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Q9BY84

- DUS16_HUMAN

UniProt

Q9BY84 - DUS16_HUMAN

Protein

Dual specificity protein phosphatase 16

Gene

DUSP16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Dual specificity protein phosphatase involved in the inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2.2 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei244 – 2441Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. dephosphorylation Source: UniProtKB
    2. inactivation of MAPK activity Source: UniProtKB
    3. MAPK export from nucleus Source: UniProtKB
    4. MAPK phosphatase export from nucleus, leptomycin B sensitive Source: UniProtKB
    5. protein dephosphorylation Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    SignaLinkiQ9BY84.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 16 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Mitogen-activated protein kinase phosphatase 7
    Short name:
    MAP kinase phosphatase 7
    Short name:
    MKP-7
    Gene namesi
    Name:DUSP16
    Synonyms:KIAA1700, MKP7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:17909. DUSP16.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmic vesicle
    Note: After dissociation upon AGTR stimulation, re-associates with ARRB2 on endocytic vesicles.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38475.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 665665Dual specificity protein phosphatase 16PRO_0000094826Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei446 – 4461Phosphoserine; by MAPK11 Publication
    Modified residuei501 – 5011Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated at Ser-446 by MAPK1/ERK2, which prevents its degradation, and thereby stabilizes it and blocks JNK MAPK activity.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BY84.
    PaxDbiQ9BY84.
    PRIDEiQ9BY84.

    PTM databases

    PhosphoSiteiQ9BY84.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BY84.
    BgeeiQ9BY84.
    CleanExiHS_DUSP16.
    GenevestigatoriQ9BY84.

    Organism-specific databases

    HPAiHPA020326.

    Interactioni

    Subunit structurei

    Interacts with ARRB2.1 Publication

    Protein-protein interaction databases

    BioGridi123321. 7 interactions.
    IntActiQ9BY84. 1 interaction.
    STRINGi9606.ENSP00000228862.

    Structurei

    Secondary structure

    1
    665
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103
    Helixi12 – 198
    Beta strandi21 – 244
    Beta strandi26 – 305
    Helixi34 – 396
    Helixi52 – 598
    Helixi65 – 717
    Beta strandi83 – 886
    Helixi95 – 973
    Helixi103 – 11412
    Beta strandi118 – 1214
    Helixi124 – 1318
    Helixi133 – 1353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VSWX-ray2.20A/B5-150[»]
    3TG3X-ray2.68A/B/C/D5-138[»]
    ProteinModelPortaliQ9BY84.
    SMRiQ9BY84. Positions 5-138, 158-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BY84.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 137116RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini227 – 28963Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000082452.
    HOVERGENiHBG005541.
    InParanoidiQ9BY84.
    KOiK04459.
    OMAiQMEFGES.
    OrthoDBiEOG747PJD.
    PhylomeDBiQ9BY84.
    TreeFamiTF105122.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR000340. 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]
    PRINTSiPR01764. 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]

    Sequencei

    Sequence statusi: Complete.

    Q9BY84-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHEMIGTQI VTERLVALLE SGTEKVLLID SRPFVEYNTS HILEAININC    50
    SKLMKRRLQQ DKVLITELIQ HSAKHKVDID CSQKVVVYDQ SSQDVASLSS 100
    DCFLTVLLGK LEKSFNSVHL LAGGFAEFSR CFPGLCEGKS TLVPTCISQP 150
    CLPVANIGPT RILPNLYLGC QRDVLNKELM QQNGIGYVLN ASNTCPKPDF 200
    IPESHFLRVP VNDSFCEKIL PWLDKSVDFI EKAKASNGCV LVHCLAGISR 250
    SATIAIAYIM KRMDMSLDEA YRFVKEKRPT ISPNFNFLGQ LLDYEKKIKN 300
    QTGASGPKSK LKLLHLEKPN EPVPAVSEGG QKSETPLSPP CADSATSEAA 350
    GQRPVHPASV PSVPSVQPSL LEDSPLVQAL SGLHLSADRL EDSNKLKRSF 400
    SLDIKSVSYS ASMAASLHGF SSSEDALEYY KPSTTLDGTN KLCQFSPVQE 450
    LSEQTPETSP DKEEASIPKK LQTARPSDSQ SKRLHSVRTS SSGTAQRSLL 500
    SPLHRSGSVE DNYHTSFLFG LSTSQQHLTK SAGLGLKGWH SDILAPQTST 550
    PSLTSSWYFA TESSHFYSAS AIYGGSASYS AYSCSQLPTC GDQVYSVRRR 600
    QKPSDRADSR RSWHEESPFE KQFKRRSCQM EFGESIMSEN RSREELGKVG 650
    SQSSFSGSME IIEVS 665
    Length:665
    Mass (Da):73,102
    Last modified:June 1, 2001 - v1
    Checksum:i1BD853FF08460DFF
    GO

