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Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
The members of the R7 family of RGS proteins [1] are more complex structures than the R4 family and are closely related to the C. elegans homologues EGL-10 and EAT-16 that were identified in the early stage of RGS protein research [2,5]. Apart from the RGS domain, several additional domains are present in these proteins that mediate protein-protein interactions, sub-cellular localization and protein stability. All R7 family members form obligatory dimers with Gβ5 through the G-γ like (GGL) domain and the disheveled-EGL10-Pleckstrin homology (DEP) domain [6]. The DEP and DEP helical extension domain interact with R7 binding protein (R7BP) or RGS9 anchoring protein (R9AP; in retina) that serves as a plasma membrane anchoring mechanism [3-4].
RGS6 (regulator of G-protein signaling 6) C Show summary » More detailed page |
RGS7 (regulator of G-protein signaling 7) C Show summary » More detailed page |
RGS9 (regulator of G-protein signaling 9) C Show summary » More detailed page |
RGS11 (regulator of G-protein signaling 11) C Show summary » More detailed page |
Database page citation (select format):
Concise Guide to PHARMACOLOGY citation:
Alexander SPH, Kelly E, Mathie AA, Peters JA, Veale EL, Armstrong JF, Buneman OP, Faccenda E, Harding SD, Spedding M, Cidlowski JA, Fabbro D, Davenport AP, Striessnig J, Davies JA et al. (2023) The Concise Guide to PHARMACOLOGY 2023/24: Introduction and Other Protein Targets. Br J Pharmacol. 180 Suppl 2:S1-22.