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Protein

Dual specificity protein phosphatase 23

Gene

DUSP23

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=1.498 mM for p-nitrophenylphosphate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei95 – 951Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    SABIO-RKQ9BVJ7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 23 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Low molecular mass dual specificity phosphatase 3
    Short name:
    LDP-3
    VH1-like phosphatase Z
    Gene namesi
    Name:DUSP23
    Synonyms:LDP3, VHZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:21480. DUSP23.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB-SubCell
    • extracellular exosome Source: UniProtKB
    • nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134983082.

    Polymorphism and mutation databases

    BioMutaiDUSP23.
    DMDMi73620828.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 150150Dual specificity protein phosphatase 23PRO_0000094835Add
    BLAST

    Proteomic databases

    MaxQBiQ9BVJ7.
    PaxDbiQ9BVJ7.
    PeptideAtlasiQ9BVJ7.
    PRIDEiQ9BVJ7.

    PTM databases

    DEPODiQ9BVJ7.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in spleen, prostate, colon, adrenal gland, mammary gland, thyroid and trachea. Expressed at lower level in uterus, small intestine, bladder, bone marrow, brain, spinal cord and stomach.2 Publications

    Gene expression databases

    BgeeiQ9BVJ7.
    CleanExiHS_DUSP23.
    GenevisibleiQ9BVJ7. HS.

    Organism-specific databases

    HPAiHPA045792.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EXOSC8Q96B263EBI-724940,EBI-371922
    NIF3L1Q9GZT83EBI-724940,EBI-740897

    Protein-protein interaction databases

    BioGridi120275. 24 interactions.
    IntActiQ9BVJ7. 23 interactions.
    MINTiMINT-1412836.
    STRINGi9606.ENSP00000357087.

    Structurei

    Secondary structure

    1
    150
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 124Combined sources
    Turni13 – 153Combined sources
    Beta strandi16 – 205Combined sources
    Helixi25 – 339Combined sources
    Beta strandi36 – 416Combined sources
    Beta strandi43 – 453Combined sources
    Helixi50 – 523Combined sources
    Beta strandi56 – 605Combined sources
    Helixi71 – 8616Combined sources
    Beta strandi90 – 945Combined sources
    Beta strandi96 – 994Combined sources
    Helixi100 – 11415Combined sources
    Helixi118 – 12811Combined sources
    Helixi136 – 14914Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IMGX-ray1.93A2-150[»]
    4ERCX-ray1.15A/B1-150[»]
    ProteinModelPortaliQ9BVJ7.
    SMRiQ9BVJ7. Positions 1-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BVJ7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini75 – 14066Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    GeneTreeiENSGT00390000010254.
    HOGENOMiHOG000108423.
    HOVERGENiHBG056524.
    InParanoidiQ9BVJ7.
    KOiK14165.
    OMAiCERKPPN.
    OrthoDBiEOG7PK90Q.
    PhylomeDBiQ9BVJ7.
    TreeFamiTF105125.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PfamiPF00782. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BVJ7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS
    60 70 80 90 100
    DSCPGLTLHR LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG
    110 120 130 140 150
    RTGTMLACYL VKERGLAAGD AIAEIRRLRP GSIETYEQEK AVFQFYQRTK
    Length:150
    Mass (Da):16,588
    Last modified:June 1, 2001 - v1
    Checksum:i4B72EFA0434B1B5F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti132 – 1321S → P in BAA91172 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti124 – 1241E → V.
    Corresponds to variant rs11544443 [ dbSNP | Ensembl ].
    VAR_051756
    Natural varianti131 – 1311G → S.
    Corresponds to variant rs1129923 [ dbSNP | Ensembl ].
    VAR_023199

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB164404 mRNA. Translation: BAD12141.1.
    AK000449 mRNA. Translation: BAA91172.1.
    AL590560 Genomic DNA. Translation: CAH71101.1.
    BC001140 mRNA. Translation: AAH01140.1.
    CCDSiCCDS1187.1.
    RefSeqiNP_060293.2. NM_017823.3.
    XP_005245346.1. XM_005245289.1.
    UniGeneiHs.425801.

