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ASH2L (ash2 (absent, small, or homeotic)-like (Drosophila))

Written2011-08Paul F South, Scott D Briggs
Department of Biochemistry, Purdue University Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesASH2L1
ash2 (absent
Alias_symbol (synonym)ASH2L2
ASH2
Bre2
Other alias
HGNC (Hugo) ASH2L
LocusID (NCBI) 9070
Atlas_Id 44404
Location 8p11.23  [Link to chromosome band 8p11]
Location_base_pair Starts at 37963311 and ends at 37997598 bp from pter ( according to hg19-Feb_2009)  [Mapping ASH2L.png]
 
  Figure 1. Map of chromosome 8 with region 8p11.2 highlighted as the location of the gene ASH2L.
Fusion genes
(updated 2016)
ASH2L (8p11.23) / BCORL1 (Xq26.1)ASH2L (8p11.23) / C8orf86 (8p11.22)ASH2L (8p11.23) / MEMO1 (2p23.1)
ASH2L (8p11.23) / MGME1 (20p11.23)RPLP1 (15q23) / ASH2L (8p11.23)

DNA/RNA

Description 16 exons spanning over 34218 base pairs.
Transcription mRNA is 2368 base pairs long.

Protein

 
  Figure 2. Schematic model of the three known isoforms of ASH2L and the amino acid sequence changes compared to the canonical isoform 1 (aa 1-628). The positions of known domains within ASH2L are displayed. PHD finger (aa 95-161), WH motif (aa 162-273), SPRY domain (aa 360-583), and SDI domain (aa 602-628). Isoform 2 and 3 are numbered according to isoform 1.
Description There are three known isoforms of ASH2L (Wang et al., 2001). Isoform 1 is considered the canonical sequence and consists of 628 amino acids (Wang et al., 2001). Isoform 2 is missing amino acids 1-94 and 541-573 from isoform 1 (Wang et al., 2001). Isoform 3 is missing the amino acids 1-94 from isoform 1 (figure 2) (Wang et al., 2001). There are four identified domains within ASH2L which include a N-terminus containing a PHD finger and a winged helix motif (WH) and the C-terminus containing a SPRY domain and the Sdc1 DPY-30 Interacting domain (SDI) (figure 2) (Chen et al., 2011; Roguev et al., 2001; Sarvan et al., 2011; South et al., 2010; Wang et al., 2001). The largest of the three identified domains within ASH2L is the SPRY domain, which is also conserved from yeast to humans. SPRY domains were originally named after the SPIa kinase and the RYanodine receptor proteins in which it was first identified (Rhodes et al., 2005). Crystal structures of SPRY domain containing proteins show primarily a beta-sandwich structure with extending loops (Filippakopoulos et al., 2010; Kuang et al., 2009; Simonet et al., 2007; Woo et al., 2006b). The SPRY domain is thought to be a specific protein-protein interaction domain with specific partners, but instead of recognizing a particular motif or interaction domain the SPRY domain binds to interaction partners using non-conserved binding loops (Filippakopoulos et al., 2010; Woo et al., 2006a; Woo et al., 2006b). Recent work has shown that the C-terminus of ASH2L that contains the SPRY domain and the SDI domain are able to interact with the other MLL complex member RBBP5 in vitro (Avdic et al., 2011).
ASH2L also contains a putative Plant Homeo Domain (PHD) finger in its N-terminus (Wang et al., 2001). The structure of PHD fingers shows that conserved cysteine and histidine residues bind to Zn2+ ions (Champagne et al., 2008; Champagne and Kutateladze, 2009; van Ingen et al., 2008). There is no known function attributed to the PHD finger in ASH2L, though in conjunction with the winged helix motif it may be necessary for DNA binding.
The N-terminal winged helix (WH) motif was recently discovered when the crystal structure of the N-terminus of ASH2L was solved (Chen et al., 2011; Sarvan et al., 2011). Using in vitro DNA binding analyses as well as chromatin immunoprecipitation, it was determined that ASH2L can bind DNA at the HS2 promoter region and the beta-globin locus as well as non-specific DNA sequence (Chen et al., 2011; Sarvan et al., 2011).
