FBXO4
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| Location (UCSC) | Chr 5: 41.93 – 41.94 Mb | Chr 15: 3.99 – 4.01 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
F-box only protein 4 is a protein that in humans is encoded by the FBXO4 gene.[5][6][7]
Function
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the
WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Alternative splicing of this gene generates 2 transcript variants.[7]
Interactions
FBXO4 has been shown to
interact
with:
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000151876 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022184 – 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.
- ^ S2CID 7467493.
- S2CID 14341845.
- ^ a b "Entrez Gene: FBXO4 F-box protein 4".
- ^ PMID 17353931.
- S2CID 7467493.
Further reading
- Chiaur DS, Murthy S, Cenciarelli C, Parks W, Loda M, Inghirami G, Demetrick D, Pagano M (2000). "Five human genes encoding F-box proteins: chromosome mapping and analysis in human tumors". Cytogenet. Cell Genet. 88 (3–4): 255–8. S2CID 431704.
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. PMID 15302935.
- Jin J, Cardozo T, Lovering RC, Elledge SJ, Pagano M, Harper JW (2005). "Systematic analysis and nomenclature of mammalian F-box proteins". Genes Dev. 18 (21): 2573–80. PMID 15520277.
- Lee TH, Perrem K, Harper JW, Lu KP, Zhou XZ (2006). "The F-box protein FBX4 targets PIN2/TRF1 for ubiquitin-mediated degradation and regulates telomere maintenance". J. Biol. Chem. 281 (2): 759–68. PMID 16275645.
- Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. PMID 16344560.
- Liu Y, Hedvat CV, Mao S, Zhu XH, Yao J, Nguyen H, Koff A, Nimer SD (2006). "The ETS Protein MEF Is Regulated by Phosphorylation-Dependent Proteolysis via the Protein-Ubiquitin Ligase SCFSkp2". Mol. Cell. Biol. 26 (8): 3114–23. PMID 16581786.
- Lin DI, Barbash O, Kumar KG, Weber JD, Harper JW, Klein-Szanto AJ, Rustgi A, Fuchs SY, Diehl JA (2006). "Phosphorylation-dependent ubiquitination of cyclin D1 by the SCFFBX4-αBcrystallin complex". Mol. Cell. 24 (3): 355–66. PMID 17081987.
- Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. PMID 17353931.
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