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ATMIN (ATM Interactor)

Written2014-07Jörg Heierhorst
St. Vincent's Institute of Medical Research,, Department of Medicine St Vincent's Hospital, The University of Melbourne, 9 Princes Street, Fitzroy, Victoria 3065, Australia

Abstract Review on ASCIZ/ATMIN, with data on DNA/RNA, on the protein encoded and where the gene is implicated.

Keywords Apoptosis, dynein, DNA damage, transcription factor, lung

(Note : for Links provided by Atlas : click)

Identity

Alias_symbol (synonym)ASCIZ
KIAA0431
ZNF822
Other alias
HGNC (Hugo) ATMIN
LocusID (NCBI) 23300
Atlas_Id 45745
Location 16q23.2  [Link to chromosome band 16q23]
Location_base_pair Starts at 81070787 and ends at 81080951 bp from pter ( according to hg19-Feb_2009)  [Mapping ATMIN.png]
Local_order Gene orientation: centromere -5' ASCIZ/ATMIN 3'-telomere. ASCIZ/ATMIN is flanked towards the centromere by CENPN (in the same transcriptional orientiation) and towards the telomere by C16orf46 in opposite transcriptional orientation (NCBI Gene view, gene ID 23300, version 3-Jun-2014).
 
  Diagram 1. Genomic context of the human ASCIZ/ATMIN gene. Numbers indicate the nucleotide positions on chromosome 16 (location 16q23.2). Arrows indicate the 5' to 3' orientation of each gene. Modified from NCBI Map Viewer.
Fusion genes
(updated 2016)
ATMIN (16q23.2) / ATP6V1C2 (2p25.1)ATMIN (16q23.2) / BCL2L1 (20q11.21)ATMIN (16q23.2) / EIF4E2 (2q37.1)
Note The gene was originally reported to encode an ATM-substrate Chk2-interacting Zinc-finger protein and referred to by the name ASCIZ in NCBI/Genbank, before the official gene name was changed to ATMIN by HGNC.

DNA/RNA

 
  Diagram 2. ASCIZ/ATMIN gene structure and main alternative splice isforms. ASCIZ/ATMIN contains 5 exons (A-E, center) that are spliced to two main open reading frames based on NCBI AceView. The lower splice isoform accounts for ~85% of transcripts collected in NCBI AceView and encodes an 823 amino acid residue protein with four N-terminal Zinc-fingers. The upper splice isoforms represent ~15% of transcripts and encodes a 667 residue protein with two N-terminal Zinc-fingers. Protein coding sequences are indicated by black boxes; non-coding exon sequences are indicated by open boxes; the grey part of exon C contains coding sequences when spliced into the 4-Zinc-finger transcript, but is out-of-frame as part of the 2-Zinc-finger transcript. The asterisk indicates an in-frame stop-codon in the 5'-UTR of the 2-Zinc-finger isoform. The scale bar on top represents 1 kb per notch.
Description The human ASCIZ/ATMIN gene contains five exons over 11497 bases. The main transcript results from splicing of exon A, parts of exon C, and exons D and E and gives rise to the "full-length" protein containing 823 amino acids with four Zinc-fingers. Two alternative transcripts - comprising either exon B, part of exon C and exons D and E, or a longer exon C and exons D and E - give rise to a shorter 667-residue protein with only two Zinc-fingers. The mouse ASCIZ gene structure may be simpler with only four exons and single main mRNA encoding an 818-residue protein similar to the human 4-Zinc-finger product.
Transcription In Northern and Western blot experiments, the two main isoforms of ASCIZ/ATMIN are expressed at relatively similar levels in a wide range of human tissues and all cancer-derived cell lines tested (McNees et al., 2005). Northern blots of various mouse tissues also indicate relatively similar expression levels in a wide range of organs (Jurado et al., 2010).
Pseudogene Two ASCIZ/ATMIN pseudogenes have been detected on chromosome 9 (LOC643342) and chromosome 12 (LOC100418940).

Protein

Note The human ASCIZ protein occurs in two isoforms. The more abundant long isoform contains 823 amino acid residues with a mass of 88.3 kDa. The shorter isoform contains 667 residues with a mass of 72.3 kDa. The two isoforms are identical except that the first 156 residues (including the first two Zinc fingers) of the longer form are missing in the shorter protein. Mouse ASCIZ contains 818 amino acids and is generally similar to the longer human isoform. Human and mouse ASCIZ exhibit atypical electrophoretic mobility on SDS-PAGE Western blots with an apparent mass of ~115 kDa rather than the predicted ~88 kDa (McNees et al., 2005). The aberrant mobility is unlikely to be caused by post-translational modifications, as similar mobility retardation is also observed with bacterially expressed recombinant fragments encompassing the SQ/TQ cluster.
 