    Genome annotation databases

    EnsembliENST00000368107; ENSP00000357087; ENSG00000158716.
    ENST00000368108; ENSP00000357088; ENSG00000158716.
    ENST00000368109; ENSP00000357089; ENSG00000158716.
    GeneIDi54935.
    KEGGihsa:54935.
    UCSCiuc001ftz.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB164404 mRNA. Translation: BAD12141.1.
    AK000449 mRNA. Translation: BAA91172.1.
    AL590560 Genomic DNA. Translation: CAH71101.1.
    BC001140 mRNA. Translation: AAH01140.1.
    CCDSiCCDS1187.1.
    RefSeqiNP_060293.2. NM_017823.3.
    XP_005245346.1. XM_005245289.1.
    UniGeneiHs.425801.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IMGX-ray1.93A2-150[»]
    4ERCX-ray1.15A/B1-150[»]
    ProteinModelPortaliQ9BVJ7.
    SMRiQ9BVJ7. Positions 1-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi120275. 24 interactions.
    IntActiQ9BVJ7. 23 interactions.
    MINTiMINT-1412836.
    STRINGi9606.ENSP00000357087.

    Chemistry

    BindingDBiQ9BVJ7.
    ChEMBLiCHEMBL2396506.

    PTM databases

    DEPODiQ9BVJ7.

    Polymorphism and mutation databases

    BioMutaiDUSP23.
    DMDMi73620828.

    Proteomic databases

    MaxQBiQ9BVJ7.
    PaxDbiQ9BVJ7.
    PeptideAtlasiQ9BVJ7.
    PRIDEiQ9BVJ7.

    Protocols and materials databases

    DNASUi54935.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000368107; ENSP00000357087; ENSG00000158716.
    ENST00000368108; ENSP00000357088; ENSG00000158716.
    ENST00000368109; ENSP00000357089; ENSG00000158716.
    GeneIDi54935.
    KEGGihsa:54935.
    UCSCiuc001ftz.1. human.

    Organism-specific databases

    CTDi54935.
    GeneCardsiGC01P159750.
    HGNCiHGNC:21480. DUSP23.
    HPAiHPA045792.
    neXtProtiNX_Q9BVJ7.
    PharmGKBiPA134983082.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG2453.
    GeneTreeiENSGT00390000010254.
    HOGENOMiHOG000108423.
    HOVERGENiHBG056524.
    InParanoidiQ9BVJ7.
    KOiK14165.
    OMAiCERKPPN.
    OrthoDBiEOG7PK90Q.
    PhylomeDBiQ9BVJ7.
    TreeFamiTF105125.

    Enzyme and pathway databases

    SABIO-RKQ9BVJ7.

    Miscellaneous databases

    EvolutionaryTraceiQ9BVJ7.
    GeneWikiiDUSP23.
    GenomeRNAii54935.
    NextBioi58050.
    PROiQ9BVJ7.

    Gene expression databases

    BgeeiQ9BVJ7.
    CleanExiHS_DUSP23.
    GenevisibleiQ9BVJ7. HS.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PfamiPF00782. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterization of a novel low-molecular-mass dual-specificity phosphatase-3 (LDP-3) that enhances activation of JNK and p38."
      Takagaki K., Satoh T., Tanuma N., Masuda K., Takekawa M., Shima H., Kikuchi K.
      Biochem. J. 383:447-455(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Carcinoma.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Lung.
    5. "The minimal essential core of a cysteine-based protein-tyrosine phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ."
      Alonso A., Burkhalter S., Sasin J., Tautz L., Bogetz J., Huynh H., Bremer M.C.D., Holsinger L.J., Godzik A., Mustelin T.
      J. Biol. Chem. 279:35768-35774(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Molecular cloning and characterization of a novel dual-specificity phosphatase 23 gene from human fetal brain."
      Wu Q., Li Y., Gu S., Li N., Zheng D., Li D., Zheng Z., Ji C., Xie Y., Mao Y.
      Int. J. Biochem. Cell Biol. 36:1542-1553(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Structure of human dual specificity protein phosphatase 23, VHZ, enzyme-substrate/product complex."
      Agarwal R., Burley S.K., Swaminathan S.
      J. Biol. Chem. 283:8946-8953(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 2-150.

    Entry informationi

    Entry nameiDUS23_HUMAN
    AccessioniPrimary (citable) accession number: Q9BVJ7
    Secondary accession number(s): Q9NX48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: June 1, 2001
    Last modified: June 24, 2015
    This is version 128 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    Was originally erroneously termed DUSP25.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.