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Q9BV47

- DUS26_HUMAN

UniProt

Q9BV47 - DUS26_HUMAN

Protein

Dual specificity protein phosphatase 26

Gene

DUSP26

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Inactivates MAPK1 and MAPK3 which leads to dephosphorylation of heat shock factor protein 4 and a reduction in its DNA-binding activity. Inhibits MAP kinase p38 by dephosphorylating it and inhibits p38-mediated apoptosis in anaplastic thyroid cancer cells. Can also induce activation of MAP kinase p38 and c-Jun N-terminal kinase (JNK).4 Publications

    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 sitei152 – 1521Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. p53 binding Source: UniProt
    2. phosphoprotein phosphatase activity Source: UniProt
    3. phosphoserine phosphatase activity Source: UniProt
    4. protein binding Source: IntAct
    5. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    6. protein tyrosine phosphatase activity Source: UniProt
    7. RNA polymerase II activating transcription factor binding Source: UniProt

    GO - Biological processi

    1. negative regulation of ERK1 and ERK2 cascade Source: UniProt
    2. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProt
    3. negative regulation of transcription from RNA polymerase II promoter Source: UniProt
    4. peptidyl-tyrosine dephosphorylation Source: GOC
    5. positive regulation of cell adhesion Source: UniProt
    6. positive regulation of peptidyl-serine dephosphorylation Source: UniProt
    7. protein dephosphorylation Source: UniProt

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 26 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Dual specificity phosphatase SKRP3
    Low-molecular-mass dual-specificity phosphatase 4
    Short name:
    DSP-4
    Short name:
    LDP-4
    Mitogen-activated protein kinase phosphatase 8
    Short name:
    MAP kinase phosphatase 8
    Short name:
    MKP-8
    Novel amplified gene in thyroid anaplastic cancer
    Gene namesi
    Name:DUSP26
    Synonyms:DUSP24, LDP4, MKP8, NATA1, SKRP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:28161. DUSP26.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi apparatus Source: UniProt
    4. mitochondrion Source: Ensembl
    5. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi152 – 1521C → A or S: Loss of activity. 3 Publications

    Organism-specific databases

    PharmGKBiPA142671921.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211Dual specificity protein phosphatase 26PRO_0000292219Add
    BLAST

    Proteomic databases

    PaxDbiQ9BV47.
    PRIDEiQ9BV47.

    Expressioni

    Tissue specificityi

    Brain. In the brain it is expressed ubiquitously except in the hippocampus. Expressed in embryonal cancers (retinoblastoma, neuroepithilioma and neuroblastoma) and in anaplatic thyroid cancer.4 Publications

    Gene expression databases

    ArrayExpressiQ9BV47.
    BgeeiQ9BV47.
    CleanExiHS_DUSP26.
    GenevestigatoriQ9BV47.

    Organism-specific databases

    HPAiHPA018221.

    Interactioni

    Subunit structurei

    Interacts with HSF4.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TP53P046379EBI-2924519,EBI-366083

    Protein-protein interaction databases

    BioGridi122457. 1 interaction.
    IntActiQ9BV47. 1 interaction.
    STRINGi9606.ENSP00000256261.

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi62 – 665
    Beta strandi69 – 724
    Helixi74 – 774
    Helixi80 – 867
    Beta strandi90 – 934
    Turni98 – 1003
    Helixi106 – 1094
    Beta strandi112 – 1154
    Helixi127 – 14216
    Beta strandi148 – 1514
    Beta strandi153 – 1564
    Helixi157 – 17014
    Helixi175 – 18410
    Helixi192 – 20716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E0TX-ray1.67A61-211[»]
    4B04X-ray2.20A/B/C/D61-211[»]
    4HRFX-ray1.68A/B/C/D61-211[»]
    ProteinModelPortaliQ9BV47.
    SMRiQ9BV47. Positions 61-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BV47.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini61 – 206146Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000233767.
    HOVERGENiHBG001524.
    InParanoidiQ9BV47.
    KOiK14165.
    OMAiMAFMSRF.
    OrthoDBiEOG7CZK7N.
    PhylomeDBiQ9BV47.
    TreeFamiTF105128.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR020417. Atypical_DUSP.
    IPR020405. Atypical_DUSP_famA.
    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.
    PR01909. ADSPHPHTASEA.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BV47-1) [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

    MCPGNWLWAS MTFMARFSRS SSRSPVRTRG TLEEMPTVQH PFLNVFELER    50
    LLYTGKTACN HADEVWPGLY LGDQDMANNR RELRRLGITH VLNASHSRWR 100
    GTPEAYEGLG IRYLGVEAHD SPAFDMSIHF QTAADFIHRA LSQPGGKILV 150
    HCAVGVSRSA TLVLAYLMLY HHLTLVEAIK KVKDHRGIIP NRGFLRQLLA 200
    LDRRLRQGLE A 211
    Length:211
    Mass (Da):23,946
    Last modified:June 1, 2001 - v1
    Checksum:i60E944304905086D
    GO
    Isoform 2 (identifier: Q9BV47-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-125: Missing.

