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Q6NMS0

- GSTUC_ARATH

UniProt

Q6NMS0 - GSTUC_ARATH

Protein

Glutathione S-transferase U12

Gene

GSTU12

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 2 (19 Oct 2011)
      Previous versions | rss
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    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: TAIR

    GO - Biological processi

    1. glutathione metabolic process Source: TAIR
    2. response to stress Source: UniProtKB-KW
    3. response to toxic substance Source: UniProtKB-KW
    4. toxin catabolic process Source: TAIR

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Detoxification, Stress response

    Enzyme and pathway databases

    BioCyciARA:AT1G69920-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase U12 (EC:2.5.1.18)
    Short name:
    AtGSTU12
    Alternative name(s):
    GST class-tau member 12
    Gene namesi
    Name:GSTU12
    Ordered Locus Names:At1g69920
    ORF Names:T17F3.5
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G69920.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: TAIR
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 254254Glutathione S-transferase U12PRO_0000413558Add
    BLAST

    Expressioni

    Inductioni

    By fungal elicitor.1 Publication

    Gene expression databases

    GenevestigatoriQ6NMS0.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT1G69920.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6NMS0.
    SMRiQ6NMS0. Positions 35-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 11482GST N-terminalAdd
    BLAST
    Domaini120 – 252133GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 442Glutathione bindingBy similarity
    Regioni71 – 722Glutathione bindingBy similarity
    Regioni85 – 862Glutathione bindingBy similarity
    Regioni98 – 992Glutathione bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi19 – 235Nuclear localization signalSequence Analysis

    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

    eggNOGiNOG303122.
    HOGENOMiHOG000125749.
    InParanoidiQ6NMS0.
    KOiK00799.
    OMAiKFRAHEA.

    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.

    Q6NMS0-1 [UniParc]FASTAAdd to Basket

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    MLKNKKSDNS LSRDTLQIKK RKKTTMAQNG SNTTVKLIGT WASPFAIRAQ    50
    VALHLKSVEH EYVEETDVLK GKSDLLIKSN PIHKKVPVLI HGDVSICESL 100
    NIVQYVDESW PSDLSILPTL PSERAFARFW AHFVDGKLFE SIDAVAGAKD 150
    DAARMTLAGN LMENLAALEE AFQKSSKGGD FFGGGNIGFV DITVGAIVGP 200
    ISVIEAFSGV KFLRPDTTPG LIQWAEKFRA HEAVKPYMPT VAEFIEFAKK 250
    KFSV 254
    Length:254
    Mass (Da):27,923
    Last modified:October 19, 2011 - v2
    Checksum:i2A152B61669ABA85
    GO

    Sequence cautioni

    The sequence AAG52553.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti244 – 2441F → S in AAR20744. (PubMed:14593172)Curated
    Sequence conflicti244 – 2441F → S in AAS46639. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC010675 Genomic DNA. Translation: AAG52553.1. Different initiation.
    CP002684 Genomic DNA. Translation: AEE34998.1.
    BT010687 mRNA. Translation: AAR20744.1.
    BT011586 mRNA. Translation: AAS46639.1.
    PIRiF96721.
    RefSeqiNP_177150.2. NM_105660.5.
    UniGeneiAt.35363.

    Genome annotation databases

    EnsemblPlantsiAT1G69920.1; AT1G69920.1; AT1G69920.
    GeneIDi843328.
    KEGGiath:AT1G69920.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC010675 Genomic DNA. Translation: AAG52553.1 . Different initiation.
    CP002684 Genomic DNA. Translation: AEE34998.1 .
    BT010687 mRNA. Translation: AAR20744.1 .
    BT011586 mRNA. Translation: AAS46639.1 .
    PIRi F96721.
    RefSeqi NP_177150.2. NM_105660.5.
    UniGenei At.35363.

    3D structure databases

    ProteinModelPortali Q6NMS0.
    SMRi Q6NMS0. Positions 35-251.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT1G69920.1-P.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G69920.1 ; AT1G69920.1 ; AT1G69920 .
    GeneIDi 843328.
    KEGGi ath:AT1G69920.

    Organism-specific databases

    TAIRi AT1G69920.

    Phylogenomic databases

    eggNOGi NOG303122.
    HOGENOMi HOG000125749.
    InParanoidi Q6NMS0.
    KOi K00799.
    OMAi KFRAHEA.

    Enzyme and pathway databases

    BioCyci ARA:AT1G69920-MONOMER.

    Gene expression databases

    Genevestigatori Q6NMS0.

    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

    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.
      , 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. "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.
    4. "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.
    5. "Necrosis- and ethylene-inducing peptide from Fusarium oxysporum induces a complex cascade of transcripts associated with signal transduction and cell death in Arabidopsis."
      Bae H., Kim M.S., Sicher R.C., Bae H.J., Bailey B.A.
      Plant Physiol. 141:1056-1067(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    6. "Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily."
      Dixon D.P., Hawkins T., Hussey P.J., Edwards R.
      J. Exp. Bot. 60:1207-1218(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiGSTUC_ARATH
    AccessioniPrimary (citable) accession number: Q6NMS0
    Secondary accession number(s): F4I3V4, Q9CAS5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2011
    Last sequence update: October 19, 2011
    Last modified: October 1, 2014
    This is version 79 of the entry and version 2 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