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WWC1 (WW and C2 domain containing 1)

Written2013-08Lin Zhang, Jixin Dong
Eppley Institute for Research in Cancer, Allied Diseases, University of Nebraska Medical Center, 985950 Nebraska Medical Center, Omaha, NE 68198-5950, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesregulatory subunit 168
Alias_symbol (synonym)KIBRA
KIAA0869
PPP1R168
Other aliasHBEBP3
HBEBP36
HGNC (Hugo) WWC1
LocusID (NCBI) 23286
Atlas_Id 45810
Location 5q34  [Link to chromosome band 5q34]
Location_base_pair Starts at 168292060 and ends at 168472303 bp from pter ( according to hg19-Feb_2009)  [Mapping WWC1.png]
Fusion genes
(updated 2016)
WWC1 (5q34) / ADRBK2 (22q12.1)WWC1 (5q34) / SNTG2 (2p25.3)WWC1 (5q34) / TENM2 (5q34)
WWC1 (5q34) / TRAF3IP3 (1q32.2)

DNA/RNA

 
  Diagram of WWC1 DNA which contains 23 exons shown with blue boxes.
Description The gene of WWC1 locates on chromosome 5q34, with 23 exons crossing 180244bp (including un-translated regions) on the plus strand. In total 137 single nucleotide polymorphisms are present in ≥ 1% of samples according to UCSC database.
Transcription The open reading frame of mRNA contains 3360bp. Three transcript variants encoding different isoforms have been found for this gene (provided by RefSeq, Mar 2010).
Pseudogene No pseudogene of WWC1 is known.

Protein

Note Preferred names: protein KIBRA
Names:
- protein KIBRA
- protein WWC1
- HBeAg-binding protein 3
- kidney and brain protein
- WW, C2 and coiled-coil domain containing 1
 
