Skip Header

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

Q9ZW27

- GSTU4_ARATH

UniProt

Q9ZW27 - GSTU4_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutathione S-transferase U4

Gene

GSTU4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. response to toxic substance Source: UniProtKB-KW
  2. toxin catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Detoxification

Enzyme and pathway databases

BioCyciARA:AT2G29460-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase U4 (EC:2.5.1.18)
Short name:
AtGSTU4
Alternative name(s):
GST class-tau member 4
Glutathione S-transferase 22
Gene namesi
Name:GSTU4
Synonyms:GST22
Ordered Locus Names:At2g29460
ORF Names:F16P2.16
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G29460.

Subcellular locationi

Cytoplasmcytosol Curated

GO - Cellular componenti

  1. cytoplasm Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 224224Glutathione S-transferase U4PRO_0000413551Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei151 – 1511Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ9ZW27.

Expressioni

Gene expression databases

GenevestigatoriQ9ZW27.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT2G29460.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9ZW27.
SMRiQ9ZW27. Positions 6-221.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 8580GST N-terminalAdd
BLAST
Domaini90 – 217128GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 172Glutathione bindingBy similarity
Regioni42 – 432Glutathione bindingBy similarity
Regioni56 – 572Glutathione bindingBy similarity
Regioni69 – 702Glutathione bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG288793.
HOGENOMiHOG000125749.
InParanoidiQ9ZW27.
KOiK00799.
OMAiEYLEQDI.
PhylomeDBiQ9ZW27.

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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 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.

Q9ZW27-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEKEEDVKL LGFWASPFTR RVEMAFKLKG VPYEYLEQDI VNKSPLLLQI
60 70 80 90 100
NPVYKKVPVL VYKGKILSES HVILEYIDQI WKNNPILPQD PYEKAMALFW
110 120 130 140 150
AKFVDEQVGP VAFMSVAKAE KGVEVAIKEA QELFMFLEKE VTGKDFFGGK
160 170 180 190 200
TIGFLDLVAG SMIPFCLARG WEGMGIDMIP EEKFPELNRW IKNLKEIEIV
210 220
RECIPPREEQ IEHMKKVVER IKSA
Length:224
Mass (Da):25,839
Last modified:May 1, 1999 - v1
Checksum:i3810B34656614BE0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731G → D in AAK62449. (PubMed:14593172)Curated
Sequence conflicti173 – 1731G → D in AAO30062. (PubMed:14593172)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF288186 mRNA. Translation: AAG30135.1.
AC004561 Genomic DNA. Translation: AAC95192.1.
CP002685 Genomic DNA. Translation: AEC08257.1.
AF387004 mRNA. Translation: AAK62449.1.
BT003399 mRNA. Translation: AAO30062.1.
PIRiF84696.
RefSeqiNP_180507.1. NM_128500.3.
UniGeneiAt.12688.
At.67637.
At.68148.

Genome annotation databases

EnsemblPlantsiAT2G29460.1; AT2G29460.1; AT2G29460.
GeneIDi817495.
KEGGiath:AT2G29460.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF288186 mRNA. Translation: AAG30135.1 .
AC004561 Genomic DNA. Translation: AAC95192.1 .
CP002685 Genomic DNA. Translation: AEC08257.1 .
AF387004 mRNA. Translation: AAK62449.1 .
BT003399 mRNA. Translation: AAO30062.1 .
PIRi F84696.
RefSeqi NP_180507.1. NM_128500.3.
UniGenei At.12688.
At.67637.
At.68148.

3D structure databases

ProteinModelPortali Q9ZW27.
SMRi Q9ZW27. Positions 6-221.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT2G29460.1-P.

Proteomic databases

PRIDEi Q9ZW27.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT2G29460.1 ; AT2G29460.1 ; AT2G29460 .
GeneIDi 817495.
KEGGi ath:AT2G29460.

Organism-specific databases

TAIRi AT2G29460.

Phylogenomic databases

eggNOGi NOG288793.
HOGENOMi HOG000125749.
InParanoidi Q9ZW27.
KOi K00799.
OMAi EYLEQDI.
PhylomeDBi Q9ZW27.

Enzyme and pathway databases

BioCyci ARA:AT2G29460-MONOMER.

Gene expression databases

Genevestigatori Q9ZW27.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF13417. GST_N_3. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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.
    , 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. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.

Entry informationi

Entry nameiGSTU4_ARATH
AccessioniPrimary (citable) accession number: Q9ZW27
Secondary accession number(s): Q94EZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3