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Q8NEJ0

- DUS18_HUMAN

UniProt

Q8NEJ0 - DUS18_HUMAN

Protein

Dual specificity protein phosphatase 18

Gene

DUSP18

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. In vitro, dephosphorylates p-nitrophenyl phosphate (pNPP).

    Catalytic activityi

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

    Enzyme regulationi

    Activated by manganese ions, inhibited by iodoaretic acid.

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei104 – 1041Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
    2. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    3. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. peptidyl-tyrosine dephosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 18 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Low molecular weight dual specificity phosphatase 20
    Short name:
    LMW-DSP20
    Gene namesi
    Name:DUSP18
    Synonyms:LMWDSP20
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:18484. DUSP18.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731D → A: Abolishes most of in vitro phosphatase activity. 1 Publication
    Mutagenesisi102 – 1021L → V: No effect on in vitro phosphatase activity. 1 Publication
    Mutagenesisi104 – 1041C → S: Abolishes most of in vitro phosphatase activity. 1 Publication
    Mutagenesisi110 – 1101R → K: Abolishes most of in vitro phosphatase activity. 1 Publication
    Mutagenesisi111 – 1111S → A: Abolishes most of in vitro phosphatase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134928498.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 188188Dual specificity protein phosphatase 18PRO_0000094828Add
    BLAST

    Proteomic databases

    MaxQBiQ8NEJ0.
    PaxDbiQ8NEJ0.
    PRIDEiQ8NEJ0.

    PTM databases

    PhosphoSiteiQ8NEJ0.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in liver, brain, ovary and testis.2 Publications

    Gene expression databases

    ArrayExpressiQ8NEJ0.
    BgeeiQ8NEJ0.
    CleanExiHS_DUSP18.
    GenevestigatoriQ8NEJ0.

    Organism-specific databases

    HPAiCAB034070.
    HPA051349.

    Interactioni

    Protein-protein interaction databases

    BioGridi127280. 1 interaction.
    STRINGi9606.ENSP00000333917.

    Structurei

    Secondary structure

    1
    188
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 244
    Beta strandi27 – 304
    Helixi34 – 363
    Helixi38 – 436
    Beta strandi48 – 514
    Beta strandi65 – 684
    Helixi79 – 824
    Helixi83 – 9513
    Beta strandi100 – 1034
    Beta strandi105 – 1095
    Helixi110 – 12213
    Helixi127 – 13711
    Helixi145 – 15915
    Helixi176 – 1783

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ESBX-ray2.00A1-188[»]
    ProteinModelPortaliQ8NEJ0.
    SMRiQ8NEJ0. Positions 18-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8NEJ0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 14970Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000233766.
    HOVERGENiHBG051422.
    InParanoidiQ8NEJ0.
    KOiK14165.
    OMAiASPCAFP.
    PhylomeDBiQ8NEJ0.
    TreeFamiTF316009.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR020417. Atypical_DUSP.
    IPR020420. Atypical_DUSP_famB.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    [Graphical view]
    PRINTSiPR01908. ADSPHPHTASE.
    PR01910. ADSPHPHTASEB.
    SMARTiSM00195. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8NEJ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAPSCAFPV QFRQPSVSGL SQITKSLYIS NGVAANNKLM LSSNQITMVI    50
    NVSVEVVNTL YEDIQYMQVP VADSPNSRLC DFFDPIADHI HSVEMKQGRT 100
    LLHCAAGVSR SAALCLAYLM KYHAMSLLDA HTWTKSCRPI IRPNSGFWEQ 150
    LIHYEFQLFG KNTVHMVSSP VGMIPDIYEK EVRLMIPL 188
    Length:188
    Mass (Da):21,066
    Last modified:October 1, 2002 - v1
    Checksum:iA6EDECC3624F570F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21T → A in AAN77931. (PubMed:12591617)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF533017 mRNA. Translation: AAN59787.1.
    AF461689 mRNA. Translation: AAN77931.1.
    CR456406 mRNA. Translation: CAG30292.1.
    AK056074 mRNA. Translation: BAG51616.1.
    CH471095 Genomic DNA. Translation: EAW59913.1.
    BC030987 mRNA. Translation: AAH30987.1.
    CCDSiCCDS13883.1.
    RefSeqiNP_689724.3. NM_152511.3.
    XP_005261423.1. XM_005261366.1.
    XP_005261424.1. XM_005261367.1.
    XP_005261425.1. XM_005261368.2.
    XP_006724211.1. XM_006724148.1.
    UniGeneiHs.517544.

