Reviewed, UniProtKB/Swiss-Prot P08263 (GSTA1_HUMAN)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase A1
      Short name=GTH1
      Short name=HA subunit 1
    EC=2.5.1.18
Alternative name(s):
    GST-epsilon
    GSTA1-1
    GST class-alpha member 1

Gene names

Name:

GSTA1

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.
Domain	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 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	glutathione metabolic process Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Non-traceable author statement. Source: UniProtKB
Molecular function	glutathione transferase activity Ref.5 Non-traceable author statement. 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.9

Chain

2 – 222

221

Glutathione S-transferase A1

PRO_0000185783

Regions

Domain

3 – 83

81

GST N-terminal

Domain

85 – 207

123

GST C-terminal

Natural variations

Natural variant

19

1

T → I: dbSNP rs1051578.

VAR_033978

Natural variant

113

1

P → Q: dbSNP rs1051745.

VAR_049482

Natural variant

117

1

K → Q: dbSNP rs1051757.

VAR_049483

Experimental info

Sequence conflict

18

1

S → C in AAA36174. Ref.3

Sequence conflict

56 – 58

3

PMV → AML in AAA36174. Ref.3

Sequence conflict

212

1

S → L AA sequence Ref.10

Sequence conflict

216

1

A → S AA sequence Ref.9

Secondary structure

1

.

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222

Helix Strand Turn

Details...

Beta strand

6 – 13

8

Turn

14 – 16

3

Helix

17 – 26

10

Beta strand

31 – 35

5

Helix

38 – 46

9

Beta strand

57 – 60

4

Beta strand

63 – 67

5

Helix

68 – 78

11

Helix

86 – 108

23

Helix

109 – 111

3

Helix

114 – 130

17

Helix

132 – 143

12

Beta strand

146 – 149

4

Helix

155 – 170

16

Turn

172 – 177

6

Helix

179 – 190

12

Helix

192 – 198

7

Helix

210 – 220

11

Sequences

	Sequence		Length	Mass (Da)
	P08263-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C8B6786DCD761350	FASTA	222	25,631
	10 20 30 40 50 60 MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI 70 80 90 100 110 120 DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA DLGEMILLLP VCPPEEKDAK 130 140 150 160 170 180 LALIKEKIKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL 190 200 210 220 LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEEARKIF RF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3800996] [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: 3036131] [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: 3678589] [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: 3031680] [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: 1731620] [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: 1330133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]	"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]. Tissue: Brain.
[8]	"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: 3138230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-9.
[9]	"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.
[10]	"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 16-36; 63-155 AND 208-212.
[11]	"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: 2018473] [Abstract] Cited for: PROTEIN SEQUENCE OF 200-222.
[12]	"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: 8331657] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[13]	"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: 8591048] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
BC053578 mRNA. Translation: AAH53578.1.

IPI

IPI00657682.

PIR

A56666. A25909.
S29657.

RefSeq

NP_665683.1.

UniGene

Hs.446309

3D structure databases

PDBPDBe

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	2-221	[»]
1K3O	X-ray	1.80	A/B	2-221	[»]
1K3Y	X-ray	1.30	A/B	2-221	[»]
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	2-221	[»]
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	1-210	[»]
3I6A	X-ray	1.98	A/B/C/D/E/F/G/H	1-210	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P08263.

PTM databases

PhosphoSite

P08263.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00657682.

Proteomic databases

PRIDE

P08263.

Genome annotation databases

Ensembl

ENST00000334575; ENSP00000335620; ENSG00000187919; Homo sapiens. [Genome view]

GeneID

2938.

KEGG

hsa:2938.

UCSC

uc003paz.1. human.

Organism-specific databases

CTD

2938.

GeneCards

GC06M052764.

H-InvDB

HIX0025088.

HGNC

HGNC:4626. GSTA1.

HPA

HPA004342.

MIM

138359. gene.

PharmGKB

PA29016.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P08263.

HOVERGEN

P08263.

OMA

KCVESAK.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13429.

BRENDA

2.5.1.18. 247.

Reactome

REACT_13433. Biological oxidations.

Gene expression databases

ArrayExpress

P08263.

Bgee

P08263.

CleanEx

HS_GSTA1.

Genevestigator

P08263.

GermOnline

ENSG00000187919. Homo sapiens.

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

DB00276. Amsacrine.
DB01008. Busulfan.
DB00143. Glutathione.

NextBio

11643.

SOURCE

Search...

Entry information

Entry name

GSTA1_HUMAN

Accession

Primary (citable) accession number: P08263
Secondary accession number(s): Q14750

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 119 of the entry and version 3 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.