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Q05923

- DUS2_HUMAN

UniProt

Q05923 - DUS2_HUMAN

Protein

Dual specificity protein phosphatase 2

Gene

DUSP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.

    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 sitei257 – 2571Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. endoderm formation Source: RefGenome
    2. inactivation of MAPK activity Source: ProtInc
    3. peptidyl-tyrosine dephosphorylation Source: GOC
    4. protein dephosphorylation Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    SignaLinkiQ05923.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 2 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Dual specificity protein phosphatase PAC-1
    Gene namesi
    Name:DUSP2
    Synonyms:PAC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3068. DUSP2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27525.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314Dual specificity protein phosphatase 2PRO_0000094793Add
    BLAST

    Proteomic databases

    PaxDbiQ05923.
    PRIDEiQ05923.

    PTM databases

    PhosphoSiteiQ05923.

    Expressioni

    Tissue specificityi

    Expressed in hematopoietic tissues.

    Inductioni

    By mitogens.

    Gene expression databases

    BgeeiQ05923.
    CleanExiHS_DUSP2.
    GenevestigatoriQ05923.

    Interactioni

    Protein-protein interaction databases

    BioGridi108177. 2 interactions.
    IntActiQ05923. 2 interactions.
    MINTiMINT-8214530.
    STRINGi9606.ENSP00000288943.

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi174 – 1763
    Turni177 – 1793
    Beta strandi180 – 1823
    Helixi188 – 19710
    Beta strandi200 – 2045
    Beta strandi206 – 2138
    Beta strandi215 – 2217
    Helixi236 – 24813
    Beta strandi253 – 2553
    Beta strandi258 – 2625
    Helixi263 – 27412
    Helixi279 – 2879
    Helixi305 – 3117

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M3GNMR-A170-314[»]
    ProteinModelPortaliQ05923.
    SMRiQ05923. Positions 25-143, 170-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05923.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 144122RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 30266Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000294080.
    HOVERGENiHBG007347.
    InParanoidiQ05923.
    KOiK04459.
    OMAiCLAYLMQ.
    OrthoDBiEOG75MVWD.
    PhylomeDBiQ05923.
    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]
    PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
    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.

    Q05923-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLEAARELE CAALGTLLRD PREAERTLLL DCRPFLAFCR RHVRAARPVP    50
    WNALLRRRAR GPPAAVLACL LPDRALRTRL VRGELARAVV LDEGSASVAE 100
    LRPDSPAHVL LAALLHETRA GPTAVYFLRG GFDGFQGCCP DLCSEAPAPA 150
    LPPTGDKTSR SDSRAPVYDQ GGPVEILPYL FLGSCSHSSD LQGLQACGIT 200
    AVLNVSASCP NHFEGLFRYK SIPVEDNQMV EISAWFQEAI GFIDWVKNSG 250
    GRVLVHCQAG ISRSATICLA YLMQSRRVRL DEAFDFVKQR RGVISPNFSF 300
    MGQLLQFETQ VLCH 314
    Length:314
    Mass (Da):34,400
    Last modified:February 1, 1994 - v1
    Checksum:iFDD3543C6DE10CA5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11329 mRNA. Translation: AAA50779.1.
    U23853 Genomic DNA. Translation: AAA86112.1.
    AC012307 Genomic DNA. Translation: AAY24222.1.
    CH471207 Genomic DNA. Translation: EAW71385.1.
    BC007771 mRNA. Translation: AAH07771.1.
    CCDSiCCDS2016.1.
    PIRiA57126.
    RefSeqiNP_004409.1. NM_004418.3.
    UniGeneiHs.1183.

    Genome annotation databases

    EnsembliENST00000288943; ENSP00000288943; ENSG00000158050.
    GeneIDi1844.
    KEGGihsa:1844.
    UCSCiuc002svk.4. human.

    Polymorphism databases

    DMDMi464334.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11329 mRNA. Translation: AAA50779.1 .
    U23853 Genomic DNA. Translation: AAA86112.1 .
    AC012307 Genomic DNA. Translation: AAY24222.1 .
    CH471207 Genomic DNA. Translation: EAW71385.1 .
    BC007771 mRNA. Translation: AAH07771.1 .
    CCDSi CCDS2016.1.
    PIRi A57126.
    RefSeqi NP_004409.1. NM_004418.3.
    UniGenei Hs.1183.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M3G NMR - A 170-314 [» ]
    ProteinModelPortali Q05923.
    SMRi Q05923. Positions 25-143, 170-314.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108177. 2 interactions.
    IntActi Q05923. 2 interactions.
    MINTi MINT-8214530.
    STRINGi 9606.ENSP00000288943.

    Chemistry

    ChEMBLi CHEMBL2157858.

    PTM databases

    PhosphoSitei Q05923.

    Polymorphism databases

    DMDMi 464334.

    Proteomic databases

    PaxDbi Q05923.
    PRIDEi Q05923.

    Protocols and materials databases

    DNASUi 1844.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288943 ; ENSP00000288943 ; ENSG00000158050 .
    GeneIDi 1844.
    KEGGi hsa:1844.
    UCSCi uc002svk.4. human.

    Organism-specific databases

    CTDi 1844.
    GeneCardsi GC02M096808.
    HGNCi HGNC:3068. DUSP2.
    MIMi 603068. gene.
    neXtProti NX_Q05923.
    PharmGKBi PA27525.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000294080.
    HOVERGENi HBG007347.
    InParanoidi Q05923.
    KOi K04459.
    OMAi CLAYLMQ.
    OrthoDBi EOG75MVWD.
    PhylomeDBi Q05923.
    TreeFami TF105122.

    Enzyme and pathway databases

    SignaLinki Q05923.

    Miscellaneous databases

    EvolutionaryTracei Q05923.
    GeneWikii DUSP2.
    GenomeRNAii 1844.
    NextBioi 7551.
    PROi Q05923.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q05923.
    CleanExi HS_DUSP2.
    Genevestigatori Q05923.

    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 ]
    PIRSFi PIRSF000939. MAPK_Ptase. 1 hit.
    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. "PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase."
      Rohan P., Davis P., Moskaluk C.A., Kearns M., Krutzsch H., Siebenlist U., Kelly K.
      Science 259:1763-1766(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Genomic organization and chromosomal localization of the DUSP2 gene, encoding a MAP kinase phosphatase, to human 2p11.2-q11."
      Yi H., Morton C.C., Weremowicz S., McBride O.W., Kelly K.
      Genomics 28:92-96(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: B-cell.
    6. "Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP."
      Farooq A., Plotnikova O., Chaturvedi G., Yan S., Zeng L., Zhang Q., Zhou M.M.
      Structure 11:155-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 170-314.

    Entry informationi

    Entry nameiDUS2_HUMAN
    AccessioniPrimary (citable) accession number: Q05923
    Secondary accession number(s): Q53T45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 146 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 2
      Human chromosome 2: 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