MYO9B — Myosin IXB
MYO9B belongs to a gene co-expression module in 4 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.
MYO9B's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| CD4⁺ T cells | Leukocyte Motility migration & adhesion | ATP2A3, HSH2D, LRP12, LZTFL1, MYO1G, NBEAL2, PPARG, TBC1D31 +1 more | View in SCUBA |
| Gamma-delta T cells | T Cell Migration migration & adhesion | BCL2, BPNT2, CCDC88B, DNM2, EDC4, GMDS, LRRC58, MARK3 +14 more | |
| Macrophages | Transcriptional Repression Housekeeping | AKAP8, ANKRD11, ARIH2, BACH1, CCNT2, CDK13, CEP95, CSNK1D +23 more | View in SCUBA |
| Mucosal-associated invariant T cell | Rho GTPase Migration migration & adhesion | GNA13, HAPSTR1, HIPK1, LEMD3, LUZP1, PPP1CB, PPP1R16B, PPP4R3A +4 more |
About the gene
| Synonyms | CELIAC4 |
|---|---|
| Chromosome | 19: 17075777-17214537 |
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Disease related genes, Human disease related genes, Plasma proteins, Predicted intracellular proteins |
| Molecular function | Actin-binding, Calmodulin-binding, GTPase activation, Motor protein, Myosin |
Function
Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions. Also acts as a GTPase activator for RHOA. Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.