P10649 (GSTM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase Mu 1
EC=2.5.1.18

Alternative name(s):
GST 1-1
GST class-mu 1
Glutathione S-transferase GT8.7
pmGT10

Gene names

Name:

Gstm1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the GST superfamily. Mu family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.
Mass spectrometry	Molecular mass is 25838.4±2 Da from positions 2 - 218. Determined by ESI. Ref.9

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to drug Inferred from direct assay Ref.3. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutathione transferase activity Inferred from electronic annotation. Source: EC protein heterodimerization activity Inferred from direct assay Ref.2. Source: MGI protein homodimerization activity Inferred from direct assay Ref.2. Source: MGI
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 Ref.7 Ref.8
	Chain	2 – 218	217	Glutathione S-transferase Mu 1		PRO_0000185826
Regions
	Domain	2 – 88	87	GST N-terminal
	Domain	90 – 208	119	GST C-terminal
	Region	7 – 8	2	Glutathione binding By similarity
	Region	46 – 50	5	Glutathione binding By similarity
	Region	59 – 60	2	Glutathione binding By similarity
	Region	72 – 73	2	Glutathione binding By similarity
Sites
	Binding site	116	1	Substrate By similarity
Amino acid modifications
	Modified residue	23	1	Phosphotyrosine Ref.10
	Modified residue	33	1	Phosphotyrosine Ref.11
	Modified residue	34	1	Phosphothreonine Ref.11

Sequences

	Sequence		Length	Mass (Da)
	P10649 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 91AE34A1B5B44599	FASTA	218	25,970
	10 20 30 40 50 60 MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL 70 80 90 100 110 120 PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF 130 140 150 160 170 180 EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN 190 200 210 LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Tissue-specific induction of murine glutathione transferase mRNAs by butylated hydroxyanisole." Pearson W.R., Reinhart J., Sisk S.C., Anderson K.S., Adler P.N. J. Biol. Chem. 263:13324-13332(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Isolation, characterization, and expression in Escherichia coli of two murine Mu class glutathione S-transferase cDNAs homologous to the rat subunits 3 (Yb1) and 4 (Yb2)." Townsend A.J., Goldsmith M.E., Pickett C.B., Cowan K.H. J. Biol. Chem. 264:21582-21590(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The structure of two murine class-mu glutathione transferase genes coordinately induced by butylated hydroxyanisole." Reinhart J., Pearson W.R. Arch. Biochem. Biophys. 303:383-393(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[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]. Strain: C57BL/6 and FVB/N. Tissue: Brain and Liver.
[6]	"Increased synthesis of glutathione S-transferases in response to anticarcinogenic antioxidants. Cloning and measurement of messenger RNA." Pearson W.R., Windle J.J., Morrow J.F., Benson A.M., Talalay P. J. Biol. Chem. 258:2052-2062(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-41.
[7]	"Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties." Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H. Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-25.
[8]	Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11; 19-31; 33-43; 53-78; 97-108; 137-144; 153-168; 174-192 AND 203-211, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[9]	"Purification, mass spectrometric characterization, and covalent modification of murine glutathione S-transferases." Mitchell A.E., Morin D., Lame M.W., Jones A.D. Chem. Res. Toxicol. 8:1054-1062(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, MASS SPECTROMETRY. Strain: CD-1. Tissue: Liver.
[10]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-23, MASS SPECTROMETRY. Tissue: Brain.
[11]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-33 AND THR-34, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03952 mRNA. Translation: AAA37747.1. J04632 mRNA. Translation: AAA37705.1. L13448 Genomic DNA. No translation available. AL671877, AC079042 Genomic DNA. Translation: CAM17697.1. BC003822 mRNA. Translation: AAH03822.1. BC046758 mRNA. Translation: AAH46758.1. BC091763 mRNA. Translation: AAH91763.1.
IPI	IPI00230212.
PIR	H24735. S30373. S33860.
RefSeq	NP_034488.1. NM_010358.5.
UniGene	Mm.37199.
3D structure databases
ProteinModelPortal	P10649.
SMR	P10649. Positions 2-218.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10649. 1 interaction.
PTM databases
PhosphoSite	P10649.
2D gel databases
REPRODUCTION-2DPAGE	P10649.
SWISS-2DPAGE	P10649.
Proteomic databases
PaxDb	P10649.
PRIDE	P10649.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000004140; ENSMUSP00000004140; ENSMUSG00000058135.
GeneID	14862.
KEGG	mmu:14862.
UCSC	uc008qxx.2. mouse.
Organism-specific databases
CTD	2944.
MGI	MGI:95860. Gstm1.
Phylogenomic databases
eggNOG	NOG300089.
GeneTree	ENSGT00550000074559.
HOGENOM	HOG000115735.
HOVERGEN	HBG106842.
KO	K00799.
OMA	CALLEYT.
OrthoDB	EOG4RXZ24.
Gene expression databases
ArrayExpress	P10649.
Bgee	P10649.
CleanEx	MM_GSTM1.
Genevestigator	P10649.
GermOnline	ENSMUSG00000058135. Mus musculus.
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 1 hit.
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]
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
ChEMBL	CHEMBL3722.
ChiTaRS	GSTM1. mouse.
NextBio	287105.
SOURCE	Search...

Entry information

Entry name

GSTM1_MOUSE

Accession

Primary (citable) accession number: P10649
Secondary accession number(s): A2AE90, Q58ET5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program