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TNKS (tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase)

Written2011-06Yury Shebzukhov, Sergei Nedospasov
German Rheumatism Research Center, a Leibniz Institute, Berlin, Germany (YS, SN); Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia (SN)

(Note : for Links provided by Atlas : click)

Identity

Alias_namestankyrase
Alias_symbol (synonym)TIN1
TINF1
TNKS1
PARP-5a
PARP5A
pART5
Other aliasPARPL
HGNC (Hugo) TNKS
LocusID (NCBI) 8658
Atlas_Id 43534
Location 8p23.1  [Link to chromosome band 8p23]
Location_base_pair Starts at 9555935 and ends at 9782346 bp from pter ( according to hg19-Feb_2009)  [Mapping TNKS.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
CDC42SE1 (1q21.3) / TNKS (8p23.1)SARAF (8p12) / TNKS (8p23.1)TNKS (8p23.1) / ASAH1 (8p22)
TNKS (8p23.1) / DMTN (8p21.3)TNKS (8p23.1) / GPC3 (Xq26.2)TNKS (8p23.1) / RHOT1 (17q11.2)

DNA/RNA

Description Spans 226410 bp, 27 exons.
Transcription 9599 bp long mRNA, containing 3984 bp long ORF.

Protein

 
  TNKS protein. HPS: region containing homopolymeric runs of His, Pro, and Ser; ANK: ankyrin domain; SAM: multimerization domain homologous to the sterile alpha motif; PARP: PARP catalytic domain.
Description Isoform 1 (1327 amino acids) contains region with homopolymeric runs of His, Pro, and Ser (HPS domain, aa 1-181), 15 ankyrin repeats (ANK 1 to 15, aa 215-934), multimerization domain homologous to the sterile alpha motif (SAM domain, aa 1030-1089) and PARP catalytic domain (aa 1112-1317). Isoform 2 (643 amino acids) contains only HPS domain and 9 ANK repeats.
Expression Ubiquitous, high expression in brain and ganglions, skin and cardiac tissue.
Localisation Nuclear and cytoplasmic.
Function Poly(ADP-ribosyl)ation (PARsylation) of target proteins: TNKS itself, TNKS2/TNKL, TRF1, IRAP, TAB182/TNKS1BP1, EBNA-1, Mcl-1L, Mcl-1S, NuMA, AXIN1, AXIN2.
TNKS PARsylates TRF1 (telomeric repeat-binding factor 1), a negative regulator of telomere length maintenance. PARsylated TRF1 dissociates from telomeres, enhancing telomerase-mediated telomere elongation (Smith and de Lange, 2000; Cook et al., 2002).
PARsylation of NuMA (nuclear mitotic apparatus protein) by TNKS contributes to mitotic spindle pole assembly (Sbodio and Chi, 2002).
TNKS can PARsylate Mcl-1L and Mcl-1S and inhibit their anti- and pro-apoptotic function correspondingly (Bae et al., 2003).
TNKS inhibits Epstein-Barr virus OriP function by binding and modifying Epstein-Barr nuclear antigen 1 (EBNA1) (Deng et al., 2002; Deng et al., 2005).
PARsylation activity of TNKS increases after phosphorilation by mitogen-activated protein kinase (MAPK) upon insulin stimulation (Chi and Lodish, 2000).
TNKS together with its partner IRAP enhances insulin-stimulated exocytosis of GLUT4 (Yeh et al., 2007).
TNKS PARsylates AXIN1 and AXIN2 components of beta-catenin (the Wnt pathway transcription factor) destruction complex (Huang et al., 2009).
TNKS is a target of the FANCD2, the key protein involved in development of Fanconi anemia. FANCD binds tankyrase-1 and inhibits its PARsylation at telomeres (Lyakhovich et al., 2011).
Homology With TNKS2/TNKL.

Mutations

Somatic Frameshift mutations are found in exons 9 and 10 in gastric and colorectal malignant tumors (Kim et al., 2011).

