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Q9ZR37

- DUS1_ARATH

UniProt

Q9ZR37 - DUS1_ARATH

Protein

Dual specificity protein phosphatase 1

Gene

DSPTP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Has a dual specificity toward Ser/Thr and Tyr-containing proteins. Dephosphorylates MPK4 in vitro.1 Publication

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Enzyme regulationi

    Inhibited by sodium vanadate and sodium tungstate. NaF and spermifine repress specifically phosphoserine and phosphothreonine phosphatase activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei135 – 1351Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. protein tyrosine/serine/threonine phosphatase activity Source: UniProtKB
    2. protein tyrosine phosphatase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Calmodulin-binding

    Enzyme and pathway databases

    BioCyciARA:AT3G23610-MONOMER.
    ARA:GQT-877-MONOMER.
    ReactomeiREACT_208246. ERKs are inactivated.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 1 (EC:3.1.3.16, EC:3.1.3.48)
    Short name:
    AtDsPTP1
    Gene namesi
    Name:DSPTP1
    Ordered Locus Names:At3g23610
    ORF Names:MDB19.10
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G23610.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321I → R: Impaired CaM binding and loss of phosphatase activity. 1 Publication
    Mutagenesisi35 – 351L → R: Impaired CaM binding. 1 Publication
    Mutagenesisi135 – 1351C → S: Loss of phosphatase activity. 1 Publication
    Mutagenesisi166 – 1661K → E: Impaired CaM binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 198198Dual specificity protein phosphatase 1PRO_0000415896Add
    BLAST

    Proteomic databases

    PRIDEiQ9ZR37.

    Expressioni

    Tissue specificityi

    Expressed in roots, stems, leaves and flowers.1 Publication

    Gene expression databases

    GenevestigatoriQ9ZR37.

    Interactioni

    Subunit structurei

    Interacts with calmodulin (CaM) in a calcium Ca2+-dependent manner.1 Publication

    Protein-protein interaction databases

    STRINGi3702.AT3G23610.2-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZR37.
    SMRiQ9ZR37. Positions 57-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini118 – 18265Tyrosine-protein phosphataseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 4722CaM binding domain 1Add
    BLAST
    Regioni151 – 18030CaM binding domain 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi8 – 1710Poly-Ser

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000233767.
    InParanoidiQ9ZR37.
    KOiK05766.
    OMAiQDFEKSL.
    PhylomeDBiQ9ZR37.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR020417. Atypical_DUSP.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    [Graphical view]
    PRINTSiPR01908. ADSPHPHTASE.
    SMARTiSM00195. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9ZR37-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSSRDRGSPS SSSSSSSLPG IEKYNEKVKN QIQALVRVIK VARTYRDDNV    50
    PSLIEQGLYL GSVAAASNKN VLKSYNVTHI LTVASSLRPA HPDDFVYKVV 100
    RVVDKEDTNL EMYFDECVDF IDEAKRQGGS VLVHCFVGKS RSVTIVVAYL 150
    MKKHGMTLAQ ALQHVKSKRP VASPNAGFIR QLQDLEKSMQ VSDQFFSF 198
    Length:198
    Mass (Da):22,017
    Last modified:May 1, 1999 - v1
    Checksum:iEBF1C98A177E6450
    GO
    Isoform 2 (identifier: Q9ZR37-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         191-198: VSDQFFSF → GKQVTIAQCQA

    Note: Derived from EST data. No experimental confirmation available.

    Show »
    Length:201
    Mass (Da):22,187
    Checksum:i2FA50431F9A00273
    GO
    Isoform 3 (identifier: Q9ZR37-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         192-198: SDQFFSF → VVEEKTVPCKYLLHASSFFSIKQGSKLRLHNVRREDH

    Note: Constructed according to the conserved gene model. No experimental confirmation available.

