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Protein-coding gene in the species Homo sapiens
Epsin-1 is a protein that in humans is encoded by the EPN1 gene .[ 5] [ 6] [ 7]
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][ 7]
EPN1 has been shown to interact with REPS2 ,[ 6] AP2A2 [ 5] EPS15 .[ 5]
^ a b c GRCh38: Ensembl release 89: ENSG00000063245 – Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035203 – Ensembl , May 2017^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ a b c Chen H, Fre S, Slepnev VI, Capua MR, Takei K, Butler MH, Di Fiore PP, De Camilli P (Sep 1998). "Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis". Nature . 394 (6695): 793–7. Bibcode :1998Natur.394..793C . doi :10.1038/29555 . PMID 9723620 . S2CID 4430975 . ^ a b Morinaka K, Koyama S, Nakashima S, Hinoi T, Okawa K, Iwamatsu A, Kikuchi A (Dec 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 . ^ a b "Entrez Gene: EPN1 epsin 1" .
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" (PDF) . J. Biol. Chem . 275 (9): 6479–89. doi :10.1074/jbc.275.9.6479 PMID 10692452 . S2CID 22584410 . 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. Bibcode :2002Natur.419..361F . doi :10.1038/nature01020 . PMID 12353027 . S2CID 4372368 . 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. Bibcode :2002PNAS...9916899M . 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 . S2CID 13317798 . 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 . S2CID 7827573 .
PDB gallery
1edu : CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1
1eyh : CRYSTAL STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN AT 1.56 ANGSTROM RESOLUTION
1h0a : EPSIN ENTH BOUND TO INS(1,4,5)P3
1inz : SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN OF HUMAN EPSIN
