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Q8GYM1 (GSTUM_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 82. 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
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 U22
Short name=AtGSTU22
EC=2.5.1.18
Alternative name(s):
GST class-tau member 22
Gene names
Name:GSTU22
Ordered Locus Names:At1g78340
ORF Names:F3F9.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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

Cytoplasm › cytosol Probable.

Sequence similarities

Belongs to the GST superfamily. Tau family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence caution

The sequence AAF71799.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

toxin catabolic process

Traceable author statement Ref.7. Source: TAIR

   Cellular_componentcytoplasm

Non-traceable author statement Ref.7. Source: TAIR

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 218218Glutathione S-transferase U22
PRO_0000413567

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

Sequences

Sequence LengthMass (Da)Tools
Q8GYM1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: FC90AD02D8259633

FASTA21825,282
        10         20         30         40         50         60 
MADEVILLDF WPSPFGVRAR IALREKGVEF EYREENLRDK SPLLLQMNPV HKKIPVLIHN 

        70         80         90        100        110        120 
GKPVCESMNV VQYIDEVWSD KNPILPSDPY QRAQARFWVD FVDTKLFEPA DKIWQTKGEE 

       130        140        150        160        170        180 
QETAKKEYIE ALKILETELG DKPYFGGDTF GFVDIAMTGY YSWFEASEKL ANFSIEPECP 

       190        200        210 
TLMASAKRCL QRESVVQSLH DSEKILAFAY KIRKIYCV

« 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]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC013430 Genomic DNA. Translation: AAF71799.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE36096.1.
AK117519 mRNA. Translation: BAC42182.1.
BT005427 mRNA. Translation: AAO63847.1.
AK176247 mRNA. Translation: BAD44010.1.
AY086469 mRNA. Translation: AAM63471.1.
IPIIPI00547593.
RefSeqNP_177956.1. NM_106482.1.
UniGeneAt.34312.

3D structure databases

HSSPHSSP built from PDB template 1OYJ based on UniProtKB O65032.
ProteinModelPortalQ8GYM1.
SMRQ8GYM1. Positions 1-214.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8GYM1. 2 interactions.
STRING3702.AT1G78340.1-P.

Proteomic databases

PaxDbQ8GYM1.
PRIDEQ8GYM1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G78340.1; AT1G78340.1; AT1G78340.
GeneID844169.
KEGGath:AT1G78340.

Organism-specific databases

TAIRAt1g78340.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125749.
InParanoidQ8GYM1.
KOK00799.
OMAFEYREEN.
PhylomeDBQ8GYM1.
ProtClustDBCLSN2912683.

Gene expression databases

ArrayExpressQ8GYM1.
GenevestigatorQ8GYM1.

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.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
[Graphical view]
SUPFAMSSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSTUM_ARATH
AccessionPrimary (citable) accession number: Q8GYM1
Secondary accession number(s): Q8LCP9, Q9M9F2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: March 1, 2003
Last modified: April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents