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FBXO31 (F-box protein 31)

Written2008-06Anthony J Bais
Immunogene Therapy Surgical Research Division, Boston University School of Medicine, Roger Williams Medical Center, 825 Chalkstone Avenue, Providence, RI 02908, USA

(Note : for Links provided by Atlas : click)

Identity

Alias (NCBI)FBX14
Fbx31
FBX31
FBXO14
DKFZP434B027
DKFZp434J1815
FLJ22477
MGC15419
MGC9527
pp2386
HGNC (Hugo) FBXO31
HGNC Alias symbFBX14
FBXO14
Fbx31
MGC15419
HGNC Previous nameF-box only protein 31
LocusID (NCBI) 79791
Atlas_Id 44280
Location 16q24.2  [Link to chromosome band 16q24]
Location_base_pair Starts at 87326987 and ends at 87383776 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping FBXO31.png]
Local_order telomere; centromeric to JPH3 and telomeric to FOXL1
Fusion genes
(updated 2017)		Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
DEF8 (16q24.3)::FBXO31 (16q24.2)DSTN (20p12.1)::FBXO31 (16q24.2)

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.
  • 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

    Note
      
    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.
      

    Bibliography

    Multiple polysomies in breast carcinomas: preferential gain of chromosomes 1, 5, 6, 7, 12, 16, 17, 18, and 19.
    Adeyinka A, Mertens F, Idvall I, Bondeson L, Pandis N.
    Cancer Genet Cytogenet 1999; 111: 144-148.
    PMID 10347552
     
    p27 deregulation in breast cancer: prognostic significance and implications for therapy.
    Alkarain A, Jordan R, Slingerland J.
    J Mammary Gland Biol Neoplasia 2004; 9: 67-80.
    PMID 15082919
     
    SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box.
    Bai C, Sen P, Hofmann K, Ma L, Goebl M, Harper JW, Elledge SJ.
    Cell 1996;86:263-274.
    PMID 8706131
     
    Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase.
    Bashir T, Dorrello NV, Amador V, Guardavaccaro D, Pagano M.
    Nature 2004; 428: 190-193.
    PMID 15014502
     
    The proteasome: paradigm of a self-compartmentalizing protease.
    Baumeister W, Walz J, Zuhl F, Seemuller E.
    Cell 1998;92: 367-380.
    PMID 9476896
     
    Deregulated degradation of the cdk inhibitor p27 and malignant transformation.
    Bloom J, Pagano M.
    Semin Cancer Biol 2003; 13: 41-47.
    PMID 12507555
     
    SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27.
    Carrano AC, Eytan E, Hershko A, Pagano M.
    Nat Cell Biol 1999;1:193-199.
    PMID 10559916
     
    Allelic loss of chromosomes 16q and 10q in human prostate cancer.
    Carter BS, Ewing CM, Ward WS, Treiger BF, Aalders TW, Schalken JA, Epstein JI, Isaacs WB.
    Proc Natl Acad Sci U S A 1990; 87: 8751-8755.
    PMID 1978938
     
    Identification of a family of human F-box proteins.
    Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M.
    Curr Biol 1999; 9: 1177-1179.
    PMID 10531035
     
    Frequent allelic loss on chromosomes 4q and 16q associated with human hepatocellular carcinoma in Taiwan.
    Chou YH, Chung KC, Jeng LB, Chen TC, Liaw YF.
    Cancer Lett 1998; 123: 1-6.
    PMID 9461010
     
    Hypoxia inducible factor-alpha binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein.
    Cockman ME, Masson N, Mole DR, Jaakkola P, Chang GW, Clifford SC, Maher ER, Pugh CW, Ratcliffe PJ, Maxwell PH.
    J Biol Chem 2000; 275: 25733-25741.
    PMID 10823831
     
    Regulation of the G1 to S transition by the ubiquitin pathway.
    DeSalle LM, Pagano M.
    FEBS Lett 2001; 490: 179-189.
    PMID 1978938
     
    Genetic profiling of colorectal cancer liver metastases by combined comparative genomic hybridization and G-banding analysis.
    Diep CB, Parada LA, Teixeira MR, Eknaes M, Nesland JM, Johansson B, Lothe RA.
    Genes Chromosomes Cancer 2003; 36: 189-197.
    PMID 12508247
     
    Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN).
    Friesen WJ, Dreyfuss G.
    J Biol Chem 2000; 275: 26370 26375.
    PMID 10851237
     
    Allelic imbalance mapping of chromosome 16 shows two regions of common deletion in prostate adenocarcinoma.
    Godfrey TE, Cher ML, Chhabra V, Jensen RH.
    Cancer Genet Cytogenet 1997; 98: 36-42.
    PMID 9309116
     
    Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy.
    Gomes MD, Lecker SH, Jagoe RT, Navon A, Goldberg AL.
    Proc Natl Acad Sci U S A 2001; 98: 14440-14445.
    PMID 11717410
     
    Allelic imbalance on 16q in small, unifocal hepatocellular carcinoma: correlation with HBV and HCV infections and cellular proliferation rate.
    Gramantieri L, Trere D, Pession A, Piscaglia F, Masi L, Gaiani S, Mazziotti A, Bolondi L.
    Dig Dis Sci 2000; 45: 306-311.
    PMID 10711443
     
    Pathways of ubiquitin conjugation.
    Haas AL, Siepmann TJ.
    FASEB J 1997;11:1257-1268.
    PMID 9409544
     
    Allelic imbalance in selected chromosomal regions in ovarian cancer.
    Hansen LL, Jensen LL, Dimitrakakis C, Michalas S, Gilbert F, Barber HR, Overgaard J, Arzimanoglou II.
    Cancer Genet Cytogenet 2002; 139: 1-8.
     
    Loss of heterozygosity in chromosomal region 16q24.3 associated with progression of prostate cancer.
    Harkonen P, Kyllonen AP, Nordling S, Vihko P.
    Prostate 2005; 62: 267-274.
    PMID 15389780
     
    The ubiquitin system.
    Hershko A, Ciechanover A.
    Annu Rev Biochem 1998; 67: 425-479.
    PMID 9759494
     
    Ubiquitin-dependent protein degradation.
    Hochstrasser M.
    Annu Rev Genet 1996;30:405-439.
    PMID 8982460
     
    Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region.
    Hsu JM, Lee YC, Yu CT, Huang CY.
    J Biol Chem 2004; 279: 32592-32602.
    PMID 15145941
     
    Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex.
    Iwai K, Yamanaka K, Kamura T, Minato N, Conaway RC, Conaway JW, Klausner RD, Pause A.
    Proc Natl Acad Sci U S A 1999; 96: 12436-12441.
    PMID 10535940
     
    Functional identification of a BAC clone from 16q24 carrying a senescence gene SEN16 for breast cancer cells.
    Kaur GP, Reddy DE, Zimonjic DB, de Riel JK, Athwal RS.
    Oncogene 2005; 24: 47-54.
    PMID 15558027
     
    The novel human DNA helicase hFBH1 is an F-box protein.
    Kim J, Kim JH, Lee SH, Kim DH, Kang HY, Bae SH, Pan ZQ, Seo YS.
    J Biol Chem 2002;277:24530-24537.
    PMID 11956208
     
    The F-box protein family.
    Kipreos ET, Pagano M.
    Genome Biol 2000; 1: 3002.
    PMID 11178263
     
    Loss of heterozygosity at chromosome 16q in prostate adenocarcinoma: identification of three independent regions.
    Latil A, Cussenot O, Fournier G, Driouch K, Lidereau R.
    Cancer Res 1997; 57: 1058-1062.
    PMID 9067271
     
    Loss of heterozygosity at chromosomes 3, 6, 8, 11, 16, and 17 in ovarian cancer: correlation to clinicopathological variables.
    Launonen V, Mannermaa A, Stenback F, Kosma VM, Puistola U, Huusko P, Anttila M, Bloigu R, Saarikoski S, Kauppila A, Winqvist R.
    Cancer Genet Cytogenet 2000; 122: 49-54.
    PMID 11104033
     
    Evidence of chromosome regions and gene involvement in inflammatory breast cancer.
    Lerebours F, Bertheau P, Bieche I, Driouch K, De The H, Hacene K, Espie M, Marty M, Lidereau R.
    Int J Cancer 2002; 102: 618-622.
    PMID 12448004
     
    Defective ubiquitination of cerebral proteins in Alzheimer's disease.
    Lopez Salon M, Morelli L, Castano EM, Soto EF, Pasquini JM.
    J Neurosci Res 2000; 62: 302-310.
    PMID 11020223
     
    Clinical significance of chromosome 8p, 10q, and 16q deletions in prostate cancer.
    Matsuyama H, Pan Y, Yoshihiro S, Kudren D, Naito K, Bergerheim US, Ekman P.
    Prostate 2003; 54: 103-111.
    PMID 12497583
     