    Genome annotation databases

    EnsembliENST00000334679; ENSP00000333917; ENSG00000167065.
    ENST00000377087; ENSP00000366291; ENSG00000167065.
    ENST00000404885; ENSP00000385463; ENSG00000167065.
    ENST00000407308; ENSP00000386063; ENSG00000167065.
    GeneIDi150290.
    KEGGihsa:150290.
    UCSCiuc003aiu.3. human.

    Polymorphism databases

    DMDMi29840768.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF533017 mRNA. Translation: AAN59787.1 .
    AF461689 mRNA. Translation: AAN77931.1 .
    CR456406 mRNA. Translation: CAG30292.1 .
    AK056074 mRNA. Translation: BAG51616.1 .
    CH471095 Genomic DNA. Translation: EAW59913.1 .
    BC030987 mRNA. Translation: AAH30987.1 .
    CCDSi CCDS13883.1.
    RefSeqi NP_689724.3. NM_152511.3.
    XP_005261423.1. XM_005261366.1.
    XP_005261424.1. XM_005261367.1.
    XP_005261425.1. XM_005261368.2.
    XP_006724211.1. XM_006724148.1.
    UniGenei Hs.517544.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ESB X-ray 2.00 A 1-188 [» ]
    ProteinModelPortali Q8NEJ0.
    SMRi Q8NEJ0. Positions 18-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127280. 1 interaction.
    STRINGi 9606.ENSP00000333917.

    PTM databases

    PhosphoSitei Q8NEJ0.

    Polymorphism databases

    DMDMi 29840768.

    Proteomic databases

    MaxQBi Q8NEJ0.
    PaxDbi Q8NEJ0.
    PRIDEi Q8NEJ0.

    Protocols and materials databases

    DNASUi 150290.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334679 ; ENSP00000333917 ; ENSG00000167065 .
    ENST00000377087 ; ENSP00000366291 ; ENSG00000167065 .
    ENST00000404885 ; ENSP00000385463 ; ENSG00000167065 .
    ENST00000407308 ; ENSP00000386063 ; ENSG00000167065 .
    GeneIDi 150290.
    KEGGi hsa:150290.
    UCSCi uc003aiu.3. human.

    Organism-specific databases

    CTDi 150290.
    GeneCardsi GC22M031048.
    HGNCi HGNC:18484. DUSP18.
    HPAi CAB034070.
    HPA051349.
    MIMi 611446. gene.
    neXtProti NX_Q8NEJ0.
    PharmGKBi PA134928498.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000233766.
    HOVERGENi HBG051422.
    InParanoidi Q8NEJ0.
    KOi K14165.
    OMAi ASPCAFP.
    PhylomeDBi Q8NEJ0.
    TreeFami TF316009.

    Miscellaneous databases

    EvolutionaryTracei Q8NEJ0.
    GeneWikii DUSP18.
    GenomeRNAii 150290.
    NextBioi 86394.
    PROi Q8NEJ0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8NEJ0.
    Bgeei Q8NEJ0.
    CleanExi HS_DUSP18.
    Genevestigatori Q8NEJ0.

    Family and domain databases

    Gene3Di 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.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    [Graphical view ]
    PRINTSi PR01908. ADSPHPHTASE.
    PR01910. ADSPHPHTASEB.
    SMARTi SM00195. DSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of two novel low-molecular-weight dual specificity phosphatases."
      Hood K.L., Tobin J.F., Yoon C.
      Biochem. Biophys. Res. Commun. 298:545-551(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Colon tumor.
    2. "Molecular cloning and characterization of a novel dual-specificity phosphatase18 gene from human fetal brain."
      Wu Q., Gu S., Dai J., Dai J., Wang L., Li Y., Zeng L., Xu J., Ye X., Zhao W., Ji C., Xie Y., Mao Y.
      Biochim. Biophys. Acta 1625:296-304(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-73; LEU-102; CYS-104; ARG-110 AND SER-111.
      Tissue: Fetal brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Placenta.
    7. "Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family."
      Jeong D.G., Cho Y.H., Yoon T.S., Kim J.H., Son J.H., Ryu S.E., Kim S.J.
      Acta Crystallogr. D 62:582-588(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiDUS18_HUMAN
    AccessioniPrimary (citable) accession number: Q8NEJ0
    Secondary accession number(s): B3KPA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 106 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3