict121I → T in CAA46642. Ref.3
Sequence conflict191I → T AA sequence Ref.6
Sequence conflict891K → R AA sequence Ref.6
Sequence conflict1281T → I AA sequence Ref.6

Secondary structure

.................................... 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09210 [UniParc].

Last modified February 20, 2007. Version 4.
Checksum: 2823565A693A30AC

FASTA22225,664
        10         20         30         40         50         60 
MAEKPKLHYS NIRGRMESIR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI 

        70         80         90        100        110        120 
DGMKLVQTRA ILNYIASKYN LYGKDIKEKA LIDMYIEGIA DLGEMILLLP FSQPEEQDAK 

       130        140        150        160        170        180 
LALIQEKTKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL 

       190        200        210        220 
LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEESRKIF RF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16594 mRNA. Translation: AAA52616.1.
S45640 expand/collapse EMBL AC list , S45627, S45629, S45636, S45637, S45639 Genomic DNA. Translation: AAB23672.1.
X65727 expand/collapse EMBL AC list , X65728, X65729, X65730, X65731, X65732 Genomic DNA. Translation: CAA46642.1.
AL109918 Genomic DNA. Translation: CAB92770.1.
BC002895 mRNA. Translation: AAH02895.1.
PIRS24330.
S29658.
RefSeqNP_000837.3. NM_000846.4.
UniGeneHs.94107.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP09210.
SMRP09210. Positions 2-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000420168.

Chemistry

BindingDBP09210.
ChEMBLCHEMBL2241.
DrugBankDB01424. Aminophenazone.
DB00276. Amsacrine.
DB01008. Busulfan.
DB00291. Chlorambucil.
DB00608. Chloroquine.
DB00568. Cinnarizine.
DB00636. Clofibrate.
DB00903. Ethacrynic acid.
DB00143. Glutathione.
DB00888. Mechlorethamine.
DB01058. Praziquantel.
DB00163. Vitamin E.

PTM databases

PhosphoSiteP09210.

Polymorphism databases

DMDM126302551.

2D gel databases

REPRODUCTION-2DPAGEIPI00745233.

Proteomic databases

PaxDbP09210.
PRIDEP09210.

Protocols and materials databases

DNASU2939.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000493422; ENSP00000420168; ENSG00000244067.
GeneID2939.
KEGGhsa:2939.
UCSCuc003pay.3. human.

Organism-specific databases

CTD2939.
GeneCardsGC06M052614.
H-InvDBHIX0200871.
HGNCHGNC:4627. GSTA2.
HPAHPA004342.
MIM138360. gene.
neXtProtNX_P09210.
PharmGKBPA29017.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266414.
HOGENOMHOG000115734.
HOVERGENHBG053749.
InParanoidP09210.
KOK00799.
OMANIRGRME.
OrthoDBEOG79CZ0K.
PhylomeDBP09210.
TreeFamTF105321.

Enzyme and pathway databases

BioCycMetaCyc:HS01846-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP09210.

Gene expression databases

BgeeP09210.
CleanExHS_GSTA2.
GenevestigatorP09210.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11571:SF4. PTHR11571:SF4. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01266. GSTRNSFRASEA.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09210.
GeneWikiGSTA2.
GenomeRNAi2939.
NextBio11647.
PROP09210.
SOURCESearch...

Entry information

Entry nameGSTA2_HUMAN
AccessionPrimary (citable) accession number: P09210
Secondary accession number(s): Q12759, Q16491, Q9NTY6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 20, 2007
Last modified: April 16, 2014
This is version 158 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM