P28161 (GSTM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase Mu 2
EC=2.5.1.18

Alternative name(s):
GST class-mu 2
GSTM2-2

Gene names

Name:	GSTM2
Synonyms:	GST4

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	218 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. Ref.8
Catalytic activity	RX + glutathione = HX + R-S-glutathione. Ref.8
Subunit structure	Homodimer. Ref.7
Subcellular location	Cytoplasm.
Tissue specificity	Muscle.
Sequence similarities	Belongs to the GST superfamily. Mu 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 direct assay Ref.8. Source: UniProtKB xenobiotic catabolic process Inferred from direct assay Ref.8. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione transferase activity Inferred from direct assay Ref.8. 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

Chain

2 – 218

217

Glutathione S-transferase Mu 2

PRO_0000185818

Regions

Domain

2 – 88

87

GST N-terminal

Domain

90 – 208

119

GST C-terminal

Region

7 – 8

2

Glutathione binding

Region

46 – 50

5

Glutathione binding

Region

59 – 60

2

Glutathione binding

Region

72 – 73

2

Glutathione binding

Sites

Binding site

116

1

Substrate By similarity

Site

210

1

Important for substrate specificity

Natural variations

Natural variant

173

1

S → N.
Corresponds to variant rs2229050 [ dbSNP | Ensembl ].

VAR_049486

Experimental info

Mutagenesis

210

1

T → C, F, H, I, K, L, R, Y or W: Reduced enzyme activity. Ref.8

Sequence conflict

2

1

P → S in AAV38750. Ref.2

Sequence conflict

9

1

N → D in AAV38750. Ref.2

Secondary structure

1

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218

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Helix

12 – 14

3

Helix

15 – 23

9

Beta strand

28 – 33

6

Turn

38 – 41

4

Helix

44 – 47

4

Turn

48 – 51

4

Beta strand

60 – 65

6

Beta strand

68 – 72

5

Helix

73 – 83

11

Helix

91 – 116

26

Helix

120 – 142

23

Beta strand

150 – 152

3

Helix

155 – 170

16

Turn

172 – 177

6

Helix

179 – 190

12

Helix

192 – 199

8

Beta strand

214 – 216

3

Sequences

	Sequence		Length	Mass (Da)
	P28161 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 15203709D4A63789	FASTA	218	25,745
	10 20 30 40 50 60 MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL 70 80 90 100 110 120 PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF 130 140 150 160 170 180 EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN 190 200 210 LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus." Vorachek W.R., Pearson W.R., Rule G.S. Proc. Natl. Acad. Sci. U.S.A. 88:4443-4447(1991) [PubMed: 2034681] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Muscle.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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.
[4]	"Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript." Ross V.L., Board P.G. Biochem. J. 294:373-380(1993) [PubMed: 8373352] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS. Tissue: Testis.
[5]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 53-69 AND 153-182, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity." Raghunathan S., Chandross R.J., Kretsinger R.H., Allison T.J., Penington C.J., Rule G.S. J. Mol. Biol. 238:815-832(1994) [PubMed: 8182750] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.
[8]	"Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution." Norrgard M.A., Ivarsson Y., Tars K., Mannervik B. Proc. Natl. Acad. Sci. U.S.A. 103:4876-4881(2006) [PubMed: 16549767] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, MUTAGENESIS OF THR-210, CATALYTIC ACTIVITY.
[9]	"Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases." Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F., Federici G., Caccuri A.M. Cancer Res. 69:8025-8034(2009) [PubMed: 19808963] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NBDHEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M63509 mRNA. Translation: AAA60963.1.
BT019947 mRNA. Translation: AAV38750.1.
BC105038 mRNA. Translation: AAI05039.1.
BC105066 mRNA. Translation: AAI05067.1.

IPI

IPI00219067.

PIR

A39375.

RefSeq

NP_000839.1. NM_000848.3.

UniGene

Hs.279837.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HNA	X-ray	1.85	A	2-218	[»]
1HNB	X-ray	3.50	A/B	2-218	[»]
1HNC	X-ray	3.00	A/B/C/D	2-218	[»]
1XW5	X-ray	1.80	A/B	2-217	[»]
1YKC	X-ray	2.10	A/B	2-217	[»]
2AB6	X-ray	2.50	A/B/C/D	2-217	[»]
2C4J	X-ray	1.35	A/B/C/D	2-217	[»]
2GTU	X-ray	2.55	A/B	2-217	[»]
3GTU	X-ray	2.80	A/C	2-217	[»]
3GUR	X-ray	2.50	A/B/C/D	2-218	[»]

ProteinModelPortal

P28161.

SMR

P28161. Positions 2-218.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-129N.

STRING

P28161.

PTM databases

PhosphoSite

P28161.

Polymorphism databases

DMDM

232204.

2D gel databases

OGP

P28161.

REPRODUCTION-2DPAGE

P28161.

Proteomic databases

PRIDE

P28161.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000241337; ENSP00000241337; ENSG00000213366.

GeneID

2946.

KEGG

hsa:2946.

NMPDR

fig|9606.3.peg.1647.

UCSC

uc001dyi.1. human.

Organism-specific databases

CTD

2946.

GeneCards

GC01P110210.

H-InvDB

HIX0000856.

HGNC

HGNC:4634. GSTM2.

HPA

CAB040547.

MIM

138380. gene.

neXtProt

NX_P28161.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17587.

HOVERGEN

HBG106842.

PhylomeDB

P28161.

Gene expression databases

CleanEx

HS_GSTM2.

Genevestigator

P28161.

GermOnline

ENSG00000168765. 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.
IPR004046. GST_C.
IPR003081. GST_mu.
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.

Pfam

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

PRINTS

PR01267. GSTRNSFRASEM.

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

DB00143. Glutathione.

NextBio

11674.

SOURCE

Search...

Entry information

Entry name

GSTM2_HUMAN

Accession

Primary (citable) accession number: P28161
Secondary accession number(s): Q2M318, Q5TZY5, Q8WWE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 126 of the entry and version 2 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.