  Diagram 3. Topology of the ASCIZ protein. Only the long form is depicted. The shorter form is identical except for lack of the N-terminal 156 residues including the first two Zinc fingers (ZF). Lollipops indicate the 20 SQ/TQ motifs that are potential ATM/ATR kinase phosphorylation sites, including the 11 TQT motif DYNLL1-binding sites in the transcription activation domain.
Description ASCIZ contains four (or two in the shorter isoform) C2H2 Zinc-fingers at the N-terminus, a so-called core domain, and a C-terminal transcription activation domain. Human ASCIZ contains 20 potential ATM/ATR kinase phosphorylation sites, most of which are clustered in an SQ/TQ cluster domain coinciding with the transcription activation domain (Heierhorst et al., 2011). 11 of these sites are TQT motifs and represent binding sites for the DYNLL1 protein (Rapali et al., 2011; Jurado et al., 2012a).
Expression Based on Western blots, the ASCIZ protein is ubiquitously expressed at similar levels in all mouse tissues, with slightly higher levels in brain and testis (Jurado et al., 2010). Protein expression has not been systematically analysed in human tissues but is expected to be similar to mRNA expression profiles by Northern blots suggesting ubiquitous expression (McNees et al., 2005).
Localisation The ASCIZ protein is predominantly, if not exclusively, located to the nucleus but not the nucleolus (McNees et al., 2005; Kanu and Behrens, 2007). The protein forms discrete sub-nuclear foci after treatment with methylating and oxidating DNA base damaging agents (McNees et al., 2005; Rapali et al., 2011).
Function ASCIZ was originally identified as an ATM/ATR-substrate and Chk2-interacting protein involved in the DNA base damage response (McNees et al., 2005), and later independently re-isolated as an ATM-interacting protein (Kanu and Behrens, 2007). However, based on recent genetic analyses its main role seems to involve essential developmental functions such as a Zinc-finger transcription factor (Heierhorst et al., 2011).
Knockout mice that completely lack Asciz/Atmin die late during gestation (Jurado et al., 2010; Kanu et al., 2010) and exhibit a range of severe organogenesis defects, including most strikingly a complete absence of lungs (Jurado et al., 2010). An N-ethyl-N-nitrosourea (ENU)-generated mouse mutant, gasping-6, that contains a missense mutations of a Zinc-chelating Cys residue in the third Zinc-finger domain of Asciz/Atmin also dies during late gestation with overall similar phenotypic defects to the Asciz/Atmin null mice, including absent or hypomorphic lungs (Goggolidou et al., 2014). Conditional Asciz/Atmin KO mice generated using B lympoid-specific Cd19-Cre (Loizou et al., 2011) or Mb1-Cre (Jurado et al., 2012b) have reduced peripheral B cell numbers due to increased apoptotic cell death during B cell development in the bone marrow.
The most highly downregulated gene in Asciz-deficient cells is the dynein light chain subunit Dynll1 (Jurado et al., 2012a). Strikingly, DYNLL1 protein can in turn bind to about a dozen individual sites - mostly encompassing TQT motifs - in the ASCIZ transcription activation domain (Rapali et al., 2011; Jurado et al., 2012a) and thereby inhibit its transcriptional activity in a concentration-dependent manner (Jurado et al., 2012a), which provides a feedback mechanism to maintain stable DYNLL1 protein levels. The ability of ASCIZ to regulate expression of and bind to the DYNLL1-like dynein light chain (called Cutup) is conserved in Drosophila (Zaytseva et al., 2014).
The importance of DYNLL1 as an ASCIZ target is highlighted by findings that B cell developmental defects in conditional Mb1-Cre Asciz KO mice can be rescued by ectopic expression of DYNLL1, or simultaneous KO of the pro-apoptotic protein Bim whose activity is inhibited by DYNLL1 (Jurado et al., 2012b). Likewise, in Drosophila, RNAi knockdown of ASCIZ or Cutup lead to similar developmental defects, which in case of dASCIZ RNAi can be rescued by Cutup overexpression (Zaytseva et al., 2014).
The role of ASCIZ in DNA damage responses remains unclear. Loss of ASCIZ leads to increased cell death in response to methylating or oxidating DNA damage in human, mouse and chicken cells (McNees et al., 2005; Oka et al., 2008; Jurado et al., 2010; Kanu et al., 2010), and increased basal IgV gene conversion rates in the chicken DT40 B cell line (Oka et al., 2008). ASCIZ focus formation in response to methylating agents depends on DYNLL1 (Jurado et al., 2012a), but it is not known whether this also involves its transcription factor function. The B cell developmental defect of conditional Asciz/Atmin KO mice could not be rescued by deletion of tp53 or complementation with a pre-arranged B cell receptor transgene (Jurado et al., 2012b), supporting a DNA damage-independent mechanism as cause of the B cell deficiency. ASCIZ was earlier reported to be required for ATM protein stability (and thus termed ATMIN) (Kanu and Behrens, 2007), but this was shown to be incorrect in several subsequent studies (Jurado et al., 2010; Loizou et al., 2011; Zhang et al., 2012). ASCIZ was reported to regulate ATM activation by DNA damage-independent chromatin perturbations (Kanu and Behrens, 2007; Zhang et al., 2012) but this was not confirmed in another study (Jurado et al., 2010).
Homology ASCIZ protein sequences are highly conserved amongst all vertebrates from fish to mammals (Kanu and Behrens, 2007; Jurado et al., 2012a). The ASCIZ protein is structurally and functionally conserved in Drosophila, where it also contains four N-terminal Zinc-fingers and a TQT-rich C-terminal transcription activation domain, condensed into only 388 amino acid residues (Zaytseva et al., 2014).

