Biology:EPN1
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Epsin-1 is a protein that in humans is encoded by the EPN1 gene.[1][2][3]
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][3]
Interactions
EPN1 has been shown to interact with REPS2,[2] AP2A2[1] and EPS15.[1]
References
- ↑ 1.0 1.1 1.2 "Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis". Nature 394 (6695): 793–7. Sep 1998. doi:10.1038/29555. PMID 9723620. Bibcode: 1998Natur.394..793C.
- ↑ 2.0 2.1 "Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis". Oncogene 18 (43): 5915–22. Dec 1999. doi:10.1038/sj.onc.1202974. PMID 10557078.
- ↑ 3.0 3.1 "Entrez Gene: EPN1 epsin 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29924.
Further reading
- "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. 2000. doi:10.1074/jbc.275.9.6479. PMID 10692452. http://www.pitt.edu/~traub/publications/6479.pdf.
- 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. PMID 10791968.
- "Interaction of two structurally distinct sequence types with the clathrin terminal domain beta-propeller". J. Biol. Chem. 276 (31): 28700–9. 2001. 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. Bibcode: 2002Natur.419..361F.
- 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. Bibcode: 2002PNAS...9916899M.
- "Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin". J. Struct. Funct. Genomics 2 (1): 1–8. 2003. 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. PMID 15489334.
- "The U-box ligase carboxyl-terminus of Hsc 70-interacting protein ubiquitylates Epsin". Biochem. Biophys. Res. Commun. 328 (2): 550–9. 2005. doi:10.1016/j.bbrc.2005.01.022. PMID 15694383. https://zenodo.org/record/1258784.
- 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. 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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