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BYSL (Bystin-Like)

Written2013-09Michiko N Fukuda, Kazuhiro Sugihara
Tumor Microenvironment Program, Cancer Center, Sanford-Burnham Medical Research Institute, La Jolla, CA, USA (MNF); Department of Gynecology, Obstetrics, Hamamatsu University School of Medicine, Hamamatsu City, Shizuoka, Japan (KS)

(Note : for Links provided by Atlas : click)

Identity

Alias_namesbystin-like
Other aliasBYSTIN
HGNC (Hugo) BYSL
LocusID (NCBI) 705
Atlas_Id 857
Location 6p21.1  [Link to chromosome band 6p21]
Location_base_pair Starts at 41921227 and ends at 41933046 bp from pter ( according to hg19-Feb_2009)  [Mapping BYSL.png]
Local_order In human chromosome, BYSL gene localizes in chromosome 6, between TRFP encoding a transcription mediator, and CCND3 encoding cyclin D3 (Figure 1).
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
BYSL (6p21.1) / BYSL (6p21.1)

DNA/RNA

 
  Figure 1. Genomic organization of BYSL.
Description BYSL locates on 6 chromosome 6p21.1 (Pack et al., 1998). It contains 8 exons spanning 10.7 kb of genomic DNA.

Protein

Description Human bystin is a 49.6 kDa cytoplasmic protein composed of 437 amino acid residues. Bystin is a basic protein with isoelectric point 8.10. Bystin protein contains many potential protein kinase phosphorylation sites, suggesting an active role of bystin in signal transduction. However, no known structural motif is found in bystin protein.
Expression BYSL is expressed in trophectoderm cells and endometrial epithelial cells during embryo implantation in human (Aoki and Fukuda, 2000; Nakayama et al., 2003; Suzuki et al., 1999; Suzuki et al., 1998). The expression pattern of mouse bystin at peri-implantation (Aoki et al., 2006) is similar to that of mouse trophinin (Nadano et al., 2002).
In the mouse, bystin protein was found in the blastocyst embryo and endometrial epithelial cells during peri-implantation period (Aoki et al., 2006). Bystin is expressed in mouse endometrial luminal and glandular epithelial cells throughout hormonal cycles (Aoki et al., 2006). Bystin in the luminal epithelia showed a distinct blastocyst-dependent pattern: in the presence of blastocysts, bystin proteins localized to the apical side of the epithelia, whereas in their absence bystin protein was localized to the abluminal or basal side of the epithelia (Figure 2). This observation suggests the existence of an embryonic factor affecting in a way determining the localization of bystin in the maternal epithelia. The molecular basis underlying apical or basal localization of bystin is presently unknown.
Bysl is strongly expressed in the adult rat brain after injury (Ma et al., 2006; Sheng et al., 2004). Bystin is expressed after optic nerve injury in zebra fish (Neve et al., 2012).
Bystin protein was found in mature sperm, of which function is implicated to sperm motility (Hatakeyama et al., 2008). Bystin is overexpressed in hepatocellular carcinoma, suggesting its function in cell proliferation in liver cancer (Wang et al., 2009).
In the Drosophila embryo, bys expression is ubiquitous but relatively weak at early stages, but at later stages bys expression is strong and specifically localized to larval imaginal discs, suggesting a role of bys in cell adhesion. In particular, bys expression is strong in the region of the wing pouch giving rise to two epithelial sheets of the adult wing that adhere to one another after the disc everts (Stewart and Nordquist, 2005).
 