  Structure of human KIBRA. KIBRA contains two WW domains, a C2 domain, a glutamic acid-rich domain and a PDZ binding motif.
Description KIBRA protein consists of 1119 amino acids (isoform 1), with a predicted molecular weight of 125kDa. It was first cloned and identified as a protein that interacts with the postsynaptic protein dendrin (Kremerskothen et al., 2003). KIBRA is constituted by two N-terminal WW domains, a C2 domain, a glutamic acid-rich domain and a PDZ binding motif. The WW domains which contain two conserved tryptophan residues are responsible for recognizing PPxY motifs in various proteins containing proline-rich sequences (PPxY). The C2 domain located between amino acids 655 and 783 is implied to be involved in binding phospholipids under assistance of two or three calcium ions. In addition to the WW and C2 domain, a glutamic acid-rich region can be found between amino acids 845 and 873 (Kremerskothen et al., 2003; Rayala et al., 2006) and a PDZ-binding motif is located between amino acids 1110 and 1113 at the C terminus (isoform 2) (Duning et al., 2008). Further, a conserved motif containing serine residue (Ser539) between the WW and C2 domains of KIBRA, is phosphorylated and regulated by aurora kinase and protein phosphatase 1 (Xiao et al., 2011b). Recently, KIBRA Ser542 and Ser931 have been identified as main phosphorylation sites for CDK1 (Ji et al., 2012).
Expression KIBRA is predominately expressed in human kidney and brain (Kremerskothen et al., 2003). Gene expression studies and immunohistological staining have shown that KIBRA is mainly expressed in memory-related regions of the brain, such as hippocampus and cortex (Papassotiropoulos et al., 2006; Johannsen et al., 2008). In kidney, KIBRA is expressed in glomerular podocytes, tubules and some collecting ducts (Duning et al., 2008). KIBRA can also be detected in heart and colon.
Localisation The localization of endogenously expressed KIBRA depends on the cell type. KIBRA localizes in the apical domain and at cell junctions in epithelial cells (Yoshihama et al., 2011). In brain, KIBRA co-localizes with protein kinase Mzeta (PKMzeta) in the mouse hippocampus (Yoshihama et al., 2009). In mouse kidney, KIBRA localizes in the distal tubular epithelial cells (Yoshihama et al., 2011). In migrating cells, KIBRA accumulates in the leading edge (Duning et al., 2008).
Function KIBRA is a cytoplasmatic protein that is involved in various cellular processes and regulates a variety of cellular functions such as cell growth and apoptosis, directional cell migration, mitotic spindle assembly and mitogen-activated protein kinase (MAPK) activation.
In the field of neuroscience, KIBRA is associated with human memory performance (Papassotiropoulos et al., 2006). The single nucleotide polymorphism (SNP) of the ninth intron of KIBRA gene, rs17070145, is associated with human episodic memory performance. Carriers of the T to C single nucleotide in the ninth intron have better performance on episodic memory tasks (Papassotiropoulos et al., 2006). After that, several other groups also reported the association of KIBRA with human memory performance in different subject populations (Almeida et al., 2008; Bates et al., 2009; Schaper et al., 2008). KIBRA gene is also associated with Alzheimer's disease and recurrent depressive disorders (Corneveaux et al., 2010; Galecki et al., 2010). Besides, KIBRA interacts with PKCzeta, which is involved in synaptic plasticity (Büther et al.,2004).
Three recent studies independently identified KIBRA in Drosophila as a tumor suppressor that regulates Hippo signaling pathway, which controls tissue growth and organ size (Baumgartner et al., 2010; Genevet et al., 2010; Yu et al., 2010). This function of KIBRA seems to be conserved in mammals. Loss of KIBRA expression in immortalized breast epithelial cells exhibits epithelial-to-mesenchymal transition (EMT) features and reduced expression of KIBRA in breast cancer specimens correlates with poor prognosis (Moleirinho et al., 2013). However, a recent study reported that overexpression of KIBRA in gastric cancer correlates with lymphatic invasion and poor prognosis (Yoshihama et al., 2013). In podocytes, KIBRA interacts with PATJ and synaptopodin and positively modulates directional cell migration (Duning et al., 2008). Methylation status of KIBRA is correlated with prognosis of chronic lymphocytic leukemia and specific genetic event in B-cell acute lymphocytic leukemia (Shinawi et al., 2012; Hill et al., 2011). KIBRA also plays an important role in mitosis. KIBRA interacts with and regulates mitotic kinase aurora and is required for precise mitotic spindle assembly and chromosome alignment (Xiao et al., 2011b; Zhang et al., 2012). Additionally, KIBRA is also regulated by cyclin-dependent kinase 1 (CDK1) and cell division cycle 14A/B phosphatases (CDC14A, CDC14B) and thus regulates cell-cycle progression (Ji et al., 2012).
 
Homology The KIBRA gene is conserved in chimpanzee, Rhesus monkey, dog, cow, mouse, rat, chicken, zebrafish, fruit fly, and mosquito (Provided by Pubmed). Two parologs of KIBRA have been discovered in human: WWC2 and WWC3. One ortholog of KIBRA (Kibra) has been identified in Drosophila. KIBRA and WWC3 exist in fish, and KIBRA and WWC2 are present in mice.

Mutations

Note No mutations of WWC1 are known.

Implicated in

Note
  
Entity Memory performance
Note The single nucleotide polymorphism (SNP) of the ninth intron of KIBRA gene, rs17070145, is associated with human episodic memory performance (Papassotiropoulos et al., 2006). A recent study using KIBRA-knockout mice showed that KIBRA is necessary for the contextual and trace fear memory in adult mice (Makuch et al., 2011). KIBRA is also associated with Alzheimer's disease and recurrent depressive disorders (Corneveaux et al., 2008; Galecki et al., 2010).
  
  
Entity Various cancers
Note Genetic studies have identified Kibra as a tumor suppressor in Drosophila. Kibra functions together with Merlin and Expanded to regulate Hippo signaling pathway, which controls tissue growth and organ size (Baumgartner et al., 2010; Genevet et al., 2010; Yu et al., 2010). This function of KIBRA is also conserved in mammals. Methylation status of KIBRA is correlated with prognosis of chronic lymphocytic leukemia and specific genetic event in B-cell acute lymphocytic leukemia (Shinawi et al., 2012; Hill et al., 2011).
  
