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Q05922

- DUS2_MOUSE

UniProt

Q05922 - DUS2_MOUSE

Protein

Dual specificity protein phosphatase 2

Gene

Dusp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.

    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 sitei261 – 2611Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
    2. mitogen-activated protein kinase binding Source: MGI
    3. phosphoprotein phosphatase activity Source: MGI
    4. protein binding Source: IntAct
    5. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    6. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. endoderm formation Source: RefGenome
    2. protein dephosphorylation Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 2 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Dual specificity protein phosphatase PAC-1
    Gene namesi
    Name:Dusp2
    Synonyms:Pac-1, Pac1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:101911. Dusp2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 318318Dual specificity protein phosphatase 2PRO_0000094794Add
    BLAST

    Proteomic databases

    PRIDEiQ05922.

    PTM databases

    PhosphoSiteiQ05922.

    Expressioni

    Tissue specificityi

    In hematopoietic tissues such as spleen and thymus.

    Inductioni

    By mitogens.

    Gene expression databases

    BgeeiQ05922.
    CleanExiMM_DUSP2.
    GenevestigatoriQ05922.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAPK1P284822EBI-7898692,EBI-959949From a different organism.

    Protein-protein interaction databases

    BioGridi199340. 3 interactions.
    IntActiQ05922. 2 interactions.
    MINTiMINT-8214532.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05922.
    SMRiQ05922. Positions 29-147, 174-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 148122RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini241 – 30666Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    GeneTreeiENSGT00700000104321.
    HOGENOMiHOG000294080.
    HOVERGENiHBG007347.
    InParanoidiQ80ZN1.
    KOiK04459.
    OMAiCLAYLMQ.
    OrthoDBiEOG75MVWD.
    TreeFamiTF105122.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR020417. Atypical_DUSP.
    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.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q05922-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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.

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    MPIAMGLETA CELECAALGA LLREPREAER TLLLDCRPFL AFCRSHVRAA    50
    RPVPWNALLR RRARGTPAAA LACLLPDRAL RARLGRGELA RAVVLDESSA 100
    SVAELPPDGP AHLLLAALQH EMRGGPTTVC FLRGGFKSFQ TYCPDLCSEA 150
    PAQALPPAGA ENSNSDPRVP IYDQGGPVEI LPYLYLGSCN HSSDLQGLQA 200
    CGITAVLNVS ASCPNHFEGL FHYKSIPVED NQMVEISAWF QEAISFIDSV 250
    KNSGGRVLVH CQAGISRSAT ICLAYLIQSH RVRLDEAFDF VKQRRGVISP 300
    NFSFMGQLLQ LETQVLCH 318
    Length:318
    Mass (Da):34,576
    Last modified:July 27, 2011 - v2
    Checksum:iAAB6A01BA598C5C9
    GO
    Isoform 2 (identifier: Q05922-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         175-179: GGPVE → VSSDL
         180-318: Missing.

    Show »
    Length:179
    Mass (Da):19,209
    Checksum:iE10BE72F8835521A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 122CE → WQ in AAA85136. (PubMed:7896276)Curated
    Sequence conflicti20 – 201A → V in AAA85136. (PubMed:7896276)Curated
    Sequence conflicti64 – 641R → P in AAA19666. (PubMed:7681221)Curated
    Sequence conflicti64 – 641R → P in AAA85136. (PubMed:7896276)Curated
    Sequence conflicti103 – 1031A → T in AAA19666. (PubMed:7681221)Curated
    Sequence conflicti103 – 1031A → T in AAA85136. (PubMed:7896276)Curated
    Sequence conflicti156 – 1561P → A in AAA85136. (PubMed:7896276)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei175 – 1795GGPVE → VSSDL in isoform 2. CuratedVSP_005135
    Alternative sequencei180 – 318139Missing in isoform 2. CuratedVSP_005136Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11330 mRNA. Translation: AAA19666.1.
    U09268 Genomic DNA. Translation: AAA85136.1.
    AK134067 mRNA. Translation: BAE21999.1.
    AL845368 Genomic DNA. Translation: CAM17446.1.
    BC048696 mRNA. Translation: AAH48696.1.
    CCDSiCCDS16699.1. [Q05922-1]
    PIRiB57126.
    RefSeqiNP_034220.2. NM_010090.2. [Q05922-1]
    UniGeneiMm.4729.

    Genome annotation databases

    EnsembliENSMUST00000028846; ENSMUSP00000028846; ENSMUSG00000027368. [Q05922-1]
    GeneIDi13537.
    KEGGimmu:13537.
    UCSCiuc008mff.1. mouse. [Q05922-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11330 mRNA. Translation: AAA19666.1 .
    U09268 Genomic DNA. Translation: AAA85136.1 .
    AK134067 mRNA. Translation: BAE21999.1 .
    AL845368 Genomic DNA. Translation: CAM17446.1 .
    BC048696 mRNA. Translation: AAH48696.1 .
    CCDSi CCDS16699.1. [Q05922-1 ]
    PIRi B57126.
    RefSeqi NP_034220.2. NM_010090.2. [Q05922-1 ]
    UniGenei Mm.4729.

    3D structure databases

    ProteinModelPortali Q05922.
    SMRi Q05922. Positions 29-147, 174-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199340. 3 interactions.
    IntActi Q05922. 2 interactions.
    MINTi MINT-8214532.

    PTM databases

    PhosphoSitei Q05922.

    Proteomic databases

    PRIDEi Q05922.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028846 ; ENSMUSP00000028846 ; ENSMUSG00000027368 . [Q05922-1 ]
    GeneIDi 13537.
    KEGGi mmu:13537.
    UCSCi uc008mff.1. mouse. [Q05922-1 ]

    Organism-specific databases

    CTDi 1844.
    MGIi MGI:101911. Dusp2.

    Phylogenomic databases

    eggNOGi COG2453.
    GeneTreei ENSGT00700000104321.
    HOGENOMi HOG000294080.
    HOVERGENi HBG007347.
    InParanoidi Q80ZN1.
    KOi K04459.
    OMAi CLAYLMQ.
    OrthoDBi EOG75MVWD.
    TreeFami TF105122.

    Miscellaneous databases

    ChiTaRSi DUSP2. mouse.
    NextBioi 284136.
    PROi Q05922.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q05922.
    CleanExi MM_DUSP2.
    Genevestigatori Q05922.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR020417. Atypical_DUSP.
    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.
    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. "PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase."
      Rohan P., Davis P., Moskaluk C.A., Kearns M., Krutzsch H., Siebenlist U., Kelly K.
      Science 259:1763-1766(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structure of the gene encoding the murine dual specificity tyrosine-threonine phosphatase PAC1."
      Gerondakis S., Economou C., Grumont R.J.
      Genomics 24:182-184(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
      Strain: 129.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Thymus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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] (ISOFORM 1).
      Tissue: Limb.

    Entry informationi

    Entry nameiDUS2_MOUSE
    AccessioniPrimary (citable) accession number: Q05922
    Secondary accession number(s): Q60640, Q80ZN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 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