EPN1

Protein-coding gene in the species Homo sapiens
EPN1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1INZ

Identifiers
AliasesEPN1, epsin 1
External IDsOMIM: 607262; MGI: 1333763; HomoloGene: 32172; GeneCards: EPN1; OMA:EPN1 - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for EPN1
Genomic location for EPN1
Band19q13.42Start55,675,226 bp[1]
End55,709,858 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for EPN1
Genomic location for EPN1
Band7|7 A1Start5,080,235 bp[2]
End5,098,178 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • apex of heart

  • body of stomach

  • mucosa of transverse colon

  • right frontal lobe

  • right auricle

  • anterior cingulate cortex

  • left testis

  • muscle of thigh

  • right testis

  • body of pancreas
Top expressed in
  • Ileal epithelium

  • perirhinal cortex

  • CA3 field

  • entorhinal cortex

  • primary visual cortex

  • superior frontal gyrus

  • dentate gyrus of hippocampal formation granule cell

  • lactiferous gland

  • choroid plexus of fourth ventricle

  • ankle joint
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • protein binding
  • lipid binding
Cellular component
  • cytoplasm
  • plasma membrane
  • clathrin-coated pit
  • membrane
  • 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
SpeciesHumanMouse
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 MbChr 7: 5.08 – 5.1 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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]

Interactions

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

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000063245 – Ensembl, May 2017
  2. ^ a b c 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. ^ 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.
  6. ^ 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.
  7. ^ a b "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. 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.
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    1inz: SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN OF HUMAN EPSIN


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