Aliases for MYH14 Gene
External Ids for MYH14 Gene
Previous HGNC Symbols for MYH14 Gene
Previous GeneCards Identifiers for MYH14 Gene
This gene encodes a member of the myosin superfamily. The protein represents a conventional non-muscle myosin; it should not be confused with the unconventional myosin-14 (MYO14). Myosins are actin-dependent motor proteins with diverse functions including regulation of cytokinesis, cell motility, and cell polarity. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2011]
GeneCards Summary for MYH14 Gene
MYH14 (Myosin, Heavy Chain 14, Non-Muscle) is a Protein Coding gene. Diseases associated with MYH14 include deafness, autosomal dominant 4a and peripheral neuropathy, myopathy, hoarseness, and hearing loss. Among its related pathways are RhoGDI Pathway and Regulation of actin cytoskeleton. GO annotations related to this gene include calmodulin binding and microfilament motor activity. An important paralog of this gene is MYH4.
UniProtKB/Swiss-Prot for MYH14 Gene
Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.
Myosins are a large family of motor proteins that share the common features of ATP hydrolysis, actin binding and potential for kinetic energy transduction. Originally isolated from muscle cells (hence the name), almost all eukaryotic cells are now known to contain myosins. Structurally, mysoins contain a head domain that binds to actin filaments (microfilaments) and is the site of ATP hydrolysis. The tail domain interacts with cargo molecules, and the neck acts as a linker between the head and tail and is the site of regulatory myosin light chain binding. There are 17 myosin families and the most well characterized is myosin II. Myosin II is found predominantly in myocytes and mediates plus-ended movement along microfilaments. It is involved in muscle contraction through cyclic interactions with actin-rich thin filaments, creating a contractile force. It is regulated by phosphorylation via myosin light chain kinase (MLCK) and by intracellular Ca2+ concentrations.