ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q12390


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GST2_YEAST
Primary accession number Q12390
Secondary accession numbers None
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 67)
Name and origin of the protein
Protein name Glutathione S-transferase 2
Synonyms EC 2.5.1.18
GST-II
Gene name
Name: GTT2
OrderedLocusNames: YLL060C
ORFNames: L0560
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
Wedler H., Wambutt R.;
"Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces cerevisiae including the subtelomeric region of the left arm.";
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169871 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
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).
Comments
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
Z47973; CAA87997.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73165; CAA97513.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY557940; AAS56266.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S50960; S50960.
RefSeq NP_013040.1; -.
3D structure databases
HSSP Q9ZVQ3; 1E6B. [HSSP ENTRY / PDB]
ModBase Q12390.
Protein-protein interaction databases
DIP DIP:2981N; -.
IntAct Q12390; 1.
Organism-specific databases
CYGD YLL060c; -.
SGD S000003983; GTT2.
Yeast-GFP YLL060C.
Gene expression databases
GermOnline YLL060C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0004364; Molecular function: glutathione transferase activity (inferred from electronic annotation from EC).
GO:0006749; Biological process: glutathione metabolic process (inferred from direct assay from SGD).
GO:0009636; Biological process: response to toxin (inferred from expression pattern from SGD).
QuickGo view.
Family and domain databases
InterPro IPR010987; Glutathione-S-Trfase_C-like.
IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1050.10; GST_C_like; 1.
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).
Proteomic databases
PeptideAtlas Q12390; -.
Genome annotation databases
Ensembl YLL060C; Saccharomyces cerevisiae. [Contig view]
GeneID 850666; -.
GenomeReviews Y13138_GR; YLL060C.
KEGG sce:YLL060C; -.
NMPDR fig|4932.3.peg.4031; -.
Phylogenomic databases
HOGENOM Q12390; -.
Other
LinkHub Q12390; -.
NextBio 966644; -.
ProtoNet Q12390.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   233  233     Glutathione S-transferase 2. PRO_0000185988
DOMAIN   17   101  85     GST N-terminal. 
DOMAIN   106   233  128     GST C-terminal. 
Sequence information
Length: 233 AA [This is the length of the unprocessed precursor] Molecular weight: 26340 Da [This is the MW of the unprocessed precursor] CRC64: B5EE0E47D5A37175 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNGRGFLIYN GGEKMKQKMI IYDTPAGPYP ARVRIALAEK NMLSSVQFVR INLWKGEHKK 

        70         80         90        100        110        120 
PEFLAKNYSG TVPVLELDDG TLIAECTAIT EYIDALDGTP TLTGKTPLEK GVIHMMNKRA 

       130        140        150        160        170        180 
ELELLDPVSV YFHHATPGLG PEVELYQNKE WGLRQRDKAL HGMHYFDTVL RERPYVAGDS 

       190        200        210        220        230 
FSMADITVIA GLIFAAIVKL QVPEECEALR AWYKRMQQRP SVKKLLEIRS KSS 

Q12390 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!