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CHKA (choline kinase alpha)

Written2008-04Ana Ramírez de Molina, María Álvarez-Miranda, Juan Carlos Lacal
Centro Nacional de Biotecnologia (CNB), Darwin 3, 28049 Madrid, Spain

(Note : for Links provided by Atlas : click)

Identity

Alias_namesCHK
choline kinase
Alias_symbol (synonym)CKI
Other aliasCHETK-alpha
CK
HGNC (Hugo) CHKA
LocusID (NCBI) 1119
Atlas_Id 44009
Location 11q13.2  [Link to chromosome band 11q13]
Location_base_pair Starts at 68052859 and ends at 68121391 bp from pter ( according to hg19-Feb_2009)  [Mapping CHKA.png]
Fusion genes
(updated 2016)
CHKA (11q13.2) / CASC3 (17q21.1)CHKA (11q13.2) / GDPD5 (11q13.4)CHKA (11q13.2) / HNF1B (17q12)
CHKA (11q13.2) / NDUFAF4 (6q16.1)CHKA (11q13.2) / PC (11q13.2)CHKA (11q13.2) / PPIH (1p34.2)

DNA/RNA

Transcription The DNA sequence contains 6 exons and the length is of 1374 nt translated to a 457 residues protein.

Protein

Description Choline Kinase alpha (CHKA, though we have proposed to name it as ChoKα in order to distinguish it from check point kinase CHK) encodes two different isoforms. Choline Kinase alpha isoform a (ChoKαa) has 457 amino acid residues with a molecular mass of approximatively 52 kDa. Choline Kinase alpha isoform b (ChoKαb) has the same N- and C-termini but is shorter compared to isoform a, resulting in a variant of 439 amino acids and a molecular mass of approximatively 50 kDa.
Both isoforms are active only in an oligomeric form (di- or tetrameric) and require ATP and Mg2+ for their catalytic activity (Wittenberg and Kornberg 1953).
  • ChoKα structure:
    Choline Kinase alpha isoform a (NM_001277) has been crystallized in complex with ADP and phosphocholine (referred in the paper as Choline Kinase alpha2). ATP binds in a cavity where residues from both de N and C-terminal lobes contribute to form a cleft, while the choline-binding site constitutes a deep hydrophobic groove in the C-terminal domain with a rim composed of negative charged residues. Upon binding of choline, the enzyme undergoes conformational changes independently affecting the N-terminal domain and the ATP binding loop (Malito et al. 2006).
  • ChoKα regulation:
    Although much work has been made in other organisms (Paddon et al. 1982; Warden and Friedkin 1985; Kim and Carman 1999; Ramirez de Molina et al. 2002; Yu et al. 2002; Choi et al. 2005; Soto 2008), little is known about human ChoKα regulation.
    It has been described that in HeLa cells, both EGF and insulin increase ChoK activity promoting the conversion of Cho to PCho, accompanied by an expansion of the PCho pool in treated cells (Uchida 1996). On the other hand, it has been suggested that Hypoxia-Inducible Factor-1α (HIF-1α) regulates ChoKα expression in a human prostate cancer model. An increase in cellular PCho and total Cho, as well as ChoK expression, has been observed following exposure of PC-3 cells to hypoxia. Furthermore, HIF-1α can directly bind to some putative hypoxia response elements (HRE) within ChoKα promoter, suggesting that HIF-1α activation of HREs within the putative ChoKα promoter region can increase ChoKα expression in hypoxic environments (Glunde et al. 2008).
  • Expression Choline Kinase is expressed ubiquitously and concurrently (Aoyama et al. 2002). It is a vital enzyme, as homozygous ChoKa knock-out mice are lethal, indicating the indispensable role of ChoKα in early embryogenesis (Wu et al. 2008).
    Localisation ChoKα is found in the cytoplasm.
    Function Choline Kinase activation is necessary for membranes maintenance, cell growth and cell proliferation. It is also necessary for restoring phospholipids degraded during signal transduction. Consequently, ChoKα has an essential role in growth control and signal transduction and it has been implicated in the carcinogenic process.
  • Role in metabolic process:
    Choline Kinase is the first enzyme in the Kennedy pathway, responsible for de novo synthesis of phosphatidylcholine (PC), one of the major lipid components of plasma membranes in mammal cells, that is also essential for structural stability and cell proliferation. The Kennedy pathway consists of four steps. First Choline Kinase catalyzes choline phosphorylation, then phosphocholine (PCho) cytidylyl-transferase (CCT) catalyzes the formation of CDP-choline from PCho and CTP, and cholinephosphotransferase (CPT) catalyzes the final condensation reaction of CDP-choline with diacylglycerol (DAG) to generate PC. Finally, Phospholipase D (PLD) catalyses the hydrolysis of PC to generate phosphatidic acid (PA) and free choline.
