EPN1

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Epsin 1
PDB rendering based on 1edu.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols EPN1 ;
External IDs Template:OMIM5 Template:MGI HomoloGene32172
Orthologs
Template:GNF Ortholog box
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

Epsin 1, also known as EPN1, is a human gene.[1]

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][1]

References

  1. 1.0 1.1 "Entrez Gene: EPN1 epsin 1".

Further reading

  • Chen H, Fre S, Slepnev VI; et al. (1998). "Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis". Nature. 394 (6695): 793–7. doi:10.1038/29555. PMID 9723620.
  • Morinaka K, Koyama S, Nakashima S; et al. (1999). "Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis". Oncogene. 18 (43): 5915–22. doi:10.1038/sj.onc.1202974. PMID 10557078.
  • 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. 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 NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF)". J. Cell Biol. 149 (3): 537–46. 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. 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. 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. 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 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly". PLoS Biol. 4 (9): e262. doi:10.1371/journal.pbio.0040262. 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.

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