| + |
AURKB | down-regulates activity 
phosphorylation
|
GFAP |
0.449 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100165 |
Ser13 |
ITSAARRsYVSSGEM |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100169 |
Ser38 |
LGPGTRLsLARMPPP |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100173 |
Thr7 |
tSAARRSY |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PRKACA | down-regulates activity
phosphorylation
|
GFAP |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249711 |
Ser13 |
ITSAARRsYVSSGEM |
in vitro |
|
| pmid |
sentence |
| 2155236 |
GFAP can serve as a substrate for phosphorylation by CAMP-dependent protein kinase. CAMP-dependent protein kinase or protein kinase C phosphorylated Ser-8, Ser-13, and Ser-34.each phosphorylation was shown to induce disassembly of the glial filaments. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249713 |
Ser38 |
LGPGTRLsLARMPPP |
in vitro |
|
| pmid |
sentence |
| 2155236 |
GFAP can serve as a substrate for phosphorylation by CAMP-dependent protein kinase. CAMP-dependent protein kinase or protein kinase C phosphorylated Ser-8, Ser-13, and Ser-34.each phosphorylation was shown to induce disassembly of the glial filaments. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249712 |
Thr7 |
tSAARRSY |
in vitro |
|
| pmid |
sentence |
| 2155236 |
GFAP can serve as a substrate for phosphorylation by CAMP-dependent protein kinase. CAMP-dependent protein kinase or protein kinase C phosphorylated Ser-8, Ser-13, and Ser-34.each phosphorylation was shown to induce disassembly of the glial filaments. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PRKCA | down-regulates activity
phosphorylation
|
GFAP |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248860 |
Ser13 |
ITSAARRsYVSSGEM |
in vitro |
|
| pmid |
sentence |
| 2155236 |
Glial fibrillary acidic protein (GFAP), the intermediate filament component of astroglial cells, can serve as an excellent substrate for both cAMP-dependent protein kinase and protein kinase C, in vitro. GFAP phosphorylated by each protein kinase does not polymerize, and the filaments that do polymerize tend to depolymerize after phosphorylation. Dephosphorylation of phospho-GFAP by phosphatase led to a recovery of the polymerization competence of GFAP. Most of the phosphorylation sites for cAMP-dependent protein kinase and protein kinase C on GFAP are the same, Ser-8, Ser-13, and Ser-34. cAMP-dependent protein kinase has one additional phosphorylation site, Thr-7. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248862 |
Ser38 |
LGPGTRLsLARMPPP |
in vitro |
|
| pmid |
sentence |
| 2155236 |
Glial fibrillary acidic protein (GFAP), the intermediate filament component of astroglial cells, can serve as an excellent substrate for both cAMP-dependent protein kinase and protein kinase C, in vitro. GFAP phosphorylated by each protein kinase does not polymerize, and the filaments that do polymerize tend to depolymerize after phosphorylation. Dephosphorylation of phospho-GFAP by phosphatase led to a recovery of the polymerization competence of GFAP. Most of the phosphorylation sites for cAMP-dependent protein kinase and protein kinase C on GFAP are the same, Ser-8, Ser-13, and Ser-34. cAMP-dependent protein kinase has one additional phosphorylation site, Thr-7. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CAMK2A | down-regulates activity
phosphorylation
|
GFAP |
0.438 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250626 |
Ser13 |
ITSAARRsYVSSGEM |
in vitro |
|
| pmid |
sentence |
| 7822264 |
On the other hand, GFAP was phosphorylated to approximately 1.9 mol of phosphate/mol of GFAP by Ca(2+)-CaM-dependent protein kinase II, and this phosphorylation did induce disassembly of the filament. Sequential analysis of the purified phosphopeptides revealed that only Ser8 on GFAP was phosphorylated by cdc2 kinase, whereas Ser13, Ser17, Ser34, and Ser389 on GFAP were phosphorylated by Ca(2+)-CaM-dependent protein kinase II. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250627 |
Ser17 |
ARRSYVSsGEMMVGG |
in vitro |
|
| pmid |
sentence |
| 7822264 |
On the other hand, GFAP was phosphorylated to approximately 1.9 mol of phosphate/mol of GFAP by Ca(2+)-CaM-dependent protein kinase II, and this phosphorylation did induce disassembly of the filament. Sequential analysis of the purified phosphopeptides revealed that only Ser8 on GFAP was phosphorylated by cdc2 kinase, whereas Ser13, Ser17, Ser34, and Ser389 on GFAP were phosphorylated by Ca(2+)-CaM-dependent protein kinase II. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250628 |
Ser38 |
LGPGTRLsLARMPPP |
in vitro |
|
| pmid |
sentence |
| 7822264 |
On the other hand, GFAP was phosphorylated to approximately 1.9 mol of phosphate/mol of GFAP by Ca(2+)-CaM-dependent protein kinase II, and this phosphorylation did induce disassembly of the filament. Sequential analysis of the purified phosphopeptides revealed that only Ser8 on GFAP was phosphorylated by cdc2 kinase, whereas Ser13, Ser17, Ser34, and Ser389 on GFAP were phosphorylated by Ca(2+)-CaM-dependent protein kinase II. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250629 |
Ser393 |
NLQIRETsLDTKSVS |
in vitro |
|
| pmid |
sentence |
| 7822264 |
On the other hand, GFAP was phosphorylated to approximately 1.9 mol of phosphate/mol of GFAP by Ca(2+)-CaM-dependent protein kinase II, and this phosphorylation did induce disassembly of the filament. Sequential analysis of the purified phosphopeptides revealed that only Ser8 on GFAP was phosphorylated by cdc2 kinase, whereas Ser13, Ser17, Ser34, and Ser389 on GFAP were phosphorylated by Ca(2+)-CaM-dependent protein kinase II. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
ROCK1 | down-regulates activity
phosphorylation
|
GFAP |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100181 |
Ser13 |
ITSAARRsYVSSGEM |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100188 |
Ser38 |
LGPGTRLsLARMPPP |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100192 |
Thr7 |
tSAARRSY |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
GFAP | up-regulates quantity 
binding
|
ACTB |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269271 |
|
|
Homo sapiens |
Astrocyte |
| pmid |
sentence |
| 31626364 |
GFAP is the major cytoskeletal element and scaffold of astrocytes In astrocytes, GFAP has close interaction with F-actin molecularly and functionally. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
GFAP
- 
- 