| + |
SH3GL1 | up-regulates 
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263885 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25517094 |
Endocytosis is required for internalization of micronutrients and turnover of membrane components. Endophilin has been assigned as a component of clathrin-mediated endocytosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP-2 complex | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260416 |
|
|
Rattus norvegicus |
Brain |
| pmid |
sentence |
| 15496985 |
Intersectins 1 and 2, epsin2, NECAP and sorting nexin9 were identified as α‐appendage ligands in mass spectrometry of these samples |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
MYO1E | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265426 |
|
|
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 |
| + |
SH3GL2 | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263883 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25517094 |
Endocytosis is required for internalization of micronutrients and turnover of membrane components. Endophilin has been assigned as a component of clathrin-mediated endocytosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SH3GLB2 | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263887 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25517094 |
Endocytosis is required for internalization of micronutrients and turnover of membrane components. Endophilin has been assigned as a component of clathrin-mediated endocytosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SH3GL3 | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263884 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25517094 |
Endocytosis is required for internalization of micronutrients and turnover of membrane components. Endophilin has been assigned as a component of clathrin-mediated endocytosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP-2/clathrin vescicle | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260705 |
|
|
|
|
| pmid |
sentence |
| 24130457 |
AP-2 is the core-organizing element in clathrin-mediated endocytosis. During the formation of clathrin-coated vesicles, clathrin and endocytic accessory proteins interact with AP-2 in a temporally and spatially controlled manner |
|
| Publications: |
1 |
| + |
ACTB | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260608 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19121306 |
However, we did detect WAFL binding to bothWIP and actin by immunoprecipitation (Fig. 4). In conclusion, we propose a model whereby WAFL associates toendocytic vesicles by its coiled-coil domain and is involved in actin-based movement of early endosomes via WIP and binding to actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WIPF1 | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260609 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19121306 |
However, we did detect WAFL binding to bothWIP and actin by immunoprecipitation (Fig. 4). In conclusion, we propose a model whereby WAFL associates toendocytic vesicles by its coiled-coil domain and is involved in actin-based movement of early endosomes via WIP and binding to actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SH3GLB1 | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263886 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25517094 |
Endocytosis is required for internalization of micronutrients and turnover of membrane components. Endophilin has been assigned as a component of clathrin-mediated endocytosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARF6 | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272154 |
|
|
|
|
| pmid |
sentence |
| 14973189 |
ADP-ribosylation factors (ARF) are 20-kDa GTPases of the ras superfamily that regulate vesicular transport in eukaryotic cells. There are three classes of ARFs: class I (ARF1–3), which function in endoplasmic reticulum-Golgi trafficking; the much less studied class II (ARF4–5); and class III (ARF6), with significant roles in endocytotic pathways and cytoskeletal dynamics near the cell surface |
|
| Publications: |
1 |
3.0
Endocytosis