    ChoKα can also function as an ethanolamine kinase (EtnK) as it is able to phosphorylate ethanolamine. For a long time choline kinase and ethanolamine kinase have been considered as the same enzyme, because ChoK preparations of highly purified or recombinant enzymes from mammalian sources has been shown to have also a significant EtnK activity. Subsequently, separate genes that would encode EtnK-specific enzymes were identified (Aoyama et al. 2004).
  • Role in signal transduction, precursor of second messengers:
    PC hydrolysis has been implicated in cell signalling. Due to the relative abundance of PC, its hydrolysis can sustain a prolonged liberation of catabolites without drastic changes in membrane phospholipids content. These long-lasting signals are thought to be important in the acquisition of the transformed phenotype. Under mitogenic stimulation by growth factors or oncogenic transformation, PLD-driven PC hydrolysis gives choline and phosphatidic acid (PA). PA can be hydrolyzed or deacylated to form DAG or lysophosphatidic acid (LPA) respectively, both with mitogenic activity. On the other hand, PCho generated from Cho by ChoK is an essential event for growth factors such as platelet-derived growth factor (PDGF) or fibroblast growth factor (FGF). Furthermore, it has been suggested a mitogenic role for PCho (Lacal 2001; Janardhan et al. 2006).
  • Role in the regulation of cell proliferation:
    The accumulation of PC is necessary for the entrance of S phase of the cycle and cell division. It has been recently proposed that ChoKα participates in the regulation of G1-->S transition of the cell cycle at different levels (Ramirez de Molina et al. 2004). ChoKα over-expression induces the transcriptional regulation of genes involved in cell cycle such as p21, p27, and Cyclin D1 and Cyclin D3, whereas ChoKα specific inhibition reverses this effect on the regulation of cell cycle promoting genes. These results suggest the existence of ChoKα-driven co-regulated mechanism to maintain cell growth through the activation of G1-->S transition of the cell cycle (Ramirez de Molina et al. 2008).
  • Role in carcinogenesis:
    PCho is an important lipid metabolite that is involved in cell proliferation as well as in tumorogenesis (Glunde et al. 2006). A role for ChoK in generation of human tumours has been reported. Studies with nuclear magnetic resonance (NMR) reveals elevated levels of PCho in human tumoral tissues in comparison with normal ones (Ruiz-Cabello and Cohen 1992; Smith et al. 1993). The generation of PCho through Kennedy pathway is considered to be one of the crucial steps in regulating growth factor stimulated cell proliferation, malignant transformation, invasion and metastasis (Lacal 2001; Rodriguez-Gonzalez et al. 2003; Glunde et al. 2006). Confirming the role of ChoK in the generation of PCho in the carcinogenic process, this enzyme has been recently described as a novel oncogene that potentiates the tumorogenic ability of other oncogenes such as RhoA (Ramirez de Molina et al. 2005).
    ChoKα is over-expressed in different tumour-derived cell lines as well as in different human tumours including breast, lung, prostate and colorectal colon cancers (Ramirez de Molina et al. 2002; Ramirez de Molina et al. 2002). In addition to ChoKα over-expression, an increased enzymatic activity has been observed in human tumours such as breast (Ramirez de Molina et al. 2002) and colon cancer (Nakagami et al. 1999). Furthermore, ChoKα has been recently described as a new prognostic factor to predict patient outcome in early-stage non-small-cell lung cancer patients (Ramirez de Molina et al. 2007).
    Consequently, ChoKα inhibition constitutes an efficient antitumour strategy with demonstrated antiproliferative activity in vitro and antitumoral activity in vivo (Hernandez-Alcoceba et al. 1997; Hernandez-Alcoceba et al. 1999). A dramatic difference in the response to MN58b, a specific ChoK inhibitor, has been observed between normal and tumour cells. Whereas blockage of de novo PCho synthesis by MN58b in primary cells induces pRb dephosphorylation and results in reversible cell cycle arrest in G0/G1 phase, tumour cells suffer a drastic wobble in the metabolism of main membrane lipids PC and sphingomyelin, resulting in a significant increase in the intracellular levels of ceramides that promotes cells to apoptosis (Rodriguez-Gonzalez et al. 2003; Rodriguez-Gonzalez et al. 2004; Rodriguez-Gonzalez et al. 2005).
  • Mutations

