EPN1

Epsin-1 is a protein that in humans is encoded by the EPN1 gene.[5][6][7]

EPN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1INZ
Identifiers
Aliases	EPN1, epsin 1
External IDs	OMIM: 607262 MGI: 1333763 HomoloGene: 32172 GeneCards: EPN1
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19q13.42 Start 55,675,226 bp[1] End 55,709,858 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 A1 Start 5,080,235 bp[2] End 5,098,178 bp[2]
Gene ontology Molecular function • GO:0001948 protein binding • lipid binding Cellular component • cytoplasm • cell membrane • clathrin-coated pit • membrane • cell nucleus • cytosol Biological process • Notch signaling pathway • female pregnancy • negative regulation of epidermal growth factor receptor signaling pathway • in utero embryonic development • endocytosis • embryonic organ development • membrane organization • negative regulation of sprouting angiogenesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	29924	13854
Ensembl	ENSG00000063245	ENSMUSG00000035203
UniProt	Q9Y6I3	Q80VP1
RefSeq (mRNA)	NM_001130071 NM_001130072 NM_013333 NM_001321263	NM_001252454 NM_010147
RefSeq (protein)	NP_001123543 NP_001123544 NP_001308192 NP_037465	NP_001239383 NP_034277 NP_001359429
Location (UCSC)	Chr 19: 55.68 – 55.71 Mb	Chr 7: 5.08 – 5.1 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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]

Interactions

EPN1 has been shown to interact with REPS2,[6] AP2A2[5] and EPS15.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000063245 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000035203 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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. doi:10.1038/29555. PMID 9723620.
6. 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.
7. "Entrez Gene: EPN1 epsin 1".

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" (PDF). 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.