The last identifiable domain within ASH2L is the SDI domain. There is no structural information on the SDI domain but the functional importance was determined biochemically. The function of the SDI domain was determined using in vitro binding experiments. ASH2L was shown to directly interact with DPY-30 without any additional MLL or Set1 complex components (South et al., 2010). The function of the SDI domain is conserved from yeast to humans because the yeast ASH2L homolog Bre2 was also shown to interact with the DPY-30 homolog Sdc1 (South et al., 2010). There are conserved hydrophobic residues in both the SDI domain of ASH2L and the Dpy-30 domain of DPY-30 that are important for binding, which suggests that the interaction between the SDI domain of ASH2L and the DPY-30 domain of DPY-30 is through hydrophobic interactions (South et al., 2010).
Expression Northern blot analysis from multiple tissues revealed that ASH2L expression is expressed in 14 different tissue types with the highest expression in fetal liver and testes (Lüscher-Firzlaff et al., 2008). ASH2L transcripts were also found to be expressed higher in various Leukemia cell lines, such as K562, Hel, and Dami cells (Lüscher-Firzlaff et al., 2008).
Localisation Nucleus.
Function Biochemical data has shown that ASH2L is found in a methyltransferase core complex composed of ASH2L, RBBP5, DPY30, WDR5, and the catalytic SET domain containing protein. This core complex is highly conserved and similar to the budding yeast Set1 complex that consists of Set1 (MLL/SET1), Bre2 (ASH2L), Swd1 (RBBP5), Swd3 (WDR5), Swd2 (WDR82), Sdc1 (DPY-30), Spp1 (CFP1/CGBP). ASH2L is also known to associate with numerous additional factors. Many of these additional factors are thought to associate with ASH2L and the H3K4 methyltransferase complexes to target the complex to specific sites within the genome (Cho et al., 2007; Dou et al., 2006; Hughes et al., 2004; Steward et al., 2006; Stoller et al., 2010). Knock-down of ASH2L using siRNA globally decreases H3K4 trimethylation (Dou et al., 2006; Steward et al., 2006). ASH2L and H3K4 methylation both appear to play a key role in oncogenesis (Hess, 2006). ASH2L is found to be over abundant in many cancer cell lines and knock-down of ASH2L by siRNA can prevent tumorigenesis (Lüscher-Firzlaff et al., 2008). Recent work has suggested that ASH2L in combination with WDR5 and RBBP5 exhibits H3K4 methyltransferase activity (Cao et al., 2010; Patel et al., 2009; Patel et al., 2011). In addition, this catalytic activity is not dependent on the SET domain containing proteins such as MLL1 (Cao et al., 2010; Patel et al., 2009; Patel et al., 2011).
Alternative to ASH2L's function in H3K4 methylation ASH2L may also be playing a role in endosomal trafficking (Xu et al., 2009). ASH2L, DPY-30 and WDR5 were originally implicated in endosomal trafficking when siRNA knock-down of these genes increased the amount of internalized CD8-CIMPR and overexpression increased the amount of cells displaying a altered CIMPR distribution (Xu et al., 2009).
Homology ASH2L has homologs in eukaryotes from yeast to humans.

Implicated in

Note
  
Entity Various cancers
Note ASH2L mRNA expression does not appear to be misregulated in human cancer cell or primary cell lines. However, expression of ASH2L protein is increased in many cancer cell lines as well as tumor samples (Lüscher-Firzlaff et al., 2008). There was detectable increased staining in the nucleus of ASH2L protein in a wide array of tumors including squamous cell carcinoma of the larynx and the cervix, melanomas, adenocarcinoma of the pancreas, and acinar and ductal breast cancers (Lüscher-Firzlaff et al., 2008). ASH2L protein appears to be more stable in cancer cell lines compared to the normal cell line counterparts and knockdown of ASH2L can prevent tumerogenesis suggesting a role in tumor cell proliferation (Lüscher-Firzlaff et al., 2008).
  