    A third Wilms' tumor locus on chromosome 16q.
    Maw MA, Grundy PE, Millow LJ, Eccles MR, Dunn RS, Smith PJ, Feinberg AP, Law DJ, Paterson MC, Telzerow PE, et al.
    Cancer Res 1992; 52: 3094-3098.
    PMID 1317258
     
    Chromosome band 16q24 is frequently deleted in human gastric cancer.
    Mori Y, Matsunaga M, Abe T, Fukushige S, Miura K, Sunamura M, Shiiba K, Sato M, Nukiwa T, Horii A.
    Br J Cancer 1999; 80: 556-562.
    PMID 10408866
     
    Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein.
    Ohh M, Park CW, Ivan M, Hoffman MA, Kim TY, Huang LE, Pavletich N, Chau V, Kaelin WG.
    Nat Cell Biol 2000; 2: 423-427.
    PMID 10878807
     
    SCF and APC: the Yin and Yang of cell cycle regulated proteolysis.
    Peters JM.
    Curr Opin Cell Biol 1998; 10: 759-768.
    PMID 9914180
     
    Sequencing, transcript identification, and quantitative gene expression profiling in the breast cancer loss of heterozygosity region 16q24.3 reveal three potential tumor-suppressor genes.
    Powell JA, Gardner AE, Bais AJ, Hinze SJ, Baker E, Whitmore S, Crawford J, Kochetkova M, Spendlove HE, Doggett NA, Sutherland GR, Callen DF, Kremmidiotis G.
    Genomics 2002; 80: 303-310.
    PMID 12213200
     
    Identification of a YAC from 16q24 carrying a senescence gene for breast cancer cells.
    Reddy DE, Keck CL, Popescu N, Athwal RS, Kaur GP.
    Oncogene 2000; 19: 217-222.
    PMID 10644999
     
    Identification of a gene at 16q24.3 that restores cellular senescence in immortal mammary tumor cells.
    Reddy DE, Sandhu AK, DeRiel JK, Athwal RS, Kaur GP.
    Oncogene 1999; 18: 5100-5117.
    PMID 10490846
     
    Ratchets and clocks: the cell cycle, ubiquitylation and protein turnover.
    Reed SI.
    Nat Rev Mol Cell Biol 2003; 4: 855-864.
    PMID 14625536
     
    Fine mapping of Wilms' tumors with 16q loss of heterozygosity localizes the putative tumor suppressor gene to a region of 6.7 megabases.
    Safford SD, Goyeau D, Freemerman AJ, Bentley R, Everett ML, Grundy PE, Skinner MA.
    Ann Surg Oncol 2003; 10: 136-143.
    PMID 12620908
     
    Loss of heterozygosity on chromosome 16 in hepatocellular carcinoma.
    Sakai K, Nagahara H, Abe K, Obata H.
    J Gastroenterol Hepatol 1992; 7: 288-292.
    PMID 1351753
     
    Identification of a 910-kb region of common allelic loss in chromosome bands 16q24.1-q24.2 in human lung cancer.
    Sato M, Mori Y, Sakurada A, Fukushige S, Ishikawa Y, Tsuchiya E, Saito Y, Nukiwa T, Fujimura S, Horii A.
    Genes Chromosomes Cancer 1998; 22: 1-8.
    PMID 9591628
     
    Accumulation of genetic alterations and progression of primary breast cancer.
    Sato T, Akiyama F, Sakamoto G, Kasumi F, Nakamura Y.
    Cancer Res 1991; 51: 5794-5799.
    PMID 1682035
     
    HIF-1: using two hands to flip the angiogenic switch.
    Semenza GL.
    Cancer Metastasis Rev 2000; 19: 59-65.
    PMID 11191064
     
    Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase.
    Shimura H, Hattori N, Kubo S, Mizuno Y, Asakawa S, Minoshima S, Shimizu N, Iwai K, Chiba T, Tanaka K, Suzuki T.
    Nat Genet 2000; 25: 302-305.
    PMID 10888878
     
    Oncogenic role of the ubiquitin ligase subunit Skp2 in human breast cancer.
    Signoretti S, Di Marcotullio L, Richardson A, Ramaswamy S, Isaac B, Rue M, Monti F, Loda M, Pagano M.
    J Clin Invest 2002; 110: 633-641.
    PMID 12208864
     
