FBXO4 (original) (raw)

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Protein-coding gene in the species Homo sapiens

FBXO4
Available structuresPDBOrtholog search: PDBe RCSB List of PDB id codes3L2O, 3L82
Identifiers
Aliases	FBXO4, FBX4, F-box protein 4
External IDs	OMIM: 609090; MGI: 2146220; HomoloGene: 8134; GeneCards: FBXO4; OMA:FBXO4 - orthologs
Gene location (Human)Chr.Chromosome 5 (human)[1]Band5p13.1Start41,925,254 bp[1]End41,941,743 bp[1]
Gene location (Mouse)Chr.Chromosome 15 (mouse)[2]Band15|15 A1Start3,994,927 bp[2]End4,009,055 bp[2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inAchilles tendonbody of pancreastesticlegastric mucosaright uterine tubeskin of armtibial nerveright lobe of thyroid glandright lobe of liverleft lobe of thyroid glandTop expressed insacculeciliary bodyproximal tubuleotic vesicleright kidneysubcutaneous adipose tissuewhite adipose tissuespermatocyteduodenumcalvariaMore reference expression dataBioGPSn/a
Gene ontologyMolecular 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
OrthologsSpeciesHuman MouseEntrez26272106052EnsemblENSG00000151876ENSMUSG00000022184UniProtQ9UKT5Q8CHQ0RefSeq (mRNA)NM_001297437NM_012176NM_033484NM_134099RefSeq (protein)NP_001284366NP_036308NP_277019NP_598860Location (UCSC)Chr 5: 41.93 – 41.94 MbChr 15: 3.99 – 4.01 MbPubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

F-box only protein 4 is a protein that in humans is encoded by the FBXO4 gene.[5][6][7]

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.[7]

FBXO4 has been shown to interact with:

• CUL1,[5][8] and
• SKP1A.[8][9]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000151876 – Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022184 – 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 Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M (Dec 1999). "Identification of a family of human F-box proteins". Curr Biol. 9 (20): 1177–9. Bibcode:1999CBio....9.1177C. doi:10.1016/S0960-9822(00)80020-2. PMID 10531035. S2CID 7467493.
6. ^ Winston JT, Koepp DM, Zhu C, Elledge SJ, Harper JW (Dec 1999). "A family of mammalian F-box proteins". Curr Biol. 9 (20): 1180–2. Bibcode:1999CBio....9.1180W. doi:10.1016/S0960-9822(00)80021-4. PMID 10531037. S2CID 14341845.
7. ^ a b "Entrez Gene: FBXO4 F-box protein 4".
8. ^ a b 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: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
9. ^ Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M (Oct 1999). "Identification of a family of human F-box proteins". Curr. Biol. 9 (20): 1177–9. Bibcode:1999CBio....9.1177C. doi:10.1016/S0960-9822(00)80020-2. PMID 10531035. S2CID 7467493.

• 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.