Bibliography

Structural and biochemical insights into MLL1 core complex assembly.
Avdic V, Zhang P, Lanouette S, Groulx A, Tremblay V, Brunzelle J, Couture JF.
Structure. 2011 Jan 12;19(1):101-8.
PMID 21220120
 
An Ash2L/RbBP5 heterodimer stimulates the MLL1 methyltransferase activity through coordinated substrate interactions with the MLL1 SET domain.
Cao F, Chen Y, Cierpicki T, Liu Y, Basrur V, Lei M, Dou Y.
PLoS One. 2010 Nov 23;5(11):e14102.
PMID 21124902
 
Structural insight into histone recognition by the ING PHD fingers.
Champagne KS, Kutateladze TG.
Curr Drug Targets. 2009 May;10(5):432-41. (REVIEW)
PMID 19442115
 
Crystal structure of the N-terminal region of human Ash2L shows a winged-helix motif involved in DNA binding.
Chen Y, Wan B, Wang KC, Cao F, Yang Y, Protacio A, Dou Y, Chang HY, Lei M.
EMBO Rep. 2011 Jun 10;12(8):797-803. doi: 10.1038/embor.2011.101.
PMID 21660059
 
PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex.
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J Biol Chem. 2007 Jul 13;282(28):20395-406. Epub 2007 May 11.
PMID 17500065
 
Regulation of MLL1 H3K4 methyltransferase activity by its core components.
Dou Y, Milne TA, Ruthenburg AJ, Lee S, Lee JW, Verdine GL, Allis CD, Roeder RG.
Nat Struct Mol Biol. 2006 Aug;13(8):713-9. Epub 2006 Jul 30.
PMID 16878130
 
Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-containing proteins SPSB1, SPSB2, and SPSB4.
Filippakopoulos P, Low A, Sharpe TD, Uppenberg J, Yao S, Kuang Z, Savitsky P, Lewis RS, Nicholson SE, Norton RS, Bullock AN.
J Mol Biol. 2010 Aug 20;401(3):389-402. Epub 2010 Jun 16.
PMID 20561531
 
MLL: Deep Insight.
Hess JL.
Atlas Genet Cytogenet Oncol Haematol. August 2003 .
 
Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus.
Hughes CM, Rozenblatt-Rosen O, Milne TA, Copeland TD, Levine SS, Lee JC, Hayes DN, Shanmugam KS, Bhattacharjee A, Biondi CA, Kay GF, Hayward NK, Hess JL, Meyerson M.
Mol Cell. 2004 Feb 27;13(4):587-97.
PMID 14992727
 
SPRY domain-containing SOCS box protein 2: crystal structure and residues critical for protein binding.
Kuang Z, Yao S, Xu Y, Lewis RS, Low A, Masters SL, Willson TA, Kolesnik TB, Nicholson SE, Garrett TJ, Norton RS.
J Mol Biol. 2009 Feb 27;386(3):662-74. Epub 2009 Jan 6.
PMID 19154741
 
The human trithorax protein hASH2 functions as an oncoprotein.
Luscher-Firzlaff J, Gawlista I, Vervoorts J, Kapelle K, Braunschweig T, Walsemann G, Rodgarkia-Schamberger C, Schuchlautz H, Dreschers S, Kremmer E, Lilischkis R, Cerni C, Wellmann A, Luscher B.
Cancer Res. 2008 Feb 1;68(3):749-58.
PMID 18245475
 
On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex.
Patel A, Dharmarajan V, Vought VE, Cosgrove MS.
J Biol Chem. 2009 Sep 4;284(36):24242-56. Epub 2009 Jun 25.
PMID 19556245
 
A novel non-SET domain multi-subunit methyltransferase required for sequential nucleosomal histone H3 methylation by the mixed lineage leukemia protein-1 (MLL1) core complex.
Patel A, Vought VE, Dharmarajan V, Cosgrove MS.
J Biol Chem. 2011 Feb 4;286(5):3359-69. Epub 2010 Nov 24.
PMID 21106533
 