    The ubiquitin-proteasome pathway in cancer.
    Spataro V, Norbury C, Harris AL.
    Br J Cancer 1998; 77: 448-455.
    PMID 9472642
     
    Three distinct commonly deleted regions of chromosome arm 16q in human primary and metastatic prostate cancers.
    Suzuki H, Komiya A, Emi M, Kuramochi H, Shiraishi T, Yatani R, Shimazaki J.
    Genes Chromosomes Cancer 1996; 17: 225-233.
    PMID 8946204
     
    Loss of heterozygosity on 6q, 16q, and 17p in human central nervous system primitive neuroectodermal tumors.
    Thomas GA, Raffel C.
    Cancer Res 1991; 51: 639-643.
    PMID 1670763
     
    Allele loss on chromosome 16 associated with progression of human hepatocellular carcinoma.
    Tsuda H, Zhang WD, Shimosato Y, Yokota J, Terada M, Sugimura T, Miyamura T, Hirohashi S.
    Proc Natl Acad Sci U S A 1990; 87: 6791-6794.
    PMID 2168560
     
    Allelotype of pediatric rhabdomyosarcoma.
    Visser M, Sijmons C, Bras J, Arceci RJ, Godfried M, Valentijn LJ, Voute PA, Baas F.
    Oncogene 1997; 15: 1309-1314.
    PMID 9315099
     
    Cervical metastases of head and neck squamous cell carcinoma correlate with loss of heterozygosity on chromosome 16q.
    Wang X, Gleich L, Pavelic ZP, Li YQ, Gale N, Hunt S, Gluckman JL, Stambrook PJ.
    Int J Oncol 1999; 14: 557-561.
    PMID 10024691
     
    Loss of heterozygosity and its correlation with expression profiles in subclasses of invasive breast cancers.
    Wang ZC, Lin M, Wei LJ, Li C, Miron A, Lodeiro G, Harris L, Ramaswamy S, Tanenbaum DM, Meyerson M, Iglehart JD, Richardson A.
    Cancer Res 2004; 64: 64-71.
    PMID 14729609
     
    A family of mammalian F-box proteins.
    Winston JT, Koepp DM, Zhu C, Elledge SJ, Harper JW.
    Curr Biol 1999; 9: 1180-1182.
    PMID 10531037
     
    Identification of homozygous deletions at chromosome 16q23 in aflatoxin B1 exposed hepatocellular carcinoma.
    Yakicier MC, Legoix P, Vaury C, Gressin L, Tubacher E, Capron F, Bayer J, Degott C, Balabaud C, Zucman-Rossi J.
    Oncogene 2001; 20: 5232-5238.
    PMID 11526514
     
    Novel chromosomal alterations detected in primary nasopharyngeal carcinoma by comparative genomic hybridization.
    Yan J, Fang Y, Liang Q, Huang Y, Zeng Y.
    Chin Med J 2001; 114: 418-421.
    PMID 11780468
     
    Loss of heterozygosity in ductal lavage for breast tumor and the contralateral breast.
    Yonekura Y, Yamamoto D, Okugawa H, Tanaka K, Kamiyama Y.
    Oncol Rep 2005; 13: 739-743.
    PMID 15756451
     
    E3 ubiquitin ligase that recognizes sugar chains.
    Yoshida Y, Chiba T, Tokunaga F, Kawasaki H, Iwai K, Suzuki T, Ito Y, Matsuoka K, Yoshida M, Tanaka K, Tai T.
    Nature 2002; 418: 438-442.
    PMID 12140560
     
    Frequent loss of heterozygosity on chromosomes 16 and 4 in human hepatocellular carcinoma.
    Zhang WD, Hirohashi S, Tsuda H, Shimosato Y, Yokota J, Terada M, Sugimura T.
    Jpn J Cancer Res 1990; 81: 108-111.
    PMID 1970554
     
    Comparative genomic hybridization detects losses of chromosomes 22 and 16 as the most common recurrent genetic alterations in primary ependymomas.
    Zheng PP, Pang JC, Hui AB, Ng HK.
    Cancer Genet Cytogenet 2000; 122: 18-25.
    PMID 11104027
     
    Timing of APC/C substrate degradation is determined by fzy/fzr specificity of destruction boxes.
    Zur A, Brandeis M.
    EMBO J 2002; 21: 4500-4510.
    PMID 12198152
     
