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ACHE (acetylcholinesterase)

Written2012-05Hermona Soreq, David S Greenberg
Department of Biological Chemistry, the Edmond, Lily Safra Center of Neuroscience, The Hebrew University of Jerusalem, 91904 Jerusalem, Israel

(Note : for Links provided by Atlas : click)

Identity

Alias_namesYT
acetylcholinesterase (YT blood group)
acetylcholinesterase (Yt blood group)
Other aliasACEE
ARACHE
N-ACHE
HGNC (Hugo) ACHE
LocusID (NCBI) 43
Atlas_Id 44317
Location 7q22.1  [Link to chromosome band 7q22]
Location_base_pair Starts at 100889994 and ends at 100895971 bp from pter ( according to hg19-Feb_2009)  [Mapping ACHE.png]
Fusion genes
(updated 2016)		CDK6 (7q21.2) / ACHE (7q22.1)CUX1 (7q22.1) / ACHE (7q22.1)

DNA/RNA

 
  The human AChE gene is located at q22 of the long arm of chromosome 7. The AChE mRNA has multiple isoforms which arise from both alternative promoter usage in the 5' of the gene and alternative splicing of exons 4, 5 and 6.
Description The ACHE gene spans about 6 kilobases on chromosome 7q22.
Transcription The gene gives rise to multiple alternatively spliced transcripts. These include AChE-Synaptic (AChE-S), AChE-Erythrocyte (AChE-E) and AChE-Read through (AChE-R). AChE-S is the major neuronal transcript. Alternative 3' splicing gives rise to AChE-E, a dimeric glycophosphatidylinositol (GPI)-anchored isoform expressed primarily in erythrocytes. The third variant AChE-R is produced by the inclusion of the normally spliced out intron 4 and is reported to be elevated during stress. In addition, the existence of multiple promoters leads to the production of several variants with extended N-terminal sequences which are transcribed from the alternative promoters although their expression patterns have not yet been well characterized (Soreq and Seidman, 2001; Meshorer and Soreq, 2006).
Pseudogene None.

Protein

Description Acetylcholinesterase (AChE) is a 57 kDa protein. AChE can be monomeric (AChE-R), dimeric (AChE-E) or tetrameric (AChE-S). Tetrameric AChE-S can further interact with collagen Q (ColQ), enabling anchorage to neuromuscular junctions (NMJs), and a proline-rich membrane anchor protein (PRiMA) is responsible for the synaptic docking of AChE-S in the brain. AChE-R is a soluble monomer with a unique naturally unfolded C-terminal peptide. Because AChE-E and AChE-R are incapable of anchorage to the NMJ or to synaptic membranes through ColQ or PRiMA, only the AChE-S form of the enzyme is regarded as truly "synaptic" (Massoulié et al., 1993; Taylor et al., 1993; Silman and Sussman, 2008).
Expression Functional heterogeneity in AChE activity is regulated at the transcriptional, post-transcriptional and post-translational levels, leading to complex expression patterns that reflect tissue and cell-type specificity, differentiation state, physiological condition and response to external stimuli. Recent studies have also looked at regulation of AChE expression by microRNA (Hanin and Soreq, 2011).
Localisation Intracellular, extracellular, plasma, cerebrospinal fluid.
Function Acetylcholinesterase is a type B hydrolase that rapidly and selectively hydrolyzes the neurotransmitter acetylcholine (ACh) at cholinergic synapses, as well as at neuromuscular junctions (Soreq and Seidman, 2001). In addition to its catalytic function of the hydrolysis of acetylcholine, AChE has been shown to be involved in many non-cholinergic functions, such as cell growth, stem cell differentiation (Sperling et al., 2008; Falugi and Aluigi, 2012), neuritogenesis, cell adhesion (Paraoanu and Layer, 2008), synaptogenesis, activation of dopaminergic neurons, tumorigenesis, amyloid fibril assembly (Inestrosa et al., 1996; Alvarez et al., 1997), haematopoiesis and thrombopoiesis (Greenfield, 1996; Layer, 1996; Small et al., 1996). The role of acetylcholinesterase in modulating the regulation of cholinergic function is still being investigated (Shaked et al., 2009; Schliebs and Arendt, 2011). The role of AChE inhibitors in many neurodegenerative and neurodevelopmental pathologies is also being studied (Hargreaves, 2012; Li et al., 2012).
Homology AChE is widely conserved in the animal kingdom and is found in mammals, Drosophila, C. elegans and Torpedo californica, among others.