Implicated in

Note
  
Entity Cancer
Note TNKS is considered as a potential target for anticancer treatment.
Inhibition of PARP activities of TNKS blocks Wnt/beta-catenin pathway and increases efficiency of telomerase inhibitors (Seimiya et al., 2005; Huang et al., 2009; Zhang et al., 2010).
Disease TNKS expression increased in some tumors (compared to adjacent normal tissues), including breast, bladder and gastric cancer (Gelmini et al., 2004; Gelmini et al., 2007; Poonepalli et al., 2008; Gao et al., 2011), but in other tumors, e.g. malignant glioma and colorectal cancer TNKS expression might be downregulated (Shervington et al., 2007; Shebzukhov et al., 2008), Fanconi anemia (Lyakhovich et al., 2011).
  

Bibliography

Tankyrase 1 interacts with Mcl-1 proteins and inhibits their regulation of apoptosis.
Bae J, Donigian JR, Hsueh AJ.
J Biol Chem. 2003 Feb 14;278(7):5195-204. Epub 2002 Dec 9.
PMID 12475993
 
Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles.
Chi NW, Lodish HF.
J Biol Chem. 2000 Dec 8;275(49):38437-44.
PMID 10988299
 
Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres.
Cook BD, Dynek JN, Chang W, Shostak G, Smith S.
Mol Cell Biol. 2002 Jan;22(1):332-42.
PMID 11739745
 
Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1.
Deng Z, Atanasiu C, Zhao K, Marmorstein R, Sbodio JI, Chi NW, Lieberman PM.
J Virol. 2005 Apr;79(8):4640-50.
PMID 15795250
 
Telomeric proteins regulate episomal maintenance of Epstein-Barr virus origin of plasmid replication.
Deng Z, Lezina L, Chen CJ, Shtivelband S, So W, Lieberman PM.
Mol Cell. 2002 Mar;9(3):493-503.
PMID 11931758
 
Expression of Tankyrase 1 in Gastric Cancer and Its Correlation with Telomerase Activity.
Gao J, Zhang J, Long Y, Tian Y, Lu X.
Pathol Oncol Res. 2011 Apr 1. [Epub ahead of print]
PMID 21455637
 
Tankyrase, a positive regulator of telomere elongation, is over expressed in human breast cancer.
Gelmini S, Poggesi M, Distante V, Bianchi S, Simi L, Luconi M, Raggi CC, Cataliotti L, Pazzagli M, Orlando C.
Cancer Lett. 2004 Dec 8;216(1):81-7.
PMID 15500951
 
Tankyrase-1 mRNA expression in bladder cancer and paired urine sediment: preliminary experience.
Gelmini S, Quattrone S, Malentacchi F, Villari D, Travaglini F, Giannarini G, Della Melina A, Pazzagli M, Nicita G, Selli C, Orlando C.
Clin Chem Lab Med. 2007;45(7):862-6.
PMID 17617028
 
Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling.
Huang SM, Mishina YM, Liu S, Cheung A, Stegmeier F, Michaud GA, Charlat O, Wiellette E, Zhang Y, Wiessner S, Hild M, Shi X, Wilson CJ, Mickanin C, Myer V, Fazal A, Tomlinson R, Serluca F, Shao W, Cheng H, Shultz M, Rau C, Schirle M, Schlegl J, Ghidelli S, Fawell S, Lu C, Curtis D, Kirschner MW, Lengauer C, Finan PM, Tallarico JA, Bouwmeester T, Porter JA, Bauer A, Cong F.
Nature. 2009 Oct 1;461(7264):614-20. Epub 2009 Sep 16.
PMID 19759537
 
Frameshift mutations of poly(adenosine diphosphate-ribose) polymerase genes in gastric and colorectal cancers with microsatellite instability.
Kim MS, An CH, Kim SS, Yoo NJ, Lee SH.
Hum Pathol. 2011 Feb 16. [Epub ahead of print]
PMID 21333322
 
