ID:EPN1_HUMAN DESCRIPTION: RecName: Full=Epsin-1; AltName: Full=EH domain-binding mitotic phosphoprotein; AltName: Full=EPS-15-interacting protein 1; FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis. SUBUNIT: Monomer. Binds clathrin, ZBTB16/ZNF145 and ITSN1. Binds ubiquitinated proteins (By similarity). Binds REPS2, EPS15, AP2A1 and AP2A2. Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis. Interacts with AP2B1. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane; Peripheral membrane protein (By similarity). Nucleus (By similarity). Membrane, clathrin-coated pit (By similarity). 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. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 (By similarity). 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 with the AP-2 complex subunit AP2B1 (By similarity). 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. PTM: Ubiquitinated (By similarity). 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";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9Y6I3
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.