| + |
DYRK1A | down-regulates 
phosphorylation
|
AMPH |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126839 |
Ser262 |
LRIAKTPsPPEEPSP |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Recent studies show that phosphorylation of amphiphysin1 prd by cdk5 inhibited the association of amphiphysin1 with ap-2 in synaptic vesicle endocytosis (7, 8) similar to that by mapk (present report). Cdk5 appears to phosphorylate amphiphysin1 at serines 261, 272, 276, and 285 and threonine 310, located in the prd |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126843 |
Ser272 |
EEPSPLPsPTASPNH |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Recent studies show that phosphorylation of amphiphysin1 prd by cdk5 inhibited the association of amphiphysin1 with ap-2 in synaptic vesicle endocytosis (7, 8) similar to that by mapk (present report). Cdk5 appears to phosphorylate amphiphysin1 at serines 261, 272, 276, and 285 and threonine 310, located in the prd |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126847 |
Ser276 |
PLPSPTAsPNHTLAP |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Recent studies show that phosphorylation of amphiphysin1 prd by cdk5 inhibited the association of amphiphysin1 with ap-2 in synaptic vesicle endocytosis (7, 8) similar to that by mapk (present report). Cdk5 appears to phosphorylate amphiphysin1 at serines 261, 272, 276, and 285 and threonine 310, located in the prd |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126851 |
Ser285 |
NHTLAPAsPAPARPR |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Recent studies show that phosphorylation of amphiphysin1 prd by cdk5 inhibited the association of amphiphysin1 with ap-2 in synaptic vesicle endocytosis (7, 8) similar to that by mapk (present report). Cdk5 appears to phosphorylate amphiphysin1 at serines 261, 272, 276, and 285 and threonine 310, located in the prd |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146906 |
Ser295 |
PARPRSPsQTRKGPP |
Homo sapiens |
|
| pmid |
sentence |
| 16733250 |
Here we report that amphiphysin i (amph i) is also a mnb/dyrk1a substrate. This kinase phosphorylated native amph i in rodent brains and recombinant human amph i expressed in escherichia coli. Serine 293 (ser-293) was identified as the major site, whereas serine 295 and threonine 310 were found as minor kinase sitesamph i phosphorylated by mnb/dyrk1a decreased endophilin binding in vitro. From these results we conclude that amph i at ser-293 is phosphorylated by mnb/dyrk1a and that the phosphorylation has physiological significance in controlling the interaction of amphiphysin with endocytic accessory proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126855 |
Thr310 |
VPPLPKVtPTKELQQ |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Recent studies show that phosphorylation of amphiphysin1 prd by cdk5 inhibited the association of amphiphysin1 with ap-2 in synaptic vesicle endocytosis (7, 8) similar to that by mapk (present report). Cdk5 appears to phosphorylate amphiphysin1 at serines 261, 272, 276, and 285 and threonine 310, located in the prd |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146910 |
Thr310 |
VPPLPKVtPTKELQQ |
Homo sapiens |
|
| pmid |
sentence |
| 16733250 |
Here we report that amphiphysin i (amph i) is also a mnb/dyrk1a substrate. This kinase phosphorylated native amph i in rodent brains and recombinant human amph i expressed in escherichia coli. Serine 293 (ser-293) was identified as the major site, whereas serine 295 and threonine 310 were found as minor kinase sitesamph i phosphorylated by mnb/dyrk1a decreased endophilin binding in vitro. From these results we conclude that amph i at ser-293 is phosphorylated by mnb/dyrk1a and that the phosphorylation has physiological significance in controlling the interaction of amphiphysin with endocytic accessory proteins. |
|
| Publications: |
7 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
CDK5 |
phosphorylation
|
AMPH |
0.537 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250648 |
Ser272 |
EEPSPLPsPTASPNH |
in vitro |
|
| pmid |
sentence |
| 11113134 |
Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250649 |
Ser276 |
PLPSPTAsPNHTLAP |
in vitro |
|
| pmid |
sentence |
| 11113134 |
Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250650 |
Ser285 |
NHTLAPAsPAPARPR |
in vitro |
|
| pmid |
sentence |
| 11113134 |
Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CyclinB/CDK1 |
phosphorylation
|
AMPH |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250644 |
Ser272 |
EEPSPLPsPTASPNH |
in vitro |
|
| pmid |
sentence |
| 11113134 |
Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250645 |
Ser276 |
PLPSPTAsPNHTLAP |
in vitro |
|
| pmid |
sentence |
| 11113134 |
Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250646 |
Ser285 |
NHTLAPAsPAPARPR |
in vitro |
|
| pmid |
sentence |
| 11113134 |
Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CDKL5 | down-regulates activity
phosphorylation
|
AMPH |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245881 |
Ser293 |
PAPARPRsPSQTRKG |
Mus musculus |
|
| pmid |
sentence |
| 23651931 |
This 120-kDa protein was identified as amphiphysin 1 (Amph1) by LC-MS/MS analysis, and the site of phosphorylation by CDKL5 was determined to be Ser-293.| The phosphorylation mimic mutants, Amph1(S293E) and Amph1(S293D), showed significantly reduced affinity for endophilin, a protein involved in synaptic vesicle endocytosis |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MAPK1 | down-regulates activity
phosphorylation
|
AMPH |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126859 |
Ser293 |
PAPARPRsPSQTRKG |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Thus, we propose that mapk phosphorylation of amphiphysin1 controls ngf receptor/trka-mediated endocytosis by terminating the amphiphysin1-ap-2 interaction.Our results indicate that phosphorylation of amphiphysin 1 at ser-285 and/or ser-293 affects the function of amphiphysin1.Mapk phosphorylation of ser-285 and ser-293 could modulate the interaction between prd and ap-2, resulting in the dissociation of amphiphysin1 from ap-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