    Note No mutations has been described in ChoKα.

    Implicated in

    Note
      
    Entity Breast carcinoma
    Oncogenesis Normal and tumoral tissues from patients with breast carcinomas were analysed for ChoKα activity and expression. ChoKα activity was increased in 38.5% of tumoral tissues, whereas ChoKα over-expression determined by WB analysis was found in 17% of the 53 samples analysed (Ramirez de Molina et al, 2002).
      
      
    Entity Ovarian carcinoma
    Oncogenesis Choline Kinase activity in human epithelial ovarian carcinoma cells (EOC) was 12- to 24-fold higher when compared with normal or immortalized ovary epithelial cells (EONT) (Iorio et al, 2005).
      
      
    Entity Lung cancer
    Oncogenesis ChoKα mRNA levels were increased in lung tumour cell lines in comparison with human primary bronchial epithelial cells (BEC). This increase was higher in small-cell lung cancer (SCLC) than in non-small-cell lung cancer (NSCLC). Moreover, protein levels and ChoK enzymatic activity were also increased in tumour cells (Ramirez de Molina et al, 2007).
    When analysing tissues from patients with NSCLC, ChoKα over-expression was also observed with an incidence of 50%. Furthermore, patients with NSCLC with ChoKα over-expression had worse disease free and overall survival than those patients with normal levels of the enzyme (Ramirez de Molina et al, 2007).
      
      
    Entity Colorectal cancer
    Oncogenesis Both ChoKα activity and PCho levels were increased in colon cancer and adenocarcinoma tissues when compared with normal tissue. PCho levels in colon cancers were about 1.5 times higher than in normal colon tissue, whereas ChoK activity was 3.7 times higher in tumoral tissues with respect to normal ones (Nakagami et al, 1999).
      
      
    Entity Prostate cancer
    Oncogenesis Increased ChoKα was found in 48% tumoral prostate tissues when compared with their normal counterparts (Ramirez de Molina et al, 2002).
      

    Bibliography

    Structure and function of choline kinase isoforms in mammalian cells.
    Aoyama C, Liao H, Ishidate K.
    Prog Lipid Res. 2004 May;43(3):266-81.
    PMID 15003397
     
    Expression and characterization of the active molecular forms of choline/ethanolamine kinase-alpha and -beta in mouse tissues, including carbon tetrachloride-induced liver.
    Aoyama C, Ohtani A, Ishidate K.
    Biochem J. 2002 May 1;363(Pt 3):777-84.
    PMID 11964179
     
    Phosphorylation of the yeast choline kinase by protein kinase C. Identification of Ser25 and Ser30 as major sites of phosphorylation.
    Choi MG, Kurnov V, Kersting MC, Sreenivas A, Carman GM.
    J Biol Chem. 2005 Jul 15;280(28):26105-12. Epub 2005 May 25.
    PMID 15919656
     
    Choline phospholipid metabolism in cancer: consequences for molecular pharmaceutical interventions.
    Glunde K, Ackerstaff E, Mori N, Jacobs MA, Bhujwalla ZM.
    Mol Pharm. 2006 Sep-Oct;3(5):496-506.
    PMID 17009848
     