  
Entity Cell cycle
Note KIBRA is regulated by cyclin-dependent kinase 1 (CDK1) and cell division cycle 14A/B phosphatases (CDC14) and thus regulates cell-cycle progression (Ji et al., 2012). Besides, KIBRA interacts and regulates mitotic kinase aurora during mitosis and is required for precise mitotic spindle assembly and chromosome alignment (Xiao et al., 2011; Zhang et al., 2012).
  
  
Entity Epithelial-mesenchymal transition
Note Loss of KIBRA expression induces features of epithelial-to-mesenchymal transition (EMT) in mammary epithelial cells. Decreased expression of KIBRA in breast cancer specimens correlates with poor prognosis (Moleirinho et al., 2013).
  

Bibliography

KIBRA genetic polymorphism influences episodic memory in later life, but does not increase the risk of mild cognitive impairment.
Almeida OP, Schwab SG, Lautenschlager NT, Morar B, Greenop KR, Flicker L, Wildenauer D.
J Cell Mol Med. 2008 Sep-Oct;12(5A):1672-6. doi: 10.1111/j.1582-4934.2008.00229.x. Epub 2008 Jan 11.
PMID 18194457
 
Association of KIBRA and memory.
Bates TC, Price JF, Harris SE, Marioni RE, Fowkes FG, Stewart MC, Murray GD, Whalley LJ, Starr JM, Deary IJ.
Neurosci Lett. 2009 Jul 24;458(3):140-3. doi: 10.1016/j.neulet.2009.04.050. Epub 2009 May 3.
PMID 19397951
 
The WW domain protein Kibra acts upstream of Hippo in Drosophila.
Baumgartner R, Poernbacher I, Buser N, Hafen E, Stocker H.
Dev Cell. 2010 Feb 16;18(2):309-16. doi: 10.1016/j.devcel.2009.12.013.
PMID 20159600
 
KIBRA is a novel substrate for protein kinase Czeta.
Buther K, Plaas C, Barnekow A, Kremerskothen J.
Biochem Biophys Res Commun. 2004 May 7;317(3):703-7.
PMID 15081397
 
Evidence for an association between KIBRA and late-onset Alzheimer's disease.
Corneveaux JJ, Liang WS, Reiman EM, Webster JA, Myers AJ, Zismann VL, Joshipura KD, Pearson JV, Hu-Lince D, Craig DW, Coon KD, Dunckley T, Bandy D, Lee W, Chen K, Beach TG, Mastroeni D, Grover A, Ravid R, Sando SB, Aasly JO, Heun R, Jessen F, Kolsch H, Rogers J, Hutton ML, Melquist S, Petersen RC, Alexander GE, Caselli RJ, Papassotiropoulos A, Stephan DA, Huentelman MJ.
Neurobiol Aging. 2010 Jun;31(6):901-9. doi: 10.1016/j.neurobiolaging.2008.07.014. Epub 2008 Sep 13.
PMID 18789830
 
KIBRA modulates directional migration of podocytes.
Duning K, Schurek EM, Schluter M, Bayer M, Reinhardt HC, Schwab A, Schaefer L, Benzing T, Schermer B, Saleem MA, Huber TB, Bachmann S, Kremerskothen J, Weide T, Pavenstadt H.
J Am Soc Nephrol. 2008 Oct;19(10):1891-903. doi: 10.1681/ASN.2007080916. Epub 2008 Jul 2.
PMID 18596123
 
Single nucleotide polymorphism of the KIBRA gene in recurrent depressive disorders.
Galecki P, Szemraj J, Florkowski A, Talarowska M, Bienkiewicz M, Galecka E, Lewinski A.
Neuro Endocrinol Lett. 2010;31(1):97-102.
PMID 20150879
 
Kibra is a regulator of the Salvador/Warts/Hippo signaling network.
Genevet A, Wehr MC, Brain R, Thompson BJ, Tapon N.
Dev Cell. 2010 Feb 16;18(2):300-8. doi: 10.1016/j.devcel.2009.12.011.
PMID 20159599
 