  Figure 2. Blastocyst-dependent localization of bystin protein in the mouse endometrial epithelia. Above: mouse endometrium with implanting blastocyst (Bl) shows bystin protein (red) on the apical side of epithelia. below: mouse endometrium from pseudopregnant female shows bystin at abluminal side of epithelia. Glandular epithelia (ge); luminal epithelia (le).
Localisation In 6 weeks human placenta, bystin protein was found in the cytoplasm of the syncytiotrophoblast and cytotrophoblast in the chorionic villi, and in endometrial decidual cells at the utero placental interface. In 10 weeks placenta, bystin was exclusively in the nucli of cytotrophoblast (Suzuki et al., 1999). In cultured cells, bystin localizes to both the nucleus and cytoplasm (Aoki et al., 2006; Miyoshi et al., 2007). In the nucleus, bystin was often found in the nucleoli.
Function Bystin function in human embryo implantation: Bystin was originally identified as a cytoplasmic protein that forms a complex with trophinin and tastin in human trophoblastic embryonal carcinoma HT-H cells (Fukuda and Nozawa, 1999; Suzuki et al., 1998). While genes encoding trophinin and tastin are only found in mammals, the bystin gene is conserved across a wide range of eukaryotes, including yeast, nematodes, insects, snakes, and mammals (Roos et al., 1997; Stewart and Denell, 1993; Stewart and Nordquist, 2005; Trachtulec and Forejt, 2001). Trophinin is an intrinsic membrane protein that mediates cell adhesion by homophilic trophinin-trophinin binding (Fukuda et al., 1995). Tastin and bystin are cytoplasmic proteins required for trophinin to function efficiently as a cell adhesion molecule. In humans, trophinin, tastin and bystin are expressed at the utero-placental interface or at implantation sites (Suzuki et al., 1999). These proteins are expressed in human placenta at early stages of pregnancy but disappear from the placenta after 10 weeks of pregnancy (Aoki and Fukuda, 2000; Fukuda and Nozawa, 1999; Suzuki et al., 1999).
In trophoblastic HT-H cells, bystin protein associates with trophinin and ErbB4 in the cytoplasm (Sugihara et al., 2007). When trophinin-mediated cell adhesion takes place on the cell surface, bystin dissociates from trophinin and tyrosine phosphorylation of ErbB4 takes place, suggesting the mechanism underlying the trophectoderm cell activation upon human embryo implantation (Figure 3). Bystin functions as molecular switch in trophinin-mediated signal transduction in trophoblastic cells (Fukuda and Sugihara, 2007; Fukuda and Sugihara,2008; Fukuda and Sugihara,2012).
Bystin function in mouse embryo: Bystin null mouse embryos implanted successfully but died soon after implantation (Aoki et al., 2006), suggesting that bystin is essential for mouse embryo survival after implantation. However, as described below, Bysl gene knockdown experiments show that bystin is also required for survival of pre-implantation stage mouse embryos (Adachi et al., 2007). In the knockout mouse, it is likely that maternally derived Bysl mRNA masks loss of Bysl at pre-implantation stages.
When Bysl siRNAs were microinjected into fertilized eggs, compaction at the eight-cell stage occurred normally in vitro (Adachi et al., 2007). Bysl siRNA-injected embryos showed slightly reduced expression of cytokeratin 8 (EndoA), an early trophectoderm marker (Oshima et al., 1983). While control blastocysts showed assembled cytokeratin structures in the trophectoderm layer, no organized structures were detected in Bysl siRNA-injected embryos. Consequently, blastocyst formation was completely inhibited. These embryos failed to hatch from the zona pellucida and could not outgrow in culture, suggesting that the bystin functions in trophectoderm differentiation. Bysl knockdown also inhibited embryonic stem cell proliferation (Adachi et al., 2007).
Bystin function in stem cells: Mouse bystin gene Bysl has been identified as the stem cell marker commonly expressed in embryonal, neuronal and hematopoietic stem cells (Ramalho-Santos et al., 2002). BYSL is also identified as the major target of MYC in B-cells (Basso et al., 2005). Since MYC is one of essential genes for converting somatic cells into induced pluripotent stem cell (iPS) (Takahashi and Yamanaka, 2006), these observations suggest strongly an essential role of bystin in pluripotent stem cells. Bysl is included in a gene cluster of stem cell markers found on mouse chromosome 16 (Ramalho-Santos et al., 2002).
Bystin function in human sperm motility: Bystin regulates sperm motility (Hatakeyama et al., 2008). Trophinin plays multiple roles in each cell type under different conditions.
Bystin function in ribosomal biogenesis: The yeast bystin homologue ENP1 is essential for budding yeast to survive (Roos et al., 1997). A temperature-sensitive ENP1-null mutant showed defective processing of ribosomal RNA (rRNA) (Chen et al., 2003). Studies of ribosomal biogenesis in yeast indicate that Enp1 is required to synthesize 40S ribosomal subunits by functioning in their nuclear export (Schafer et al., 2003).
Eukaryotic ribosome formation occurs predominantly in nucleoli, but late maturation steps occur in both the nucleoplasm and cytoplasm. Location of bystin in the cytoplasm during G1 and its nuclear localization prior to mitosis suggest that bystin plays dual roles in cell growth and proliferation in mammalian cells.
Although bystin exhibits activities similar to Enp1, human bystin cannot rescue the lethal phenotype of Enp1-null yeast mutant, suggesting that ribosomal RNA processing pathways in multicellular organisms differ from those in yeast and that bystin's activities may have been modified during evolution. Recent studies reveal that maturation of the 40S ribosomal subunit precursors in mammals includes an additional step during processing of the internal transcribed spacer 1 (ITS1), and that coordination between maturation and nuclear export of pre-40S particles has evolved differently in yeast and mammalian cells (Carron et al., 2011). In higher organisms, it was long believed that rRNA processing is completed within the nucleus. However, maturation of the 40S subunit, including final processing of 18S rRNA, occurs in the cytoplasm in human cells (Zemp and Kutay, 2007). Since part of cytoplasmic bystin is associated with the 40S subunit before translation in human cells (Miyoshi et al., 2007), bystin may also function in the final step of 40S subunit synthesis in the cytoplasm.
Bystin associates with undefined nuclear particles following actinomycin D treatment of HeLa cells (Miyoshi et al., 2007). Soluble proteins involved in ribosome biogenesis may shuttle between the nucleolus and nucleoplasm (Dez and Tollervey, 2004). Given the dependence of cell proliferation on ribosome biogenesis, when biogenesis is halted by nucleolar stress this system may allow rapid ribosome re-synthesis following relief from stress (Phipps et al., 2011).
 
