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Description for Protein KCNMB1

potassium large conductance calcium-activated channel, subfamily M, beta member 1
4 total interacting proteins; 2 platelet interacting proteins
Icon Book Platelet Evidence (proteome studies/others : 0/0)
(Not detected in platelets)
Summary:
MaxiK channels are large conductance, voltage and calcium-sensitive potassium channels which are fundamental to the control of smooth muscle tone and neuronal excitability. MaxiK channels can be formed by 2 subunits: the pore-forming alpha subunit and the product of this gene, the modulatory beta subunit. Intracellular calcium regulates the physical association between the alpha and beta subunits. [provided by RefSeq] (PubMed Links)
Domains and Motifs:
  • TM: Transmembrane domain

  • Gene Ontology:
    Gene Ontology Annotations

    KEGG - Enzyme ID(s):
    None Available
    KEGG - Orthology:
    K04937
    KEGG - Pathway(s):
    hsa04270
    (The yellow boxes represents platelet proteins)
    Nomenclature / Alternative Names:
    Hbeta1; BKbeta1; Slo-beta; Hslo-beta; K(VCA)beta; BK channel beta subunit; Maxi K channel beta subunit; Charybdotoxin receptor beta subunit 1; Calcium-activated potassium channel beta-subunit; Large conductance Ca2+-activated K+ channel beta 1 subunit; Potassium large conductance calcium activated channel subfamily M beta member 1 protein
    Approved Symbol:
    KCNMB1
    (De-) Phosphorylations:
    Total (de-) phosphorylation sites: 0
    No human (de-) phosphorylation sites; 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):

  • Miconazole(db)


    Associated Genetic Diseases:

  • Hypertension, diastolic, resistance to(Pd)
  • Predicted Transmembrane Domains:
  • Isoform 1 : 2
  • Additional Identifiers:

    HPRD: 10358 Entrez Gene ID: 3779 OMIM ID: 603951 Swissprot Accession: Q16558