Epsin-2 is a protein that in humans is encoded by the EPN2gene.[1][2]
This gene encodes a protein which interacts with clathrin and adaptor-related protein complex 2, alpha 1 subunit. The protein is found in a brain-derived clathrin-coated vesicle fraction and localizes to the peri-Golgi region and the cell periphery. The protein is thought to be involved in clathrin-mediated endocytosis. Alternate splicing of this gene results in two transcript variants encoding different isoforms.[2]
References
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Yamabhai M, Hoffman NG, Hardison NL, et al. (1998). "Intersectin, a novel adaptor protein with two Eps15 homology and five Src homology 3 domains". J. Biol. Chem. 273 (47): 31401–7. doi:10.1074/jbc.273.47.31401. PMID9813051.
Kikuno R, Nagase T, Ishikawa K, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (3): 197–205. doi:10.1093/dnares/6.3.197. PMID10470851.
Ford MG, Mills IG, Peter BJ, et al. (2002). "Curvature of clathrin-coated pits driven by epsin". Nature. 419 (6905): 361–6. doi:10.1038/nature01020. PMID12353027.
Hussain NK, Yamabhai M, Bhakar AL, et al. (2003). "A role for epsin N-terminal homology/AP180 N-terminal homology (ENTH/ANTH) domains in tubulin binding". J. Biol. Chem. 278 (31): 28823–30. doi:10.1074/jbc.M300995200. PMID12750376.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID15324660.
Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID15345747.