EPS15

From Wikipedia, the free encyclopedia


Epidermal growth factor receptor pathway substrate 15
PDB rendering based on 1c07.
Available structures: 1c07, 1eh2, 1f8h, 1ff1, 1qjt
Identifiers
Symbol(s) EPS15; AF-1P; AF1P; MLLT5
External IDs OMIM: 600051 MGI104583 HomoloGene81627
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 2060 13858
Ensembl ENSG00000085832 ENSMUSG00000028552
Uniprot P42566 Q8C431
Refseq NM_001981 (mRNA)
NP_001972 (protein)
NM_007943 (mRNA)
NP_031969 (protein)
Location Chr 1: 51.59 - 51.76 Mb Chr 4: 108.78 - 108.89 Mb
Pubmed search [1] [2]

Epidermal growth factor receptor pathway substrate 15, also known as EPS15, is a human gene.

This gene encodes a protein that is part of the EGFR pathway. The protein is present at clathrin-coated pits and is involved in receptor-mediated endocytosis of EGF. Notably, this gene is rearranged with the HRX/ALL/MLL gene in acute myelogeneous leukemias. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.[1]

[edit] References

[edit] Further reading

  • Schumacher C, Knudsen BS, Ohuchi T, et al. (1995). "The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R.". J. Biol. Chem. 270 (25): 15341–7. PMID 7797522. 
  • Bernard OA, Mauchauffe M, Mecucci C, et al. (1994). "A novel gene, AF-1p, fused to HRX in t(1;11)(p32;q23), is not related to AF-4, AF-9 nor ENL.". Oncogene 9 (4): 1039–45. PMID 8134107. 
  • Wong WT, Kraus MH, Carlomagno F, et al. (1994). "The human eps15 gene, encoding a tyrosine kinase substrate, is conserved in evolution and maps to 1p31-p32.". Oncogene 9 (6): 1591–7. PMID 8183552. 
  • Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474. 
  • Benmerah A, Bégue B, Dautry-Varsat A, Cerf-Bensussan N (1996). "The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein.". J. Biol. Chem. 271 (20): 12111–6. PMID 8662627. 
  • Matsuda M, Ota S, Tanimura R, et al. (1996). "Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins.". J. Biol. Chem. 271 (24): 14468–72. PMID 8662907. 
  • van Delft S, Schumacher C, Hage W, et al. (1997). "Association and colocalization of Eps15 with adaptor protein-2 and clathrin.". J. Cell Biol. 136 (4): 811–21. PMID 9049247. 
  • Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174. 
  • Tebar F, Confalonieri S, Carter RE, et al. (1997). "Eps15 is constitutively oligomerized due to homophilic interaction of its coiled-coil region.". J. Biol. Chem. 272 (24): 15413–8. PMID 9182572. 
  • Salcini AE, Confalonieri S, Doria M, et al. (1997). "Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module.". Genes Dev. 11 (17): 2239–49. PMID 9303539. 
  • Cupers P, ter Haar E, Boll W, Kirchhausen T (1998). "Parallel dimers and anti-parallel tetramers formed by epidermal growth factor receptor pathway substrate clone 15.". J. Biol. Chem. 272 (52): 33430–4. PMID 9407139. 
  • Haffner C, Takei K, Chen H, et al. (1998). "Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15.". FEBS Lett. 419 (2-3): 175–80. PMID 9428629. 
  • Benmerah A, Lamaze C, Bègue B, et al. (1998). "AP-2/Eps15 interaction is required for receptor-mediated endocytosis.". J. Cell Biol. 140 (5): 1055–62. PMID 9490719. 
  • de Beer T, Carter RE, Lobel-Rice KE, et al. (1998). "Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.". Science 281 (5381): 1357–60. PMID 9721102. 
  • 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. 
  • Lewin DA, Sheff D, Ooi CE, et al. (1998). "Cloning, expression, and localization of a novel gamma-adaptin-like molecule.". FEBS Lett. 435 (2-3): 263–8. PMID 9762922. 
  • Sengar AS, Wang W, Bishay J, et al. (1999). "The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15.". EMBO J. 18 (5): 1159–71. doi:10.1093/emboj/18.5.1159. PMID 10064583. 
  • Poupon V, Bègue B, Gagnon J, et al. (1999). "Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesterase.". J. Biol. Chem. 274 (27): 19188–94. PMID 10383425. 
  • Nakashima S, Morinaka K, Koyama S, et al. (1999). "Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors.". EMBO J. 18 (13): 3629–42. doi:10.1093/emboj/18.13.3629. PMID 10393179. 
  • Stephens DJ, Banting G (1999). "Direct interaction of the trans-Golgi network membrane protein, TGN38, with the F-actin binding protein, neurabin.". J. Biol. Chem. 274 (42): 30080–6. PMID 10514494.