Fanconi anemia protein FANCD2 inhibits TRF1 polyADP-ribosylation through tankyrase1-dependent manner.
Lyakhovich A, Ramirez MJ, Castellanos A, Castella M, Simons AM, Parvin JD, Surralles J.
Genome Integr. 2011 Feb 12;2(1):4.
PMID 21314979
 
Telomere-mediated genomic instability and the clinico-pathological parameters in breast cancer.
Poonepalli A, Banerjee B, Ramnarayanan K, Palanisamy N, Putti TC, Hande MP.
Genes Chromosomes Cancer. 2008 Dec;47(12):1098-109.
PMID 18720522
 
Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner.
Sbodio JI, Chi NW.
J Biol Chem. 2002 Aug 30;277(35):31887-92. Epub 2002 Jun 21.
PMID 12080061
 
Tankyrase 1 as a target for telomere-directed molecular cancer therapeutics.
Seimiya H, Muramatsu Y, Ohishi T, Tsuruo T.
Cancer Cell. 2005 Jan;7(1):25-37.
PMID 15652747
 
Human tankyrases are aberrantly expressed in colon tumors and contain multiple epitopes that induce humoral and cellular immune responses in cancer patients.
Shebzukhov YV, Lavrik IN, Karbach J, Khlgatian SV, Koroleva EP, Belousov PV, Kashkin KN, Knuth A, Jager E, Chi NW, Kuprash DV, Nedospasov SA.
Cancer Immunol Immunother. 2008 Jun;57(6):871-81. Epub 2007 Nov 20.
PMID 18026951
 
Telomerase subunits expression variation between biopsy samples and cell lines derived from malignant glioma.
Shervington A, Patel R, Lu C, Cruickshanks N, Lea R, Roberts G, Dawson T, Shervington L.
Brain Res. 2007 Feb 23;1134(1):45-52. Epub 2007 Jan 2.
PMID 17196947
 
Tankyrase promotes telomere elongation in human cells.
Smith S, de Lange T.
Curr Biol. 2000 Oct 19;10(20):1299-302.
PMID 11069113
 
Insulin-stimulated exocytosis of GLUT4 is enhanced by IRAP and its partner tankyrase.
Yeh TY, Sbodio JI, Tsun ZY, Luo B, Chi NW.
Biochem J. 2007 Mar 1;402(2):279-90.
PMID 17059388
 
Inhibition of tankyrase 1 in human gastric cancer cells enhances telomere shortening by telomerase inhibitors.
Zhang H, Yang MH, Zhao JJ, Chen L, Yu ST, Tang XD, Fang DC, Yang SM.
Oncol Rep. 2010 Oct;24(4):1059-65.
PMID 20811689
 

Citation

This paper should be referenced as such :
Shebzukhov, Y ; Nedospasov, S
TNKS (tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(12):1030-1032.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/TNKSID43534ch8p23.html


