EPN1

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Epsin 1
PDB rendering based on 1edu.
Available structures: 1edu, 1eyh, 1h0a, 1inz
Identifiers
Symbol(s) EPN1;
External IDs OMIM: 607262 MGI: 1333763 HomoloGene: 32172
Orthologs
Human Mouse
Entrez 29924 13854
Ensembl ENSG00000063245 ENSMUSG00000035203
Uniprot Q9Y6I3 Q80VP1
Refseq NM_013333 (mRNA)
NP_037465 (protein)		 XM_977106 (mRNA)
XP_982200 (protein)
Location Chr 19: 60.88 - 60.9 Mb Chr 7: 4.68 - 4.7 Mb
Pubmed search [1] [2]

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]

[edit] References

  1. ^ a b Entrez Gene: EPN1 epsin 1.

[edit] 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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