P09210 (GSTA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GSTA2
Synonyms:	GST2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glutathione metabolic process Inferred from sequence or structural similarity. Source: UniProtKB xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	glutathione transferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 222

221

Glutathione S-transferase A2

PRO_0000185784

Regions

Domain

3 – 83

81

GST N-terminal

Domain

85 – 207

123

GST C-terminal

Region

54 – 55

2

Glutathione binding

Region

67 – 68

2

Glutathione binding

Sites

Binding site

9

1

Glutathione

Binding site

45

1

Glutathione

Natural variations

Natural variant

110

1

P → S.
Corresponds to variant rs2234951 [ dbSNP | Ensembl ].

VAR_014495

Natural variant

112

1

S → T. Ref.1 Ref.5 Ref.10
Corresponds to variant rs2180314 [ dbSNP | Ensembl ].

VAR_012205

Natural variant

149

1

V → A.
Corresponds to variant rs2266631 [ dbSNP | Ensembl ].

VAR_014496

Natural variant

210

1

E → A. Ref.2 Ref.3 Ref.10
Corresponds to variant rs6577 [ dbSNP | Ensembl ].

VAR_012206

Experimental info

Sequence conflict

10 – 12

3

SNI → FNA AA sequence Ref.6

Sequence conflict

12

1

I → T in CAA46642. Ref.3

Sequence conflict

19

1

I → T AA sequence Ref.6

Sequence conflict

89

1

K → R AA sequence Ref.6

Sequence conflict

128

1

T → I AA sequence Ref.6

Secondary structure

1

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222

Helix Strand Turn

Details...

Beta strand

6 – 9

4

Helix

17 – 25

9

Beta strand

31 – 34

4

Helix

38 – 46

9

Beta strand

57 – 59

3

Beta strand

64 – 67

4

Helix

68 – 78

11

Helix

86 – 96

11

Helix

105 – 108

4

Helix

109 – 111

3

Turn

114 – 116

3

Helix

117 – 130

14

Helix

132 – 142

11

Helix

155 – 170

16

Turn

172 – 177

6

Helix

179 – 190

12

Helix

192 – 197

6

Helix

210 – 220

11

Sequences

	Sequence		Length	Mass (Da)
	P09210 [UniParc]. Last modified February 20, 2007. Version 4. Checksum: 2823565A693A30AC	FASTA	222	25,664
	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

References

	« Hide 'large scale' referencesShow '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: 3036131] [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: 1329668] [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: 1497629] [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: 14574404] [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: 15489334] [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: 8431482] [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: 2604726] [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: 7892174] [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: 20083122] [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: 11668220] [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 , 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.

IPI

IPI00745233.

PIR

S24330.
S29658.

RefSeq

NP_000837.3. NM_000846.4.

UniGene

Hs.94107.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P09210.

SMR

P09210. Positions 2-222.

ModBase

Search...

Protein-protein interaction databases

STRING

P09210.

PTM databases

PhosphoSite

P09210.

Polymorphism databases

DMDM

126302551.

2D gel databases

REPRODUCTION-2DPAGE

IPI00745233.

Proteomic databases

PRIDE

P09210.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000493422; ENSP00000420168; ENSG00000244067.

GeneID

2939.

KEGG

hsa:2939.

UCSC

uc003pay.1. human.

Organism-specific databases

CTD

2939.

GeneCards

GC06M052614.

H-InvDB

HIX0200871.

HGNC

HGNC:4627. GSTA2.

HPA

HPA004342.

MIM

138360. gene.

neXtProt

NX_P09210.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18946.

HOGENOM

HBG443985.

HOVERGEN

HBG053749.

InParanoid

P09210.

OMA

NIRGRME.

OrthoDB

EOG49ZXQ6.

PhylomeDB

P09210.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13430.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P09210.

Bgee

P09210.

CleanEx

HS_GSTA2.

Genevestigator

P09210.

Family and domain databases

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

KO

K00799.

PANTHER

PTHR11571:SF4. GST_alpha. 1 hit.

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PRINTS

PR01266. GSTRNSFRASEA.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01424. 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.

NextBio

11647.

SOURCE

Search...

Entry information

Entry name

GSTA2_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 137 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.