| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Epsin-1,
Epsin-1
|
| http://www.biopax.org/relea... |
EPN1_RAT,
EPN1_RAT
|
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
EPS-15-interacting protein 1,
EPS-15-interacting protein 1
|
| http://www.biopax.org/relea... |
FUNCTION: Binds to membranes enriched in phosphatidylinositol-4,5- biphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis. SUBUNIT: Monomer. Binds REPS2 and ITSN1 (By similarity). Binds EPS15, clathrin, ZBTB16/ZNF145, AP2A1 and AP2A2. Binds ubiquitinated proteins. Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis. Interacts with AP2B1. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Membrane, clathrin-coated pit. Note=Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Colocalizes with clathrin at the Golgi complex. Detected in presynaptic nerve terminals and in synaptosomes. May shuttle to the nucleus when associated with ZBTB16/ZNF145. TISSUE SPECIFICITY: Ubiquitous. DOMAIN: The NPF repeat domain is involved in EPS15 binding. DOMAIN: The DPW repeat domain is involved in AP2A2 and clathrin binding. DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1 (By similarity). PTM: Ubiquitinated. PTM: Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation. SIMILARITY: Belongs to the epsin family. SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain. SIMILARITY: Contains 3 UIM (ubiquitin-interacting motif) repeats. WEB RESOURCE: Name=Protein Spotlight; Note=The bubble's bend - Issue 42 of January 2004; URL="http://web.expasy.org/spotlight/back_issues/sptlt042.shtml"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Binds to membranes enriched in phosphatidylinositol-4,5- biphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis. SUBUNIT: Monomer. Binds REPS2 and ITSN1 (By similarity). Binds EPS15, clathrin, ZBTB16/ZNF145, AP2A1 and AP2A2. Binds ubiquitinated proteins. Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis. Interacts with AP2B1. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Membrane, clathrin-coated pit. Note=Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Colocalizes with clathrin at the Golgi complex. Detected in presynaptic nerve terminals and in synaptosomes. May shuttle to the nucleus when associated with ZBTB16/ZNF145. TISSUE SPECIFICITY: Ubiquitous. DOMAIN: The NPF repeat domain is involved in EPS15 binding. DOMAIN: The DPW repeat domain is involved in AP2A2 and clathrin binding. DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1 (By similarity). PTM: Ubiquitinated. PTM: Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation. SIMILARITY: Belongs to the epsin family. SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain. SIMILARITY: Contains 3 UIM (ubiquitin-interacting motif) repeats. WEB RESOURCE: Name=Protein Spotlight; Note=The bubble's bend - Issue 42 of January 2004; URL="http://web.expasy.org/spotlight/back_issues/sptlt042.shtml"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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