External links

Nomenclature
HGNC (Hugo)TNKS   11941
Cards
AtlasTNKSID43534ch8p23
Entrez_Gene (NCBI)TNKS  8658  tankyrase
AliasesARTD5; PARP-5a; PARP5A; PARPL; 
TIN1; TINF1; TNKS1; pART5
GeneCards (Weizmann)TNKS
Ensembl hg19 (Hinxton)ENSG00000173273 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000173273 [Gene_View]  chr8:9555935-9782346 [Contig_View]  TNKS [Vega]
ICGC DataPortalENSG00000173273
TCGA cBioPortalTNKS
AceView (NCBI)TNKS
Genatlas (Paris)TNKS
WikiGenes8658
SOURCE (Princeton)TNKS
Genetics Home Reference (NIH)TNKS
Genomic and cartography
GoldenPath hg38 (UCSC)TNKS  -     chr8:9555935-9782346 +  8p23.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)TNKS  -     8p23.1   [Description]    (hg19-Feb_2009)
EnsemblTNKS - 8p23.1 [CytoView hg19]  TNKS - 8p23.1 [CytoView hg38]
Mapping of homologs : NCBITNKS [Mapview hg19]  TNKS [Mapview hg38]
OMIM603303   
Gene and transcription
Genbank (Entrez)AB209339 AF070613 AF082556 AF082557 AF082558
RefSeq transcript (Entrez)NM_003747
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)TNKS
Cluster EST : UnigeneHs.370267 [ NCBI ]
CGAP (NCI)Hs.370267
Alternative Splicing GalleryENSG00000173273
Gene ExpressionTNKS [ NCBI-GEO ]   TNKS [ EBI - ARRAY_EXPRESS ]   TNKS [ SEEK ]   TNKS [ MEM ]
Gene Expression Viewer (FireBrowse)TNKS [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)8658
GTEX Portal (Tissue expression)TNKS
Human Protein AtlasENSG00000173273-TNKS [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO95271   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtO95271  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO95271
Splice isoforms : SwissVarO95271
Catalytic activity : Enzyme2.4.2.30 [ Enzyme-Expasy ]   2.4.2.302.4.2.30 [ IntEnz-EBI ]   2.4.2.30 [ BRENDA ]   2.4.2.30 [ KEGG ]   
PhosPhoSitePlusO95271
Domaine pattern : Prosite (Expaxy)ANK_REP_REGION (PS50297)    ANK_REPEAT (PS50088)    PARP_CATALYTIC (PS51059)    SAM_DOMAIN (PS50105)   
Domains : Interpro (EBI)Ankyrin_rpt    Ankyrin_rpt-contain_dom    Poly(ADP-ribose)pol_cat_dom    SAM    SAM/pointed    TNKS   
Domain families : Pfam (Sanger)Ank (PF00023)    Ank_2 (PF12796)    Ank_3 (PF13606)    PARP (PF00644)    SAM_2 (PF07647)   
Domain families : Pfam (NCBI)pfam00023    pfam12796    pfam13606    pfam00644    pfam07647   
Domain families : Smart (EMBL)ANK (SM00248)  SAM (SM00454)  
Conserved Domain (NCBI)TNKS
DMDM Disease mutations8658
Blocks (Seattle)TNKS
PDB (SRS)2RF5    3UDD    3UH2    3UH4    4DVI    4I9I    4K4E    4K4F    4KRS    4LI6    4LI7    4LI8    4MSG    4MSK    4MT9    4N3R    4N4V    4OA7    4TOR    4TOS    4U6A    4UUH    4UW1    4W5S    4W6E    5EBT    5ECE    5ETY    5JHQ    5JTI    5JU5    5KNI   
PDB (PDBSum)2RF5    3UDD    3UH2    3UH4    4DVI    4I9I    4K4E    4K4F    4KRS    4LI6    4LI7    4LI8    4MSG    4MSK    4MT9    4N3R    4N4V    4OA7    4TOR    4TOS    4U6A    4UUH    4UW1    4W5S    4W6E    5EBT    5ECE    5ETY    5JHQ    5JTI    5JU5    5KNI   
PDB (IMB)2RF5    3UDD    3UH2    3UH4    4DVI    4I9I    4K4E    4K4F    4KRS    4LI6    4LI7    4LI8    4MSG    4MSK    4MT9    4N3R    4N4V    4OA7    4TOR    4TOS    4U6A    4UUH    4UW1    4W5S    4W6E    5EBT    5ECE    5ETY    5JHQ    5JTI    5JU5    5KNI   
PDB (RSDB)2RF5    3UDD    3UH2    3UH4    4DVI    4I9I    4K4E    4K4F    4KRS    4LI6    4LI7    4LI8    4MSG    4MSK    4MT9    4N3R    4N4V    4OA7    4TOR    4TOS    4U6A    4UUH    4UW1    4W5S    4W6E    5EBT    5ECE    5ETY    5JHQ    5JTI    5JU5    5KNI   
