Human Gene FBXO3 (uc001muz.3) Description and Page Index
Description: Homo sapiens F-box protein 3 (FBXO3), transcript variant 1, mRNA. RefSeq Summary (NM_012175): 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 protein 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 diverging at the 3' end. [provided by RefSeq, Jul 2008]. Transcript (Including UTRs) Position: hg19 chr11:33,762,490-33,796,071 Size: 33,582 Total Exon Count: 11 Strand: - Coding Region Position: hg19 chr11:33,763,454-33,796,043 Size: 32,590 Coding Exon Count: 11
ID:FBX3_HUMAN DESCRIPTION: RecName: Full=F-box only protein 3; FUNCTION: Substrate recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. In the presence of PML, HIPK2 ubiquitination still occurs, but degradation is prevented. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53- dependent transactivation. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex consisting of FBXO3, SKP1, CUL1 and RBX1. Interacts with PML, interaction is direct and takes place either alone or within the SCF complex. INTERACTION: P04608:tat (xeno); NbExp=3; IntAct=EBI-2509901, EBI-6164389; SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with PML at the peripheries of nuclear bodies. SIMILARITY: Contains 1 apaG domain. SIMILARITY: Contains 1 F-box domain.
Genetic Association Studies of Complex Diseases and Disorders
Interleukin-6 Emelia J Benjamin et al. BMC medical genetics 2007, Genome-wide association with select biomarker traits in the Framingham Heart Study., BMC medical genetics.
The Framingham GWAS represents a resource to describe potentially novel genetic influences on systemic biomarker variability. The newly described associations will need to be replicated in other studies.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9UK99
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.