Mutations

Note No natural disease-causing mutations have been reported but a number of single nucleotide polymorphisms (SNPs) are known which may affect transcriptional activity and immune properties.

Implicated in

Note
  
Entity Primary ovarian carcinomas
Note Significant amplification and mutagenesis of both the ache and the highly homologous BChE gene were identified in malignant tumors. The frequent co-amplification in ovarian carcinomas of ACHE implicates cholinesterases in neoplastic growth and/or proliferation (Zakut et al., 1990).
  
  
Entity Glioblastoma multiforme
Note AChE mRNA accumulates in primary human astrocytomas in a manner associated with these tumors' grade of aggressiveness (Perry et al., 2002). CREB regulation allows AChE-R-induced, PKA-mediated proliferation of glioblastoma tumors (Perry et al., 2004).
  
  
Entity Leukemia
Note AChE-S may be a regulator of hematopoiesis, affecting cell fate decisions downstream to the GEMM progenitor cells (Perry et al., 2007). Deletion of the acetylcholinesterase locus at 7q22 is associated with myelodysplastic syndromes (MDS) and acute myeloid leukaemia (AML) (Stephenson et al., 1996).
  
  
Entity Breast cancer
Note In a recent study, amplifications and deletions in the AChE and BChE genes were investigated in sporadic breast tumors using real-time polymerase chain reaction and the relative quantification method and the majority of the tumor tissues showed a notable number of both deletions and amplifications of both the AChE and BChE genes (Bernardi et al., 2010).
  
  
Entity Alzheimer's disease
Note The loss of cholinergic neurons has long been believed to be an important aspect of Alzheimer's pathology (Oddo and LaFerla, 2006; Schliebs and Arendt, 2011) and increasing the level of acetylcholine by the use of cholinesterase inhibitors is one of the few pharmacological interventions available for the treatment of Alzheimer's disease (Birks, 2006; Shanks et al., 2009). AChE has been identified in the amyloid plaques found in Alzheimers disease and the isoforms of AChE have different effects on the extent of plaque development (Berson et al., 2008).
  
  
Entity Inflammation
Note Being a major regulator of acetylcholine levels, AChE may relieve the cholinergic blockade of inflammation (Shaked et al., 2009). Correspondingly, increasing levels of the AChE-targeted microRNA-132, and presumably other AChE-targeted microRNAs can potentiate this blockade (Hanin and Soreq, 2011).
  

Bibliography

Acetylcholinesterase promotes the aggregation of amyloid-beta-peptide fragments by forming a complex with the growing fibrils.
Alvarez A, Opazo C, Alarcon R, Garrido J, Inestrosa NC.
J Mol Biol. 1997 Sep 26;272(3):348-61.
PMID 9325095
 
Amplification and deletion of the ACHE and BCHE cholinesterase genes in sporadic breast cancer.
Bernardi CC, Ribeiro Ede S, Cavalli IJ, Chautard-Freire-Maia EA, Souza RL.
Cancer Genet Cytogenet. 2010 Mar;197(2):158-65.
PMID 20193849
 
Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology.
Berson A, Knobloch M, Hanan M, Diamant S, Sharoni M, Schuppli D, Geyer BC, Ravid R, Mor TS, Nitsch RM, Soreq H.
Brain. 2008 Jan;131(Pt 1):109-19. Epub 2007 Dec 3.
PMID 18056160
 
Cholinesterase inhibitors for Alzheimer's disease.
Birks J.
Cochrane Database Syst Rev. 2006 Jan 25;(1):CD005593. (REVIEW)
PMID 16437532
 
Early appearance and possible functions of non-neuromuscular cholinesterase activities.
Falugi C, Aluigi MG.
Front Mol Neurosci. 2012;5:54. Epub 2012 Apr 20.
PMID 22529777
 
Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease.
Greenfield S.
Neurochem Int. 1996 May-Jun;28(5-6):485-90. (REVIEW)
PMID 8792328
 
Cholinesterase-Targeting microRNAs Identified in silico Affect Specific Biological Processes.
Hanin G, Soreq H.
Front Mol Neurosci. 2011;4:28. Epub 2011 Oct 5.
PMID 22007158
 
Neurodegenerations induced by organophosphorous compounds.
Hargreaves AJ.
Adv Exp Med Biol. 2012;724:189-204. (REVIEW)
PMID 22411244
 
Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme.
Inestrosa NC, Alvarez A, Perez CA, Moreno RD, Vicente M, Linker C, Casanueva OI, Soto C, Garrido J.
Neuron. 1996 Apr;16(4):881-91.
PMID 8608006
 
Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease.
Layer PG.
Neurochem Int. 1996 May-Jun;28(5-6):491-5. (REVIEW)
PMID 8792329
 
Evaluation of epidemiology and animal data for risk assessment: chlorpyrifos developmental neurobehavioral outcomes.
Li AA, Lowe KA, McIntosh LJ, Mink PJ.
J Toxicol Environ Health B Crit Rev. 2012;15(2):109-84. (REVIEW)
PMID 22401178
 
Structure and functions of acetylcholinesterase and butyrylcholinesterase.
Massoulie J, Sussman J, Bon S, Silman I.
Prog Brain Res. 1993;98:139-46. (REVIEW)
PMID 8248501
 
Virtues and woes of AChE alternative splicing in stress-related neuropathologies.
Meshorer E, Soreq H.
Trends Neurosci. 2006 Apr;29(4):216-24. Epub 2006 Mar 3. (REVIEW)
PMID 16516310
 
The role of nicotinic acetylcholine receptors in Alzheimer's disease.
Oddo S, LaFerla FM.
J Physiol Paris. 2006 Mar-May;99(2-3):172-9. Epub 2006 Jan 30. (REVIEW)
PMID 16448808
 
Acetylcholinesterase in cell adhesion, neurite growth and network formation.
Paraoanu LE, Layer PG.
FEBS J. 2008 Feb;275(4):618-24. Epub 2008 Jan 17. (REVIEW)
PMID 18205832
 
Acetylcholinesterase/C terminal binding protein interactions modify Ikaros functions, causing T lymphopenia.
Perry C, Pick M, Podoly E, Gilboa-Geffen A, Zimmerman G, Sklan EH, Ben-Shaul Y, Diamant S, Soreq H.
Leukemia. 2007 Jul;21(7):1472-80. Epub 2007 May 3.
PMID 17476278
 
CREB regulates AChE-R-induced proliferation of human glioblastoma cells.
Perry C, Sklan EH, Soreq H.
Neoplasia. 2004 May-Jun;6(3):279-86.
PMID 15153340
 
The cholinergic system in aging and neuronal degeneration.
Schliebs R, Arendt T.
Behav Brain Res. 2011 Aug 10;221(2):555-63. Epub 2010 Dec 9. (REVIEW)
PMID 21145918
 
MicroRNA-132 potentiates cholinergic anti-inflammatory signaling by targeting acetylcholinesterase.
Shaked I, Meerson A, Wolf Y, Avni R, Greenberg D, Gilboa-Geffen A, Soreq H.
Immunity. 2009 Dec 18;31(6):965-73. Epub 2009 Dec 10.
PMID 20005135
 
Cholinesterase inhibition: is there evidence for disease-modifying effects?
Shanks M, Kivipelto M, Bullock R, Lane R.
Curr Med Res Opin. 2009 Oct;25(10):2439-46. (REVIEW)
PMID 19678754
 
Acetylcholinesterase: how is structure related to function?
Silman I, Sussman JL.
Chem Biol Interact. 2008 Sep 25;175(1-3):3-10. Epub 2008 Jun 6. (REVIEW)
PMID 18586019
 
Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease.
Small DH, Michaelson S, Sberna G.
Neurochem Int. 1996 May-Jun;28(5-6):453-83. (REVIEW)
PMID 8792327
 