    Hypoxia regulates choline kinase expression through hypoxia-inducible factor-1 alpha signaling in a human prostate cancer model.
    Glunde K, Shah T, Winnard PT Jr, Raman V, Takagi T, Vesuna F, Artemov D, Bhujwalla ZM.
    Cancer Res. 2008 Jan 1;68(1):172-80.
    PMID 18172309
     
    In vivo antitumor activity of choline kinase inhibitors: a novel target for anticancer drug discovery.
    Hernandez-Alcoceba R, Fernandez F, Lacal JC.
    Cancer Res. 1999 Jul 1;59(13):3112-8.
    PMID 10397253
     
    Alterations of choline phospholipid metabolism in ovarian tumor progression.
    Iorio E, Mezzanzanica D, Alberti P, Spadaro F, Ramoni C, D'Ascenzo S, Millimaggi D, Pavan A, Dolo V, Canevari S, Podo F.
    Cancer Res. 2005 Oct 15;65(20):9369-76.
    PMID 16230400
     
    Choline kinase: an important target for cancer.
    Janardhan S, Srivani P, Sastry GN.
    Curr Med Chem. 2006;13(10):1169-86.
    PMID 16719778
     
    Phosphorylation and regulation of choline kinase from Saccharomyces cerevisiae by protein kinase A.
    Kim KH, Carman GM.
    J Biol Chem. 1999 Apr 2;274(14):9531-8.
    PMID 10092638
     
    Choline kinase: a novel target for antitumor drugs.
    Lacal JC.
    IDrugs. 2001 Apr;4(4):419-26.
    PMID 16015482
     
    Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine.
    Malito E, Sekulic N, Too WC, Konrad M, Lavie A.
    J Mol Biol. 2006 Nov 24;364(2):136-51. Epub 2006 Sep 3.
    PMID 17007874
     
    Increased choline kinase activity and elevated phosphocholine levels in human colon cancer.
    Nakagami K, Uchida T, Ohwada S, Koibuchi Y, Suda Y, Sekine T, Morishita Y.
    Jpn J Cancer Res. 1999 Apr;90(4):419-24.
    PMID 10363580
     
    Diethylstilbestrol treatment increases the amount of choline kinase in rooster liver.
    Paddon HB, Vigo C, Vance DE.
    Biochim Biophys Acta. 1982 Jan 15;710(1):112-5.
    PMID 6275901
     
    Choline kinase as a link connecting phospholipid metabolism and cell cycle regulation: Implications in cancer therapy.
    Ramirez de Molina A, Gallego-Ortega D, Sarmentero-Estrada J, Lagares D, Gomez Del Pulgar T, Bandres E, Garcia-Foncillas J, Lacal JC.
    Int J Biochem Cell Biol. 2008 Jan 19 [Epub ahead of print]
    PMID 18296102
     
    Inhibition of choline kinase renders a highly selective cytotoxic effect in tumour cells through a mitochondrial independent mechanism.
    Rodriguez-Gonzalez A, Ramirez de Molina A, Banez-Coronel M, Megias D, Lacal JC.
    Int J Oncol. 2005 Apr;26(4):999-1008.
    PMID 15753995
     
    Phospholipid metabolites as indicators of cancer cell function.
    Ruiz-Cabello J, Cohen JS.
    NMR Biomed. 1992 Sep-Oct;5(5):226-33.
    PMID 1449961
     
    Phospholipid metabolites, prognosis and proliferation in human breast carcinoma.
    Smith TA, Bush C, Jameson C, Titley JC, Leach MO, Wilman DE, McCready VR.
    NMR Biomed. 1993 Sep-Oct;6(5):318-23.
    PMID 8268064
     
    Regulation of the Saccharomyces cerevisiae CKI1-encoded Choline Kinase by Zinc Depletion.
    Soto A, Carman GM.
    J Biol Chem. 2008 Apr 11;283(15):10079-88. Epub 2008 Feb 14.
    PMID 18276583
     
