protein | Protein subunit | Protein-protein interaction | Hfq protein | protein domain | Protein-protein_interaction | Protein Data Bank | RNA-binding protein | Promyelocytic leukemia protein | G protein | Wiskott–Aldrich syndrome protein | Protein G | protein dimer | Protein A | C-reactive protein | Bone morphogenetic protein 2 | AMP-activated protein kinase | Transmembrane protein | Tau protein | Sterol regulatory element-binding protein | SR protein | Rab escort protein | Protein structure | protein structure | Protein phosphatase 2 | protein kinase | Protein Information Resource | Protein folding | protein folding | Protein domain |
In molecular biology, the BPS domain (Between PH and SH2) domain is a protein domain of approximately 45 amino acids found in the adaptor proteins Grb7Grb10/Grb14.
RIAM (Rap1–GTP-interacting adapter molecule) is a broadly expressed adapter protein that contains an RA (Ras association)-like domain, a PH domain, and several proline-rich sequences.
The interaction between GAB2 and Grb2 at the cell membrane recruits another adaptor protein, the Src homology domain-containing transforming protein 1 (SHC1), before being able to recruit SH2 domain containing molecules.
IFNγ suppresses osteoclast formation by rapidly degrading the RANK adaptor protein TRAF6 in the RANK-RANKL signaling pathway, which otherwise stimulates the production of NF-κB.
Ensuing binding of Ephrin-B3 to the cytoplasmic adaptor protein, Grb4, leads to the recruitment and binding of Dock180 and p21 activated kinases (PAK).
TIRAP, toll-interleukin 1 receptor domain containing adaptor protein