PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16160139-0 2005 A key serine for the GTPase-activating protein function of regulator of G protein signaling proteins is not a general target for 14-3-3 interactions. Serine 6-12 paired like homeodomain 2 Homo sapiens 59-91 21870221-7 2011 As an alternative approach, we have utilized a glycine-to-serine mutation in the switch 1 region of Galpha subunits that prevents RGS binding. Serine 58-64 paired like homeodomain 2 Homo sapiens 130-133 17540411-12 2007 Since this serine residue is conserved in RGS domains of many RGS proteins, the phosphorylation at Ser166 by PKC might act as a molecular switch and have functional significance. Serine 11-17 paired like homeodomain 2 Homo sapiens 42-45 17540411-12 2007 Since this serine residue is conserved in RGS domains of many RGS proteins, the phosphorylation at Ser166 by PKC might act as a molecular switch and have functional significance. Serine 11-17 paired like homeodomain 2 Homo sapiens 62-65 16160139-4 2005 We confirm that the interaction of RGS3 with 14-3-3tau and 14-3-3zeta requires Ser264 and not the RGS domain and show both that mutation of the conserved RGS domain serine, Ser496 in RGS3, to either alanine or aspartate does not prevent binding of 14-3-3 proteins and that 14-3-3 proteins do not inhibit GTPase-activating protein (GAP) activity against receptor-activated Galpha(o1). Serine 165-171 paired like homeodomain 2 Homo sapiens 35-38 16160139-6 2005 We mutated the equivalent serine residue in the family B/R4 RGS proteins RGS1 and RGS16. Serine 26-32 paired like homeodomain 2 Homo sapiens 60-63 10993892-6 2000 This stimulation and the phosphorylation of GAIP by Erk2 were abrogated when serine at position 151 in the RGS domain was substituted by an alanine residue using site-directed mutagenesis. Serine 77-83 paired like homeodomain 2 Homo sapiens 107-110 9468476-9 1998 Our data suggest that the Ser residue at position 202 of Gtalpha is critical for the specificity of RGS proteins toward Gi and Gq families of G-proteins. Serine 26-29 paired like homeodomain 2 Homo sapiens 100-103 15735747-8 2005 Interestingly, an alpha(13) mutant where a conserved Gly was mutated to a Ser (G205S) retained its ability to bind to p115RhoGEF, induce p115RhoGEF recruitment to the PM, and activate Rho-dependent signaling, even though identical Gly to Ser mutations in other alpha disrupt their interaction with regulator of G-protein signaling (RGS) proteins. Serine 74-77 paired like homeodomain 2 Homo sapiens 332-335 10387017-0 1999 Modulation of the affinity and selectivity of RGS protein interaction with G alpha subunits by a conserved asparagine/serine residue. Serine 118-124 paired like homeodomain 2 Homo sapiens 46-49