Mutations

Note No specific disease-associated mutations of ASCIZ/ATMIN have so far been reported in humans, but an Asciz/Atmin mis-sense mutation has recently been identified as the cause of the gasping6 (Gpg6) ENU mouse mutant (Goggolidou et al., 2014).
Germinal The gasping6 mouse mutation was isolated in an ENU mutagenesis screen (Ermakov et al., 2009). Asciz/Atmingpg6 mice exhibit exencephaly, edema and absent or small lungs (Ermakov et al., 2009) and a modest kidney cell polarity defect (Goggolidou et al., 2014). Gpg6 mice contain a point mutation that converts the canonical fourth Zinc-chelating Cys residue in the third Zinc-finger domain to a non-chelating Ser residue (Goggolidou et al., 2014). Dynll1 was the most highly reduced mRNA amongst the analyzed transcripts in affected kidneys (Goggolidou et al., 2014).

Implicated in

Note
  
Entity B cell lymphoma
Note Cd19-Cre conditional Asciz/Atmin deletion has been reported to cause B cell lymphoma in ~40% of mice (whose genetic background was not specified) before 1 year of age (Loizou et al., 2011), but deletion via Mb1-Cre (which is more efficient than Cd19-Cre during early B lympoid stages) in C57BL/6 mice did not lead to B cell lymphoma until at least 2 years of age (Jurado et al., 2012b). Irrespective of genetic background, no lymphomas were observed when Asciz/Atmin was deleted in earlier haematopoietic stem/progenitor cells via Mx1-Cre (Jurado et al., 2012b) or Vav2-Cre (Cremona and Behrens, 2014).
  
  
Entity Embryonic development/organogenesis
Note Germline mutations of Asciz/Atmin in mice lead to late embryonic lethality (Jurado et al., 2010; Kanu et al., 2010; Goggolidou et al., 2014). Mice exhibit exencephaly, complete absence of lungs in the Asciz null mutation or a combination of absent and small lungs in the Asciz/Atmingpg6 point mutant, cardiac defects with oedema, and kidney defects.
  
  
Entity Haematopoiesis/B cell development
Note Conditional Asciz/Atmin deletion during early B cell developmental stages in mice in the bone marrow leads to peripheral B cell deficiency, which is more severe with Mb1-Cre (Jurado et al., 2012b) than Cd19-Cre (Loizou et al., 2011). Pan-haematopoietic inducible Asciz/Atmin deletion in adolescent mice via Mx1-Cre also leads to a statistically significant but modest and well tolerated anemia (Jurado et al., 2012b).
  

Bibliography

ATM signalling and cancer.
Cremona CA, Behrens A.
Oncogene. 2014 Jun 26;33(26):3351-60. doi: 10.1038/onc.2013.275. Epub 2013 Jul 15. (REVIEW)
PMID 23851492
 
Mouse mutagenesis identifies novel roles for left-right patterning genes in pulmonary, craniofacial, ocular, and limb development.
Ermakov A, Stevens JL, Whitehill E, Robson JE, Pieles G, Brooker D, Goggolidou P, Powles-Glover N, Hacker T, Young SR, Dear N, Hirst E, Tymowska-Lalanne Z, Briscoe J, Bhattacharya S, Norris DP.
Dev Dyn. 2009 Mar;238(3):581-94. doi: 10.1002/dvdy.21874.
PMID 19235720
 