Relationship between SPRY and B30.2 protein domains. Evolution of a component of immune defence?
Rhodes DA, de Bono B, Trowsdale J.
Immunology. 2005 Dec;116(4):411-7. (REVIEW)
PMID 16313355
 
The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4.
Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, Aasland R, Stewart AF.
EMBO J. 2001 Dec 17;20(24):7137-48.
PMID 11742990
 
Crystal structure of the trithorax group protein ASH2L reveals a forkhead-like DNA binding domain.
Sarvan S, Avdic V, Tremblay V, Chaturvedi CP, Zhang P, Lanouette S, Blais A, Brunzelle JS, Brand M, Couture JF.
Nat Struct Mol Biol. 2011 Jun 5;18(7):857-9. doi: 10.1038/nsmb.2093.
PMID 21642971
 
Antagonistic functions of SET-2/SET1 and HPL/HP1 proteins in C. elegans development.
Simonet T, Dulermo R, Schott S, Palladino F.
Dev Biol. 2007 Dec 1;312(1):367-83. Epub 2007 Oct 29.
PMID 17967446
 
A conserved interaction between the SDI domain of Bre2 and the Dpy-30 domain of Sdc1 is required for histone methylation and gene expression.
South PF, Fingerman IM, Mersman DP, Du HN, Briggs SD.
J Biol Chem. 2010 Jan 1;285(1):595-607. Epub 2009 Nov 6.
PMID 19897479
 
Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes.
Steward MM, Lee JS, O'Donovan A, Wyatt M, Bernstein BE, Shilatifard A.
Nat Struct Mol Biol. 2006 Sep;13(9):852-4. Epub 2006 Aug 6.
PMID 16892064
 
Ash2l interacts with Tbx1 and is required during early embryogenesis.
Stoller JZ, Huang L, Tan CC, Huang F, Zhou DD, Yang J, Gelb BD, Epstein JA.
Exp Biol Med (Maywood). 2010 May;235(5):569-76.
PMID 20463296
 
ASH2L: alternative splicing and downregulation during induced megakaryocytic differentiation of multipotential leukemia cell lines.
Wang J, Zhou Y, Yin B, Du G, Huang X, Li G, Shen Y, Yuan J, Qiang B.
J Mol Med (Berl). 2001 Jul;79(7):399-405.
PMID 11466562
 
Structural and functional insights into the B30.2/SPRY domain.
Woo JS, Imm JH, Min CK, Kim KJ, Cha SS, Oh BH.
EMBO J. 2006a Mar 22;25(6):1353-63. Epub 2006 Feb 23.
PMID 16498413
 
Structural basis for protein recognition by B30.2/SPRY domains.
Woo JS, Suh HY, Park SY, Oh BH.
Mol Cell. 2006b Dec 28;24(6):967-76.
PMID 17189197
 
A role of histone H3 lysine 4 methyltransferase components in endosomal trafficking.
Xu Z, Gong Q, Xia B, Groves B, Zimmermann M, Mugler C, Mu D, Matsumoto B, Seaman M, Ma D.
J Cell Biol. 2009 Aug 10;186(3):343-53. Epub 2009 Aug 3.
PMID 19651892
 
Structural insight into the recognition of the H3K4me3 mark by the TFIID subunit TAF3.
van Ingen H, van Schaik FM, Wienk H, Ballering J, Rehmann H, Dechesne AC, Kruijzer JA, Liskamp RM, Timmers HT, Boelens R.
Structure. 2008 Aug 6;16(8):1245-56.
PMID 18682226
 

Citation

This paper should be referenced as such :
South, PF ; Briggs, SD
ASH2L (ash2 (absent, small, or homeotic)-like (Drosophila))
Atlas Genet Cytogenet Oncol Haematol. 2012;16(1):30-33.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/ASH2LID44404ch8p11.html


