ACHE (acetylcholinesterase)

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ACHE (acetylcholinesterase)

Written	2012-05	Hermona 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_names	YT
	acetylcholinesterase (YT blood group)
	acetylcholinesterase (Yt blood group)
Other alias	ACEE
	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 100896133 bp from pter ( according to hg19-Feb_2009) [Mapping ACHE.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)

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
Atlas	ACHEID44317ch7q22
Entrez_Gene (NCBI)	ACHE 43 acetylcholinesterase (Cartwright blood group)
Aliases	ACEE; ARACHE; N-ACHE; YT
GeneCards (Weizmann)	ACHE
Ensembl hg19 (Hinxton)	ENSG00000087085 [Gene_View]
Ensembl hg38 (Hinxton)	ENSG00000087085 [Gene_View] ENSG00000087085 [Sequence] chr7:100889994-100896133 [Contig_View] ACHE [Vega]
ICGC DataPortal	ENSG00000087085
TCGA cBioPortal	ACHE
AceView (NCBI)	ACHE
Genatlas (Paris)	ACHE
WikiGenes	43
SOURCE (Princeton)	ACHE
Genetics Home Reference (NIH)	ACHE
	Genomic and cartography
GoldenPath hg38 (UCSC)	ACHE - chr7:100889994-100896133 - 7q22.1 [Description] (hg38-Dec_2013)
GoldenPath hg19 (UCSC)	ACHE - 7q22.1 [Description] (hg19-Feb_2009)
Ensembl	ACHE - 7q22.1 [CytoView hg19] ACHE - 7q22.1 [CytoView hg38]
Mapping of homologs : NCBI	ACHE [Mapview hg19] ACHE [Mapview hg38]
OMIM	100740 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 : Unigene	Hs.154495 [ NCBI ]
CGAP (NCI)	Hs.154495
Alternative Splicing Gallery	ENSG00000087085
Gene Expression	ACHE [ 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]
Genevestigator	Expression in : [tissues] [cell-lines] [cancer] [perturbations]
BioGPS (Tissue expression)	43
GTEX Portal (Tissue expression)	ACHE
Human Protein Atlas	ENSG00000087085-ACHE [pathology] [cell] [tissue]
	Protein : pattern, domain, 3D structure
UniProt/SwissProt	P22303 [function] [subcellular_location] [family_and_domains] [pathology_and_biotech] [ptm_processing] [expression] [interaction]
NextProt	P22303 [Sequence] [Exons] [Medical] [Publications]
With graphics : InterPro	P22303
Splice isoforms : SwissVar	P22303
Catalytic activity : Enzyme	3.1.1.7 [ Enzyme-Expasy ] 3.1.1.7 3.1.1.7 [ IntEnz-EBI ] 3.1.1.7 [ BRENDA ] 3.1.1.7 [ KEGG ]
PhosPhoSitePlus	P22303
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 mutations	43
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 KnowledgeBase	1B41 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
Superfamily	P22303
Human Protein Atlas [tissue]	ENSG00000087085-ACHE [tissue]
Peptide Atlas	P22303
HPRD	00010
IPI	IPI00220026 IPI00844209 IPI00913969 IPI00552259 IPI00952760 IPI00816389 IPI00926567 IPI00925931 IPI00925335 IPI00925143 IPI00924429
	Protein Interaction databases
DIP (DOE-UCLA)	P22303
IntAct (EBI)	P22303
FunCoup	ENSG00000087085
BioGRID	ACHE
STRING (EMBL)	ACHE
ZODIAC	ACHE
	Ontologies - Pathways
QuickGO	P22303
Ontology : AmiGO	acetylcholine catabolic process in synaptic cleft amyloid-beta 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-EBI	acetylcholine catabolic process in synaptic cleft amyloid-beta 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 : KEGG	Glycerophospholipid metabolism
REACTOME	P22303 [protein]
REACTOME Pathways	R-HSA-422085 [pathway]
NDEx Network	ACHE
Atlas of Cancer Signalling Network	ACHE
Wikipedia pathways	ACHE
	Orthology - Evolution
OrthoDB	43
GeneTree (enSembl)	ENSG00000087085
Phylogenetic Trees/Animal Genes : TreeFam	ACHE
HOVERGEN	P22303
HOGENOM	P22303
Homologs : HomoloGene	ACHE
Homology/Alignments : Family Browser (UCSC)	ACHE
	Gene fusions - Rearrangements
Fusion : Quiver	ACHE
	Polymorphisms : SNP and Copy number variants
NCBI Variation Viewer	ACHE [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)	ACHE
dbVar	ACHE
ClinVar	ACHE
1000_Genomes	ACHE
Exome Variant Server	ACHE
ExAC (Exome Aggregation Consortium)	ENSG00000087085
GNOMAD Browser	ENSG00000087085
Genetic variants : HAPMAP	43
Genomic Variants (DGV)	ACHE [DGVbeta]
DECIPHER	ACHE [patients] [syndromes] [variants] [genes]
CONAN: Copy Number Analysis	ACHE
	Mutations
ICGC Data Portal	ACHE
TCGA Data Portal	ACHE
Broad Tumor Portal	ACHE
OASIS Portal	ACHE [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMIC	ACHE [overview] [genome browser] [tissue] [distribution]
Mutations and Diseases : HGMD	ACHE
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
BioMuta	search 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)
intoGen	ACHE
NCG5 (London)	ACHE
Cancer3D	ACHE(select the gene name)
Impact of mutations	[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
	Diseases
OMIM	100740 112100
Orphanet
DisGeNET	ACHE
Medgen	ACHE
Genetic Testing Registry	ACHE
NextProt	P22303 [Medical]
TSGene	43
GENETests	ACHE
Target Validation	ACHE
Huge Navigator	ACHE [HugePedia]
snp3D : Map Gene to Disease	43
BioCentury BCIQ	ACHE
ClinGen	ACHE
	Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD	43
Chemical/Pharm GKB Gene	PA20
Clinical trial	ACHE
	Miscellaneous
canSAR (ICR)	ACHE (select the gene name)
	Probes
	Litterature
PubMed	194 Pubmed reference(s) in Entrez
GeneRIFs	Gene References Into Functions (Entrez)
CoreMine	ACHE
EVEX	ACHE
GoPubMed	ACHE
iHOP	ACHE

REVIEW articles	automatic search in PubMed
Last year publications	automatic search in PubMed

Search in all EBI NCBI

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