Frequent epigenetic inactivation of KIBRA, an upstream member of the Salvador/Warts/Hippo (SWH) tumor suppressor network, is associated with specific genetic event in B-cell acute lymphocytic leukemia.
Hill VK, Dunwell TL, Catchpoole D, Krex D, Brini AT, Griffiths M, Craddock C, Maher ER, Latif F.
Epigenetics. 2011 Mar;6(3):326-32. Epub 2011 Mar 1.
PMID 21173572
 
Phospho-regulation of KIBRA by CDK1 and CDC14 phosphatase controls cell-cycle progression.
Ji M, Yang S, Chen Y, Xiao L, Zhang L, Dong J.
Biochem J. 2012 Oct 1;447(1):93-102. doi: 10.1042/BJ20120751.
PMID 22784093
 
Temporal-spatial expression and novel biochemical properties of the memory-related protein KIBRA.
Johannsen S, Duning K, Pavenstadt H, Kremerskothen J, Boeckers TM.
Neuroscience. 2008 Sep 9;155(4):1165-73. doi: 10.1016/j.neuroscience.2008.06.054. Epub 2008 Jul 3.
PMID 18672031
 
Characterization of KIBRA, a novel WW domain-containing protein.
Kremerskothen J, Plaas C, Buther K, Finger I, Veltel S, Matanis T, Liedtke T, Barnekow A.
Biochem Biophys Res Commun. 2003 Jan 24;300(4):862-7.
PMID 12559952
 
Regulation of AMPA receptor function by the human memory-associated gene KIBRA.
Makuch L, Volk L, Anggono V, Johnson RC, Yu Y, Duning K, Kremerskothen J, Xia J, Takamiya K, Huganir RL.
Neuron. 2011 Sep 22;71(6):1022-9. doi: 10.1016/j.neuron.2011.08.017. Epub 2011 Sep 21.
PMID 21943600
 
KIBRA exhibits MST-independent functional regulation of the Hippo signaling pathway in mammals.
Moleirinho S, Chang N, Sims AH, Tilston-Lunel AM, Angus L, Steele A, Boswell V, Barnett SC, Ormandy C, Faratian D, Gunn-Moore FJ, Reynolds PA.
Oncogene. 2013 Apr 4;32(14):1821-30. doi: 10.1038/onc.2012.196. Epub 2012 May 21.
PMID 22614006
 
Common Kibra alleles are associated with human memory performance.
Papassotiropoulos A, Stephan DA, Huentelman MJ, Hoerndli FJ, Craig DW, Pearson JV, Huynh KD, Brunner F, Corneveaux J, Osborne D, Wollmer MA, Aerni A, Coluccia D, Hanggi J, Mondadori CR, Buchmann A, Reiman EM, Caselli RJ, Henke K, de Quervain DJ.
Science. 2006 Oct 20;314(5798):475-8.
PMID 17053149
 
Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells.
Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R.
J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9.
PMID 16684779
 
KIBRA gene variants are associated with episodic memory in healthy elderly.
Schaper K, Kolsch H, Popp J, Wagner M, Jessen F.
Neurobiol Aging. 2008 Jul;29(7):1123-5. Epub 2007 Mar 13.
PMID 17353070
 
KIBRA gene methylation is associated with unfavorable biological prognostic parameters in chronic lymphocytic leukemia.
Shinawi T, Hill V, Dagklis A, Baliakas P, Stamatopoulos K, Agathanggelou A, Stankovic T, Maher ER, Ghia P, Latif F.
Epigenetics. 2012 Mar;7(3):211-5. doi: 10.4161/epi.7.3.19222.
PMID 22430796
 
KIBRA protein phosphorylation is regulated by mitotic kinase aurora and protein phosphatase 1.
Xiao L, Chen Y, Ji M, Volle DJ, Lewis RE, Tsai MY, Dong J.
J Biol Chem. 2011b Oct 21;286(42):36304-15. doi: 10.1074/jbc.M111.246850. Epub 2011 Aug 30.
PMID 21878642
 
High expression of KIBRA in low atypical protein kinase C-expressing gastric cancer correlates with lymphatic invasion and poor prognosis.
Yoshihama Y, Izumisawa Y, Akimoto K, Satoh Y, Mizushima T, Satoh K, Chida K, Takagawa R, Akiyama H, Ichikawa Y, Kunisaki C, Inayama Y, Endo I, Nagashima Y, Ohno S.
Cancer Sci. 2013 Feb;104(2):259-65. doi: 10.1111/cas.12066. Epub 2012 Dec 27.
PMID 23163744
 