External links

Nomenclature
HGNC (Hugo)ASH2L   744
Cards
AtlasASH2LID44404ch8p11
Entrez_Gene (NCBI)ASH2L  9070  ash2 (absent, small, or homeotic)-like (Drosophila)
AliasesASH2; ASH2L1; ASH2L2; Bre2
GeneCards (Weizmann)ASH2L
Ensembl hg19 (Hinxton)ENSG00000129691 [Gene_View]  chr8:37963311-37997598 [Contig_View]  ASH2L [Vega]
Ensembl hg38 (Hinxton)ENSG00000129691 [Gene_View]  chr8:37963311-37997598 [Contig_View]  ASH2L [Vega]
ICGC DataPortalENSG00000129691
TCGA cBioPortalASH2L
AceView (NCBI)ASH2L
Genatlas (Paris)ASH2L
WikiGenes9070
SOURCE (Princeton)ASH2L
Genetics Home Reference (NIH)ASH2L
Genomic and cartography
GoldenPath hg19 (UCSC)ASH2L  -     chr8:37963311-37997598 +  8p11.2   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)ASH2L  -     8p11.2   [Description]    (hg38-Dec_2013)
EnsemblASH2L - 8p11.2 [CytoView hg19]  ASH2L - 8p11.2 [CytoView hg38]
Mapping of homologs : NCBIASH2L [Mapview hg19]  ASH2L [Mapview hg38]
OMIM604782   
Gene and transcription
Genbank (Entrez)AB020982 AF056717 AF056718 AK291750 AK291938
RefSeq transcript (Entrez)NM_001105214 NM_001261832 NM_001282272 NM_004674
RefSeq genomic (Entrez)NC_000008 NC_018919 NT_167187 NW_004929337
Consensus coding sequences : CCDS (NCBI)ASH2L
Cluster EST : UnigeneHs.521530 [ NCBI ]
CGAP (NCI)Hs.521530
Alternative Splicing GalleryENSG00000129691
Gene ExpressionASH2L [ NCBI-GEO ]   ASH2L [ EBI - ARRAY_EXPRESS ]   ASH2L [ SEEK ]   ASH2L [ MEM ]
Gene Expression Viewer (FireBrowse)ASH2L [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)9070
GTEX Portal (Tissue expression)ASH2L
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9UBL3   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9UBL3  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9UBL3
Splice isoforms : SwissVarQ9UBL3
PhosPhoSitePlusQ9UBL3
Domaine pattern : Prosite (Expaxy)B302_SPRY (PS50188)   
Domains : Interpro (EBI)B30.2/SPRY    ConA-like_dom    SPRY_dom   
Domain families : Pfam (Sanger)SPRY (PF00622)   
Domain families : Pfam (NCBI)pfam00622   
Domain families : Smart (EMBL)SPRY (SM00449)  
Conserved Domain (NCBI)ASH2L
DMDM Disease mutations9070
Blocks (Seattle)ASH2L
PDB (SRS)3RSN    3S32    3TOJ    4RIQ    4X8N    4X8P   
PDB (PDBSum)3RSN    3S32    3TOJ    4RIQ    4X8N    4X8P   
PDB (IMB)3RSN    3S32    3TOJ    4RIQ    4X8N    4X8P   
PDB (RSDB)3RSN    3S32    3TOJ    4RIQ    4X8N    4X8P   
Structural Biology KnowledgeBase3RSN    3S32    3TOJ    4RIQ    4X8N    4X8P   
SCOP (Structural Classification of Proteins)3RSN    3S32    3TOJ    4RIQ    4X8N    4X8P   
CATH (Classification of proteins structures)3RSN    3S32    3TOJ    4RIQ    4X8N    4X8P   
SuperfamilyQ9UBL3
Human Protein AtlasENSG00000129691
Peptide AtlasQ9UBL3
HPRD05309
IPIIPI00328658   IPI00328659   IPI00333837   IPI00976113   IPI00973798   IPI00974058   IPI01021413   
Protein Interaction databases
DIP (DOE-UCLA)Q9UBL3
IntAct (EBI)Q9UBL3
FunCoupENSG00000129691
BioGRIDASH2L
STRING (EMBL)ASH2L
ZODIACASH2L
Ontologies - Pathways
QuickGOQ9UBL3
Ontology : AmiGODNA binding  protein binding  nucleus  nucleus  nucleoplasm  nuclear euchromatin  transcription, DNA-templated  regulation of transcription, DNA-templated  transcription from RNA polymerase II promoter  cellular response to DNA damage stimulus  beta-catenin binding  positive regulation of cell proliferation  histone-lysine N-methyltransferase activity  hemopoiesis  histone methyltransferase complex  histone methyltransferase complex  histone methyltransferase activity (H3-K4 specific)  response to estrogen  transcription regulatory region DNA binding  MLL3/4 complex  positive regulation of transcription from RNA polymerase II promoter  metal ion binding  Set1C/COMPASS complex  histone H3-K4 methylation  MLL1 complex  beta-catenin-TCF complex assembly  euchromatin binding  
