SCUBA

MYO10 — Myosin X

MYO10 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

MYO10's module in each cell type

Cell typeModuleShares the module with
EndothelialECM Fibrotic Remodeling
ECM remodeling
ADAMTS7, ANGPTL2, CD276, CETP, COL18A1, COLGALT1, DDI2, ERO1A +7 moreView in SCUBA
Goblet cellsChromatin Remodeling
chromatin regulation & transcription
BAZ2B, BPTF, GTF2I, INSR, PDZD8, RERE, TOP2B, ZKSCAN1View in SCUBA

About the gene

SynonymsKIAA0799, MyoX
Chromosome5: 16661907-16936288
Predicted locationIntracellular
Essential geneNo
Protein classPlasma proteins, Predicted intracellular proteins
Molecular functionActin-binding, Calmodulin-binding, Motor protein, Myosin
Biological processTransport

Function

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 a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. 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. Plays a role in formation of the podosome belt in osteoclasts. Functions as a dominant-negative regulator of isoform 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion (By similarity)

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.