Kibra functions as a tumor suppressor protein that regulates Hippo signaling in conjunction with Merlin and Expanded.
Yu J, Zheng Y, Dong J, Klusza S, Deng WM, Pan D.
Dev Cell. 2010 Feb 16;18(2):288-99. doi: 10.1016/j.devcel.2009.12.012.
PMID 20159598
 
KIBRA regulates aurora kinase activity and is required for precise chromosome alignment during mitosis.
Zhang L, Iyer J, Chowdhury A, Ji M, Xiao L, Yang S, Chen Y, Tsai MY, Dong J.
J Biol Chem. 2012 Oct 5;287(41):34069-77. doi: 10.1074/jbc.M112.385518. Epub 2012 Aug 17.
PMID 22904328
 

Citation

This paper should be referenced as such :
Zhang, L ; Dong, J
WWC1 (WW, C2 domain containing 1)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(4):243-246.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/WWC1ID45810ch5q34.html


External links

Nomenclature
HGNC (Hugo)WWC1   29435
Cards
AtlasWWC1ID45810ch5q34
Entrez_Gene (NCBI)WWC1  23286  WW and C2 domain containing 1
AliasesHBEBP3; HBEBP36; KIBRA; MEMRYQTL; 
PPP1R168
GeneCards (Weizmann)WWC1
Ensembl hg19 (Hinxton)ENSG00000113645 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000113645 [Gene_View]  chr5:168292060-168472303 [Contig_View]  WWC1 [Vega]
ICGC DataPortalENSG00000113645
TCGA cBioPortalWWC1
AceView (NCBI)WWC1
Genatlas (Paris)WWC1
WikiGenes23286
SOURCE (Princeton)WWC1
Genetics Home Reference (NIH)WWC1
Genomic and cartography
GoldenPath hg38 (UCSC)WWC1  -     chr5:168292060-168472303 +  5q34   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)WWC1  -     5q34   [Description]    (hg19-Feb_2009)
EnsemblWWC1 - 5q34 [CytoView hg19]  WWC1 - 5q34 [CytoView hg38]
Mapping of homologs : NCBIWWC1 [Mapview hg19]  WWC1 [Mapview hg38]
OMIM610533   615602   
Gene and transcription
Genbank (Entrez)AB020676 AF506799 AF530058 AK001727 AK027022
RefSeq transcript (Entrez)NM_001161661 NM_001161662 NM_015238
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)WWC1
Cluster EST : UnigeneHs.484047 [ NCBI ]
CGAP (NCI)Hs.484047
Alternative Splicing GalleryENSG00000113645
Gene ExpressionWWC1 [ NCBI-GEO ]   WWC1 [ EBI - ARRAY_EXPRESS ]   WWC1 [ SEEK ]   WWC1 [ MEM ]
Gene Expression Viewer (FireBrowse)WWC1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)23286
GTEX Portal (Tissue expression)WWC1
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ8IX03   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ8IX03  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ8IX03
Splice isoforms : SwissVarQ8IX03
PhosPhoSitePlusQ8IX03
Domaine pattern : Prosite (Expaxy)WW_DOMAIN_1 (PS01159)    WW_DOMAIN_2 (PS50020)   
Domains : Interpro (EBI)C2_dom    WW_dom   
Domain families : Pfam (Sanger)C2 (PF00168)    WW (PF00397)   
Domain families : Pfam (NCBI)pfam00168    pfam00397   
Domain families : Smart (EMBL)WW (SM00456)  
Conserved Domain (NCBI)WWC1
DMDM Disease mutations23286
Blocks (Seattle)WWC1
PDB (SRS)2Z0U   
PDB (PDBSum)2Z0U   
PDB (IMB)2Z0U   
PDB (RSDB)2Z0U   
Structural Biology KnowledgeBase2Z0U   
SCOP (Structural Classification of Proteins)2Z0U   
CATH (Classification of proteins structures)2Z0U   
SuperfamilyQ8IX03
Human Protein AtlasENSG00000113645
Peptide AtlasQ8IX03
HPRD10033
IPIIPI00217340   IPI00761080   IPI00383373   IPI00936915   IPI00982520   IPI00979558   
Protein Interaction databases
DIP (DOE-UCLA)Q8IX03
IntAct (EBI)Q8IX03
FunCoupENSG00000113645
BioGRIDWWC1
STRING (EMBL)WWC1
ZODIACWWC1
Ontologies - Pathways