    Stimulation of phospholipid synthesis in HeLa cells by epidermal growth factor and insulin: activation of choline kinase and glycerophosphate acyltransferase.
    Uchida T.
    Biochim Biophys Acta. 1996 Nov 22;1304(2):89-104.
    PMID 8954133
     
    Regulation of choline kinase activity and phosphatidylcholine biosynthesis by mitogenic growth factors in 3T3 fibroblasts.
    Warden CH, Friedkin M.
    J Biol Chem. 1985 May 25;260(10):6006-11.
    PMID 2987212
     
    Choline phosphokinase.
    Wittenberg J, Kornberg A.
    J Biol Chem. 1953 May;202(1):431-44.
    PMID 13061469
     
    Early embryonic lethality caused by disruption of the gene for choline kinase alpha, the first enzyme in phosphatidylcholine biosynthesis.
    Wu G, Aoyama C, Young SG, Vance DE.
    J Biol Chem. 2008 Jan 18;283(3):1456-62. Epub 2007 Nov 19.
    PMID 18029352
     
    Phosphorylation of Saccharomyces cerevisiae choline kinase on Ser30 and Ser85 by protein kinase A regulates phosphatidylcholine synthesis by the CDP-choline pathway.
    Yu Y, Sreenivas A, Ostrander DB, Carman GM.
    J Biol Chem. 2002 Sep 20;277(38):34978-86. Epub 2002 Jul 8.
    PMID 12105205
     

    Citation

    This paper should be referenced as such :
    Ramirez, de Molina A ;Alvarez-Miranda, M ; Lacal, JC
    CHKA (choline kinase alpha)
    Atlas Genet Cytogenet Oncol Haematol. 2009;13(2):110-113.
    Free journal version : [ pdf ]   [ DOI ]
    On line version : http://AtlasGeneticsOncology.org/Genes/CHKAID44009ch11q13.html


