Biology:YWHAE
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
14-3-3 protein epsilon is a protein that in humans is encoded by the YWHAE gene.[1]
Function
This gene product belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in both plants and mammals, and this protein is 100% identical to the mouse ortholog. It interacts with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer,[2] and microdeletions associated with Miller–Dieker syndrome.[3]
Interactions
YWHAE has been shown to interact with:
- C-Raf,[4][5]
- CDC25B,[6][4]
- HDAC4,[7][8]
- HERG,[9]
- IRS1[10] and
- IGF1R,[10]
- MAP3K3,[11]
- NDEL1,[12]
- NGFRAP1,[13] and
- TGF beta 1.[14]
See also
References
- ↑ "Assignment of the human 14-3-3 epsilon isoform (YWHAE) to human chromosome 17p13 by in situ hybridization". Cytogenet Cell Genet 78 (2): 105–6. December 1997. doi:10.1159/000134638. PMID 9371399.
- ↑ "Entrez Gene: YWHAE tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, epsilon polypeptide". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7531.
- ↑ "Neurodevelopmental Genetic Diseases Associated With Microdeletions and Microduplications of Chromosome 17p13.3". Frontiers in Genetics 9: 80. 2018. doi:10.3389/fgene.2018.00080. PMID 29628935.
- ↑ 4.0 4.1 "14-3-3 proteins associate with cdc25 phosphatases". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7892–6. August 1995. doi:10.1073/pnas.92.17.7892. PMID 7644510. Bibcode: 1995PNAS...92.7892C.
- ↑ "14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules". J. Biol. Chem. 271 (33): 20029–34. August 1996. doi:10.1074/jbc.271.33.20029. PMID 8702721.
- ↑ "Specific interaction between 14-3-3 isoforms and the human CDC25B phosphatase". Oncogene 19 (10): 1257–65. March 2000. doi:10.1038/sj.onc.1203419. PMID 10713667.
- ↑ "Differential localization of HDAC4 orchestrates muscle differentiation". Nucleic Acids Res. 29 (16): 3439–47. August 2001. doi:10.1093/nar/29.16.3439. PMID 11504882.
- ↑ "Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization". Proc. Natl. Acad. Sci. U.S.A. 97 (14): 7835–40. July 2000. doi:10.1073/pnas.140199597. PMID 10869435. Bibcode: 2000PNAS...97.7835G.
- ↑ "14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity". EMBO J. 21 (8): 1889–98. April 2002. doi:10.1093/emboj/21.8.1889. PMID 11953308.
- ↑ 10.0 10.1 "14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner". J. Biol. Chem. 272 (17): 11663–9. April 1997. doi:10.1074/jbc.272.17.11663. PMID 9111084.
- ↑ "14-3-3 proteins interact with specific MEK kinases". J. Biol. Chem. 273 (6): 3476–83. February 1998. doi:10.1074/jbc.273.6.3476. PMID 9452471.
- ↑ "14-3-3epsilon is important for neuronal migration by binding to NUDEL: a molecular explanation for Miller-Dieker syndrome". Nat. Genet. 34 (3): 274–85. July 2003. doi:10.1038/ng1169. PMID 12796778.
- ↑ "14-3-3 is involved in p75 neurotrophin receptor-mediated signal transduction". J. Biol. Chem. 276 (20): 17291–300. May 2001. doi:10.1074/jbc.M005453200. PMID 11278287.
- ↑ "Conserved role for 14-3-3epsilon downstream of type I TGFbeta receptors". FEBS Lett. 490 (1–2): 65–9. February 2001. doi:10.1016/S0014-5793(01)02133-0. PMID 11172812.
Further reading
- "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1". DNA Cell Biol. 23 (4): 193–205. 2004. doi:10.1089/104454904773819789. PMID 15142377. https://zenodo.org/record/1235217.
- "Human immunodeficiency virus type-1 accessory protein Vpr: a causative agent of the AIDS-related insulin resistance/lipodystrophy syndrome?". Ann. N. Y. Acad. Sci. 1024 (1): 153–67. 2004. doi:10.1196/annals.1321.013. PMID 15265780. Bibcode: 2004NYASA1024..153K. https://zenodo.org/record/1235880.
- "Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins". FEBS Lett. 368 (1): 55–8. 1995. doi:10.1016/0014-5793(95)00598-4. PMID 7615088.
- "14-3-3 proteins associate with cdc25 phosphatases". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7892–6. 1995. doi:10.1073/pnas.92.17.7892. PMID 7644510. Bibcode: 1995PNAS...92.7892C.
- "Function of 14-3-3 proteins". Nature 382 (6589): 308. 1996. doi:10.1038/382308a0. PMID 8684458. Bibcode: 1996Natur.382..308J. https://zenodo.org/record/1233186.
- "14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules". J. Biol. Chem. 271 (33): 20029–34. 1996. doi:10.1074/jbc.271.33.20029. PMID 8702721.
- "14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome region". Genome Res. 6 (8): 735–41. 1997. doi:10.1101/gr.6.8.735. PMID 8858348.
- "14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner". J. Biol. Chem. 272 (17): 11663–9. 1997. doi:10.1074/jbc.272.17.11663. PMID 9111084.
- "Protein binding and signaling properties of RIN1 suggest a unique effector function". Proc. Natl. Acad. Sci. U.S.A. 94 (10): 4954–9. 1997. doi:10.1073/pnas.94.10.4954. PMID 9144171. Bibcode: 1997PNAS...94.4954H.
- "14-3-3 protein binds to insulin receptor substrate-1, one of the binding sites of which is in the phosphotyrosine binding domain". J. Biol. Chem. 272 (40): 25267–74. 1997. doi:10.1074/jbc.272.40.25267. PMID 9312143.
- "Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11". Mol. Endocrinol. 11 (12): 1858–67. 1997. doi:10.1210/mend.11.12.0023. PMID 9369453.
- "The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3". EMBO J. 17 (1): 149–58. 1998. doi:10.1093/emboj/17.1.149. PMID 9427749.
- "14-3-3 proteins interact with specific MEK kinases". J. Biol. Chem. 273 (6): 3476–83. 1998. doi:10.1074/jbc.273.6.3476. PMID 9452471.
- "Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins". EMBO J. 17 (7): 1892–906. 1998. doi:10.1093/emboj/17.7.1892. PMID 9524113.
- "In vivo and in vitro association of 14-3-3 epsilon isoform with calmodulin: implication for signal transduction and cell proliferation". J. Cell. Biochem. 73 (1): 31–5. 1999. doi:10.1002/(SICI)1097-4644(19990401)73:1<31::AID-JCB4>3.0.CO;2-X. PMID 10088721.
- "alpha-Synuclein shares physical and functional homology with 14-3-3 proteins". J. Neurosci. 19 (14): 5782–91. 1999. doi:10.1523/JNEUROSCI.19-14-05782.1999. PMID 10407019.
- "Phosphorylation-dependent association of the Ras-related GTP-binding protein Rem with 14-3-3 proteins". Arch. Biochem. Biophys. 368 (2): 401–12. 1999. doi:10.1006/abbi.1999.1316. PMID 10441394.
- "The kinesin-like motor protein KIF1C occurs in intact cells as a dimer and associates with proteins of the 14-3-3 family". J. Biol. Chem. 274 (47): 33654–60. 1999. doi:10.1074/jbc.274.47.33654. PMID 10559254.
- "Hepatitis C Virus Core Protein Interacts with 14-3-3 Protein and Activates the Kinase Raf-1". J. Virol. 74 (4): 1736–41. 2000. doi:10.1128/JVI.74.4.1736-1741.2000. PMID 10644344.
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