Acetylcholinesterase--new roles for an old actor.
Soreq H, Seidman S.
Nat Rev Neurosci. 2001 Apr;2(4):294-302. (REVIEW)
PMID 11283752
 
Characterisation of cholinesterase expression during murine embryonic stem cell differentiation.
Sperling LE, Steinert G, Boutter J, Landgraf D, Hescheler J, Pollet D, Layer PG.
Chem Biol Interact. 2008 Sep 25;175(1-3):156-60. Epub 2008 Jun 6.
PMID 18588865
 
Deletion of the acetylcholinesterase locus at 7q22 associated with myelodysplastic syndromes (MDS) and acute myeloid leukaemia (AML).
Stephenson J, Czepulkowski B, Hirst W, Mufti GJ.
Leuk Res. 1996 Mar;20(3):235-41.
PMID 8637218
 
Structure and regulation of expression of the acetylcholinesterase gene.
Taylor P, Li Y, Camp S, Rachinsky TL, Ekstrom T, Getman D, Fuentes ME, Vellom DC, Radic Z.
Chem Biol Interact. 1993 Jun;87(1-3):199-207. (REVIEW)
PMID 8343976
 
Acetylcholinesterase and butyrylcholinesterase genes coamplify in primary ovarian carcinomas.
Zakut H, Ehrlich G, Ayalon A, Prody CA, Malinger G, Seidman S, Ginzberg D, Kehlenbach R, Soreq H.
J Clin Invest. 1990 Sep;86(3):900-8.
PMID 2394839
 

Citation

This paper should be referenced as such :
Soreq, H ; Greenberg, DS
ACHE (acetylcholinesterase)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(10):710-713.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/ACHEID44317ch7q22.html

