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The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating

IL15RA is a cytokine receptor that specifically binds IL15 with high affinity. It shares two subunits with the receptor of IL2, the IL2R beta and IL2R gamma chains. This forms the basis of many overlapping biological activities of IL15 and IL2. The IL2 receptor requires an additional IL2-specific alpha subunit for high affinity IL2 binding. This protein is structurally related to IL2R alpha, but is capable of binding IL15 with high affinity independent of other subunits, which suggests the di

This gene was identified on the basis of its stimulationby c-Myc protein. The latter is a transcription factor thatparticipates in the regulation of cell proliferation,differentiation, and apoptosis. The exact function of this gene isnot known but studies in rat suggest a role in cellularproliferation and c-Myc-mediated transformation. Two alternativetranscripts encoding different proteins have been described.[provided by RefSeq, Jul 2008].

This gene encodes a membrane glycoprotein that is a member of the signaling lymphocyte activation molecule (SLAM) family. This family forms a subset of the larger CD2 cell-surface receptor Ig superfamily. The encoded protein is a homophilic adhesion molecule that is expressed in numerous immune cells types and is involved in regulating receptor-mediated signaling in those cells. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Oct 2011]