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Q99N11

- DUS22_MOUSE

UniProt

Q99N11 - DUS22_MOUSE

Protein

Dual specificity protein phosphatase 22

Gene

Dusp22

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Activates the Jnk signaling pathway. Dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK).1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei88 – 881Phosphocysteine intermediate

    GO - Molecular functioni

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

    GO - Biological processi

    1. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    2. positive regulation of JNK cascade Source: MGI
    3. protein dephosphorylation Source: RefGenome
    4. regulation of cell proliferation Source: MGI
    5. transforming growth factor beta receptor signaling pathway Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 22 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Low molecular weight dual specificity phosphatase 2
    Short name:
    LMW-DSP2
    Gene namesi
    Name:Dusp22
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1915926. Dusp22.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    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
    Mutagenesisi57 – 571D → A: Great decrease in activity. 1 Publication
    Mutagenesisi88 – 881C → S: Complete loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 184183Dual specificity protein phosphatase 22PRO_0000244752Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity

    Post-translational modificationi

    Myristoylation regulates subcellular location, and is necessary for activation of JNK.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate

    Proteomic databases

    PaxDbiQ99N11.
    PRIDEiQ99N11.

    Expressioni

    Tissue specificityi

    Specifically expressed in the testis.1 Publication

    Gene expression databases

    BgeeiQ99N11.
    CleanExiMM_DUSP22.
    GenevestigatoriQ99N11.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi222825. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99N11.
    SMRiQ99N11. Positions 1-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 13369Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    GeneTreeiENSGT00730000110377.
    HOGENOMiHOG000007880.
    HOVERGENiHBG054344.
    KOiK14165.
    OMAiLFIGNFK.
    OrthoDBiEOG7966HM.
    PhylomeDBiQ99N11.
    TreeFamiTF105126.

    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 (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99N11-1) [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

    MGSGMSQILP GLYIGNFKDA RDAEQLSRNK VTHILSVHDT ARPMLEGVKY    50
    LCIPAADTPS QNLTRHFKES IKFIHECRLQ GESCLVHCLA GVSRSVTLVI 100
    AYIMTVTDFG WEDALHTVRA GRSCANPNLG FQRQLQEFEK HEVHQYRQWL 150
    REEYGENPLR DAEEAKNILA APGILKYWAF LRRL 184
    Length:184
    Mass (Da):20,997
    Last modified:June 1, 2001 - v1
    Checksum:i64953325E88AB577
    GO
    Isoform 2 (identifier: Q99N11-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         170-184: AAPGILKYWAFLRRL → GKYKEQGRMEPRPSSRRWSSFSTLPPLTYNNYTTET

    Show »
    Length:205
    Mass (Da):23,489
    Checksum:i643BD84636335A75
    GO

    Sequence cautioni

    The sequence CAI24592.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei170 – 18415AAPGI…FLRRL → GKYKEQGRMEPRPSSRRWSS FSTLPPLTYNNYTTET in isoform 2. 2 PublicationsVSP_019615Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237619 mRNA. Translation: AAK15038.1.
    AK149363 mRNA. Translation: BAE28836.1.
    AL731659 Genomic DNA. Translation: CAI24592.1. Sequence problems.
    AL731659 Genomic DNA. Translation: CAI24593.1.
    AL731659 Genomic DNA. Translation: CAI24594.1.
    BC108362 mRNA. Translation: AAI08363.1.
    CCDSiCCDS26417.1. [Q99N11-1]
    CCDS26418.1. [Q99N11-2]
    RefSeqiNP_001033044.1. NM_001037955.4. [Q99N11-2]
    NP_598829.1. NM_134068.3. [Q99N11-1]
    UniGeneiMm.289646.

    Genome annotation databases

    EnsembliENSMUST00000091672; ENSMUSP00000089260; ENSMUSG00000069255. [Q99N11-1]
    ENSMUST00000095914; ENSMUSP00000093603; ENSMUSG00000069255. [Q99N11-2]
    GeneIDi105352.
    KEGGimmu:105352.
    UCSCiuc007pyx.1. mouse. [Q99N11-2]
    uc007pyy.1. mouse. [Q99N11-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237619 mRNA. Translation: AAK15038.1 .
    AK149363 mRNA. Translation: BAE28836.1 .
    AL731659 Genomic DNA. Translation: CAI24592.1 . Sequence problems.
    AL731659 Genomic DNA. Translation: CAI24593.1 .
    AL731659 Genomic DNA. Translation: CAI24594.1 .
    BC108362 mRNA. Translation: AAI08363.1 .
    CCDSi CCDS26417.1. [Q99N11-1 ]
    CCDS26418.1. [Q99N11-2 ]
    RefSeqi NP_001033044.1. NM_001037955.4. [Q99N11-2 ]
    NP_598829.1. NM_134068.3. [Q99N11-1 ]
    UniGenei Mm.289646.

    3D structure databases

    ProteinModelPortali Q99N11.
    SMRi Q99N11. Positions 1-154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 222825. 2 interactions.

    Proteomic databases

    PaxDbi Q99N11.
    PRIDEi Q99N11.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000091672 ; ENSMUSP00000089260 ; ENSMUSG00000069255 . [Q99N11-1 ]
    ENSMUST00000095914 ; ENSMUSP00000093603 ; ENSMUSG00000069255 . [Q99N11-2 ]
    GeneIDi 105352.
    KEGGi mmu:105352.
    UCSCi uc007pyx.1. mouse. [Q99N11-2 ]
    uc007pyy.1. mouse. [Q99N11-1 ]

    Organism-specific databases

    CTDi 56940.
    MGIi MGI:1915926. Dusp22.

    Phylogenomic databases

    eggNOGi COG2453.
    GeneTreei ENSGT00730000110377.
    HOGENOMi HOG000007880.
    HOVERGENi HBG054344.
    KOi K14165.
    OMAi LFIGNFK.
    OrthoDBi EOG7966HM.
    PhylomeDBi Q99N11.
    TreeFami TF105126.

    Miscellaneous databases

    NextBioi 357626.
    PROi Q99N11.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99N11.
    CleanExi MM_DUSP22.
    Genevestigatori Q99N11.

    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. "Molecular cloning and characterization of a novel dual specificity phosphatase, LMW-DSP2, that lacks the cdc25 homology domain."
      Aoyama K., Nagata M., Oshima K., Matsuda T., Aoki N.
      J. Biol. Chem. 276:27575-27583(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-57 AND CYS-88.
      Tissue: Testis.
    2. "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 2).
      Strain: C57BL/6J.
      Tissue: Retina.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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 2).
      Strain: NMRI.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiDUS22_MOUSE
    AccessioniPrimary (citable) accession number: Q99N11
    Secondary accession number(s): Q5SQN9, Q5SQP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 98 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