  Figure 3. Role of bystin protein in signal transduction. Prior to trophinin-mediated cell adhesion or in silent trophectoderm cells, ErbB4 is arrested by trophinin-bystin complex. When trophinin-mediated cell adhesion occurs or trophinin-binding GWRQ peptide mimics trophinin-mediated cell adhesion, bystin dissociates from trophinin leading into tyrosine phosphorylation of ErbB4 (Sugihara et al., 2007). Figure 4. Ribosomal biogenesis and rRNA processing in eukaryotic cells. The initial pre-rRNA transcript is first transcribed from repetitive ribosomal DNA genes by RNA polymerase I in the nucleolus. rRNA precursors are then processed, chemically modified, and folded in the nucleolus, and ribosomal proteins, which are translated in the cytoplasm and imported into this organelle, concomitantly assemble with pre-rRNAs. There are two alternative pathways for rRNA processing in human HeLa cells. Bystin is likely involved in processing of a 21S intermediate, of which the final product, 18S rRNA, is included in the 40S small subunit. Bystin is involved in 18S rRNA processing.
Homology None.

Implicated in

Note
  
Entity Various cancers
Note Cancer progression depends on cell growth and cell cycle progression. Upregulation of BYSL is implicated to following cancers.
  
  
Entity Gastric cancer
Note Genome-wide genomic copy aberration analysis of gastric cancer revealed several genes and BYSL was identified as one of them along with CDC6, SEC61G, ANP32E, BYSL and FDFT1 (Tsukamoto et al., 2008).
  
