| Description | RGS14 is a regulator of G protein signaling (RGS) protein and contains an N-terminal RGS domain, two tandem Ras-binding domains (RBDs) and a G protein regulatory (GPR, also referred to as a GoLoco) motif. It regulates G protein nucleotide exchange and hydrolysis by acting as a GTPase-activating protein (GAP) through its RGS domain, and as a guanine nucleotide dissociation inhibitor (GDI) through its GoLoco motif [ , ]. Both domains of RGS14 target members of the Gialpha subclass []. It is a microtubule-associated protein that may modulate microtubule dynamics and spindle formation [] and play an essential role during mammalian cell division []. RGS14 regulates the activation of alphaMbeta2 integrin during phagocytosis []. It is a key regulator of signalling pathways linking synaptic plasticity in CA2 pyramidal neurons to hippocampal-based learning and memory [].RGS14 binds activated H-Ras-GTP through its first RBD and interacts with Rap2-GTP and RAF kinases by the second tandem RBD. This entry represents the second RBD. RBD is structurally similar to the β-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. RGS14 modulates neuronal physiology and all of its binding partners have roles in synaptic plasticity [ , , , , ]. | Name | Regulator of G protein signaling 14, Ras-binding domain 2 |
| Short Name | RBD2_RGS14 | Type | Domain |
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