| + |
CASP3 | down-regulates quantity by destabilization 
cleavage
|
GORASP1 |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260602 |
Asp317 |
VSGISLLdNSNASVW |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11815631 |
Together, our results strongly suggest GRASP65 is a specific substrate for caspase-3.|This suggests that GRASP65 cleavage is required for fragmentation of the Golgi ribbon during apoptosis.| we analyzed the sequence in this region and identified three potential cleavage sites as SLLD320S, SFPD375S, and TLPD393G|mutation of all three aspartic acid residues completely blocked cleavage |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260603 |
Asp372 |
EFEVSFLdSPGAQAQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11815631 |
Together, our results strongly suggest GRASP65 is a specific substrate for caspase-3.|This suggests that GRASP65 cleavage is required for fragmentation of the Golgi ribbon during apoptosis.| we analyzed the sequence in this region and identified three potential cleavage sites as SLLD320S, SFPD375S, and TLPD393G|mutation of all three aspartic acid residues completely blocked cleavage |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260604 |
Asp390 |
LPQLTLPdSLTSAAS |
Homo sapiens |
|
| pmid |
sentence |
| 11815631 |
Together, our results strongly suggest GRASP65 is a specific substrate for caspase-3.|This suggests that GRASP65 cleavage is required for fragmentation of the Golgi ribbon during apoptosis.| we analyzed the sequence in this region and identified three potential cleavage sites as SLLD320S, SFPD375S, and TLPD393G|mutation of all three aspartic acid residues completely blocked cleavage |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates activity 
cleavage
|
GORASP1 |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260613 |
Asp390 |
LPQLTLPdSLTSAAS |
|
|
| pmid |
sentence |
| 17761173 |
In contrast, Caspase‐3 cleavage of GRASP‐1 releases the C‐terminal fragment, which in turn activates JNK signaling by serving as a scaffold protein |
|
| Publications: |
1 |
| + |
ERK1/2 | down-regulates activity
phosphorylation
|
GORASP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260605 |
Ser274 |
DPLPGPGsPSHSAPD |
Rattus norvegicus |
|
| pmid |
sentence |
| 18762583 |
Supporting the conclusion that phosphorylation of GRASP65 at Ser277 by ERK is critical for Golgi polarization. We have demonstrated a closely integrated mechanism in which Golgi remodeling by phosphorylation of GRASP65 acts as a negative regulator of Golgi and, surprisingly, centrosome orientation. Our data indicate that ERK phosphorylates GRASP65 in interphase cells, resulting in the loss of GRASP65 oligomerization and causing subsequent Golgi cisternal unstacking. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
MAPK1 | down-regulates activity
phosphorylation
|
GORASP1 |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262841 |
Ser274 |
DPLPGPGsPSHSAPD |
Rattus norvegicus |
NRK Cell |
| pmid |
sentence |
| 15834132 |
Here we show that GRASP65 is phosphorylated on serine 277 in interphase cells, and this is strongly enhanced in response to the addition of serum or epidermal growth factor. This is directly mediated by ERK suggesting that GRASP65 has some role in growth factor signal transduction. These results argue against Ser-277 phosphorylation alone causing the dissolution of GRASP65 oligomers and cisternal unstacking, although it may make a significant contribution to these events. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CDK1 | down-regulates activity
phosphorylation
|
GORASP1 |
0.705 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262840 |
Ser274 |
DPLPGPGsPSHSAPD |
Rattus norvegicus |
NRK Cell |
| pmid |
sentence |
| 15834132 |
Here we show that GRASP65 is phosphorylated on serine 277 in interphase cells, and this is strongly enhanced in response to the addition of serum or epidermal growth factor. This is directly mediated by ERK suggesting that GRASP65 has some role in growth factor signal transduction. Phosphorylation of Ser-277 is also dramatically increased during mitosis, however this is mediated by Cdk1 and not by ERK. These results argue against Ser-277 phosphorylation alone causing the dissolution of GRASP65 oligomers and cisternal unstacking, although it may make a significant contribution to these events. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CyclinB/CDK1 | down-regulates activity
phosphorylation
|
GORASP1 |
0.558 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260606 |
Ser373 |
FEVSFLDsPGAQAQA |
Rattus norvegicus |
|
| pmid |
sentence |
| 15678101 |
The pS376 antibody gave the strongest staining when Golgi apparatus fragmentation is initiated during prophase and in metaphase when it has become converted into a haze of small vesicles and some larger tubulovesicular remnants (Figure 4A). Therefore, GRASP65, like GM130, is phosphorylated in mitotic entry on Cdk1–cyclin B sites during the period when the Golgi apparatus is fragmented. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
GOLGA2 | up-regulates quantity by stabilization
binding
|
GORASP1 |
0.875 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260601 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16489344 |
Previous studies have implicated the GM130–GRASP65 complex in diverse Golgi functions. Therefore, GM130–GRASP65 interactions are required for Golgi ribbon formation.|A surprising clue came from the observation that GM130 was required for stability of GRASP65. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GOLGA2 | up-regulates activity
binding
|
GORASP1 |
0.875 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261239 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23555793 |
The “cis-golgin tether” is one of the most well-characterized golgin tether complexes. It is composed of the COPI vesicle-associated golgin giantin linked to Golgi membrane-associated GM130 via p115. GM130 is in turn linked to GRASP65 via a PDZ-like domain. GRASP65 is anchored to the Golgi membrane through N-terminal myristoylation as well as through binding to other Golgi proteins [10]. Together, these proteins appear to mediate vesicle tethering at the cis-Golgi membrane. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
GORASP1
- 
- 