+ |
PKA | down-regulates activity
phosphorylation
|
GRK1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274079 |
Ser21 |
AFIAARGsFDGSSSQ |
in vitro |
|
pmid |
sentence |
15946941 |
PKA Phosphorylates GRK1 on Ser21. Phosphorylation by PKA inhibits GRK1 activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260841 |
Ser21 |
AFIAARGsFDGSSSQ |
Homo sapiens |
|
pmid |
sentence |
15946941 |
Phosphorylation of GRK1 and GRK7 by cAMP-dependent Protein Kinase Attenuates Their Enzymatic Activities | We also determined that cAMP-dependent protein kinase (PKA) phosphorylates GRK1 at Ser(21) and GRK7 at Ser(23) and Ser(36) in vitro. These sites are also phosphorylated when FLAG-tagged GRK1 and GRK7 are expressed in HEK-293 cells treated with forskolin to stimulate the endogenous production of cAMP and activation of PKA. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276034 |
Ser21 |
AFIAARGsFDGSSSQ |
in vitro |
|
pmid |
sentence |
15946941 |
We also determined that cAMP-dependent protein kinase (PKA) phosphorylates GRK1 at Ser(21) and GRK7 at Ser(23) and Ser(36) in vitro. These sites are also phosphorylated when FLAG-tagged GRK1 and GRK7 are expressed in HEK-293 cells treated with forskolin to stimulate the endogenous production of cAMP and activation of PKA.Phosphorylation of GRK1 and GRK7 by PKA reduces the ability of GRK1 and GRK7 to phosphorylate rhodopsin in vitro. |
|
Publications: |
3 |
Organism: |
In Vitro, Homo Sapiens |
+ |
GRK1 | down-regulates activity
phosphorylation
|
GRK1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251186 |
Ser21 |
AFIAARGsFDGSSSQ |
in vitro |
|
pmid |
sentence |
1527025 |
The major autophosphorylation site yielded the following sequence: DVGAFS488T489VKGVAFEK, where Ser488 and Thr489 are phosphorylated. Additionally, a minor autophosphorylation site was identified at Ser21. we speculate that autophosphorylation of RK may lower the affinity of the enzyme for Rho* via repulsion between phosphorylated sites on Rho* and the kinase. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251187 |
Ser491 |
IQDVGAFsTVKGVAF |
in vitro |
|
pmid |
sentence |
1527025 |
The major autophosphorylation site yielded the following sequence: DVGAFS488T489VKGVAFEK, where Ser488 and Thr489 are phosphorylated. Additionally, a minor autophosphorylation site was identified at Ser21. we speculate that autophosphorylation of RK may lower the affinity of the enzyme for Rho* via repulsion between phosphorylated sites on Rho* and the kinase. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251188 |
Thr492 |
QDVGAFStVKGVAFD |
in vitro |
|
pmid |
sentence |
1527025 |
The major autophosphorylation site yielded the following sequence: DVGAFS488T489VKGVAFEK, where Ser488 and Thr489 are phosphorylated. Additionally, a minor autophosphorylation site was identified at Ser21. we speculate that autophosphorylation of RK may lower the affinity of the enzyme for Rho* via repulsion between phosphorylated sites on Rho* and the kinase. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
GRK1 | up-regulates activity
phosphorylation
|
RHO |
0.922 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251189 |
Ser334 |
PLGDDEAsATVSKTE |
in vitro |
|
pmid |
sentence |
8617805 |
That light-dependent phosphorylation of Rho is mediated primarily by RK. Addition of an inhibitory antibody against rhodopsin kinase (RK) lowered phosphorylation at Ser334, Ser338, and Ser343, without changing the ratio between phosphorylation sites. upon illumination, Ser334c, Ser338, and Ser343 are phosphorylated. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251190 |
Ser338 |
DEASATVsKTETSQV |
in vitro |
|
pmid |
sentence |
8617805 |
That light-dependent phosphorylation of Rho is mediated primarily by RK. Addition of an inhibitory antibody against rhodopsin kinase (RK) lowered phosphorylation at Ser334, Ser338, and Ser343, without changing the ratio between phosphorylation sites. upon illumination, Ser334c, Ser338, and Ser343 are phosphorylated. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251191 |
Ser343 |
TVSKTETsQVAPA |
in vitro |
|
pmid |
sentence |
8617805 |
That light-dependent phosphorylation of Rho is mediated primarily by RK. Addition of an inhibitory antibody against rhodopsin kinase (RK) lowered phosphorylation at Ser334, Ser338, and Ser343, without changing the ratio between phosphorylation sites. upon illumination, Ser334c, Ser338, and Ser343 are phosphorylated. |
|
Publications: |
3 |
Organism: |
In Vitro |