    Show »
    Length:86
    Mass (Da):9,652
    Checksum:i4DD29AFD5989528B
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 125125Missing in isoform 2. 1 PublicationVSP_026406Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY902194 mRNA. Translation: AAX07132.1.
    AB158288 mRNA. Translation: BAD82942.1.
    AB237597 mRNA. Translation: BAE46506.1.
    AB103376 mRNA. Translation: BAD91015.1.
    AK055704 mRNA. Translation: BAB70991.1.
    CH471080 Genomic DNA. Translation: EAW63392.1.
    CH471080 Genomic DNA. Translation: EAW63393.1.
    CH471080 Genomic DNA. Translation: EAW63394.1.
    BC001613 mRNA. Translation: AAH01613.1.
    BC003115 mRNA. Translation: AAH03115.1.
    BC067804 mRNA. Translation: AAH67804.1.
    CCDSiCCDS6092.1. [Q9BV47-1]
    RefSeqiNP_076930.1. NM_024025.1. [Q9BV47-1]
    XP_005273690.1. XM_005273633.1. [Q9BV47-1]
    XP_006716458.1. XM_006716395.1. [Q9BV47-1]
    UniGeneiHs.8719.

    Genome annotation databases

    EnsembliENST00000256261; ENSP00000256261; ENSG00000133878. [Q9BV47-1]
    ENST00000523956; ENSP00000429176; ENSG00000133878. [Q9BV47-1]
    GeneIDi78986.
    KEGGihsa:78986.
    UCSCiuc003xjp.3. human. [Q9BV47-1]

    Polymorphism databases

    DMDMi74752374.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY902194 mRNA. Translation: AAX07132.1 .
    AB158288 mRNA. Translation: BAD82942.1 .
    AB237597 mRNA. Translation: BAE46506.1 .
    AB103376 mRNA. Translation: BAD91015.1 .
    AK055704 mRNA. Translation: BAB70991.1 .
    CH471080 Genomic DNA. Translation: EAW63392.1 .
    CH471080 Genomic DNA. Translation: EAW63393.1 .
    CH471080 Genomic DNA. Translation: EAW63394.1 .
    BC001613 mRNA. Translation: AAH01613.1 .
    BC003115 mRNA. Translation: AAH03115.1 .
    BC067804 mRNA. Translation: AAH67804.1 .
    CCDSi CCDS6092.1. [Q9BV47-1 ]
    RefSeqi NP_076930.1. NM_024025.1. [Q9BV47-1 ]
    XP_005273690.1. XM_005273633.1. [Q9BV47-1 ]
    XP_006716458.1. XM_006716395.1. [Q9BV47-1 ]
    UniGenei Hs.8719.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E0T X-ray 1.67 A 61-211 [» ]
    4B04 X-ray 2.20 A/B/C/D 61-211 [» ]
    4HRF X-ray 1.68 A/B/C/D 61-211 [» ]
    ProteinModelPortali Q9BV47.
    SMRi Q9BV47. Positions 61-210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122457. 1 interaction.
    IntActi Q9BV47. 1 interaction.
    STRINGi 9606.ENSP00000256261.

    Polymorphism databases

    DMDMi 74752374.

    Proteomic databases

    PaxDbi Q9BV47.
    PRIDEi Q9BV47.

    Protocols and materials databases

    DNASUi 78986.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256261 ; ENSP00000256261 ; ENSG00000133878 . [Q9BV47-1 ]
    ENST00000523956 ; ENSP00000429176 ; ENSG00000133878 . [Q9BV47-1 ]
    GeneIDi 78986.
    KEGGi hsa:78986.
    UCSCi uc003xjp.3. human. [Q9BV47-1 ]

    Organism-specific databases

    CTDi 78986.
    GeneCardsi GC08M033448.
    HGNCi HGNC:28161. DUSP26.
    HPAi HPA018221.
    neXtProti NX_Q9BV47.
    PharmGKBi PA142671921.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000233767.
    HOVERGENi HBG001524.
    InParanoidi Q9BV47.
    KOi K14165.
    OMAi MAFMSRF.
    OrthoDBi EOG7CZK7N.
    PhylomeDBi Q9BV47.
    TreeFami TF105128.

    Miscellaneous databases

    EvolutionaryTracei Q9BV47.
    GenomeRNAii 78986.
    NextBioi 67552.
    PROi Q9BV47.

    Gene expression databases

    ArrayExpressi Q9BV47.
    Bgeei Q9BV47.
    CleanExi HS_DUSP26.
    Genevestigatori Q9BV47.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR020417. Atypical_DUSP.
    IPR020405. Atypical_DUSP_famA.
    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.
    PR01909. ADSPHPHTASEA.
    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-152, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "A novel amplification target, DUSP26, promotes anaplastic thyroid cancer cell growth by inhibiting p38 MAPK activity."
      Yu W., Imoto I., Inoue J., Onda M., Emi M., Inazawa J.
      Oncogene 26:1178-1187(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-152, FUNCTION, TISSUE SPECIFICITY.
    3. "Characterization of a novel low-molecular-mass dual specificity phosphatase-4 (LDP-4) expressed in brain."
      Takagaki K., Shima H., Tanuma N., Nomura M., Satoh T., Watanabe M., Kikuchi K.
      Mol. Cell. Biochem. 296:177-184(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Identification of a novel dual specificity phosphatase, SKRP3."
      Zama T., Aoki R., Murata M., Ikeda Y.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "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] (ISOFORM 1).
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Lung.
    8. "Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26."
      Hu Y., Mivechi N.F.
      Mol. Cell. Biol. 26:3282-3294(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-152, INTERACTION WITH HSF4, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiDUS26_HUMAN
    AccessioniPrimary (citable) accession number: Q9BV47
    Secondary accession number(s): D3DSV8, Q9BTW0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 110 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 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3