AMPH |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126867 |
Ser293 |
PAPARPRsPSQTRKG |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Thus, we propose that mapk phosphorylation of amphiphysin1 controls ngf receptor/trka-mediated endocytosis by terminating the amphiphysin1-ap-2 interaction.Our results indicate that phosphorylation of amphiphysin 1 at ser-285 and/or ser-293 affects the function of amphiphysin1.Mapk phosphorylation of ser-285 and ser-293 could modulate the interaction between prd and ap-2, resulting in the dissociation of amphiphysin1 from ap-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates activity
phosphorylation
|
AMPH |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146902 |
Ser293 |
PAPARPRsPSQTRKG |
Homo sapiens |
|
| pmid |
sentence |
| 16733250 |
Here we report that amphiphysin i (amph i) is also a mnb/dyrk1a substrate. This kinase phosphorylated native amph i in rodent brains and recombinant human amph i expressed in escherichia coli. Serine 293 (ser-293) was identified as the major site, whereas serine 295 and threonine 310 were found as minor kinase sitesamph i phosphorylated by mnb/dyrk1a decreased endophilin binding in vitro. From these results we conclude that amph i at ser-293 is phosphorylated by mnb/dyrk1a and that the phosphorylation has physiological significance in controlling the interaction of amphiphysin with endocytic accessory proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates
phosphorylation
|
AMPH |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126863 |
Ser295 |
PARPRSPsQTRKGPP |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Thus, we propose that mapk phosphorylation of amphiphysin1 controls ngf receptor/trka-mediated endocytosis by terminating the amphiphysin1-ap-2 interaction.Our results indicate that phosphorylation of amphiphysin 1 at ser-285 and/or ser-293 affects the function of amphiphysin1.Mapk phosphorylation of ser-285 and ser-293 could modulate the interaction between prd and ap-2, resulting in the dissociation of amphiphysin1 from ap-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
MAPK3 | down-regulates
phosphorylation
|
AMPH |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126871 |
Ser295 |
PARPRSPsQTRKGPP |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Thus, we propose that mapk phosphorylation of amphiphysin1 controls ngf receptor/trka-mediated endocytosis by terminating the amphiphysin1-ap-2 interaction.Our results indicate that phosphorylation of amphiphysin 1 at ser-285 and/or ser-293 affects the function of amphiphysin1.Mapk phosphorylation of ser-285 and ser-293 could modulate the interaction between prd and ap-2, resulting in the dissociation of amphiphysin1 from ap-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
CSNK2A1 | down-regulates
phosphorylation
|
AMPH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149314 |
Thr350 |
PEVKKEEtLLDLDFD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16945112 |
Amphiphysins interact directly with clathrin and have a function in clathrin-mediated synaptic vesicle recycling and clathrin-mediated endocytosis. The n-terminal domain of clathrin bound to unphosphorylated amphiphysin-1, but not to the phosphorylated protein. The assumption that casein kinase 2 phosphorylates amphiphysin-1 at t350 and t387 was corroborated by experiments showing that: casein kinase 2 phosphorylated these residues directly in vitro,. upon activation by nerve growth factor, casein kinase 2 phosphorylates amphiphysin-1 and thereby regulates the endocytosis of clathrin-coated vesicles via the interaction between clathrin and amphiphysin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149318 |
Thr387 |
LPWDLWTtSTDLVQP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16945112 |
Amphiphysins interact directly with clathrin and have a function in clathrin-mediated synaptic vesicle recycling and clathrin-mediated endocytosis. The n-terminal domain of clathrin bound to unphosphorylated amphiphysin-1, but not to the phosphorylated protein. The assumption that casein kinase 2 phosphorylates amphiphysin-1 at t350 and t387 was corroborated by experiments showing that: casein kinase 2 phosphorylated these residues directly in vitro,. upon activation by nerve growth factor, casein kinase 2 phosphorylates amphiphysin-1 and thereby regulates the endocytosis of clathrin-coated vesicles via the interaction between clathrin and amphiphysin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | down-regulates
phosphorylation
|
AMPH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270197 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Thus, we propose that mapk phosphorylation of amphiphysin1 controls ngf receptor/trka-mediated endocytosis by terminating the amphiphysin1-ap-2 interaction.Our results indicate that phosphorylation of amphiphysin 1 at ser-285 and/or ser-293 affects the function of amphiphysin1.Mapk phosphorylation of ser-285 and ser-293 could modulate the interaction between prd and ap-2, resulting in the dissociation of amphiphysin1 from ap-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
Gbeta | down-regulates
phosphorylation
|
AMPH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270102 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Thus, we propose that mapk phosphorylation of amphiphysin1 controls ngf receptor/trka-mediated endocytosis by terminating the amphiphysin1-ap-2 interaction.Our results indicate that phosphorylation of amphiphysin 1 at ser-285 and/or ser-293 affects the function of amphiphysin1.Mapk phosphorylation of ser-285 and ser-293 could modulate the interaction between prd and ap-2, resulting in the dissociation of amphiphysin1 from ap-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
3.0
AMPH
- 
- 