6hr1: Difference between revisions
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[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14. | [https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14. | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MYLK2_RABIT MYLK2_RABIT] Implicated in the level of global muscle contraction and cardiac function (By similarity). Phosphorylates a specific serine in the N-terminus of a myosin light chain. | [https://www.uniprot.org/uniprot/MYLK2_RABIT MYLK2_RABIT] Implicated in the level of global muscle contraction and cardiac function (By similarity). Phosphorylates a specific serine in the N-terminus of a myosin light chain.[https://www.uniprot.org/uniprot/MYO10_BOVIN MYO10_BOVIN] In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Stimulates the formation and elongation of filopodia. Regulates cell shape, cell spreading and cell adhesion. Plays a role in formation of the podosome belt in osteoclasts.<ref>PMID:11457842</ref> <ref>PMID:15156152</ref> <ref>PMID:15705568</ref> <ref>PMID:16894163</ref> <ref>PMID:20081229</ref> <ref>PMID:20364131</ref> <ref>PMID:20392702</ref> <ref>PMID:20930142</ref> <ref>PMID:21666676</ref> [https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).<ref>PMID:16760425</ref> <ref>PMID:23893133</ref> <ref>PMID:26969752</ref> <ref>PMID:27165696</ref> [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. | ||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||