    The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination.
    den Engelsman J, Keijsers V, de Jong WW, Boelens WC.
    J Biol Chem 2003; 278: 4699-4704.
    PMID 12468532
     
    Gene expression profiling predicts clinical outcome of breast cancer.
    van't Veer LJ, Dai H, van de Vijver MJ, He YD, Hart AA, Mao M, Peterse HL, van der Kooy K, Marton MJ, Witteveen AT, et al.
    Nature 2002; 415: 530-536.
    PMID 11823860
     

    Citation

    This paper should be referenced as such :
    Bais, AJ
    FBXO31 (F-box protein 31)
    Atlas Genet Cytogenet Oncol Haematol. 2009;13(5):338-342.
    Free journal version : [ pdf ]   [ DOI ]

    External links

     

    Nomenclature
    HGNC (Hugo)FBXO31   16510
    Cards
    AtlasFBXO31ID44280ch16q24
    Entrez_Gene (NCBI)FBXO31    F-box protein 31
    AliasesFBX14; FBXO14; Fbx31; MRT45; 
    pp2386
    GeneCards (Weizmann)FBXO31
    Ensembl hg19 (Hinxton)ENSG00000103264 [Gene_View]
    Ensembl hg38 (Hinxton)ENSG00000103264 [Gene_View]  ENSG00000103264 [Sequence]  chr16:87326987-87383776 [Contig_View]  FBXO31 [Vega]
    ICGC DataPortalENSG00000103264
    TCGA cBioPortalFBXO31
    AceView (NCBI)FBXO31
    Genatlas (Paris)FBXO31
    SOURCE (Princeton)FBXO31
    Genetics Home Reference (NIH)FBXO31
    Genomic and cartography
    GoldenPath hg38 (UCSC)FBXO31  -     chr16:87326987-87383776 -  16q24.2   [Description]    (hg38-Dec_2013)
    GoldenPath hg19 (UCSC)FBXO31  -     16q24.2   [Description]    (hg19-Feb_2009)
    GoldenPathFBXO31 - 16q24.2 [CytoView hg19]  FBXO31 - 16q24.2 [CytoView hg38]
    ImmunoBaseENSG00000103264
    Genome Data Viewer NCBIFBXO31 [Mapview hg19]  
    OMIM609102   615979   
    Gene and transcription
    Genbank (Entrez)AF318348 AF428140 AK311122 AL117444 AL576585
    RefSeq transcript (Entrez)NM_001282683 NM_024735
    Consensus coding sequences : CCDS (NCBI)FBXO31
    Gene ExpressionFBXO31 [ NCBI-GEO ]   FBXO31 [ EBI - ARRAY_EXPRESS ]   FBXO31 [ SEEK ]   FBXO31 [ MEM ]
    Gene Expression Viewer (FireBrowse)FBXO31 [ Firebrowse - Broad ]
    GenevisibleExpression of FBXO31 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
    BioGPS (Tissue expression)79791
    GTEX Portal (Tissue expression)FBXO31
    Human Protein AtlasENSG00000103264-FBXO31 [pathology]   [cell]   [tissue]
    Protein : pattern, domain, 3D structure
    UniProt/SwissProtQ5XUX0   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
    NextProtQ5XUX0  [Sequence]  [Exons]  [Medical]  [Publications]
    With graphics : InterProQ5XUX0
    PhosPhoSitePlusQ5XUX0
    Domaine pattern : Prosite (Expaxy)FBOX (PS50181)   
    Domains : Interpro (EBI)F-box-like_dom_sf    F-box_dom    FBXO31   
    Domain families : Pfam (Sanger)F-box-like (PF12937)   
    Domain families : Pfam (NCBI)pfam12937   
    Domain families : Smart (EMBL)FBOX (SM00256)  
    Conserved Domain (NCBI)FBXO31
    PDB (RSDB)5VZT    5VZU   
    PDB Europe5VZT    5VZU   
    PDB (PDBSum)5VZT    5VZU   
    PDB (IMB)5VZT    5VZU   
    Structural Biology KnowledgeBase5VZT    5VZU   
    SCOP (Structural Classification of Proteins)5VZT    5VZU   
    CATH (Classification of proteins structures)5VZT    5VZU   
    SuperfamilyQ5XUX0
    AlphaFold pdb e-kbQ5XUX0   
    Human Protein Atlas [tissue]ENSG00000103264-FBXO31 [tissue]
    HPRD10954
    Protein Interaction databases
    DIP (DOE-UCLA)Q5XUX0
    IntAct (EBI)Q5XUX0
    BioGRIDFBXO31
    STRING (EMBL)FBXO31
    ZODIACFBXO31
    Ontologies - Pathways
    QuickGOQ5XUX0