Ontology : EGO-EBIDNA binding  protein binding  nucleus  nucleus  nucleoplasm  nuclear euchromatin  transcription, DNA-templated  regulation of transcription, DNA-templated  transcription from RNA polymerase II promoter  cellular response to DNA damage stimulus  beta-catenin binding  positive regulation of cell proliferation  histone-lysine N-methyltransferase activity  hemopoiesis  histone methyltransferase complex  histone methyltransferase complex  histone methyltransferase activity (H3-K4 specific)  response to estrogen  transcription regulatory region DNA binding  MLL3/4 complex  positive regulation of transcription from RNA polymerase II promoter  metal ion binding  Set1C/COMPASS complex  histone H3-K4 methylation  MLL1 complex  beta-catenin-TCF complex assembly  euchromatin binding  
REACTOMEQ9UBL3 [protein]
REACTOME Pathways201722 [pathway]   3214841 [pathway]   3769402 [pathway]   5617472 [pathway]   
NDEx NetworkASH2L
Atlas of Cancer Signalling NetworkASH2L
Wikipedia pathwaysASH2L
Orthology - Evolution
OrthoDB9070
GeneTree (enSembl)ENSG00000129691
Phylogenetic Trees/Animal Genes : TreeFamASH2L
HOVERGENQ9UBL3
HOGENOMQ9UBL3
Homologs : HomoloGeneASH2L
Homology/Alignments : Family Browser (UCSC)ASH2L
Gene fusions - Rearrangements
Fusion : MitelmanASH2L/C8orf86 [8p11.23/8p11.22]  
Fusion : MitelmanASH2L/MGME1 [8p11.23/20p11.23]  [t(8;20)(p11;p11)]  
Fusion: TCGAASH2L 8p11.23 C20orf72 BRCA
Fusion: TCGAASH2L 8p11.23 C8orf86 8p11.22 HNSC
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerASH2L [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)ASH2L
dbVarASH2L
ClinVarASH2L
1000_GenomesASH2L 
Exome Variant ServerASH2L
ExAC (Exome Aggregation Consortium)ASH2L (select the gene name)
Genetic variants : HAPMAP9070
Genomic Variants (DGV)ASH2L [DGVbeta]
DECIPHER (Syndromes)8:37963311-37997598  ENSG00000129691
CONAN: Copy Number AnalysisASH2L 
Mutations
ICGC Data PortalASH2L 
TCGA Data PortalASH2L 
Broad Tumor PortalASH2L
OASIS PortalASH2L [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICASH2L  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDASH2L
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 ASH2L
DgiDB (Drug Gene Interaction Database)ASH2L
DoCM (Curated mutations)ASH2L (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)ASH2L (select a term)
intoGenASH2L
NCG5 (London)ASH2L
Cancer3DASH2L(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM604782   
Orphanet
MedgenASH2L
Genetic Testing Registry ASH2L
NextProtQ9UBL3 [Medical]
TSGene9070
GENETestsASH2L
Huge Navigator ASH2L [HugePedia]
snp3D : Map Gene to Disease9070
BioCentury BCIQASH2L
ClinGenASH2L
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD9070
Chemical/Pharm GKB GenePA25044
Clinical trialASH2L
Miscellaneous
canSAR (ICR)ASH2L (select the gene name)
Probes
Litterature
PubMed94 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineASH2L
EVEXASH2L
GoPubMedASH2L
iHOPASH2L
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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