MGP Database

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MGP002573

UniProt Annotations

Entry Information
Gene Namev-ral simian leukemia viral oncogene homolog B
Protein EntryRALB_HUMAN
UniProt IDP11234
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=1; IsoId=P11234-1; Sequence=Displayed; Name=2; IsoId=P11234-2; Sequence=VSP_055843; Note=No experimental confirmation available.; Name=3; IsoId=P11234-3; Sequence=VSP_055844; Note=No experimental confirmation available.;
Enzyme RegulationAlternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase- activating protein (GAP).
FunctionMultifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells. Plays a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. Required for suppression of apoptosis. {ECO:0000269|PubMed:18756269}.
PtmPrenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant does not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs). {ECO:0000269|PubMed:17875936}.
SimilarityBelongs to the small GTPase superfamily. Ras family. {ECO:0000305}.
Subcellular LocationCell membrane {ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:18756269}; Lipid-anchor {ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:18756269}; Cytoplasmic side {ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:18756269}. Note=During late cytokinesis localizes at the midbody.
SubunitInteracts with EXOC2 and EXOC8. Interacts with RALBP1 via its effector domain. {ECO:0000269|PubMed:14525976, ECO:0000269|PubMed:19166349, ECO:0000269|PubMed:20696399, ECO:0000269|PubMed:7673236}.
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