QuickGOQ8IX03
Ontology : AmiGOnegative regulation of transcription from RNA polymerase II promoter  transcription coactivator activity  protein binding  nucleus  cytoplasm  cytosol  cytosol  transcription, DNA-templated  cell migration  kinase binding  establishment of cell polarity  protein binding, bridging  regulation of intracellular transport  ruffle membrane  protein complex scaffold  hippo signaling  regulation of hippo signaling  negative regulation of hippo signaling  protein complex  positive regulation of MAPK cascade  negative regulation of organ growth  perinuclear region of cytoplasm  
Ontology : EGO-EBInegative regulation of transcription from RNA polymerase II promoter  transcription coactivator activity  protein binding  nucleus  cytoplasm  cytosol  cytosol  transcription, DNA-templated  cell migration  kinase binding  establishment of cell polarity  protein binding, bridging  regulation of intracellular transport  ruffle membrane  protein complex scaffold  hippo signaling  regulation of hippo signaling  negative regulation of hippo signaling  protein complex  positive regulation of MAPK cascade  negative regulation of organ growth  perinuclear region of cytoplasm  
Pathways : KEGGHippo signaling pathway   
REACTOMEQ8IX03 [protein]
REACTOME PathwaysR-HSA-2028269 [pathway]   
NDEx NetworkWWC1
Atlas of Cancer Signalling NetworkWWC1
Wikipedia pathwaysWWC1
Orthology - Evolution
OrthoDB23286
GeneTree (enSembl)ENSG00000113645
Phylogenetic Trees/Animal Genes : TreeFamWWC1
HOVERGENQ8IX03
HOGENOMQ8IX03
Homologs : HomoloGeneWWC1
Homology/Alignments : Family Browser (UCSC)WWC1
Gene fusions - Rearrangements
Fusion : MitelmanWWC1/ADRBK2 [5q34/22q12.1]  
Fusion : MitelmanWWC1/SNTG2 [5q34/2p25.3]  [t(2;5)(p25;q34)]  
Fusion: TCGAWWC1 5q34 ODZ2 BRCA OV
Fusion: TCGAWWC1 5q34 SNTG2 2p25.3 PRAD
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerWWC1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)WWC1
dbVarWWC1
ClinVarWWC1
1000_GenomesWWC1 
Exome Variant ServerWWC1
ExAC (Exome Aggregation Consortium)WWC1 (select the gene name)
Genetic variants : HAPMAP23286
Genomic Variants (DGV)WWC1 [DGVbeta]
DECIPHERWWC1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisWWC1 
Mutations
ICGC Data PortalWWC1 
TCGA Data PortalWWC1 
Broad Tumor PortalWWC1
OASIS PortalWWC1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICWWC1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDWWC1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch WWC1
DgiDB (Drug Gene Interaction Database)WWC1
DoCM (Curated mutations)WWC1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)WWC1 (select a term)
intoGenWWC1
NCG5 (London)WWC1
Cancer3DWWC1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM610533    615602   
Orphanet
MedgenWWC1
Genetic Testing Registry WWC1
NextProtQ8IX03 [Medical]
TSGene23286
GENETestsWWC1
Target ValidationWWC1
Huge Navigator WWC1 [HugePedia]
snp3D : Map Gene to Disease23286
BioCentury BCIQWWC1
ClinGenWWC1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD23286
Chemical/Pharm GKB GenePA143485670
Clinical trialWWC1
Miscellaneous
canSAR (ICR)WWC1 (select the gene name)
Probes
Litterature
PubMed86 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineWWC1
EVEXWWC1
GoPubMedWWC1
iHOPWWC1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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