ECT2

The protein encoded by this gene is a transforming protein that is related to Rho-specific exchange factors and yeast cell cycle regulators. The expression of this gene is elevated with the onset of DNA synthesis and remains elevated during G2 and M phases. In situ hybridization analysis showed that expression is at a high level in cells undergoing mitosis in regenerating liver. Thus, this protein is expressed in a cell cycle-dependent manner during liver regeneration, and is thought to have an important role in the regulation of cytokinesis. [provided by RefSeq]

epithelial cell transforming sequence 2 oncogene

Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death.

Activation of GTPase activity Source: UniProtKB
Activation of protein kinase activity Source: UniProtKB
Bicellular tight junction assembly Source: UniProtKB
Cell differentiation Source: UniProtKB-KW
Cell morphogenesis Source: Ensembl
Cellular response to calcium ion Source: UniProtKB
Cellular response to hydrogen peroxide Source: UniProtKB
Cellular response to ionizing radiation Source: UniProtKB
Intracellular signal transduction Source: InterPro
Mitotic cytokinesis Source: UniProtKB
Nervous system development Source: GO_Central
Positive regulation of apoptotic process Source: UniProtKB
Positive regulation of cytokinesis Source: UniProtKB
Positive regulation of GTPase activity Source: UniProtKB
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of neuron differentiation Source: UniProtKB
Positive regulation of protein import into nucleus Source: UniProtKB
Protein homooligomerization Source: UniProtKB
Protein transport Source: UniProtKB-KW
Regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
Regulation of cytokinesis, actomyosin contractile ring assembly Source: InterPro
Regulation of protein kinase activity Source: UniProtKB
Regulation of small GTPase mediated signal transduction Source: Reactome

Cytoplasm; Nucleus; Spindle; Cleavage furrow; Midbody; Cell junction; Tight junction. Sequestered within the nucleus during interphase. Dispersed throughout the cytoplasm upon breakdown of the nuclear envelope during mitosis. Colocalizes with the centralspindlin complex to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis. Colocalized with RhoA at the midbody. Its subcellular localization to tight junction is increased by calcium. Localized predominantly in the cytoplasm of numerous carcinoma cells.

Phosphorylated by PLK1 in vitro. Hyperphosphorylated during the G2 phase of the cell cycle. Phosphorylation at Thr-373 occurs during the G2/M phase, relieves its auto-inhibition status and stimulates its GEF activity. Phosphorylation at Thr-444 in G2/M phase is required for subsequent binding with PLK1 and Rho exchange activation. Dephosphorylated at the time of cytokinesis. Phosphorylation at Thr-359 is required for its transformation activity in cancer cells.