Atmin mediates kidney morphogenesis by modulating Wnt signaling.
Goggolidou P, Hadjirin NF, Bak A, Papakrivopoulou E, Hilton H, Norris DP, Dean CH.
Hum Mol Genet. 2014 Oct 15;23(20):5303-16. doi: 10.1093/hmg/ddu246. Epub 2014 May 22.
PMID 24852369
 
A breathtaking phenotype: unexpected roles of the DNA base damage response protein ASCIZ as a key regulator of early lung development.
Heierhorst J, Smyth I, Jurado S.
Cell Cycle. 2011 Apr 15;10(8):1222-4. Epub 2011 Apr 15.
PMID 21415597
 
ATM substrate Chk2-interacting Zn2+ finger (ASCIZ) Is a bi-functional transcriptional activator and feedback sensor in the regulation of dynein light chain (DYNLL1) expression.
Jurado S, Conlan LA, Baker EK, Ng JL, Tenis N, Hoch NC, Gleeson K, Smeets M, Izon D, Heierhorst J.
J Biol Chem. 2012a Jan 27;287(5):3156-64. doi: 10.1074/jbc.M111.306019. Epub 2011 Dec 13.
PMID 22167198
 
The Zinc-finger protein ASCIZ regulates B cell development via DYNLL1 and Bim.
Jurado S, Gleeson K, O'Donnell K, Izon DJ, Walkley CR, Strasser A, Tarlinton DM, Heierhorst J.
J Exp Med. 2012b Aug 27;209(9):1629-39. doi: 10.1084/jem.20120785. Epub 2012 Aug 13.
PMID 22891272
 
Dual functions of ASCIZ in the DNA base damage response and pulmonary organogenesis.
Jurado S, Smyth I, van Denderen B, Tenis N, Hammet A, Hewitt K, Ng JL, McNees CJ, Kozlov SV, Oka H, Kobayashi M, Conlan LA, Cole TJ, Yamamoto K, Taniguchi Y, Takeda S, Lavin MF, Heierhorst J.
PLoS Genet. 2010 Oct 21;6(10):e1001170. doi: 10.1371/journal.pgen.1001170.
PMID 20975950
 
ATMIN defines an NBS1-independent pathway of ATM signalling.
Kanu N, Behrens A.
EMBO J. 2007 Jun 20;26(12):2933-41. Epub 2007 May 24.
PMID 17525732
 
The ATM cofactor ATMIN protects against oxidative stress and accumulation of DNA damage in the aging brain.
Kanu N, Penicud K, Hristova M, Wong B, Irvine E, Plattner F, Raivich G, Behrens A.
J Biol Chem. 2010 Dec 3;285(49):38534-42. doi: 10.1074/jbc.M110.145896. Epub 2010 Oct 2.
PMID 20889973
 
ATMIN is required for maintenance of genomic stability and suppression of B cell lymphoma.
Loizou JI, Sancho R, Kanu N, Bolland DJ, Yang F, Rada C, Corcoran AE, Behrens A.
Cancer Cell. 2011 May 17;19(5):587-600. doi: 10.1016/j.ccr.2011.03.022.
PMID 21575860
 
ASCIZ regulates lesion-specific Rad51 focus formation and apoptosis after methylating DNA damage.
McNees CJ, Conlan LA, Tenis N, Heierhorst J.
EMBO J. 2005 Jul 6;24(13):2447-57. Epub 2005 Jun 2.
PMID 15933716
 
DNA damage response protein ASCIZ links base excision repair with immunoglobulin gene conversion.
Oka H, Sakai W, Sonoda E, Nakamura J, Asagoshi K, Wilson SH, Kobayashi M, Yamamoto K, Heierhorst J, Takeda S, Taniguchi Y.
Biochem Biophys Res Commun. 2008 Jun 27;371(2):225-9. doi: 10.1016/j.bbrc.2008.04.052. Epub 2008 Apr 21.
PMID 18433721
 
LC8 dynein light chain (DYNLL1) binds to the C-terminal domain of ATM-interacting protein (ATMIN/ASCIZ) and regulates its subcellular localization.
Rapali P, Garcia-Mayoral MF, Martnez-Moreno M, Tarnok K, Schlett K, Albar JP, Bruix M, Nyitray L, Rodriguez-Crespo I.
Biochem Biophys Res Commun. 2011 Oct 28;414(3):493-8. doi: 10.1016/j.bbrc.2011.09.093. Epub 2011 Sep 24.
PMID 21971545
 