External links

Nomenclature
HGNC (Hugo)ACHE   108
LRG (Locus Reference Genomic)LRG_804
Cards
AtlasACHEID44317ch7q22
Entrez_Gene (NCBI)ACHE  43  acetylcholinesterase (Cartwright blood group)
AliasesACEE; ARACHE; N-ACHE; YT
GeneCards (Weizmann)ACHE
Ensembl hg19 (Hinxton)ENSG00000087085 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000087085 [Gene_View]  chr7:100889994-100895971 [Contig_View]  ACHE [Vega]
ICGC DataPortalENSG00000087085
TCGA cBioPortalACHE
AceView (NCBI)ACHE
Genatlas (Paris)ACHE
WikiGenes43
SOURCE (Princeton)ACHE
Genetics Home Reference (NIH)ACHE
Genomic and cartography
GoldenPath hg38 (UCSC)ACHE  -     chr7:100889994-100895971 -  7q22.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)ACHE  -     7q22.1   [Description]    (hg19-Feb_2009)
EnsemblACHE - 7q22.1 [CytoView hg19]  ACHE - 7q22.1 [CytoView hg38]
Mapping of homologs : NCBIACHE [Mapview hg19]  ACHE [Mapview hg38]
OMIM100740   112100   
Gene and transcription
Genbank (Entrez)AF334270 AI831696 AK223443 AK291321 AY389977
RefSeq transcript (Entrez)NM_000665 NM_001282449 NM_001302621 NM_001302622 NM_015831
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)ACHE
Cluster EST : UnigeneHs.154495 [ NCBI ]
CGAP (NCI)Hs.154495
Alternative Splicing GalleryENSG00000087085
Gene ExpressionACHE [ NCBI-GEO ]   ACHE [ EBI - ARRAY_EXPRESS ]   ACHE [ SEEK ]   ACHE [ MEM ]
Gene Expression Viewer (FireBrowse)ACHE [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)43
GTEX Portal (Tissue expression)ACHE
Protein : pattern, domain, 3D structure
UniProt/SwissProtP22303   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP22303  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP22303
Splice isoforms : SwissVarP22303
Catalytic activity : Enzyme3.1.1.7 [ Enzyme-Expasy ]   3.1.1.73.1.1.7 [ IntEnz-EBI ]   3.1.1.7 [ BRENDA ]   3.1.1.7 [ KEGG ]   
PhosPhoSitePlusP22303
Domaine pattern : Prosite (Expaxy)CARBOXYLESTERASE_B_1 (PS00122)    CARBOXYLESTERASE_B_2 (PS00941)   
Domains : Interpro (EBI)AB_hydrolase    AChE_tetra    CarbesteraseB    Carboxylesterase_B_AS    Carboxylesterase_B_CS    Cholinesterase   
Domain families : Pfam (Sanger)AChE_tetra (PF08674)    COesterase (PF00135)   
Domain families : Pfam (NCBI)pfam08674    pfam00135   
Domain structure : Prodom (Prabi Lyon)AChE_tetra (PD415333)   
Conserved Domain (NCBI)ACHE
DMDM Disease mutations43
Blocks (Seattle)ACHE
PDB (SRS)1B41    1F8U    1PUV    1PUW    1VZJ    2CLJ    2X8B    3LII    4BDT    4EY4    4EY5    4EY6    4EY7    4EY8    4M0E    4M0F    4PQE    5FOQ    5FPQ    5HF5    5HF6    5HF8    5HF9    5HFA   
PDB (PDBSum)1B41    1F8U    1PUV    1PUW    1VZJ    2CLJ    2X8B    3LII    4BDT    4EY4    4EY5    4EY6    4EY7    4EY8    4M0E    4M0F    4PQE    5FOQ    5FPQ    5HF5    5HF6    5HF8    5HF9    5HFA   
PDB (IMB)1B41    1F8U    1PUV    1PUW    1VZJ    2CLJ    2X8B    3LII    4BDT    4EY4    4EY5    4EY6    4EY7    4EY8    4M0E    4M0F    4PQE    5FOQ    5FPQ    5HF5    5HF6    5HF8    5HF9    5HFA   
PDB (RSDB)1B41    1F8U    1PUV    1PUW    1VZJ    2CLJ    2X8B    3LII    4BDT    4EY4    4EY5    4EY6    4EY7    4EY8    4M0E    4M0F    4PQE    5FOQ    5FPQ    5HF5    5HF6    5HF8    5HF9    5HFA   
Structural Biology KnowledgeBase1B41    1F8U    1PUV    1PUW    1VZJ    2CLJ    2X8B    3LII    4BDT    4EY4    4EY5    4EY6    4EY7    4EY8    4M0E    4M0F    4PQE    5FOQ    5FPQ    5HF5    5HF6    5HF8    5HF9    5HFA   
SCOP (Structural Classification of Proteins)1B41    1F8U    1PUV    1PUW    1VZJ    2CLJ    2X8B    3LII    4BDT    4EY4    4EY5    4EY6    4EY7    4EY8    4M0E    4M0F    4PQE    5FOQ    5FPQ    5HF5    5HF6    5HF8    5HF9    5HFA   
CATH (Classification of proteins structures)1B41    1F8U    1PUV    1PUW    1VZJ    2CLJ    2X8B    3LII    4BDT    4EY4    4EY5    4EY6    4EY7    4EY8    4M0E    4M0F    4PQE    5FOQ    5FPQ    5HF5    5HF6    5HF8    5HF9    5HFA   
SuperfamilyP22303
Human Protein AtlasENSG00000087085
Peptide AtlasP22303
HPRD00010
IPIIPI00220026   IPI00844209   IPI00913969   IPI00552259   IPI00952760   IPI00816389   IPI00926567   IPI00925931   IPI00925335   IPI00925143   IPI00924429   
Protein Interaction databases
DIP (DOE-UCLA)P22303
IntAct (EBI)P22303
FunCoupENSG00000087085
BioGRIDACHE
STRING (EMBL)ACHE
ZODIACACHE
Ontologies - Pathways
QuickGOP22303
