[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169870 [NCBI, ExPASy, EBI, Israel, Japan] Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; Nature 387:84-87(1997).
[2]	CHARACTERIZATION. DOI=10.1074/jbc.273.45.29915; PubMed=9792709 [NCBI, ExPASy, EBI, Israel, Japan] Choi J.H., Lou W., Vancura A.; "A novel membrane-bound glutathione S-transferase functions in the stationary phase of the yeast Saccharomyces cerevisiae."; J. Biol. Chem. 273:29915-29922(1998).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).

Comments

CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
SUBUNIT: Homodimer.
INTERACTION:
P40260:MEP1; NbExp=1; IntAct=EBI-7941, EBI-10714;
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein.
SIMILARITY: Belongs to the GST superfamily.
SIMILARITY: Contains 1 GST C-terminal domain.
SIMILARITY: Contains 1 GST N-terminal domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z38061; CAA86198.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S48500; S48500.

RefSeq

NP_012304.1; -.

3D structure databases

ModBase

P40582.

Protein-protein interaction databases

DIP

DIP:2103N; -.

IntAct

P40582; -.

Organism-specific databases

YIR038c; -.

S000001477; GTT1.

Gene expression databases

ArrayExpress

P40582; -.

GermOnline

YIR038C; Saccharomyces cerevisiae.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005741;	Cellular component: mitochondrial outer membrane (inferred from direct assay from SGD).
GO:0004602;	Molecular function: glutathione peroxidase activity (inferred from direct assay from SGD).
GO:0004364;	Molecular function: glutathione transferase activity (inferred from electronic annotation from EC).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006749;	Biological process: glutathione metabolic process (inferred from direct assay from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P40582.

Genome annotation databases

Ensembl

YIR038C; Saccharomyces cerevisiae. [Contig view]

854856; -.

Z47047_GR; YIR038C.

sce:YIR038C; -.

fig|4932.3.peg.1849; -.

Phylogenomic databases

HOGENOM

P40582; -.

Other

LinkHub

P40582; -.

NextBio

977767; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Endoplasmic reticulum; Membrane; Phosphoprotein; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 234`	`234`	`Glutathione S-transferase 1.`	`PRO_0000185987`
`DOMAIN`	`3 90`	`88`	`GST N-terminal.`
`DOMAIN`	`96 234`	`139`	`GST C-terminal.`
`MOD_RES`	`56 56`		`Phosphoserine.`

Sequence information

Length: 234 AA [This is the length of the unprocessed precursor]

Molecular weight: 26795 Da [This is the MW of the unprocessed precursor]

CRC64: 3C07D40D29F60DFF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLPIIKVHW LDHSRAFRLL WLLDHLNLEY EIVPYKRDAN FRAPPELKKI HPLGRSPLLE 

        70         80         90        100        110        120 
VQDRETGKKK ILAESGFIFQ YVLQHFDHSH VLMSEDADIA DQINYYLFYV EGSLQPPLMI 

       130        140        150        160        170        180 
EFILSKVKDS GMPFPISYLA RKVADKISQA YSSGEVKNQF DFVEGEISKN NGYLVDGKLS 

       190        200        210        220        230 
GADILMSFPL QMAFERKFAA PEDYPAISKW LKTITSEESY AASKEKARAL GSNF

P40582 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools