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FBXO31 (F-box protein 31)

Identity

Other namesFBX14
Fbx31
FBX31
FBXO14
DKFZP434B027
DKFZp434J1815
FLJ22477
MGC15419
MGC9527
pp2386
HGNC (Hugo) FBXO31
Location 16q24.2
Location_base_pair Starts at 85920445 and ends at 85974895 bp from pter ( according to hg18-Mar_2006)  [Mapping]
Local_order telomere; centromeric to JPH3 and telomeric to FOXL1

DNA/RNA

Description FBXO31 encodes one mRNA transcript, published analyses have not reordered alternative five prime transcript or start sequences.
  • FBXO31 is 3,635-bp in length, composed of 9 exons (1 to 9) spanning approximately 55-kb of genomic DNA, and has an ORF of 1,620-bp encoding a protein of 539 amino acids with a predicted mass of 61-kDa.
  • Alternative five prime transcripts may exist. Homologous mouse cDNA sequences extending further five prime have been used for RT-PCR to identify putative translation start sites and established that alternatively spliced five prime exons result in short and long isoforms. The short isoform is 3,635-bp in length (i.e. approximately with poly A), and is the predicted primary transcript. The long isoform is 3,725-bp in length, contains an additional five prime exon of 87-bp and has an ORF of 1,707-bp encoding a protein of 568 amino acids. An additional smaller isoform of 3,099-bp with an ORF of 1,104-bp and 367 amino acids was predicted in GenBank.
  • FBXO31 contains a moderate density C + G rich region (66% G + G with 9% CpG) spanning approximately 2.48-kb located within and five prime to the 350-bp exon 1.
  • The FBXO31 transcript has and an uncharacteristically short 23-bp five prime untranslated region.
    • Pseudogene None identified.

    Protein

    Description FBXO31 contains no significant homology to other known proteins apart from a characteristic 40 amino acid F-box domain at the COOH-terminal end.
  • The F-box motif first described in cyclin F consists of approximately 50 amino acids that define an expanding family of eukaryotic proteins. There are currently three subdivisions of the F-box protein family based on the type of carboxy terminal motifs present in the protein sequences. Following proposed patterns the nomenclature adopted by HUGO denotes F-boxes that contain LRRs as FBXL, those containing WD repeats as FBXW, and those lacking all known protein-interaction domains as FBXO.
  • FBXO31 forms part of the FBXO class of F-box proteins. Comparison of FBXO31 with the F-box domain of functionally demonstrated F-box proteins (i.e. Fbx1, Fbx2, Fbw1a, Fbw1b and Fbl1 ) indicates that FBXO31 matches the F-box consensus more closely than recognized F-box proteins from each of the three classes. Most F-box proteins notated as FBXO do not have recognizable substrate binding domains. In one instance Fbx7 has been shown to contain a proline-rich region that functions with SCF complexes in regulating Cdk1 - cyclin B - phosphorylated hepatoma up-regulated protein ( HURP ) proteolysis. This proline-rich region has been found in other FBXO proteins. The COOH-terminal end of FBXO31 contains a 175-aa glycine and arginine rich region with possible similar function.
  • FBXO31 contains six minimal D-box (RxxL) motifs. Proteins with RxxL motifs are often degraded via the APC/C( Cdh1 ) ubiquitin ligase.
    • Expression FBXO31 is widely expressed as a 3.6-kb transcript at similar levels in breast, testis, ovary, liver, uterus, prostate, colon, stomach, bladder, spinal cord, pancreas, trachea, kidney and thyroid. High expression is found in brain and low expression in bone marrow. FBXO31 is represented by the unigene cluster Hs.567582. cDNA clones from Hs.567582 express in the adrenal gland, blood, colon, germ cells, heart, kidney, liver, lung, muscle, placenta, synovial membrane, tonsil, cervix, lymph tissue, skin, mammary gland, testis, ovary, uterus, prostate, stomach, bladder, spinal cord, pancreas, thyroid and brain.
    Localisation Co-immunoprecipitation experiments indicate that the carboxy terminal domain of FBXO31 associates with the Skp1, Roc-1 and Cullin-1 proteins. Immuno-localization studies demonstrate that ectopic expression of FBXO31 causes a change of Skp1 localization from the nucleus to the cytoplasm. The Skp1 protein returns to a nuclear localization when co-expressed with a FBXO31 protein with a deleted F-box domain.
    Function FBXO31 is associated with the Skp1, Roc-1 and Cullin-1 proteins through its substrate F-box recognition domain and forms part of an SCF ubiquitination complex.
    The ubiquitin-dependant proteasome degradation pathway regulates protein abundance and the function of oncogenes, tumor suppressors, transcription factors and other signaling molecules. Ubiquitination begins with the addition of ubiquitin moieties to target proteins and follows a multi-step process, the end point being proteolysis of polyubiquitinated substrates by a 26S multi-protein complex. Ubiquitination of substrates targeted for degradation requires 3 classes of enzymes; the ubiquitin-activating enzymes (E1), the ubiquitin conjugating enzymes (E2) and the ubiquitin ligases (E3). E3 proteins participate in cell cycle progression. SCF complexes (a class of E3 ligases) regulate the G1-S phase transition. A wide variety of SCF targets include G1 phase cyclins, cyclin-dependant kinase inhibitors, DNA replication factors and transcription factors that promote cell cycle progression.
    F-box containing proteins act as substrate recognition components of the SCF ubiquitin-ligase complexes in the ubiquitin-dependant proteasome degradation pathway. These complexes contain four components; Skp1, Cullin, Rbx-Rocl-Hrtl and an F-box protein. The F-box motif tethers the F-box protein to other components of the SCF complex by binding the core SCF component Skp1. This motif is generally found in the amino half of the proteins and is often coupled with other protein domains in the variable carboxy terminus of the protein. The most common carboxy terminal domains include leucine-rich repeats (LRRs) and WD-40 domains. Regions rich in glycine and arginine have also been implicated as protein binding domains, although such domains contain a more definitive repeat region than present in FBXO31.
    F-box SCF ubiquitin ligase complexes are involved in proteolysis pathways critical to diverse cellular functions including muscle atrophy, DNA metabolism, ER-associated degradation, desmin-related myopathy, signal transduction, control of G1-S progression and orderly execution of cell cycle. Skp1, Cul1 and Rbx1 are invariant proteins of the SCF complex while the F-box proteins that bind to Skp1 are the components that impart functional specificity. For instance Skp2 specifically binds phosphorylated p27 resulting in its degradation and control of S phase entry in the cell cycle.
    Homology F-box domain containing no other significant homology.

    Mutations

    Note None recorded.

    Implicated in

    Entity Neurodegenerative disorders and cancer
    Note Aberrant ubiquitin-dependant proteasome degradation in neurodegenerative disorders and cancer.
    Precedence for disruption in neurodegenerative disorders. The Parkin gene functions as a E3 ubiquitin ligase often mutated in inherited forms of Parkinson's disease. In Alzheimer's disease defective ubiquitination of cerebral proteins has been identified. The Von Hippel-Lindau ( VHL ) tumor suppressor protein is part of a complex that functions as a ubiquitin-protein ligase E3. VHL associates the ligase complex to target proteins such as HIF1aand VDU1 (VHL interacting deubiquitinating enzyme 1). HIF-a has been shown to regulate genes involved in tumor angiogenesis; VDU1 has deubiquitinating activity.
    Aberrant ubiquitin-dependant proteasome degradation of SCF-FBXO31 complexes has been proposed as a mechanism for tumor progression. FBXO31 would function as a tumor suppressor by mediating generation of SCF-FBXO31 complexes that compete and balance levels of other SCF complexes normally targeted to degradation proteins required to maintain cell proliferation. An example is SCF complexes resulting in SCF-Skp2 E3 ligases that mediate ubiquitination and subsequent degradation of the CDK-inhibitor p27. Ectopic expression of FBXO31 would lower SCF-Skp2 complexes resulting in increased p27 and inhibition of transition from G1-S phase. This model corroborates with studies showing that high levels of Skp2 were associated with reduced levels of p27 in several cancers.
    Abnormal Protein None recorded
      
    Entity Breast cancer, Prostate cancer, and several other cancers
    Note Loss of heterozygosity (LOH) of 16q22-qter in breast cancer, prostate cancer, and several other cancers.
    This region is frequently deleted in several human cancers causing loss of heterozygosity. The 16q24.3 region including FBXO31 spans approximately 3-Mb from the marker D16S498 to the telomere and contains at least two smallest regions of overlap (SROs). These SROs are most frequently deleted in early and late stage breast cancer and in prostate cancer. Loss of normal function of FBXO31 may be a key event in the early stage of breast cancer. LOH on the whole 16q22-qter region is frequently detected in breast and prostate cancer. Micro-cell mediated transfer experiments with 16q22-qter fragments (the 360-kb YAC clone 792E1 at D16S476 and D16S498 and the 85-kb BAC clone 346J21 at D16S3048 and D16S3063) have been shown to induce senescence in human and rat breast tumor cell lines. FBXO31 encompasses the 792E1 clone and a partial region of 346J21, has been shown to induce senescence in the breast cancer cell line MCF-7 and is regarded as the cellular senescence gene. FBXO31 is a potential tumor suppressor shown to be down-regulated in breast cancer cell lines relative to normal breast expression and cause G1 phase cell cycle arrest of the MDA-MB-468 cell line.
    Quantitative gene expression analysis of 78 genes in the 16q24.3 region demonstrated that FBXO31 was one of two genes including CYBA with a moderately aberrant expression profile. Expression of FBXO31 was reduced 100 to 200-fold in MDA-MB-134 and SK-BR-3 and moderately reduced in the other cell lines. 68 other genes displayed normal expression, one displayed significantly aberrant expression ( CBFA2T3 ), six displayed mildly aberrant expression (DPEP1, CDH15, Hs.17074, Hs.189419, SLC7A5 and AA994450), and one gene displayed excessively reduced expression (CA5A). From microarray analysis FBXO31 was one of the 70-gene classifiers down-regulated in association with tumors of a favorable prognosis. The prognostic association between down-regulated FBXO31 and breast tumors corroborates with other studies demonstrating that LOH of chromosome 16q is associated with tumors of favorable prognosis.
    Disease 16q22-qter LOH is detected in bilateral breast cancer and ductal lavage, in rare inflammatory breast cancer, and in several other cancers, including central nervous system neuroectodermal ependymoma and primary ependymomas, colorectal liver metastases, gastric tumor cancer, head and neck squamous cell carcinoma, hepatocellular carcinoma, lung tumor, nasopharyngeal tumor, ovarian tumor, rhabdomyosarcoma, and Wilms' tumor. 16q22-qter LOH in ovarian, hepatocellular and particularly breast and prostate cancers, exhibit similar SROs, suggesting common molecular pathways are affected.
      

    External links

    Nomenclature
    HGNC (Hugo)FBXO31   16510
    Entrez_Gene (NCBI)FBXO31  79791  F-box protein 31
    Cards
    AtlasFBXO31ID44280ch16q24
    GeneCards (Weizmann)FBXO31
    Ensembl (Hinxton)ENSG00000103264 [Gene_View]  FBXO31 [Vega]
    AceView (NCBI)FBXO31
    Genatlas (Paris)FBXO31
    euGene (Indiana)79791
    SOURCE (Stanford)NM_024735
    Gene Expression (Array Express) ENSG00000103264
    Genomic and cartography
    GoldenPath (UCSC)FBXO31  -  16q24.2   chr16:85920445-85974895 -  16q24.2   [Description]    (hg18-Mar_2006)
    EnsemblFBXO31 - 16q24.2 [CytoView]
    Mapping of homologs : NCBIFBXO31 [Mapview]
    OMIM609102   
    Gene and transcription
    Gene : Genbank (Entrez)AF318348 AF428140 AK026130 AK311122 AL117444
    Reference sequence (RefSeq transcript) :SRSNM_024735
    Reference transcript : EntrezNM_024735
    RefSeq genomic : SRSAC_000059 AC_000148 NC_000016 NT_010498 NW_001838329 NW_926528
    RefSeq genomic : EntrezAC_000059 AC_000148 NC_000016 NT_010498 NW_001838329 NW_926528
    Consensus coding sequences : CCDS NCBIFBXO31
    Cluster EST : UnigeneHs.720783 [ SRS ] Hs.720783 [ NCBI ]
    Alternative Splicing : Fast-db (Paris)12190
    Protein : pattern, domain, 3D structure
    Protein : UniProt/SwissProtQ5XUX0 (SRS) Q5XUX0 (Expasy) Q5XUX0 (Uniprot)
    With graphics : InterProQ5XUX0
    Splice isoforms : VarSplice FASTAQ5XUX0(VarSplice FASTA)
    Domaine pattern : Prosite (SRS)FBOX (PS50181)   
    Domain pattern : Prosite (Expaxy)FBOX (PS50181)   
    Domains : Interpro (SRS)F-box   
    Domains : Interpro (EBI)F-box   
    Related proteins : CluSTrQ5XUX0
    Domain families : Pfam SRSF-box (PF00646)   
    Domain families : Pfam SangerF-box (PF00646)   
    Domain families : Pfam NCBIpfam00646   
    Domain families : Smart EMBLFBOX (SM00256)  
    Blocks (Seattle)Q5XUX0
    Crystal structure of protein : PDB SRS
    Crystal structure of protein : PDBSum
    Crystal structure of protein : IMB
    Crystal structure of protein : PDB RSDB
    HPRD10954
    Protein Interaction databases
    DIP (DOE-UCLA)Q5XUX0
    IntAct (EBI)Q5XUX0
    Polymorphism : SNP, mutations, diseases
    Single Nucleotide Polymorphism (SNP) : dbSNP NCBIFBXO31
    SNP : GeneSNP UtahFBXO31
    SNP : HGBaseFBXO31
    Genetic variants : HAPMAPFBXO31
    Somatic Mutations in Cancer : COSMICFBXO31 
    Mutations and Diseases : HGMDFBXO31
    Hereditary diseases : OMIM609102   
    Hereditary diseases : GENETests609102   
    Diseases : Genetic AssociationFBXO31
    General knowledge
    Homologs : HomoloGeneFBXO31
    Homology/Alignments : Family Browser UCSCFBXO31
    Phylogenetic Trees/Animal Genes : TreeFamFBXO31
    Chemical/Protein Interactions : CTD79791
    Keywords Ontology : AmiGOcell cycle  cyclin catabolic process  SCF ubiquitin ligase complex  modification-dependent protein catabolic process  cyclin binding  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  G1/S DNA damage checkpoint  cellular response to DNA damage stimulus  
    Keywords Ontology : EGO-EBIcell cycle  cyclin catabolic process  SCF ubiquitin ligase complex  modification-dependent protein catabolic process  cyclin binding  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  G1/S DNA damage checkpoint  cellular response to DNA damage stimulus  
    Pathways : BIOCARTA
    Pathways : KEGG
    Other databases
    Probes
    Probes : ImagenesFBXO31 Related clones (RZPD - Berlin)
    Literature
    PubMed11 Pubmed reference(s) in Entrez
    PubGeneFBXO31

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    Contributor(s)

    Written06-2008Anthony J Bais
    Immunogene Therapy Surgical Research Division, Boston University School of Medicine, Roger Williams Medical Center, 825 Chalkstone Avenue, Providence, RI 02908, USA

    Citation

    This paper should be referenced as such :
    Bais AJ . FBXO31 (F-box protein 31). Atlas Genet Cytogenet Oncol Haematol. June 2008 .
    URL : http://AtlasGeneticsOncology.org/Genes/FBXO31ID44280ch16q24.html

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