    Show »
    Length:228
    Mass (Da):25,493
    Checksum:iA8D74C6A929B00D5
    GO

    Sequence cautioni

    The sequence BAB02780.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei191 – 1988VSDQFFSF → GKQVTIAQCQA in isoform 2. CuratedVSP_042412
    Alternative sequencei192 – 1987SDQFFSF → VVEEKTVPCKYLLHASSFFS IKQGSKLRLHNVRREDH in isoform 3. CuratedVSP_042413

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y18620 mRNA. Translation: CAA77232.1.
    AB023036 Genomic DNA. Translation: BAB02780.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE76784.1.
    CP002686 Genomic DNA. Translation: AEE76785.1.
    CP002686 Genomic DNA. Translation: AEE76786.1.
    RefSeqiNP_001118683.1. NM_001125211.2. [Q9ZR37-2]
    NP_001189955.1. NM_001203026.1. [Q9ZR37-3]
    NP_189003.1. NM_113265.1. [Q9ZR37-1]
    UniGeneiAt.25373.

    Genome annotation databases

    EnsemblPlantsiAT3G23610.1; AT3G23610.1; AT3G23610. [Q9ZR37-1]
    GeneIDi821941.
    KEGGiath:AT3G23610.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y18620 mRNA. Translation: CAA77232.1 .
    AB023036 Genomic DNA. Translation: BAB02780.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE76784.1 .
    CP002686 Genomic DNA. Translation: AEE76785.1 .
    CP002686 Genomic DNA. Translation: AEE76786.1 .
    RefSeqi NP_001118683.1. NM_001125211.2. [Q9ZR37-2 ]
    NP_001189955.1. NM_001203026.1. [Q9ZR37-3 ]
    NP_189003.1. NM_113265.1. [Q9ZR37-1 ]
    UniGenei At.25373.

    3D structure databases

    ProteinModelPortali Q9ZR37.
    SMRi Q9ZR37. Positions 57-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT3G23610.2-P.

    Proteomic databases

    PRIDEi Q9ZR37.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G23610.1 ; AT3G23610.1 ; AT3G23610 . [Q9ZR37-1 ]
    GeneIDi 821941.
    KEGGi ath:AT3G23610.

    Organism-specific databases

    TAIRi AT3G23610.

    Phylogenomic databases

    HOGENOMi HOG000233767.
    InParanoidi Q9ZR37.
    KOi K05766.
    OMAi QDFEKSL.
    PhylomeDBi Q9ZR37.

    Enzyme and pathway databases

    BioCyci ARA:AT3G23610-MONOMER.
    ARA:GQT-877-MONOMER.
    Reactomei REACT_208246. ERKs are inactivated.

    Gene expression databases

    Genevestigatori Q9ZR37.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR020417. Atypical_DUSP.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    [Graphical view ]
    PRINTSi PR01908. ADSPHPHTASE.
    SMARTi SM00195. DSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a dual-specificity protein phosphatase that inactivates a MAP kinase from Arabidopsis."
      Gupta R., Huang Y., Kieber J., Luan S.
      Plant J. 16:581-589(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS DUAL-SPECIFICITY PROTEIN PHOSPHATASE, MUTAGENESIS OF CYS-135, TISSUE SPECIFICITY, ENZYME REGULATION.
      Strain: cv. Columbia.
    2. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
      Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
      DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
      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. "Regulation of the dual specificity protein phosphatase, DsPTP1, through interactions with calmodulin."
      Yoo J.H., Cheong M.S., Park C.Y., Moon B.C., Kim M.C., Kang Y.H., Park H.C., Choi M.S., Lee J.H., Jung W.Y., Yoon H.W., Chung W.S., Lim C.O., Lee S.Y., Cho M.J.
      J. Biol. Chem. 279:848-858(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF ILE-32; LEU-35 AND LYS-166.
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiDUS1_ARATH
    AccessioniPrimary (citable) accession number: Q9ZR37
    Secondary accession number(s): B3H4F5, F4J449, Q9LUG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2012
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 81 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