    External links

    Nomenclature
    HGNC (Hugo)CHKA   1937
    Cards
    AtlasCHKAID44009ch11q13
    Entrez_Gene (NCBI)CHKA  1119  choline kinase alpha
    AliasesCHK; CK; CKI; EK
    GeneCards (Weizmann)CHKA
    Ensembl hg19 (Hinxton)ENSG00000110721 [Gene_View]
    Ensembl hg38 (Hinxton)ENSG00000110721 [Gene_View]  chr11:68052859-68121391 [Contig_View]  CHKA [Vega]
    ICGC DataPortalENSG00000110721
    TCGA cBioPortalCHKA
    AceView (NCBI)CHKA
    Genatlas (Paris)CHKA
    WikiGenes1119
    SOURCE (Princeton)CHKA
    Genetics Home Reference (NIH)CHKA
    Genomic and cartography
    GoldenPath hg38 (UCSC)CHKA  -     chr11:68052859-68121391 -  11q13.2   [Description]    (hg38-Dec_2013)
    GoldenPath hg19 (UCSC)CHKA  -     11q13.2   [Description]    (hg19-Feb_2009)
    EnsemblCHKA - 11q13.2 [CytoView hg19]  CHKA - 11q13.2 [CytoView hg38]
    Mapping of homologs : NCBICHKA [Mapview hg19]  CHKA [Mapview hg38]
    OMIM118491   
    Gene and transcription
    Genbank (Entrez)AI809679 AK054792 AK092643 AL834403 BC036471
    RefSeq transcript (Entrez)NM_001277 NM_212469
    RefSeq genomic (Entrez)
    Consensus coding sequences : CCDS (NCBI)CHKA
    Cluster EST : UnigeneHs.77221 [ NCBI ]
    CGAP (NCI)Hs.77221
    Alternative Splicing GalleryENSG00000110721
    Gene ExpressionCHKA [ NCBI-GEO ]   CHKA [ EBI - ARRAY_EXPRESS ]   CHKA [ SEEK ]   CHKA [ MEM ]
    Gene Expression Viewer (FireBrowse)CHKA [ Firebrowse - Broad ]
    SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
    GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
    BioGPS (Tissue expression)1119
    GTEX Portal (Tissue expression)CHKA
    Protein : pattern, domain, 3D structure
    UniProt/SwissProtP35790   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
    NextProtP35790  [Sequence]  [Exons]  [Medical]  [Publications]
    With graphics : InterProP35790
    Splice isoforms : SwissVarP35790
    Catalytic activity : Enzyme2.7.1.32 [ Enzyme-Expasy ]   2.7.1.322.7.1.32 [ IntEnz-EBI ]   2.7.1.32 [ BRENDA ]   2.7.1.32 [ KEGG ]   
    PhosPhoSitePlusP35790
    Domains : Interpro (EBI)Kinase-like_dom   
    Domain families : Pfam (Sanger)
    Domain families : Pfam (NCBI)
    Conserved Domain (NCBI)CHKA
    DMDM Disease mutations1119
    Blocks (Seattle)CHKA
    PDB (SRS)2CKO    2CKP    2CKQ    2I7Q    3F2R    3G15    3ZM9    4BR3    4CG8    4CG9    4CGA    4DA5    5AFV    5EQE    5EQP    5EQY    5FTG    5FUT   
    PDB (PDBSum)2CKO    2CKP    2CKQ    2I7Q    3F2R    3G15    3ZM9    4BR3    4CG8    4CG9    4CGA    4DA5    5AFV    5EQE    5EQP    5EQY    5FTG    5FUT   
    PDB (IMB)2CKO    2CKP    2CKQ    2I7Q    3F2R    3G15    3ZM9    4BR3    4CG8    4CG9    4CGA    4DA5    5AFV    5EQE    5EQP    5EQY    5FTG    5FUT   
    PDB (RSDB)2CKO    2CKP    2CKQ    2I7Q    3F2R    3G15    3ZM9    4BR3    4CG8    4CG9    4CGA    4DA5    5AFV    5EQE    5EQP    5EQY    5FTG    5FUT   
    Structural Biology KnowledgeBase2CKO    2CKP    2CKQ    2I7Q    3F2R    3G15    3ZM9    4BR3    4CG8    4CG9    4CGA    4DA5    5AFV    5EQE    5EQP    5EQY    5FTG    5FUT   
    SCOP (Structural Classification of Proteins)2CKO    2CKP    2CKQ    2I7Q    3F2R    3G15    3ZM9    4BR3    4CG8    4CG9    4CGA    4DA5    5AFV    5EQE    5EQP    5EQY    5FTG    5FUT   
    CATH (Classification of proteins structures)2CKO    2CKP    2CKQ    2I7Q    3F2R    3G15    3ZM9    4BR3    4CG8    4CG9    4CGA    4DA5    5AFV    5EQE    5EQP    5EQY    5FTG    5FUT   
    SuperfamilyP35790
    Human Protein AtlasENSG00000110721
    Peptide AtlasP35790
    HPRD00327
    IPIIPI00409761   IPI00409762   IPI00980437   IPI00983356   
    Protein Interaction databases
    DIP (DOE-UCLA)P35790
    IntAct (EBI)P35790
    FunCoupENSG00000110721
    BioGRIDCHKA
    STRING (EMBL)CHKA
    ZODIACCHKA
    Ontologies - Pathways
    QuickGOP35790