Structural Biology KnowledgeBase2RF5    3UDD    3UH2    3UH4    4DVI    4I9I    4K4E    4K4F    4KRS    4LI6    4LI7    4LI8    4MSG    4MSK    4MT9    4N3R    4N4V    4OA7    4TOR    4TOS    4U6A    4UUH    4UW1    4W5S    4W6E    5EBT    5ECE    5ETY    5JHQ    5JTI    5JU5    5KNI   
SCOP (Structural Classification of Proteins)2RF5    3UDD    3UH2    3UH4    4DVI    4I9I    4K4E    4K4F    4KRS    4LI6    4LI7    4LI8    4MSG    4MSK    4MT9    4N3R    4N4V    4OA7    4TOR    4TOS    4U6A    4UUH    4UW1    4W5S    4W6E    5EBT    5ECE    5ETY    5JHQ    5JTI    5JU5    5KNI   
CATH (Classification of proteins structures)2RF5    3UDD    3UH2    3UH4    4DVI    4I9I    4K4E    4K4F    4KRS    4LI6    4LI7    4LI8    4MSG    4MSK    4MT9    4N3R    4N4V    4OA7    4TOR    4TOS    4U6A    4UUH    4UW1    4W5S    4W6E    5EBT    5ECE    5ETY    5JHQ    5JTI    5JU5    5KNI   
SuperfamilyO95271
Human Protein Atlas [tissue]ENSG00000173273-TNKS [tissue]
Peptide AtlasO95271
HPRD04490
IPIIPI00021493   IPI00221159   IPI00980790   IPI00974462   IPI00982731   IPI00984084   IPI00981733   
Protein Interaction databases
DIP (DOE-UCLA)O95271
IntAct (EBI)O95271
FunCoupENSG00000173273
BioGRIDTNKS
STRING (EMBL)TNKS
ZODIACTNKS
Ontologies - Pathways
QuickGOO95271
Ontology : AmiGOGolgi membrane  protein polyubiquitination  pericentriolar material  chromosome, centromeric region  chromosome, telomeric region  nuclear chromosome, telomeric region  spindle pole  NAD+ ADP-ribosyltransferase activity  NAD+ ADP-ribosyltransferase activity  protein binding  nuclear pore  nucleoplasm  Golgi apparatus  cytosol  protein ADP-ribosylation  mitotic spindle organization  zinc ion binding  protein transport  Wnt signaling pathway  protein deubiquitination  nuclear body  peptidyl-serine phosphorylation  peptidyl-threonine phosphorylation  nuclear membrane  nuclear membrane  regulation of telomere maintenance via telomerase  positive regulation of telomere maintenance via telomerase  positive regulation of telomere maintenance via telomerase  histone binding  positive regulation of transcription from RNA polymerase II promoter  mRNA transport  spindle assembly  cell division  positive regulation of telomerase activity  protein localization to chromosome, telomeric region  protein poly-ADP-ribosylation  protein poly-ADP-ribosylation  protein auto-ADP-ribosylation  positive regulation of canonical Wnt signaling pathway  positive regulation of canonical Wnt signaling pathway  positive regulation of telomere capping  positive regulation of telomere capping  negative regulation of telomere maintenance via telomere lengthening  negative regulation of telomeric DNA binding  negative regulation of telomeric DNA binding  negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric  
Ontology : EGO-EBIGolgi membrane  protein polyubiquitination  pericentriolar material  chromosome, centromeric region  chromosome, telomeric region  nuclear chromosome, telomeric region  spindle pole  NAD+ ADP-ribosyltransferase activity  NAD+ ADP-ribosyltransferase activity  protein binding  nuclear pore  nucleoplasm  Golgi apparatus  cytosol  protein ADP-ribosylation  mitotic spindle organization  zinc ion binding  protein transport  Wnt signaling pathway  protein deubiquitination  nuclear body  peptidyl-serine phosphorylation  peptidyl-threonine phosphorylation  nuclear