FBXO4

Protein-coding gene in the species Homo sapiens
FBXO4
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3L2O, 3L82

Identifiers
AliasesFBXO4, FBX4, F-box protein 4
External IDsOMIM: 609090; MGI: 2146220; HomoloGene: 8134; GeneCards: FBXO4; OMA:FBXO4 - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for FBXO4
Genomic location for FBXO4
Band5p13.1Start41,925,254 bp[1]
End41,941,743 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for FBXO4
Genomic location for FBXO4
Band15|15 A1Start3,994,927 bp[2]
End4,009,055 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
  • human 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
SpeciesHumanMouse
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 MbChr 15: 3.99 – 4.01 Mb
PubMed 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]

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.[7]

Interactions

FBXO4 has been shown to interact with:

References

  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.

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.


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