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P28563

- DUS1_MOUSE

UniProt

P28563 - DUS1_MOUSE

Protein

Dual specificity protein phosphatase 1

Gene

Dusp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei258 – 2581Phosphocysteine intermediate

    GO - Molecular functioni

    1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: UniProtKB
    2. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    3. protein tyrosine/threonine phosphatase activity Source: Ensembl
    4. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular response to hormone stimulus Source: Ensembl
    2. endoderm formation Source: RefGenome
    3. inactivation of MAPK activity Source: UniProtKB
    4. intracellular signal transduction Source: Ensembl
    5. mitotic cell cycle arrest Source: UniProtKB
    6. negative regulation of apoptotic process Source: Ensembl
    7. negative regulation of MAPK cascade Source: UniProtKB
    8. negative regulation of MAP kinase activity Source: UniProtKB
    9. negative regulation of meiotic cell cycle Source: UniProtKB
    10. peptidyl-threonine dephosphorylation Source: UniProtKB
    11. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    12. positive regulation of apoptotic process Source: Ensembl
    13. protein dephosphorylation Source: RefGenome
    14. regulation of apoptotic process Source: RefGenome
    15. regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
    16. response to calcium ion Source: Ensembl
    17. response to cAMP Source: Ensembl
    18. response to estradiol Source: Ensembl
    19. response to glucocorticoid Source: Ensembl
    20. response to hydrogen peroxide Source: Ensembl
    21. response to light stimulus Source: Ensembl
    22. response to retinoic acid Source: Ensembl
    23. response to testosterone Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 1 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Mitogen-activated protein kinase phosphatase 1
    Short name:
    MAP kinase phosphatase 1
    Short name:
    MKP-1
    Protein-tyrosine phosphatase 3CH134
    Protein-tyrosine phosphatase ERP
    Gene namesi
    Name:Dusp1
    Synonyms:3ch134, Mkp1, Ptpn10, Ptpn16
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:105120. Dusp1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi258 – 2581C → S: Loss of activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 367367Dual specificity protein phosphatase 1PRO_0000094791Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei359 – 3591Phosphoserine; by MAPK1 and MAPK31 Publication
    Modified residuei364 – 3641Phosphoserine; by MAPK1 and MAPK31 Publication

    Post-translational modificationi

    Phosphorylation at Ser-359 and Ser-364 by MAPK1/ERK2 and MAPK3/ERK1 reduces its rate of degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP28563.

    PTM databases

    PhosphoSiteiP28563.

    Expressioni

    Inductioni

    By growth factors.

    Gene expression databases

    ArrayExpressiP28563.
    BgeeiP28563.
    CleanExiMM_DUSP1.
    GenevestigatoriP28563.

    Interactioni

    Protein-protein interaction databases

    BioGridi202482. 3 interactions.
    DIPiDIP-29877N.
    STRINGi10090.ENSMUSP00000025025.

    Structurei

    3D structure databases

    ProteinModelPortaliP28563.
    SMRiP28563. Positions 13-136, 172-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 137118RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini175 – 367193Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000294080.
    HOVERGENiHBG007347.
    InParanoidiP28563.
    KOiK04459.
    OMAiSFNSSHI.
    OrthoDBiEOG75MVWD.
    PhylomeDBiP28563.
    TreeFamiTF105122.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR020417. Atypical_DUSP.
    IPR020420. Atypical_DUSP_famB.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR008343. MKP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR001763. Rhodanese-like_dom.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    PF00581. Rhodanese. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
    PRINTSiPR01908. ADSPHPHTASE.
    PR01910. ADSPHPHTASEB.
    PR01764. MAPKPHPHTASE.
    SMARTiSM00195. DSPc. 1 hit.
    SM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    SSF52821. SSF52821. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P28563-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVMEVGILDA GGLRALLREG AAQCLLLDCR SFFAFNAGHI AGSVNVRFST    50
    IVRRRAKGAM GLEHIVPNAE LRGRLLAGAY HAVVLLDERS ASLDGAKRDG 100
    TLALAAGALC REARSTQVFF LQGGYEAFSA SCPELCSKQS TPTGLSLPLS 150
    TSVPDSAESG CSSCSTPLYD QGGPVEILSF LYLGSAYHAS RKDMLDALGI 200
    TALINVSANC PNHFEGHYQY KSIPVEDNHK ADISSWFNEA IDFIDSIKDA 250
    GGRVFVHCQA GISRSATICL AYLMRTNRVK LDEAFEFVKQ RRSIISPNFS 300
    FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHPT 350
    NSALNYLKSP ITTSPSC 367
    Length:367
    Mass (Da):39,370
    Last modified:December 1, 1992 - v1
    Checksum:i50B5F90FEBBD19AB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61940 mRNA. Translation: CAA43944.1.
    S64851 Genomic DNA. Translation: AAB27882.1.
    BC006967 mRNA. Translation: AAH06967.1.
    CCDSiCCDS28552.1.
    PIRiA54681. S24411.
    RefSeqiNP_038670.1. NM_013642.3.
    UniGeneiMm.239041.

