Description: Homo sapiens v-ral simian leukemia viral oncogene homolog A (ras related) (RALA), mRNA. RefSeq Summary (NM_005402): The product of this gene belongs to the small GTPase superfamily, Ras family of proteins. GTP-binding proteins mediate the transmembrane signaling initiated by the occupancy of certain cell surface receptors. This gene encodes a low molecular mass ras-like GTP-binding protein that shares about 50% similarity with other ras proteins. [provided by RefSeq, Jul 2008]. Transcript (Including UTRs) Position: hg19 chr7:39,663,152-39,747,723 Size: 84,572 Total Exon Count: 5 Strand: + Coding Region Position: hg19 chr7:39,726,267-39,745,844 Size: 19,578 Coding Exon Count: 4
ID:RALA_HUMAN DESCRIPTION: RecName: Full=Ras-related protein Ral-A; Flags: Precursor; FUNCTION: Multifunctional 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. Plays a role in the early stages of cytokinesis and is required to tether the exocyst to the cytokinetic furrow. The RALA-exocyst complex regulates integrin- dependent membrane raft exocytosis and growth signaling. Key regulator of LPAR1 signaling and competes with ADRBK1 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells. ENZYME REGULATION: Alternate 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). SUBUNIT: Interacts with RALBP1 via its effector domain. Interacts with EXOC8 and EXOC2. EXOC2 and EXOC8 have overlapping binding sites and compete for RALA binding. Interacts with Clostridium exoenzyme C3. Interacts with RALGPS1. Interacts with LPAR1 and LPAR2. Interacts with ADRBK1 in response to LPAR1 activation. RALA and ADRBK1 mutually inhibit each other's binding to LPAR1. INTERACTION: O54921:Exoc2 (xeno); NbExp=2; IntAct=EBI-1036803, EBI-1036795; P30154:PPP2R1B; NbExp=6; IntAct=EBI-1036803, EBI-357094; SUBCELLULAR LOCATION: Cell surface. Cell membrane; Lipid-anchor; Cytoplasmic side. Cleavage furrow. Midbody. Note=Prior to LPA treatment found predominantly at the cell surface and in the presence of LPA co-localizes with LPAR1 and LPAR2 in the endocytic vesicles. During early cytokinesis localizes at the cleavage furrow membrane. Colocalizes with EXOC2 at the early midbody ring and persists there till maturation of the midbody. INDUCTION: Activated in an LPA-dependent manner by LPAR1 and in an LPA-independent manner by LPAR2. PTM: Prenylation 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). SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
Cholesterol, LDL Sekar Kathiresan et al. BMC medical genetics 2007, A genome-wide association study for blood lipid phenotypes in the Framingham Heart Study., BMC medical genetics.
[PubMed 17903299]
Using a 100K genome-wide scan, we have generated a set of putative associations for common sequence variants and lipid phenotypes. Validation of selected hypotheses in additional samples did not identify any new loci underlying variability in blood lipids. Lack of replication may be due to inadequate statistical power to detect modest quantitative trait locus effects (i.e., <1% of trait variance explained) or reduced genomic coverage of the 100K array. GWAS in FHS using a denser genome-wide genotyping platform and a better-powered replication strategy may identify novel loci underlying blood lipids.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P11233
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