membrane  nuclear membrane  regulation of telomere maintenance via telomerase  positive regulation of telomere maintenance via telomerase  positive regulation of telomere maintenance via telomerase  histone binding  positive regulation of transcription from RNA polymerase II promoter  mRNA transport  spindle assembly  cell division  positive regulation of telomerase activity  protein localization to chromosome, telomeric region  protein poly-ADP-ribosylation  protein poly-ADP-ribosylation  protein auto-ADP-ribosylation  positive regulation of canonical Wnt signaling pathway  positive regulation of canonical Wnt signaling pathway  positive regulation of telomere capping  positive regulation of telomere capping  negative regulation of telomere maintenance via telomere lengthening  negative regulation of telomeric DNA binding  negative regulation of telomeric DNA binding  negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric  
Pathways : BIOCARTATelomeres, Telomerase, Cellular Aging, and Immortality [Genes]   
REACTOMEO95271 [protein]
REACTOME PathwaysR-HSA-5689880 [pathway]   
NDEx NetworkTNKS
Atlas of Cancer Signalling NetworkTNKS
Wikipedia pathwaysTNKS
Orthology - Evolution
OrthoDB8658
GeneTree (enSembl)ENSG00000173273
Phylogenetic Trees/Animal Genes : TreeFamTNKS
HOVERGENO95271
HOGENOMO95271
Homologs : HomoloGeneTNKS
Homology/Alignments : Family Browser (UCSC)TNKS
Gene fusions - Rearrangements
Fusion : MitelmanCDC42SE1/TNKS [1q21.3/8p23.1]  [t(1;8)(q21;p23)]  
Fusion : MitelmanSARAF/TNKS [8p12/8p23.1]  [t(8;8)(p12;p23)]  
Fusion : MitelmanTNKS/ASAH1 [8p23.1/8p22]  [t(8;8)(p22;p23)]  
Fusion: TCGACDC42SE1 1q21.3 TNKS 8p23.1 BRCA
Fusion: TCGATMEM66 TNKS 8p23.1 PRAD
Fusion: TCGATNKS 8p23.1 AC068020.1 LUAD
Fusion: TCGATNKS 8p23.1 ASAH1 8p22 BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTNKS [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TNKS
dbVarTNKS
ClinVarTNKS
1000_GenomesTNKS 
Exome Variant ServerTNKS
ExAC (Exome Aggregation Consortium)ENSG00000173273
GNOMAD BrowserENSG00000173273
Genetic variants : HAPMAP8658
Genomic Variants (DGV)TNKS [DGVbeta]
DECIPHERTNKS [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisTNKS 
Mutations
ICGC Data PortalTNKS 
TCGA Data PortalTNKS 
Broad Tumor PortalTNKS
OASIS PortalTNKS [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICTNKS  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDTNKS
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
LOVD (Leiden Open Variation Database)**PUBLIC** CCHMC Molecular Genetics Laboratory Mutation Database
BioMutasearch TNKS
DgiDB (Drug Gene Interaction Database)TNKS
DoCM (Curated mutations)TNKS (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)TNKS (select a term)
intoGenTNKS
NCG5 (London)TNKS
Cancer3DTNKS(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM603303   
Orphanet
MedgenTNKS
Genetic Testing Registry TNKS
NextProtO95271 [Medical]
TSGene8658
GENETestsTNKS
Target ValidationTNKS
Huge Navigator TNKS [HugePedia]
snp3D : Map Gene to Disease8658
BioCentury BCIQTNKS
ClinGenTNKS
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD8658
Chemical/Pharm GKB GenePA36631
Clinical trialTNKS
Miscellaneous
canSAR (ICR)TNKS (select the gene name)
Probes
Litterature
PubMed100 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineTNKS
EVEXTNKS
GoPubMedTNKS
iHOPTNKS
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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