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	
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	
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	
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	
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