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Description for Protein DUSP14

dual specificity phosphatase 14
1 total interacting proteins;
Icon Book Platelet Evidence (proteome studies/others : 0/0)
(Not detected in platelets)
Summary:
Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP14 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM] (PubMed Links)
Domains and Motifs:
  • DSPC: Dual specificity phosphatase, catalytic domain

  • Gene Ontology:
    Gene Ontology Annotations

    KEGG - Enzyme ID(s):
    3.1.3.16; 3.1.3.48
    KEGG - Orthology:
    K04459
    KEGG - Pathway(s):
    hsa04010
    (The yellow boxes represents platelet proteins)
    Nomenclature / Alternative Names:
    MKP6; MKP-L; MKP-1 like protein tyrosine phosphatase; MAP kinase phosphatase 6; Mitogen-activated protein kinase phosphatase 6
    Approved Symbol:
    DUSP14
    (De-) Phosphorylations:
    Total (de-) phosphorylation sites: 5
    Human (de-) phosphorylation sites: 5; No platelet phosphorylation sites

    Phosphorylation Targets:
    Total phosphorylation targets: 0
    Human phosphorylation targets: 0;Predicted platelet targets: 0
    Protein Characteristics:
    Isoform-specific Information
    Icon DrugsAssociated Drugs (DrugBank Accession):

    None Available


    Associated Genetic Diseases:

    None Available
    Predicted Transmembrane Domains:
  • Isoform 1 : 0
  • Additional Identifiers:

    HPRD: 09427 Entrez Gene ID: 11072 OMIM ID: 606618 Swissprot Accession: O95147Q6FI36