    Ontology : AmiGOcholine kinase activity  choline kinase activity  cholinesterase activity  ethanolamine kinase activity  ethanolamine kinase activity  signal transducer activity  ATP binding  cytosol  ethanolamine metabolic process  lipid metabolic process  phosphatidylethanolamine biosynthetic process  phosphatidylethanolamine biosynthetic process  phosphatidylethanolamine biosynthetic process  phosphatidylcholine biosynthetic process  phosphatidylcholine biosynthetic process  CDP-choline pathway  lipid transport  signal transduction  drug binding  response to toxic substance  phosphorylation  choline metabolic process  choline binding  protein homodimerization activity  response to 3-methylcholanthrene  
    Ontology : EGO-EBIcholine kinase activity  choline kinase activity  cholinesterase activity  ethanolamine kinase activity  ethanolamine kinase activity  signal transducer activity  ATP binding  cytosol  ethanolamine metabolic process  lipid metabolic process  phosphatidylethanolamine biosynthetic process  phosphatidylethanolamine biosynthetic process  phosphatidylethanolamine biosynthetic process  phosphatidylcholine biosynthetic process  phosphatidylcholine biosynthetic process  CDP-choline pathway  lipid transport  signal transduction  drug binding  response to toxic substance  phosphorylation  choline metabolic process  choline binding  protein homodimerization activity  response to 3-methylcholanthrene  
    Pathways : KEGGGlycerophospholipid metabolism   
    REACTOMEP35790 [protein]
    REACTOME PathwaysR-HSA-1483213 [pathway]   
    NDEx NetworkCHKA
    Atlas of Cancer Signalling NetworkCHKA
    Wikipedia pathwaysCHKA
    Orthology - Evolution
    OrthoDB1119
    GeneTree (enSembl)ENSG00000110721
    Phylogenetic Trees/Animal Genes : TreeFamCHKA
    HOVERGENP35790
    HOGENOMP35790
    Homologs : HomoloGeneCHKA
    Homology/Alignments : Family Browser (UCSC)CHKA
    Gene fusions - Rearrangements
    Fusion : MitelmanCHKA/GDPD5 [11q13.2/11q13.4]  
    Fusion : MitelmanCHKA/HNF1B [11q13.2/17q12]  [t(11;17)(q13;q12)]  
    Fusion : MitelmanCHKA/PC [11q13.2/11q13.2]  [t(11;11)(q13;q13)]  
    Fusion: TCGACHKA 11q13.2 GDPD5 11q13.4 LUAD
    Fusion: TCGACHKA 11q13.2 HNF1B 17q12 LUAD
    Fusion: TCGACHKA 11q13.2 PC 11q13.2 BRCA
    Polymorphisms : SNP and Copy number variants
    NCBI Variation ViewerCHKA [hg38]
    dbSNP Single Nucleotide Polymorphism (NCBI)CHKA
    dbVarCHKA
    ClinVarCHKA
    1000_GenomesCHKA 
    Exome Variant ServerCHKA
    ExAC (Exome Aggregation Consortium)CHKA (select the gene name)
    Genetic variants : HAPMAP1119
    Genomic Variants (DGV)CHKA [DGVbeta]
    DECIPHERCHKA [patients]   [syndromes]   [variants]   [genes]  
    CONAN: Copy Number AnalysisCHKA 
    Mutations
    ICGC Data PortalCHKA 
    TCGA Data PortalCHKA 
    Broad Tumor PortalCHKA
    OASIS PortalCHKA [ Somatic mutations - Copy number]
    Somatic Mutations in Cancer : COSMICCHKA  [overview]  [genome browser]  [tissue]  [distribution]  
    Mutations and Diseases : HGMDCHKA
    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 CHKA
    DgiDB (Drug Gene Interaction Database)CHKA
    DoCM (Curated mutations)CHKA (select the gene name)
    CIViC (Clinical Interpretations of Variants in Cancer)CHKA (select a term)
    intoGenCHKA
    NCG5 (London)CHKA
    Cancer3DCHKA(select the gene name)
    Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
    Diseases
    OMIM118491   
    Orphanet
    MedgenCHKA
    Genetic Testing Registry CHKA
    NextProtP35790 [Medical]
    TSGene1119
    GENETestsCHKA
    Target ValidationCHKA
    Huge Navigator CHKA [HugePedia]
    snp3D : Map Gene to Disease1119
    BioCentury BCIQCHKA
    ClinGenCHKA
    Clinical trials, drugs, therapy
    Chemical/Protein Interactions : CTD1119
    Chemical/Pharm GKB GenePA26468
    Clinical trialCHKA
    Miscellaneous
    canSAR (ICR)CHKA (select the gene name)
    Probes
    Litterature
    PubMed55 Pubmed reference(s) in Entrez
    GeneRIFsGene References Into Functions (Entrez)
    CoreMineCHKA
    EVEXCHKA
    GoPubMedCHKA
    iHOPCHKA
    REVIEW articlesautomatic search in PubMed
    Last year publicationsautomatic search in PubMed

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    indexed on : Fri Jun 30 11:03:31 CEST 2017

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