+ |
LYPLA2 | down-regulates quantity by destabilization
deacetylation
|
GAP43 |
0.455 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266767 |
Cys3 |
cCMRRTKQ |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
21152083 |
Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral membrane-associated GAP-43. In this work, we investigated the deacylation of growth-associated protein-43 (GAP-43), a dually acylated protein at cysteine residues 3 and 4. Thus, the results demonstrate that APT-2 is the protein thioesterase involved in the acylation/deacylation cycle operating in GAP-43 subcellular distribution.we demonstrated that the reduction in the protein level was abrogated when cells were also treated with proteasome inhibitors (chloroquine, MG132 and lactacystin) which strongly suggest that GAP-43 deacylation is an early and necessary step for its later ubiquitination and degradation by the proteasome. In addition, it also suggests that acyl-protein thioesterase levels not only regulate palmitate turnover but also global protein turnover of GAP-43. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266768 |
Cys4 |
cMRRTKQV |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
21152083 |
Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral membrane-associated GAP-43. In this work, we investigated the deacylation of growth-associated protein-43 (GAP-43), a dually acylated protein at cysteine residues 3 and 4. Thus, the results demonstrate that APT-2 is the protein thioesterase involved in the acylation/deacylation cycle operating in GAP-43 subcellular distribution.we demonstrated that the reduction in the protein level was abrogated when cells were also treated with proteasome inhibitors (chloroquine, MG132 and lactacystin) which strongly suggest that GAP-43 deacylation is an early and necessary step for its later ubiquitination and degradation by the proteasome. In addition, it also suggests that acyl-protein thioesterase levels not only regulate palmitate turnover but also global protein turnover of GAP-43. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK2A1 |
phosphorylation
|
GAP43 |
0.311 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250866 |
Ser202 |
PPTETGEsSQAEENI |
in vitro |
|
pmid |
sentence |
1828073 |
Two serines located in the C-terminal end of neuromodulin, Ser-192 and Ser-193, were identified as the major casein kinase II phosphorylation sites. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250867 |
Ser203 |
PTETGESsQAEENIE |
in vitro |
|
pmid |
sentence |
1828073 |
Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin.| |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
PRKCB |
phosphorylation
|
GAP43 |
0.353 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248859 |
Ser41 |
AATKIQAsFRGHITR |
in vitro |
|
pmid |
sentence |
2140056 |
We conclude that serine-41 is the protein kinase C phosphorylation site of neuromodulin and that phosphorylation of this amino acid residue blocks binding of calmodulin to neuromodulin. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
ANKRD11 | up-regulates quantity by expression
transcriptional regulation
|
GAP43 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266736 |
|
|
Mus musculus |
|
pmid |
sentence |
29274743 |
Neurite growth-related genes such as Trkb, Bdnf, Gap43, Coronin 1B, and Rab13 are downregulated in ANKRD11-deficient neurons. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Brain |
+ |
GAP43 | up-regulates
|
Neurogenesis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266771 |
|
|
Rattus norvegicus |
|
pmid |
sentence |
26865625 |
Growth-associated protein 43 (GAP43), a protein kinase C (PKC)-activated phosphoprotein, is often implicated in axonal plasticity and regeneration. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
STAT3 | up-regulates quantity by expression
transcriptional regulation
|
GAP43 |
0.306 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266772 |
|
|
Rattus norvegicus |
Astrocyte |
pmid |
sentence |
26865625 |
In this study, we demonstrated for the first time that growth-associated protein 43 (GAP43), a well known growth cone protein that promotes axonal regeneration, can be induced in rat brain astrocytes by the proinflammatory endotoxin lipopolysaccharide via both nuclear factor-κB and signal transducer and activator of transcription 3-mediated transcriptional activation. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
NfKb-p65/p50 | up-regulates quantity by expression
transcriptional regulation
|
GAP43 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266770 |
|
|
Rattus norvegicus |
|
pmid |
sentence |
26865625 |
In this study, we demonstrated for the first time that growth-associated protein 43 (GAP43), a well known growth cone protein that promotes axonal regeneration, can be induced in rat brain astrocytes by the proinflammatory endotoxin lipopolysaccharide via both nuclear factor-κB and signal transducer and activator of transcription 3-mediated transcriptional activation. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
GAP43 | up-regulates
|
Neurite_outgrowth |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266769 |
|
|
Mus musculus |
|
pmid |
sentence |
21938722 |
Growth associated protein 43 (Gap43) is a neuron-specific phosphoprotein, which plays critical role in axon growth and synapses functions during neurogenesis. |
|
Publications: |
1 |
Organism: |
Mus Musculus |