    Genome annotation databases

    EnsembliENSMUST00000025025; ENSMUSP00000025025; ENSMUSG00000024190.
    GeneIDi19252.
    KEGGimmu:19252.
    UCSCiuc008bee.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61940 mRNA. Translation: CAA43944.1 .
    S64851 Genomic DNA. Translation: AAB27882.1 .
    BC006967 mRNA. Translation: AAH06967.1 .
    CCDSi CCDS28552.1.
    PIRi A54681. S24411.
    RefSeqi NP_038670.1. NM_013642.3.
    UniGenei Mm.239041.

    3D structure databases

    ProteinModelPortali P28563.
    SMRi P28563. Positions 13-136, 172-314.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202482. 3 interactions.
    DIPi DIP-29877N.
    STRINGi 10090.ENSMUSP00000025025.

    Chemistry

    BindingDBi P28563.
    ChEMBLi CHEMBL5623.

    PTM databases

    PhosphoSitei P28563.

    Proteomic databases

    PRIDEi P28563.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025025 ; ENSMUSP00000025025 ; ENSMUSG00000024190 .
    GeneIDi 19252.
    KEGGi mmu:19252.
    UCSCi uc008bee.2. mouse.

    Organism-specific databases

    CTDi 1843.
    MGIi MGI:105120. Dusp1.

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000294080.
    HOVERGENi HBG007347.
    InParanoidi P28563.
    KOi K04459.
    OMAi SFNSSHI.
    OrthoDBi EOG75MVWD.
    PhylomeDBi P28563.
    TreeFami TF105122.

    Miscellaneous databases

    NextBioi 296092.
    PROi P28563.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28563.
    Bgeei P28563.
    CleanExi MM_DUSP1.
    Genevestigatori P28563.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR020417. Atypical_DUSP.
    IPR020420. Atypical_DUSP_famB.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR008343. MKP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR001763. Rhodanese-like_dom.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    PF00581. Rhodanese. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000939. MAPK_Ptase. 1 hit.
    PRINTSi PR01908. ADSPHPHTASE.
    PR01910. ADSPHPHTASEB.
    PR01764. MAPKPHPHTASE.
    SMARTi SM00195. DSPc. 1 hit.
    SM00450. RHOD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    SSF52821. SSF52821. 1 hit.
    PROSITEi PS50206. RHODANESE_3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA sequence of a growth factor-inducible immediate early gene and characterization of its encoded protein."
      Charles C.H., Abler A.S., Lau L.F.
      Oncogene 7:187-190(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. "Structure, mapping, and expression of erp, a growth factor-inducible gene encoding a nontransmembrane protein tyrosine phosphatase, and effect of ERP on cell growth."
      Noguchi T., Metz R., Chen L., Mattei M.-G., Carrasco D., Bravo R.
      Mol. Cell. Biol. 13:5195-5205(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Tissue: Liver.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Czech II.
      Tissue: Mammary gland.
    4. "MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo."
      Sun H., Charles C.H., Lau L.F., Tonks N.K.
      Cell 75:487-493(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation."
      Brondello J.M., Pouyssegur J., McKenzie F.R.
      Science 286:2514-2517(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-359 AND SER-364.

    Entry informationi

    Entry nameiDUS1_MOUSE
    AccessioniPrimary (citable) accession number: P28563
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3