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Symbol MYO1C contributors: mct/npt/pgu - updated : 09-02-2016
HGNC name myosin IC
HGNC id 7597
Location 17p13.3      Physical location : 1.367.481 - 1.396.001
Synonym name
  • myosin-1 beta
  • nuclear myosin I
  • Synonym symbol(s) MYO1E, myr2, FLJ23903, NMI, MMI-beta, MMIb, NM1
    TYPE functioning gene
    STRUCTURE 28.52 kb     32 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    MAPPING cloned Y linked Y status provisional
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    32 - 4973 - 1063 - 2006 16960872
    32 - 4742 - 1044 - 2006 16960872
  • nuclear myosin I, isoform B
  • one NoLS is located in the myosin IC isoform B specific N-terminal peptide
  • 32 - 4757 - 1028 - 2006 16960872
    Type ubiquitous
       expressed in (based on citations)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Digestiveintestinesmall intestine  highly
    Reproductivefemale systemovary  highly
     male systemprostate  highly
    SystemCellPubmedSpeciesStageRna symbol
    Hearing / Equilibriumstereocilia
    Lymphoid/Immuneactivated B lymphocyte Mus musculus
    cell lineage
    cell lines
    at STAGE
  • N terminal motor domain containing ATP and actin-binding sites
  • a neck with three IQ calmodulin or calmodulin-like light chain binding domains
  • two nucleolar localization signals (NoLS), that are functional and necessary for nucleolar localization of specifically MYOIC isoform B
  • a tail with a TH motif (short tail), that can inhibit kinesin motor activity, increase the stability of microtubules (MTs), and form crosslinks between MTs and F-actin
  • a C terminal globular domain, implicated in membrane binding
    interspecies homolog to murine Myo1e
  • myosin family
  • CATEGORY motor/contractile
    SUBCELLULAR LOCALIZATION     plasma membrane
    intracellular,nuclear envelope,pore
  • single headed member of the myosin superfamily that localizes to the cytoplasm and the nucleus, where it is involved in transcription by RNA polymerases I and II, intranuclear transport, and nuclear export
  • detected in lipid rafts of B cells
  • is typically localized at the plasma membrane as a dense fibrous network and marginally in the nucleoplasm as punctate foci
  • basic FUNCTION
  • unconventional, apparently non filamentous, may be involved in the adaptation response in the inner ear
  • involved in intracellular movements
  • cooperates with WICH to facilitate transcription on chromatin
  • general transcription factor for RNA polymerases, involved in transcription by RNA polymerase I
  • playing a crucial role for the formation of the first phosphodiester bond during transcription initiation
  • participates along with nuclear actin in transcription and chromatin remodeling
  • in stereocilia of the hair cells in the inner ear, presumably serves as the adaptation motor, which regulates the opening and closing of transduction channels (A
  • mediates the cycling of SLC2A4 transporters in adipocytes by promoting the fusion of SLC2A4-containing vesicles with the cell membrane
  • novel MYO1C-dependent molecular mechanism that mediates the dynamic organization of KIRREL and NPHS1 at the slit diaphragm and is critical for podocyte function
  • is potentially involved in the regulation of MT function during mitosis
  • MYO1C-facilitated G-actin transport might be a critical node for control of cell polarity and motility
  • contributed to insulin-dependent actin filament remodeling
  • is an important mediator of VEGF-induced KDR delivery to the cell surface and plays a role in angiogenic signaling
  • involved in driving the recycling of lipid-raft enriched membranes from the perinuclear recycling compartment to the cell surface
  • role for MYO1C in regulating the actin structures, as MYO1C manipulations lead to loss of the actin filaments and to similar ER phenotype as observed after actin depolymerization
  • having nuclear myosin1 (NM1) function
  • tumor suppressor activity of INPP5K and MYO1C, with overlapping roles in phosphoinositide (PI) 3-kinase/Akt signaling, known to be vital for the cell growth and survival
    a component
  • part of a multiprotein complex that contains WICH, a chromatin remodelling complex containing BAZ1B (Williams syndrome transcription factor), SMARCA5, MYO1C
  • LMNA, EMD are part of a nuclear sub-complex, that partner with Nuclear Myosin 1 (MYO1C) and actin
    small molecule
  • binds calmodulin through its IQ motifs
  • CABP1 and CIB1 are two myristoylated proteins that bind the MYO1C regulatory domain
  • interaction between KIRREL and the motor protein MYO1C, where MYO1C plays an active role in targeting KIRREL to the podocyte cell membrane
  • similarly to KIRREL, also binds NPHS1 and reduces its localization at the podocyte cell membrane
  • MYO1C, an actin-based motor protein that associates with membranes and actin filaments, is required for insulin-induced vesicle tethering in muscle cells
  • interaction of vesicular MYO1C with cortical actin filaments is required for insulin-mediated tethering of SLC2A4 vesicles and for efficient SLC2A4 surface delivery in muscle cells
  • binds SMARCA5 with enhanced affinity upon impairment of the actin-binding function
  • CRK-MYO1C interaction, which modulates membrane dynamics by regulating RAC1 activity, is crucial for cell adhesion and spreading
  • PRKCDBP facilitates signal transduction to MAPK1 by anchoring caveolae to the membrane skeleton of the plasma membrane via MYO1C
  • relationship between MYO1C and KAT6B suggesting that the two are interacting in chromatin remodelling for gene expression
  • LMNA, and EMD modulate the nuclear localization of MYO1C
  • LMNA is a modulator of MYO1C localization in cells, as it regulates the stability of EMD-MYO1C interactions
  • LMNA and EMD partner to modulate genome organization via their cytoskeletal interactors actin and MYO1C
  • cell & other
  • binds to MTs and has a role in maintenance of spindle stability for accurate chromosome separation
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional       loss of function
    leads to an increase in total cellular cholesterol and its disrupted subcellular distribution (PMID :
    constitutional       loss of function
    ablating MYO1C function causes abnormal cholesterol distribution, which has a major selective impact on the autophagy pathway
    Variant & Polymorphism
    Candidate gene
    Therapy target