    Sequence cautioni

    The sequence BAB21791.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231T → M.
    Corresponds to variant rs36049447 [ dbSNP | Ensembl ].
    VAR_051753
    Natural varianti366 – 3661V → M.
    Corresponds to variant rs3809199 [ dbSNP | Ensembl ].
    VAR_051754

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB052156 mRNA. Translation: BAB40814.1.
    AF506796 mRNA. Translation: AAN75120.1.
    AB051487 mRNA. Translation: BAB21791.1. Different initiation.
    BC109235 mRNA. Translation: AAI09236.1.
    CCDSiCCDS8650.1.
    RefSeqiNP_085143.1. NM_030640.2.
    XP_006719218.1. XM_006719155.1.
    UniGeneiHs.536535.

    Genome annotation databases

    EnsembliENST00000228862; ENSP00000228862; ENSG00000111266.
    GeneIDi80824.
    KEGGihsa:80824.
    UCSCiuc001ran.2. human.

    Polymorphism databases

    DMDMi20137933.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB052156 mRNA. Translation: BAB40814.1 .
    AF506796 mRNA. Translation: AAN75120.1 .
    AB051487 mRNA. Translation: BAB21791.1 . Different initiation.
    BC109235 mRNA. Translation: AAI09236.1 .
    CCDSi CCDS8650.1.
    RefSeqi NP_085143.1. NM_030640.2.
    XP_006719218.1. XM_006719155.1.
    UniGenei Hs.536535.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VSW X-ray 2.20 A/B 5-150 [» ]
    3TG3 X-ray 2.68 A/B/C/D 5-138 [» ]
    ProteinModelPortali Q9BY84.
    SMRi Q9BY84. Positions 5-138, 158-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123321. 7 interactions.
    IntActi Q9BY84. 1 interaction.
    STRINGi 9606.ENSP00000228862.

    PTM databases

    PhosphoSitei Q9BY84.

    Polymorphism databases

    DMDMi 20137933.

    Proteomic databases

    MaxQBi Q9BY84.
    PaxDbi Q9BY84.
    PRIDEi Q9BY84.

    Protocols and materials databases

    DNASUi 80824.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228862 ; ENSP00000228862 ; ENSG00000111266 .
    GeneIDi 80824.
    KEGGi hsa:80824.
    UCSCi uc001ran.2. human.

    Organism-specific databases

    CTDi 80824.
    GeneCardsi GC12M012628.
    HGNCi HGNC:17909. DUSP16.
    HPAi HPA020326.
    MIMi 607175. gene.
    neXtProti NX_Q9BY84.
    PharmGKBi PA38475.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000082452.
    HOVERGENi HBG005541.
    InParanoidi Q9BY84.
    KOi K04459.
    OMAi QMEFGES.
    OrthoDBi EOG747PJD.
    PhylomeDBi Q9BY84.
    TreeFami TF105122.

    Enzyme and pathway databases

    SignaLinki Q9BY84.

    Miscellaneous databases

    ChiTaRSi DUSP16. human.
    EvolutionaryTracei Q9BY84.
    GeneWikii DUSP16.
    GenomeRNAii 80824.
    NextBioi 71232.
    PROi Q9BY84.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BY84.
    Bgeei Q9BY84.
    CleanExi HS_DUSP16.
    Genevestigatori Q9BY84.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProi 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 ]
    PRINTSi 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. "MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein."
      Masuda K., Shima H., Watanabe M., Kikuchi K.
      J. Biol. Chem. 276:39002-39011(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
    2. "MAPK phosphatase DUSP16/MKP-7, a candidate tumor suppressor for chromosome region 12p12-13, reduces BCR-ABL-induced transformation."
      Hoornaert I., Marynen P., Goris J., Sciot R., Baens M.
      Oncogene 22:7728-7736(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone marrow.
    3. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    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].
    5. "Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446."
      Masuda K., Shima H., Katagiri C., Kikuchi K.
      J. Biol. Chem. 278:32448-32456(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-446.
    6. "Dynamic interaction between the dual specificity phosphatase MKP7 and the JNK3 scaffold protein beta-arrestin 2."
      Willoughby E.A., Collins M.K.
      J. Biol. Chem. 280:25651-25658(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARRB2.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "The structure of the rhodanese domain of the human 2 dual specificity phosphatase 16."
      Structural genomics consortium (SGC)
      Submitted (JUN-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 5-150.

    Entry informationi

    Entry nameiDUS16_HUMAN
    AccessioniPrimary (citable) accession number: Q9BY84
    Secondary accession number(s): Q547C7, Q9C0G3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 121 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 12
      Human chromosome 12: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3