Reviewed, UniProtKB/Swiss-Prot P09210 (GSTA2_HUMAN)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase A2
      Short name=GTH2
      Short name=HA subunit 2
    EC=2.5.1.18
Alternative name(s):
    GST-gamma
    GSTA2-2
    GST class-alpha member 2

Gene names

Name:	GSTA2
Synonyms:	GST2

Organism

Homo sapiens (Human) [Complete proteome]

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.
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
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione transferase activity Traceable author statement. Source: ProtInc
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

Natural variations

Natural variant

110

1

P → S: dbSNP rs2234951.

VAR_014495

Natural variant

112

1

S → T: dbSNP rs2180314. Ref.1 Ref.5 Ref.9

VAR_012205

Natural variant

149

1

V → A: dbSNP rs2266631.

VAR_014496

Natural variant

210

1

E → A: dbSNP rs6577. Ref.9 Ref.2 Ref.3

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)
	P09210-1 [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).
[9]	"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

EMBLGenBankDDBJ

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.

UniGene

Hs.94107

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P09210.

PTM databases

PhosphoSite

P09210.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00745233.

Proteomic databases

PRIDE

P09210.

Genome annotation databases

Ensembl

ENST00000371034; ENSP00000360073; ENSG00000096087; Homo sapiens. [Genome view]

GeneID

2939.

KEGG

hsa:2939.

UCSC

uc003pay.1. human.

Organism-specific databases

CTD

2939.

GeneCards

GC06M052723.

H-InvDB

HIX0005956.

HGNC

HGNC:4627. GSTA2.

HPA

HPA004342.

MIM

138360. gene.

PharmGKB

PA29017.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P09210.

HOVERGEN

P09210.

OMA

NIRGRME.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13430.

BRENDA

2.5.1.18. 247.

Reactome

REACT_13433. Biological oxidations.

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.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

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

PANTHER

PTHR11571:SF4. GST_alpha. 1 hit.

Pfam

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

PRINTS

PR01266. GSTRNSFRASEA.

PROSITE

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

ProtoNet

Search...

Other Resources

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:	November 3, 2009
This is version 115 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.