Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione S-transferase 3

Gene

gst3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May have a role in the detoxification of various heavy metals.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

GO - Molecular functioni

  1. glutathione peroxidase activity Source: PomBase
  2. glutathione transferase activity Source: PomBase

GO - Biological processi

  1. metabolic process Source: GOC
  2. oxidation-reduction process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 3 (EC:2.5.1.18)
Alternative name(s):
GST-III
Gene namesi
Name:gst3
ORF Names:SPAC688.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC688.04c.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. endoplasmic reticulum Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 242242Glutathione S-transferase 3PRO_0000185986Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei228 – 2281Phosphoserine1 Publication
Modified residuei232 – 2321Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9P6M1.

Expressioni

Inductioni

By heavy metals such as cadmium and mercury.1 Publication

Interactioni

Subunit structurei

Interacts with sad1.1 Publication

Protein-protein interaction databases

BioGridi279899. 7 interactions.
IntActiQ9P6M1. 1 interaction.
MINTiMINT-4704315.
STRINGi4896.SPAC688.04c-1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7979GST N-terminalAdd
BLAST
Domaini85 – 234150GST C-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the GST superfamily.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125753.
InParanoidiQ9P6M1.
OMAiADVQMSF.
OrthoDBiEOG7BZW43.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P6M1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVLHHLKNS RSTRIVWMLE ELKVPYEIKV YDRVDGRAPP AYTKLSPLGK
60 70 80 90 100
SPIVVDDGVT YIESAAILEH LVRKYGPSFK PSEEDVAELE KYELWMHFSE
110 120 130 140 150
ASLMPFIWAS HVLDLSVNMT PIFFRYIVRQ FVNGIKSKYL SKETFLNLDY
160 170 180 190 200
IDNHLASNEY FAGEQFTAAD PQMCFPIFAA QRDYLSQKPY KNIKRWMRVV
210 220 230 240
SDRPACRIAA EKVEDNTLTL FSDVERYSHP PTPPPEQVRS DE
Length:242
Mass (Da):28,113
Last modified:April 17, 2012 - v3
Checksum:i42324A6B9B672938
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY034792 Genomic DNA. Translation: AAK58430.1.
CU329670 Genomic DNA. Translation: CAB90771.3.
RefSeqiNP_594063.3. NM_001019487.3.

Genome annotation databases

EnsemblFungiiSPAC688.04c.1; SPAC688.04c.1:pep; SPAC688.04c.
GeneIDi2543479.
KEGGispo:SPAC688.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY034792 Genomic DNA. Translation: AAK58430.1.
CU329670 Genomic DNA. Translation: CAB90771.3.
RefSeqiNP_594063.3. NM_001019487.3.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279899. 7 interactions.
IntActiQ9P6M1. 1 interaction.
MINTiMINT-4704315.
STRINGi4896.SPAC688.04c-1.

Proteomic databases

MaxQBiQ9P6M1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC688.04c.1; SPAC688.04c.1:pep; SPAC688.04c.
GeneIDi2543479.
KEGGispo:SPAC688.04c.

Organism-specific databases

PomBaseiSPAC688.04c.

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125753.
InParanoidiQ9P6M1.
OMAiADVQMSF.
OrthoDBiEOG7BZW43.

Miscellaneous databases

NextBioi20804491.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization, expression and regulation of a third gene encoding glutathione S-transferase from the fission yeast."
    Shin Y.H., Park E.-H., Fuchs J.A., Lim C.-J.
    Biochim. Biophys. Acta 1577:164-170(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  4. "Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fission yeast."
    Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.
    Mol. Genet. Genomics 270:449-461(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAD1, SUBCELLULAR LOCATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228 AND THR-232, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Augmented annotation of the Schizosaccharomyces pombe genome reveals additional genes required for growth and viability."
    Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L., Hagan I.M., Miller C.J.
    Genetics 187:1207-1217(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiGST3_SCHPO
AccessioniPrimary (citable) accession number: Q9P6M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2002
Last sequence update: April 17, 2012
Last modified: March 31, 2015
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.