// Workers AI · dad joke modeWhat did FBXO4 gene say? I've got a "four"-cast for cancer research.

FBXO4
Identifiers
Aliases	FBXO4, FBX4, F-box protein 4
External IDs	OMIM: 609090; MGI: 2146220; HomoloGene: 8134; GeneCards: FBXO4; OMA:FBXO4 - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3L2O, 3L82
Gene location (Human) Chr. Chromosome 5 (human) Band 5p13.1 Start 41,925,254 bp End 41,941,743 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15|15 A1 Start 3,994,927 bp End 4,009,055 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon body of pancreas testicle gastric mucosa right uterine tube skin of arm tibial nerve right lobe of thyroid gland right lobe of liver left lobe of thyroid gland Top expressed in saccule ciliary body proximal tubule otic vesicle right kidney subcutaneous adipose tissue white adipose tissue spermatocyte duodenum calvaria More reference expression data BioGPS n/a
Gene ontology Molecular function protein binding protein homodimerization activity ubiquitin protein ligase activity ubiquitin-protein transferase activity Cellular component ubiquitin ligase complex cytosol SCF ubiquitin ligase complex cytoplasm Biological process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process telomere maintenance positive regulation of protein ubiquitination ubiquitin-dependent protein catabolic process protein polyubiquitination common myeloid progenitor cell proliferation protein destabilization positive regulation of protein polyubiquitination ageing negative regulation of fibroblast proliferation cellular response to ionizing radiation cellular homeostasis regulation of DNA damage checkpoint negative regulation of protein localization to nucleus posttranscriptional regulation of gene expression protein ubiquitination regulation of protein stability positive regulation of telomere maintenance via telomerase post-translational protein modification Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 26272 106052 Ensembl ENSG00000151876 ENSMUSG00000022184 UniProt Q9UKT5 Q8CHQ0 RefSeq (mRNA) NM_001297437 NM_012176 NM_033484 NM_134099 RefSeq (protein) NP_001284366 NP_036308 NP_277019 NP_598860 Location (UCSC) Chr 5: 41.93 – 41.94 Mb Chr 15: 3.99 – 4.01 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

F-box only protein 4 is a protein that in humans is encoded by the FBXO4 gene.

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 ubiquitin ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing 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.

Interactions

FBXO4 has been shown to interact with:

• CUL1, and
• SKP1A.

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. doi:10.1159/000015532. PMID 10828603. 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. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. 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. doi:10.1101/gad.1255304. PMC 525538. 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. doi:10.1074/jbc.M509855200. 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. doi:10.1101/gr.4039406. PMC 1356129. 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. doi:10.1128/MCB.26.8.3114-3123.2006. PMC 1446966. 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. doi:10.1016/j.molcel.2006.09.007. PMC 1702390. 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. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.