    Ontology : AmiGOprotein polyubiquitination  protein binding  centrosome  cytosol  cellular response to DNA damage stimulus  SCF ubiquitin ligase complex  SCF ubiquitin ligase complex  cyclin binding  anaphase-promoting complex-dependent catabolic process  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  mitotic G1 DNA damage checkpoint signaling  neuronal cell body  post-translational protein modification  positive regulation of dendrite morphogenesis  positive regulation of neuron migration  
    Ontology : EGO-EBIprotein polyubiquitination  protein binding  centrosome  cytosol  cellular response to DNA damage stimulus  SCF ubiquitin ligase complex  SCF ubiquitin ligase complex  cyclin binding  anaphase-promoting complex-dependent catabolic process  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  mitotic G1 DNA damage checkpoint signaling  neuronal cell body  post-translational protein modification  positive regulation of dendrite morphogenesis  positive regulation of neuron migration  
    REACTOMEQ5XUX0 [protein]
    REACTOME PathwaysR-HSA-983168 [pathway]   
    NDEx NetworkFBXO31
    Atlas of Cancer Signalling NetworkFBXO31
    Wikipedia pathwaysFBXO31
    Orthology - Evolution
    OrthoDB79791
    GeneTree (enSembl)ENSG00000103264
    Phylogenetic Trees/Animal Genes : TreeFamFBXO31
    Homologs : HomoloGeneFBXO31
    Homology/Alignments : Family Browser (UCSC)FBXO31
    Gene fusions - Rearrangements
    Fusion : MitelmanDEF8::FBXO31 [16q24.3/16q24.2]  
    Fusion : QuiverFBXO31
    Polymorphisms : SNP and Copy number variants
    NCBI Variation ViewerFBXO31 [hg38]
    dbSNP Single Nucleotide Polymorphism (NCBI)FBXO31
    dbVarFBXO31
    ClinVarFBXO31
    MonarchFBXO31
    1000_GenomesFBXO31 
    Exome Variant ServerFBXO31
    GNOMAD BrowserENSG00000103264
    Varsome BrowserFBXO31
    ACMGFBXO31 variants
    VarityQ5XUX0
    Genomic Variants (DGV)FBXO31 [DGVbeta]
    DECIPHERFBXO31 [patients]   [syndromes]   [variants]   [genes]  
    CONAN: Copy Number AnalysisFBXO31 
    Mutations
    ICGC Data PortalFBXO31 
    TCGA Data PortalFBXO31 
    Broad Tumor PortalFBXO31
    OASIS PortalFBXO31 [ Somatic mutations - Copy number]
    Somatic Mutations in Cancer : COSMICFBXO31  [overview]  [genome browser]  [tissue]  [distribution]  
    Somatic Mutations in Cancer : COSMIC3DFBXO31
    Mutations and Diseases : HGMDFBXO31
    LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
    BioMutaFBXO31
    DgiDB (Drug Gene Interaction Database)FBXO31
    DoCM (Curated mutations)FBXO31
    CIViC (Clinical Interpretations of Variants in Cancer)FBXO31
    OncoKBFBXO31
    NCG (London)FBXO31
    Cancer3DFBXO31
    Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
    Diseases
    OMIM609102    615979   
    Orphanet11804   
    DisGeNETFBXO31
    MedgenFBXO31
    Genetic Testing Registry FBXO31
    NextProtQ5XUX0 [Medical]
    GENETestsFBXO31
    Target ValidationFBXO31
    Huge Navigator FBXO31 [HugePedia]
    ClinGenFBXO31
    Clinical trials, drugs, therapy
    MyCancerGenomeFBXO31
    Protein Interactions : CTDFBXO31
    Pharm GKB GenePA28042
    PharosQ5XUX0
    Clinical trialFBXO31
    Miscellaneous
    canSAR (ICR)FBXO31
    HarmonizomeFBXO31
    DataMed IndexFBXO31
    Probes
    Litterature
    PubMed45 Pubmed reference(s) in Entrez
    GeneRIFsGene References Into Functions (Entrez)
    EVEXFBXO31
    REVIEW articlesautomatic search in PubMed
    Last year publicationsautomatic search in PubMed

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