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Q9SHH7 (GSTUP_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase U25

Short name=AtGSTU25
EC=2.5.1.18
Alternative name(s):
GST class-tau member 25
Gene names
Name:GSTU25
Ordered Locus Names:At1g17180
ORF Names:F20D23.12A
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides By similarity.

Catalytic activity

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

Subcellular location

Cytoplasmcytosol Probable.

Sequence similarities

Belongs to the GST superfamily. Tau family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Biological processDetoxification
   Cellular componentCytoplasm
   Molecular functionTransferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to toxic substance

Inferred from electronic annotation. Source: UniProtKB-KW

toxin catabolic process

Traceable author statement Ref.5. Source: TAIR

   Cellular_componentcytoplasm

Non-traceable author statement Ref.5. Source: TAIR

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 221220Glutathione S-transferase U25
PRO_0000413570

Regions

Domain3 – 8280GST N-terminal
Domain88 – 208121GST C-terminal
Region13 – 142Glutathione binding By similarity
Region39 – 402Glutathione binding By similarity
Region53 – 542Glutathione binding By similarity
Region66 – 672Glutathione binding By similarity

Amino acid modifications

Modified residue1491Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SHH7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: BCEB3254B39364A8

FASTA22125,591
        10         20         30         40         50         60 
MADEVILLDF WPSMFGMRTR IALEEKNVKF DYREQDLWNK SPILLEMNPV HKKIPVLIHN 

        70         80         90        100        110        120 
GNPVCESLIQ IEYIDEVWPS KTPLLPSDPY QRAQAKFWGD FIDKKVYASA RLIWGAKGEE 

       130        140        150        160        170        180 
HEAGKKEFIE ILKTLESELG DKTYFGGETF GYVDIALIGF YSWFEAYEKF GSFSIEAECP 

       190        200        210        220 
KLIAWGKRCV ERESVAKSLP DSEKIIKFVP ELRKKLGIEI E 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Probing the diversity of the Arabidopsis glutathione S-transferase gene family."
Wagner U., Edwards R., Dixon D.P., Mauch F.
Plant Mol. Biol. 49:515-532(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[6]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC007651 Genomic DNA. Translation: AAD50015.1.
CP002684 Genomic DNA. Translation: AEE29555.1.
AK118907 mRNA. Translation: BAC43490.1.
BT005643 mRNA. Translation: AAO64063.1.
PIRH86307.
RefSeqNP_173161.1. NM_101579.3.
UniGeneAt.41849.

3D structure databases

ProteinModelPortalQ9SHH7.
SMRQ9SHH7. Positions 1-219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid23529. 2 interactions.
IntActQ9SHH7. 2 interactions.
STRING3702.AT1G17180.1-P.

Proteomic databases

PaxDbQ9SHH7.
PRIDEQ9SHH7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G17180.1; AT1G17180.1; AT1G17180.
GeneID838289.
KEGGath:AT1G17180.

Organism-specific databases

TAIRAT1G17180.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125749.
InParanoidQ9SHH7.
KOK00799.
OMAFEAYEKF.
PhylomeDBQ9SHH7.
ProtClustDBCLSN2681880.

Enzyme and pathway databases

BioCycARA:AT1G17180-MONOMER.

Gene expression databases

GenevestigatorQ9SHH7.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSTUP_ARATH
AccessionPrimary (citable) accession number: Q9SHH7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: May 1, 2000
Last modified: March 19, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names