EPN1

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

Epsin-1 is a protein that in humans is encoded by the EPN1 gene.

EPN1 is an endocytic accessory protein that interacts with EPS15 (MIM 600051), the alpha subunit of the clathrin adaptor AP2 (AP2A1; MIM 601026), and clathrin (see MIM 118960), as well as with other accessory proteins for the endocytosis of clathrin-coated vesicles.[supplied by OMIM]

Interactions

EPN1 has been shown to interact with REPS2, AP2A2 and EPS15.

Further reading

• Drake MT, Downs MA, Traub LM (2000). "Epsin binds to clathrin by associating directly with the clathrin-terminal domain. Evidence for cooperative binding through two discrete sites". J. Biol. Chem. 275 (9): 6479–89. doi:10.1074/jbc.275.9.6479. PMID 10692452.
• Kariya K, Koyama S, Nakashima S, et al. (2000). "Regulation of complex formation of POB1/epsin/adaptor protein complex 2 by mitotic phosphorylation". J. Biol. Chem. 275 (24): 18399–406. doi:10.1074/jbc.M000521200. PMID 10764745.
• Hyman J, Chen H, Di Fiore PP, et al. (2000). "Epsin 1 Undergoes Nucleocytosolic Shuttling and Its Eps15 Interactor Nh2-Terminal Homology (Enth) Domain, Structurally Similar to Armadillo and Heat Repeats, Interacts with the Transcription Factor Promyelocytic Leukemia Zn2+ Finger Protein (Plzf)". J. Cell Biol. 149 (3): 537–46. doi:10.1083/jcb.149.3.537. PMC 2174850. PMID 10791968.
• Drake MT, Traub LM (2001). "Interaction of two structurally distinct sequence types with the clathrin terminal domain beta-propeller". J. Biol. Chem. 276 (31): 28700–9. doi:10.1074/jbc.M104226200. PMID 11382783.
• 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. PMID 12353027.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Koshiba S, Kigawa T, Kikuchi A, Yokoyama S (2003). "Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin". J. Struct. Funct. Genomics. 2 (1): 1–8. doi:10.1023/A:1011397007366. PMID 12836669.
• 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. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Timsit YE, Miller SL, Mohney RP, O'Bryan JP (2005). "The U-box ligase carboxyl-terminus of Hsc 70-interacting protein ubiquitylates Epsin". Biochem. Biophys. Res. Commun. 328 (2): 550–9. doi:10.1016/j.bbrc.2005.01.022. PMID 15694383.
• Schmid EM, Ford MG, Burtey A, et al. (2007). "Role of the AP2 β-Appendage Hub in Recruiting Partners for Clathrin-Coated Vesicle Assembly". PLoS Biol. 4 (9): e262. doi:10.1371/journal.pbio.0040262. PMC 1540706. PMID 16903783.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.