  
Entity Hepatocellular carcinoma (HCC)
Note Expression levels of BYSL mRNA and protein in human HCC specimens were markedly increased compared with those seen in adjacent non-cancerous tissue (Wang et al., 2009). BYSL shRNA decreased HCC cell proliferation in vitro, induced apoptosis and partially arrested the cell cycle in the G2/M phase. In vivo, HCC cells treated with BYSL siRNA failed to form tumors in nude mice after subcutaneous implantation. BYSL was found at multiple stages during nucleologenesis, including in nucleolus-derived foci (NDF), perichromosomal regions and the prenucleolar body (PNB) during mitosis. BYSL depletion remarkably suppressed NDF and PNB formation, and disrupted nucleoli assembly after mitosis, resulting in increased apoptosis and reduced tolerance of HCC cells to serum starvation.
  
  
Entity Prostate cancers
Note In prostate cancer cells, which adhere to neurons, bystin protein is expressed in a manner suggesting a role in cell-cell contact and cell growth (Ayala et al., 2006).
  
  
Entity B cell lymphoma
Note Indeed BYSL and CCND3 are both elevated in B cell lymphoma (Bea, 2010; Kasugai et al., 2005), which is consistent with close proximity of BYSL and CCND3 encoding cyclin D3 (Figure 1) suggesting their co-ordinated role in normal and malignant cells.
  

Bibliography

Crucial role of Bysl in mammalian preimplantation development as an integral factor for 40S ribosome biogenesis.
Adachi K, Soeta-Saneyoshi C, Sagara H, Iwakura Y.
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PMID 17242206
 
Recent molecular approaches to elucidate the mechanism of embryo implantation: trophinin, bystin, and tastin as molecules involved in the initial attachment of blastocysts to the uterus in humans.
Aoki R, Fukuda MN.
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PMID 11299965
 
The Bysl gene product, bystin, is essential for survival of mouse embryos.
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FEBS Lett. 2006 Nov 13;580(26):6062-8. Epub 2006 Oct 16.
PMID 17055491
 
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PMID 16245277
 
Reverse engineering of regulatory networks in human B cells.
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PMID 15778709
 
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PMID 20233055
 
Analysis of two human pre-ribosomal factors, bystin and hTsr1, highlights differences in evolution of ribosome biogenesis between yeast and mammals.
Carron C, O'Donohue MF, Choesmel V, Faubladier M, Gleizes PE.
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PMID 20805244
 
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Nucleic Acids Res. 2003 Jan 15;31(2):690-9.
PMID 12527778
 
Ribosome synthesis meets the cell cycle.
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Curr Opin Microbiol. 2004 Dec;7(6):631-7. (REVIEW)
PMID 15556036
 
Trophinin, tastin, and bystin: a complex mediating unique attachment between trophoblastic and endometrial epithelial cells at their respective apical cell membranes.
Fukuda MN, Nozawa S.
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PMID 10797941
 
Trophinin and tastin, a novel cell adhesion molecule complex with potential involvement in embryo implantation.
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PMID 7758945
 
Enhancement of human sperm motility by trophinin binding peptide.
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PMID 18554632
 
Identification of CCND3 and BYSL as candidate targets for the 6p21 amplification in diffuse large B-cell lymphoma.
Kasugai Y, Tagawa H, Kameoka Y, Morishima Y, Nakamura S, Seto M.
Clin Cancer Res. 2005 Dec 1;11(23):8265-72.
PMID 16322284
 
Expression of trophinin and bystin identifies distinct cell types in the germinal zones of adult rat brain.
Ma L, Yin M, Wu X, Wu C, Yang S, Sheng J, Ni H, Fukuda MN, Zhou J.
Eur J Neurosci. 2006 May;23(9):2265-76.
PMID 16706835
 
Bystin in human cancer cells: intracellular localization and function in ribosome biogenesis.
Miyoshi M, Okajima T, Matsuda T, Fukuda MN, Nadano D.
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PMID 17381424
 
