| + |
CDK5 | up-regulates activity 
phosphorylation
|
DNM1 |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250661 |
Ser774 |
SVPAGRRsPTSSPTP |
in vitro |
|
| pmid |
sentence |
| 12855954 |
Here, we show that cyclin-dependent kinase 5 (Cdk5) phosphorylates dynamin I on Ser 774 and Ser 778 in vitro, which are identical to its endogenous phosphorylation sites in vivo. Cdk5 antagonists and expression of dominant-negative Cdk5 block phosphorylation of dynamin I, but not of amphiphysin or AP180, in nerve terminals and inhibit SVE. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250662 |
Ser778 |
GRRSPTSsPTPQRRA |
in vitro |
|
| pmid |
sentence |
| 12855954 |
Here, we show that cyclin-dependent kinase 5 (Cdk5) phosphorylates dynamin I on Ser 774 and Ser 778 in vitro, which are identical to its endogenous phosphorylation sites in vivo. Cdk5 antagonists and expression of dominant-negative Cdk5 block phosphorylation of dynamin I, but not of amphiphysin or AP180, in nerve terminals and inhibit SVE. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCA |
phosphorylation
|
DNM1 |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249039 |
Ser795 |
VPPARPGsRGPAPGP |
in vitro |
|
| pmid |
sentence |
| 10766777 |
Phosphorylation of dynamin I on Ser-795 by protein kinase C blocks its association with phospholipids. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
DYRK1A | down-regulates 
phosphorylation
|
DNM1 |
0.426 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127440 |
Ser795 |
VPPARPGsRGPAPGP |
Homo sapiens |
|
| pmid |
sentence |
| 15287745 |
Mnb/dyrk1a was shown to phosphorylate dynamin 1 and alter its interactions with several sh3 domain-containing endocytic accessory proteins.Phosphorylation At s795 and s857 was confirmed in full-length dynamin 1, and s857 was subsequently determined to be the major mnb/dyrk1a phosphorylation site in vitro. Phosphorylation at s857 was demonstrated to be the basis for altering the binding of dynamin 1 to amphiphysin 1 and grb 2 by site-directed mutants mimicking phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127444 |
Ser857 |
ASPSRPEsPRPPFDL |
Homo sapiens |
|
| pmid |
sentence |
| 15287745 |
Mnb/dyrk1a was shown to phosphorylate dynamin 1 and alter its interactions with several sh3 domain-containing endocytic accessory proteins.Phosphorylation At s795 and s857 was confirmed in full-length dynamin 1, and s857 was subsequently determined to be the major mnb/dyrk1a phosphorylation site in vitro. Phosphorylation at s857 was demonstrated to be the basis for altering the binding of dynamin 1 to amphiphysin 1 and grb 2 by site-directed mutants mimicking phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
SRC | up-regulates activity
phosphorylation
|
DNM1 |
0.621 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247124 |
Tyr231 |
LLPLRRGyIGVVNRS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 9880482 |
Src-mediated tyrosine phosphorylation of dynamin is required for beta2-adrenergic receptor internalization and mitogen-activated protein kinase signalingHere we demonstrate that activation of beta2-adrenergic receptors (beta2-ARs) leads to c-Src-mediated tyrosine phosphorylation of dynamin, which is required for receptor internalization. Two tyrosine residues, Tyr231 and Tyr597, are identified as the major phosphorylation sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247129 |
Tyr597 |
NTEQRNVyKDYRQLE |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12011079 |
Endocytosis of ligand-activated receptors requires dynamin-mediated GTP hydrolysis, which is regulated by dynamin self-assembly. Here, we demonstrate that phosphorylation of dynamin I by c-Src induces its self-assembly and increases its GTPase activity. Electron microscopic analyses reveal that tyrosine-phosphorylated dynamin I spontaneously self-assembles into large stacks of rings. Tyrosine 597 was identified as being phosphorylated both in vitro and in cultured cells following epidermal growth factor receptor stimulation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Chlorocebus Aethiops |
| + |
DNM1 | up-regulates 
|
Synaptic_vesicle_recycling |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264118 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10823955 |
The GTPase dynamin I is required for synaptic vesicle (SV) endocytosis. Our observation that dynamin binds to the SV protein synaptophysin in a Ca2+-dependent fashion suggested the possibility that a dynamin/synaptophysin complex functions in SV recycling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
DNM1 | up-regulates activity
binding
|
MYO1E |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265424 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 17257598 |
We describe binding of two PRD-containing endocytic proteins, dynamin and synaptojanin-1, to the SH3 domain of Myo1E. This interaction was detected both in vitro, using pull-downs of purified proteins, and in vivo, using immunoprecipitation of protein complexes from synapse-enriched brain extract and immunolocalization of Myo1E and dynamin. Our observation of the interaction between human Myo1E and endocytic proteins suggests that this longtailed myosin may play a role in clathrin-dependent endocytosis.Interaction between Myo1E SH3 domain and PRD-containing endocytic proteins may promote recruitment of Myo1E to clathrin-coated structures since an inactivating mutation in the SH3 domain reduced Myo1E localization to clathrin-containing puncta. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Tissue: |
Brain |
| + |
DNM1 | up-regulates activity
binding
|
SYP |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264119 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10823955 |
The GTPase dynamin I is required for synaptic vesicle (SV) endocytosis. Our observation that dynamin binds to the SV protein synaptophysin in a Ca2+-dependent fashion suggested the possibility that a dynamin/synaptophysin complex functions in SV recycling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
SNX9 | up-regulates
binding
|
DNM1 |
0.781 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133892 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15703209 |
Snx9 binds directly to bothdynamin-1 anddynamin-2. Moreover by stimulatingdynaminassembly, snx9 stimulatesdynamin's basal gtpase activity and potentiates assembly-stimulated gtpase activity on liposomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
3.0
DNM1
- 
- 