| + |
CSNK2A1 |
phosphorylation
|
GYS1 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250878 |
Ser10 |
LNRTLSMsSLPGLED |
in vitro |
|
| pmid |
sentence |
| 2117608 |
With all four peptides, prior phosphorylation significantly stimulated phosphorylation by casein kinase I. From these results, we propose that there are substrates for casein kinase I for which prior phosphorylation is a critical determinant of protein kinase action. | From analysis of 32P release during Edman degradation, no radioactively labeled phosphate was associated with Thr3 or Ser7, but could be accounted for by phosphorylation at Ser10 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250879 |
Ser645 |
RPASVPPsPSLSRHS |
in vitro |
|
| pmid |
sentence |
| 2117608 |
With all four peptides, prior phosphorylation significantly stimulated phosphorylation by casein kinase I. From these results, we propose that there are substrates for casein kinase I for which prior phosphorylation is a critical determinant of protein kinase action. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250880 |
Ser649 |
VPPSPSLsRHSSPHQ |
in vitro |
|
| pmid |
sentence |
| 2117608 |
With all four peptides, prior phosphorylation significantly stimulated phosphorylation by casein kinase I. From these results, we propose that there are substrates for casein kinase I for which prior phosphorylation is a critical determinant of protein kinase action. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250881 |
Ser653 |
PSLSRHSsPHQSEDE |
in vitro |
|
| pmid |
sentence |
| 2117608 |
With all four peptides, prior phosphorylation significantly stimulated phosphorylation by casein kinase I. From these results, we propose that there are substrates for casein kinase I for which prior phosphorylation is a critical determinant of protein kinase action. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250883 |
Ser698 |
PEWPRRAsCTSSTSG |
in vitro |
|
| pmid |
sentence |
| 2117608 |
With all four peptides, prior phosphorylation significantly stimulated phosphorylation by casein kinase I. From these results, we propose that there are substrates for casein kinase I for which prior phosphorylation is a critical determinant of protein kinase action. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250884 |
Thr713 |
SKRNSVDtATSSSLS |
in vitro |
|
| pmid |
sentence |
| 2117608 |
With all four peptides, prior phosphorylation significantly stimulated phosphorylation by casein kinase I. From these results, we propose that there are substrates for casein kinase I for which prior phosphorylation is a critical determinant of protein kinase action. |
|
| Publications: |
6 |
Organism: |
In Vitro |
| + |
GSK3B | down-regulates activity 
phosphorylation
|
GYS1 |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235793 |
Ser641 |
YRYPRPAsVPPSPSL |
Homo sapiens |
|
| pmid |
sentence |
| 14593110 |
Glycogen synthase kinase-3 (gsk-3) phosphorylates four serine residues in the cooh terminus of glycogen synthase. Phosphorylation of one of these residues, ser640 (site 3a), causes strong inactivation of glycogen synthase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251239 |
Ser641 |
YRYPRPAsVPPSPSL |
|
|
| pmid |
sentence |
| 11427888 |
Glycogen synthase has multiple serines (residues 640, 644, 648 and 652) separated by three residues, and those Ser residues are phosphorylated sequentially by GSK3 from the C-terminal end after Ser 656 has been phosphorylated by casein kinase II. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253005 |
Ser641 |
YRYPRPAsVPPSPSL |
in vitro |
|
| pmid |
sentence |
| 6772446 |
Glycogen synthase kinase-3 phosphorylates three serine residues on glycogen synthase (sites 3a, 3b and 3c) which are all located in the same nine-amino-acid segment of the polypeptide chain. The sequence in this region is: Arg-Tyr-Pro-Arg-Pro-Ala-Ser(P)-Val-Pro-Pro-Ser(P)-Pro-Ser-Leu-Ser(P)-Arg-. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253006 |
Ser645 |
RPASVPPsPSLSRHS |
in vitro |
|
| pmid |
sentence |
| 6772446 |
Glycogen synthase kinase-3 phosphorylates three serine residues on glycogen synthase (sites 3a, 3b and 3c) which are all located in the same nine-amino-acid segment of the polypeptide chain. The sequence in this region is: Arg-Tyr-Pro-Arg-Pro-Ala-Ser(P)-Val-Pro-Pro-Ser(P)-Pro-Ser-Leu-Ser(P)-Arg-. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251238 |
Ser645 |
RPASVPPsPSLSRHS |
|
|
| pmid |
sentence |
| 11427888 |
Glycogen synthase has multiple serines (residues 640, 644, 648 and 652) separated by three residues, and those Ser residues are phosphorylated sequentially by GSK3 from the C-terminal end after Ser 656 has been phosphorylated by casein kinase II. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251240 |
Ser649 |
VPPSPSLsRHSSPHQ |
|
|
| pmid |
sentence |