Significant differences between mouse and human trophinins are revealed by their expression patterns and targeted disruption of mouse trophinin gene.
Nadano D, Sugihara K, Paria BC, Saburi S, Copeland NG, Gilbert DJ, Jenkins NA, Nakayama J, Fukuda MN.
Biol Reprod. 2002 Feb;66(2):313-21.
PMID 11804944
 
Implantation-dependent expression of trophinin by maternal fallopian tube epithelia during tubal pregnancies: possible role of human chorionic gonadotrophin on ectopic pregnancy.
Nakayama J, Aoki D, Suga T, Akama TO, Ishizone S, Yamaguchi H, Imakawa K, Nadano D, Fazleabas AT, Katsuyama T, Nozawa S, Fukuda MN.
Am J Pathol. 2003 Dec;163(6):2211-9.
PMID 14633596
 
Activating transcription factor 3 and reactive astrocytes following optic nerve injury in zebrafish.
Neve LD, Savage AA, Koke JR, Garcia DM.
Comp Biochem Physiol C Toxicol Pharmacol. 2012 Mar;155(2):213-8. doi: 10.1016/j.cbpc.2011.08.006. Epub 2011 Aug 24.
PMID 21889613
 
Intermediate filament protein synthesis in preimplantation murine embryos.
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PMID 6352374
 
Assignment1 of the bystin gene BYSL to human chromosome band 6p21.1 by in situ hybridization.
Pack SD, Pak E, Tanigami A, Ledbetter DH, Fukuda MN.
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PMID 9925933
 
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Bystin as a novel marker for reactive astrocytes in the adult rat brain following injury.
Sheng J, Yang S, Xu L, Wu C, Wu X, Li A, Yu Y, Ni H, Fukuda M, Zhou J.
Eur J Neurosci. 2004 Aug;20(4):873-84.
PMID 15305856
 
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PMID 15580530
 
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Sugihara K, Sugiyama D, Byrne J, Wolf DP, Lowitz KP, Kobayashi Y, Kabir-Salmani M, Nadano D, Aoki D, Nozawa S, Nakayama J, Mustelin T, Ruoslahti E, Yamaguchi N, Fukuda MN.
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Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors.
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Citation

This paper should be referenced as such :
Fukuda, MN ; Sugihara, K
BYSL (Bystin-Like)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(5):293-298.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/BYSLID857ch6p21.html


