| Primary Identifier | IPR034377 | Type | Family |
| Short Name | G3BP2 |
| description | Ras GTPase-activating protein-binding protein (also known as GAP SH3 domain-binding protein, G3BP) is involved in several cellular functions and is implicated in stress granule assembly RNA metabolism and hereby cell motility, nuclear transportation and NFkappaB, Ras and Wnt signaling [, ]. There are three human isoforms of G3BP: G3BP1, G3BP2a and G3BP2b. The main difference between the variants is found in the number of PxxP motifs in the central region of the protein []. G3BP contains the PxxP motifs, the glutamine- and glycine rich regions, an RNA recognition motif (RRM) and an N-terminal NTF2-like domain. The NTF2-like domain is the most highly conserved part of the G3BP sequence and it has been implicated in several G3BP functions []. This entry represents G3BP2, which is a cytoplasmic protein that interacts with both IkappaBalpha and IkappaBalpha/NF-kappaB complexes, indicating that G3BP2 may play a role in the control of nucleocytoplasmic distribution of IkappaBalpha and cytoplasmic anchoring of the IkappaBalpha/NF-kappaB complex []. It also contributes to stress granule formation []. |