| 11427888 |
Glycogen synthase has multiple serines (residues 640, 644, 648 and 652) separated by three residues, and those Ser residues are phosphorylated sequentially by GSK3 from the C-terminal end after Ser 656 has been phosphorylated by casein kinase II. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253007 |
Ser649 |
VPPSPSLsRHSSPHQ |
in vitro |
|
| pmid |
sentence |
| 6772446 |
Glycogen synthase kinase-3 phosphorylates three serine residues on glycogen synthase (sites 3a, 3b and 3c) which are all located in the same nine-amino-acid segment of the polypeptide chain. The sequence in this region is: Arg-Tyr-Pro-Arg-Pro-Ala-Ser(P)-Val-Pro-Pro-Ser(P)-Pro-Ser-Leu-Ser(P)-Arg-. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251241 |
Ser653 |
PSLSRHSsPHQSEDE |
|
|
| pmid |
sentence |
| 11427888 |
Glycogen synthase has multiple serines (residues 640, 644, 648 and 652) separated by three residues, and those Ser residues are phosphorylated sequentially by GSK3 from the C-terminal end after Ser 656 has been phosphorylated by casein kinase II. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens, , In Vitro |
| Tissue: |
Muscle, Skeletal Muscle |
| Pathways: | Insulin Signaling, PI3K/AKT Signaling |
| + |
DYRK1A | down-regulates activity
phosphorylation
|
GYS1 |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260632 |
Ser641 |
YRYPRPAsVPPSPSL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14593110 |
DYRK Family Protein Kinases Phosphorylate and Inactivate Glycogen Synthase. both protein kinases phosphorylate site 3a but no other sites that affect glycogen synthase activity. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
GSK3A | down-regulates
phosphorylation
|
GYS1 |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118927 |
Ser641 |
YRYPRPAsVPPSPSL |
Homo sapiens |
|
| pmid |
sentence |
| 14593110 |
Glycogen synthase kinase-3 (gsk-3) phosphorylates four serine residues in the cooh terminus of glycogen synthase. Phosphorylation of one of these residues, ser640 (site 3a), causes strong inactivation of glycogen synthase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
DYRK1B | down-regulates activity
phosphorylation
|
GYS1 |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260633 |
Ser641 |
YRYPRPAsVPPSPSL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14593110 |
DYRK Family Protein Kinases Phosphorylate and Inactivate Glycogen Synthase. both protein kinases phosphorylate site 3a but no other sites that affect glycogen synthase activity. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PRKACA | down-regulates activity
phosphorylation
|
GYS1 |
0.489 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253009 |
Ser698 |
PEWPRRAsCTSSTSG |
in vitro |
|
| pmid |
sentence |
| 196939 |
The results presented in this paper show that the phosphorylation of glycogen synthetase a by cyclic AMP-dependent protein kinase results in the phosphorylation of two distinct serines termed site-l and site-2, which account for 90% of the total phosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253008 |
Ser8 |
MPLNRTLsMSSLPGL |
in vitro |
|
| pmid |
sentence |
| 6263629 |
A reinvestigation of the phosphorylation of Rabbit Skeletal-muscle glycogen synthase by cyclic AMP dependent Protein Kinase: identification of the third site of phosphorylation at Serine-7 |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKACA |
phosphorylation
|
GYS1 |
0.489 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249988 |
Ser8 |
MPLNRTLsMSSLPGL |
in vitro |
|
| pmid |
sentence |
| 2117608 |
Phosphorylation of rabbit muscle glycogen synthase by cyclic AMP-dependent protein kinase has been shown to enhance subsequent phosphorylation by casein kinase I . phosphorylation at Ser7 is required for modification of Ser10 by casein kinase I. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AMPK | down-regulates activity
phosphorylation
|
GYS1 |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263102 |
Ser8 |
MPLNRTLsMSSLPGL |
in vitro |
|
| pmid |
sentence |
| 22233421 |
Recombinant muscle GYS1 (glycogen synthase 1) and recombinant liver GYS2 were phosphorylated by recombinant AMPK (AMP-activated protein kinase) in a time-dependent manner and to a similar stoichiometry. The phosphorylation site in GYS2 was identified as Ser7, which lies in a favourable consensus for phosphorylation by AMPK. Phosphorylation of GYS1 or GYS2 by AMPK led to enzyme inactivation by decreasing the affinity for both UDP-Glc (UDP-glucose) [assayed in the absence of Glc-6-P (glucose-6-phosphate)] and Glc-6-P (assayed at low UDP-Glc concentrations). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MYOD1/SWI/SNF complex | up-regulates quantity by expression 
transcriptional regulation
|