External links

Nomenclature
HGNC (Hugo)BYSL   1157
Cards
AtlasBYSLID857ch6p21
Entrez_Gene (NCBI)BYSL  705  bystin like
AliasesBYSTIN
GeneCards (Weizmann)BYSL
Ensembl hg19 (Hinxton)ENSG00000112578 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000112578 [Gene_View]  chr6:41921227-41933046 [Contig_View]  BYSL [Vega]
ICGC DataPortalENSG00000112578
TCGA cBioPortalBYSL
AceView (NCBI)BYSL
Genatlas (Paris)BYSL
WikiGenes705
SOURCE (Princeton)BYSL
Genetics Home Reference (NIH)BYSL
Genomic and cartography
GoldenPath hg38 (UCSC)BYSL  -     chr6:41921227-41933046 +  6p21.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)BYSL  -     6p21.1   [Description]    (hg19-Feb_2009)
EnsemblBYSL - 6p21.1 [CytoView hg19]  BYSL - 6p21.1 [CytoView hg38]
Mapping of homologs : NCBIBYSL [Mapview hg19]  BYSL [Mapview hg38]
OMIM603871   
Gene and transcription
Genbank (Entrez)AK095253 AK314147 BC007340 BC050645 BC062627
RefSeq transcript (Entrez)NM_004053
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)BYSL
Cluster EST : UnigeneHs.106880 [ NCBI ]
CGAP (NCI)Hs.106880
Alternative Splicing GalleryENSG00000112578
Gene ExpressionBYSL [ NCBI-GEO ]   BYSL [ EBI - ARRAY_EXPRESS ]   BYSL [ SEEK ]   BYSL [ MEM ]
Gene Expression Viewer (FireBrowse)BYSL [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)705
GTEX Portal (Tissue expression)BYSL
Human Protein AtlasENSG00000112578-BYSL [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ13895   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ13895  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ13895
Splice isoforms : SwissVarQ13895
PhosPhoSitePlusQ13895
Domains : Interpro (EBI)Bystin   
Domain families : Pfam (Sanger)Bystin (PF05291)   
Domain families : Pfam (NCBI)pfam05291   
Conserved Domain (NCBI)BYSL
DMDM Disease mutations705
Blocks (Seattle)BYSL
SuperfamilyQ13895
Human Protein Atlas [tissue]ENSG00000112578-BYSL [tissue]
Peptide AtlasQ13895
HPRD04848
IPIIPI00328987   IPI00946581   IPI00947091   
Protein Interaction databases
DIP (DOE-UCLA)Q13895
IntAct (EBI)Q13895
FunCoupENSG00000112578
BioGRIDBYSL
STRING (EMBL)BYSL
ZODIACBYSL
Ontologies - Pathways
QuickGOQ13895
Ontology : AmiGOmaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)  trophectodermal cell differentiation  RNA binding  protein binding  nucleus  nucleoplasm  nucleolus  cytoplasm  cytosol  rRNA processing  cell adhesion  female pregnancy  cell proliferation  membrane  intracellular membrane-bounded organelle  apical part of cell  
Ontology : EGO-EBImaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)  trophectodermal cell differentiation  RNA binding  protein binding  nucleus  nucleoplasm  nucleolus  cytoplasm  cytosol  rRNA processing  cell adhesion  female pregnancy  cell proliferation  membrane  intracellular membrane-bounded organelle  apical part of cell  
REACTOMEQ13895 [protein]
REACTOME PathwaysR-HSA-6791226 [pathway]   
NDEx NetworkBYSL
Atlas of Cancer Signalling NetworkBYSL
Wikipedia pathwaysBYSL
Orthology - Evolution
OrthoDB705
GeneTree (enSembl)ENSG00000112578
Phylogenetic Trees/Animal Genes : TreeFamBYSL
HOVERGENQ13895
HOGENOMQ13895
Homologs : HomoloGeneBYSL
Homology/Alignments : Family Browser (UCSC)BYSL
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerBYSL [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)BYSL
dbVarBYSL
ClinVarBYSL
1000_GenomesBYSL 
Exome Variant ServerBYSL
ExAC (Exome Aggregation Consortium)ENSG00000112578
GNOMAD BrowserENSG00000112578
Genetic variants : HAPMAP705
Genomic Variants (DGV)BYSL [DGVbeta]
DECIPHERBYSL [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisBYSL 
Mutations
ICGC Data PortalBYSL 
TCGA Data PortalBYSL 
Broad Tumor PortalBYSL
OASIS PortalBYSL [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICBYSL  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDBYSL
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 BYSL
DgiDB (Drug Gene Interaction Database)BYSL
DoCM (Curated mutations)BYSL (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)BYSL (select a term)
intoGenBYSL
NCG5 (London)BYSL
Cancer3DBYSL(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM603871   
Orphanet
MedgenBYSL
Genetic Testing Registry BYSL
NextProtQ13895 [Medical]
TSGene705
GENETestsBYSL
Target ValidationBYSL
Huge Navigator BYSL [HugePedia]
snp3D : Map Gene to Disease705
BioCentury BCIQBYSL
ClinGenBYSL
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD705
Chemical/Pharm GKB GenePA25472
Clinical trialBYSL
Miscellaneous
canSAR (ICR)BYSL (select the gene name)
Probes
Litterature
PubMed40 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineBYSL
EVEXBYSL
GoPubMedBYSL
iHOPBYSL
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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