RALB

RALB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2KE5, 2KWI
Identifiers
Aliases	RALB, RAS like proto-oncogene B
External IDs	MGI: 1927244 HomoloGene: 20632 GeneCards: RALB
Gene ontology Molecular function • nucleotide binding • GDP binding • ATPase binding • GTP binding • protein binding • GTPase activity • ubiquitin protein ligase binding Cellular component • membrane • plasma membrane • autophagosome • exocyst • extracellular exosome • intracellular • midbody Biological process • positive regulation of protein phosphorylation • positive regulation of autophagosome assembly • cellular response to starvation • cytokinesis • negative regulation of protein binding • positive regulation of protein serine/threonine kinase activity • cell division • regulation of exocyst assembly • cellular response to exogenous dsRNA • cell cycle • positive regulation of protein binding • signal transduction • regulation of exocyst localization • apoptotic process • Ras protein signal transduction Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5899	64143
Ensembl	ENSG00000144118	ENSMUSG00000004451
UniProt	P11234	Q9JIW9
RefSeq (mRNA)	NM_002881	NM_022327
RefSeq (protein)	NP_002872	NP_071722
Location (UCSC)	Chr 2: 120.24 – 120.29 Mb	Chr 1: 119.47 – 119.5 Mb
PubMed search

2KE5, 2KWI

5899

64143

ENSG00000144118

ENSMUSG00000004451

P11234

Q9JIW9

NM_002881

NM_022327

NP_002872

NP_071722

Ras-related protein Ral-B (RalB) is a protein that in humans is encoded by the RALB gene on chromosome 2. This protein is one of two paralogs of the Ral protein, the other being RalA, and part of the Ras GTPase family. RalA functions as a molecular switch to activate a number of biological processes, majorly cell division and transport, via signaling pathways. Its biological role thus implicates it in many cancers.

The Ral isoforms share an 80% overall match in amino acid sequence and 100% match in their effector-binding region. The two isoforms mainly differ in the C-terminal hypervariable region, which contains multiple sites for post-translational modification, leading to diverging subcellular localization and biological function. For example, phosphorylation of Serine 194 on RalA by the kinase Aurora A results in the relocation of RalA to the , where RalA helps carry out ; whereas phosphorylation of Serine 198 on RalB by the kinase PKC results in the relocation of RalB to other internal membranes and activation of its tumorigenic function.

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