Ontology : AmiGOacetylcholine catabolic process in synaptic cleft  beta-amyloid binding  regulation of receptor recycling  osteoblast development  acetylcholinesterase activity  acetylcholinesterase activity  acetylcholinesterase activity  cholinesterase activity  protein binding  collagen binding  extracellular region  extracellular region  basal lamina  extracellular space  nucleus  Golgi apparatus  plasma membrane  DNA replication  acetylcholine catabolic process  phosphatidylcholine biosynthetic process  cell adhesion  cell adhesion  nervous system development  synapse assembly  muscle organ development  cell proliferation  response to wounding  cell surface  membrane  hydrolase activity  serine hydrolase activity  cell junction  anchored component of membrane  neuromuscular junction  receptor internalization  negative regulation of synaptic transmission, cholinergic  neurotransmitter biosynthetic process  acetylcholine binding  acetylcholine binding  protein homodimerization activity  protein homodimerization activity  amyloid precursor protein metabolic process  synaptic cleft  laminin binding  protein self-association  synapse  neurotransmitter receptor biosynthetic process  perinuclear region of cytoplasm  positive regulation of protein secretion  protein tetramerization  retina development in camera-type eye  
Ontology : EGO-EBIacetylcholine catabolic process in synaptic cleft  beta-amyloid binding  regulation of receptor recycling  osteoblast development  acetylcholinesterase activity  acetylcholinesterase activity  acetylcholinesterase activity  cholinesterase activity  protein binding  collagen binding  extracellular region  extracellular region  basal lamina  extracellular space  nucleus  Golgi apparatus  plasma membrane  DNA replication  acetylcholine catabolic process  phosphatidylcholine biosynthetic process  cell adhesion  cell adhesion  nervous system development  synapse assembly  muscle organ development  cell proliferation  response to wounding  cell surface  membrane  hydrolase activity  serine hydrolase activity  cell junction  anchored component of membrane  neuromuscular junction  receptor internalization  negative regulation of synaptic transmission, cholinergic  neurotransmitter biosynthetic process  acetylcholine binding  acetylcholine binding  protein homodimerization activity  protein homodimerization activity  amyloid precursor protein metabolic process  synaptic cleft  laminin binding  protein self-association  synapse  neurotransmitter receptor biosynthetic process  perinuclear region of cytoplasm  positive regulation of protein secretion  protein tetramerization  retina development in camera-type eye  
Pathways : KEGGGlycerophospholipid metabolism    Cholinergic synapse   
REACTOMEP22303 [protein]
REACTOME PathwaysR-HSA-422085 [pathway]   
NDEx NetworkACHE
Atlas of Cancer Signalling NetworkACHE
Wikipedia pathwaysACHE
Orthology - Evolution
OrthoDB43
GeneTree (enSembl)ENSG00000087085
Phylogenetic Trees/Animal Genes : TreeFamACHE
HOVERGENP22303
HOGENOMP22303
Homologs : HomoloGeneACHE
Homology/Alignments : Family Browser (UCSC)ACHE
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerACHE [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)ACHE
dbVarACHE
ClinVarACHE
1000_GenomesACHE 
Exome Variant ServerACHE
ExAC (Exome Aggregation Consortium)ACHE (select the gene name)
Genetic variants : HAPMAP43
Genomic Variants (DGV)ACHE [DGVbeta]
DECIPHERACHE [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisACHE 
Mutations
ICGC Data PortalACHE 
TCGA Data PortalACHE 
Broad Tumor PortalACHE
OASIS PortalACHE [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICACHE  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDACHE
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 ACHE
DgiDB (Drug Gene Interaction Database)ACHE
DoCM (Curated mutations)ACHE (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)ACHE (select a term)
intoGenACHE
NCG5 (London)ACHE
Cancer3DACHE(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM100740    112100   
Orphanet
MedgenACHE
Genetic Testing Registry ACHE
NextProtP22303 [Medical]
TSGene43
GENETestsACHE
Target ValidationACHE
Huge Navigator ACHE [HugePedia]
snp3D : Map Gene to Disease43
BioCentury BCIQACHE
ClinGenACHE
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD43
Chemical/Pharm GKB GenePA20
Clinical trialACHE
Miscellaneous
canSAR (ICR)ACHE (select the gene name)
Probes
Litterature
PubMed182 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineACHE
EVEXACHE
GoPubMedACHE
iHOPACHE
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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