GYS1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-136553 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15870273 |
Swi/snf enzymes are necessary for myod to activate muscle gene transcription / myod increased the expression of 94 genes and decreased that of 70 genes /these 94 genes (represented by 96 array features) were analyzed for their dependence on a functional brg1-based swi/snf complex. In the presence of dominant-negative brg1, 29 genes did not achieve full activation by myod, as determined by statistical criteria (q 0.05) and a twofold or more decrease in expression level (table 1; see also table s1 in the supplemental material) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PPP1R3A | up-regulates 
dephosphorylation
|
GYS1 |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37301 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8250835 |
In skeletal muscle, the activation of glycogen synthase by insulin involves the dephosphorylation of serine residues that are phosphorylated by gsk3 and dephosphorylated by the glycogen-associated form of protein phosphatase-l (pp1g). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
GYS1 | up-regulates
|
Glycogen_synthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235751 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 14593110 |
Glycogen synthase, a key enzyme in the regulation of glycogen synthesis by insulin, is controlled by multisite phosphorylation. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Insulin Signaling, PI3K/AKT Signaling |
| + |
PPP1R3B | up-regulates
binding
|
GYS1 |
0.713 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271734 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36551183 |
In the liver, PTG and PPP1R3B(GL)are expressed at roughly equivalent levels [55], and they jointly promote hepatic glycogen mobilization and storage. PTG overexpression significantly increased glycogen content, mainly due to its ability to promote the redistribution of PP1 and glycogen synthase to glycogen granules, significantly increasing GS activity and glycogen synthesis (Figure 2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Liver |
| + |
GYS1 | down-regulates quantity
chemical modification
|
UDP-alpha-D-glucose(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267938 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26882899 |
Glycogenin initiates the first step of glycogen synthesis by self glycosylation of a short 8–12 glucose oligosaccharide primer. Glycogen synthase (GYS) elongates the glucose oligossacharide primer, which utilises UDP-glucose as the glucosyl donor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycogenesis |
| + |
GYS1 | up-regulates quantity
chemical modification
|
α-D-glucosyl-glycogenin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267940 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26882899 |
Glycogenin initiates the first step of glycogen synthesis by self glycosylation of a short 8–12 glucose oligosaccharide primer. Glycogen synthase (GYS) elongates the glucose oligossacharide primer, which utilises UDP-glucose as the glucosyl donor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycogenesis |
| + |
INSR | up-regulates activity
|
GYS1 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236803 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10909964 |
In skeletal muscle, insulin activates glycogen synthase by reducing phosphorylation at both NH2- and COOH-terminal sites of the enzyme and by elevating the levels of glucose-6-phosphate, an allosteric activator of glycogen synthase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| Pathways: | Insulin Signaling |
| + |
PASK | down-regulates activity
phosphorylation
|
GYS1 |
0.523 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245866 |
|
|
in vitro |
|
| pmid |
sentence |
| 16275910 |
Recombinant human PASK (hPASK) phosphorylates purified muscle glycogen synthase, causing robust inactivation. Furthermore, hPASK interacts directly with glycogen synthase when expressed in cultured cells and this interaction and the phosphorylation of glycogen synthase by human PASK (hPASK) are inhibited by glycogen. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPP1R3C | up-regulates
binding
|
GYS1 |
0.845 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271733 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36551183 |
In the liver, PTG and PPP1R3B(GL)are expressed at roughly equivalent levels [55], and they jointly promote hepatic glycogen mobilization and storage. PTG overexpression significantly increased glycogen content, mainly due to its ability to promote the redistribution of PP1 and glycogen synthase to glycogen granules, significantly increasing GS activity and glycogen synthesis (Figure 2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Liver |
3.0
GYS1
- 
- 