RHOB

RHOB (Ras Homolog Family Member B) is a Protein Coding gene. Among its related pathways are Semaphorin interactions and ERK Signaling. Gene Ontology (GO) annotations related to this gene include GTP binding and GDP binding. An important paralog of this gene is RHOA.

Ras Homolog Family Member B

Mediates apoptosis in neoplastically transformed cells after DNA damage. Not essential for development but affects cell adhesion and growth factor signaling in transformed cells. Plays a negative role in tumorigenesis as deletion causes tumor formation. Involved in intracellular protein trafficking of a number of proteins. Targets PKN1 to endosomes and is involved in trafficking of the EGF receptor from late endosomes to lysosomes. Also required for stability and nuclear trafficking of AKT1/AKT which promotes endothelial cell survival during vascular development. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Required for genotoxic stress-induced cell death in breast cancer cells.

Biological Process actin filament organizationManual Assertion Based On ExperimentIBA:GO_Central
Biological Process angiogenesisIEA:UniProtKB-KW
Biological Process apoptotic processManual Assertion Based On ExperimentTAS:UniProtKB
Biological Process cell adhesionISS:UniProtKB
Biological Process cell differentiationIEA:UniProtKB-KW
Biological Process cell migrationManual Assertion Based On ExperimentIBA:GO_Central
Biological Process cellular response to hydrogen peroxideManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process cellular response to ionizing radiationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process cortical cytoskeleton organizationManual Assertion Based On ExperimentIBA:GO_Central
Biological Process endosome to lysosome transportManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process endothelial tube morphogenesisManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process establishment or maintenance of cell polarityManual Assertion Based On ExperimentIBA:GO_Central
Biological Process intracellular protein transportIEA:Ensembl
Biological Process mitotic cytokinesisManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of cell cycleISS:UniProtKB
Biological Process negative regulation of cell migrationManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process positive regulation of angiogenesisISS:UniProtKB
Biological Process positive regulation of apoptotic processManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of endothelial cell migrationManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process regulation of actin cytoskeleton organizationManual Assertion Based On ExperimentIBA:GO_Central
Biological Process regulation of cell migrationManual Assertion Based On ExperimentIGI:BHF-UCL
Biological Process regulation of cell shapeManual Assertion Based On ExperimentIBA:GO_Central
Biological Process Rho protein signal transductionManual Assertion Based On ExperimentTAS:UniProtKB

Late endosome membrane
Cell membrane
Nucleus
Cleavage furrow
Late endosomal membrane (geranylgeranylated form). Plasma membrane (farnesylated form). Also detected at the nuclear margin and in the nucleus. Translocates to the equatorial region before furrow formation in a ECT2-dependent manner.

Prenylation specifies the subcellular location of RHOB. The farnesylated form is localized to the plasma membrane while the geranylgeranylated form is localized to the endosome.
(Microbial infection) Glycosylated at Tyr-34 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rho and leads to actin disassembly.
(Microbial infection) Glucosylated at Thr-37 by C.difficile toxins TcdA and TcdB in the colonic epithelium (PubMed:24905543).
Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption (PubMed:24905543).