The novel zinc finger protein dASCIZ regulates mitosis in Drosophila via an essential role in dynein light-chain expression.
Zaytseva O, Tenis N, Mitchell N, Kanno S, Yasui A, Heierhorst J, Quinn LM.
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PMID 24336747
 
Competition between NBS1 and ATMIN controls ATM signaling pathway choice.
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Citation

This paper should be referenced as such :
J Heierhorst
ATMIN (ATM Interactor)
Atlas Genet Cytogenet Oncol Haematol. 2015;19(4):245-248.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/ATMINID45745ch16q23.html


External links

Nomenclature
HGNC (Hugo)ATMIN   29034
Cards
AtlasATMINID45745ch16q23
Entrez_Gene (NCBI)ATMIN  23300  ATM interactor
AliasesASCIZ; ZNF822
GeneCards (Weizmann)ATMIN
Ensembl hg19 (Hinxton)ENSG00000166454 [Gene_View]  chr16:81070787-81080951 [Contig_View]  ATMIN [Vega]
Ensembl hg38 (Hinxton)ENSG00000166454 [Gene_View]  chr16:81070787-81080951 [Contig_View]  ATMIN [Vega]
ICGC DataPortalENSG00000166454
TCGA cBioPortalATMIN
AceView (NCBI)ATMIN
Genatlas (Paris)ATMIN
WikiGenes23300
SOURCE (Princeton)ATMIN
Genetics Home Reference (NIH)ATMIN
Genomic and cartography
GoldenPath hg19 (UCSC)ATMIN  -     chr16:81070787-81080951 +  16q23.2   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)ATMIN  -     16q23.2   [Description]    (hg38-Dec_2013)
EnsemblATMIN - 16q23.2 [CytoView hg19]  ATMIN - 16q23.2 [CytoView hg38]
Mapping of homologs : NCBIATMIN [Mapview hg19]  ATMIN [Mapview hg38]
OMIM614693   
Gene and transcription
Genbank (Entrez)AB007891 AK025058 AK290943 AK301781 AK302556
RefSeq transcript (Entrez)NM_001300728 NM_015251
RefSeq genomic (Entrez)NC_000016 NC_018927 NT_010498 NW_004929402
Consensus coding sequences : CCDS (NCBI)ATMIN
Cluster EST : UnigeneHs.589959 [ NCBI ]
CGAP (NCI)Hs.589959
Alternative Splicing GalleryENSG00000166454
Gene ExpressionATMIN [ NCBI-GEO ]   ATMIN [ EBI - ARRAY_EXPRESS ]   ATMIN [ SEEK ]   ATMIN [ MEM ]
Gene Expression Viewer (FireBrowse)ATMIN [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)23300
GTEX Portal (Tissue expression)ATMIN
Protein : pattern, domain, 3D structure
UniProt/SwissProtO43313   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtO43313  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO43313
Splice isoforms : SwissVarO43313
PhosPhoSitePlusO43313
Domaine pattern : Prosite (Expaxy)ZINC_FINGER_C2H2_1 (PS00028)   
Domains : Interpro (EBI)Znf_C2H2    Znf_C2H2-like   
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Domain families : Smart (EMBL)ZnF_C2H2 (SM00355)  
Conserved Domain (NCBI)ATMIN
DMDM Disease mutations23300
Blocks (Seattle)ATMIN
SuperfamilyO43313
Human Protein AtlasENSG00000166454
Peptide AtlasO43313
HPRD17188
IPIIPI00639881   IPI00401923   
Protein Interaction databases
DIP (DOE-UCLA)O43313
IntAct (EBI)O43313
FunCoupENSG00000166454
BioGRIDATMIN
STRING (EMBL)ATMIN
ZODIACATMIN
Ontologies - Pathways
QuickGOO43313
Ontology : AmiGOprotein binding  nucleus  transcription, DNA-templated  cellular response to DNA damage stimulus  transcription regulatory region DNA binding  dynein binding  positive regulation of transcription, DNA-templated  metal ion binding  cilium morphogenesis  
Ontology : EGO-EBIprotein binding  nucleus  transcription, DNA-templated  cellular response to DNA damage stimulus  transcription regulatory region DNA binding  dynein binding  positive regulation of transcription, DNA-templated  metal ion binding  cilium morphogenesis  
NDEx NetworkATMIN
Atlas of Cancer Signalling NetworkATMIN
Wikipedia pathwaysATMIN
Orthology - Evolution
OrthoDB23300
GeneTree (enSembl)ENSG00000166454
Phylogenetic Trees/Animal Genes : TreeFamATMIN
HOVERGENO43313
HOGENOMO43313
Homologs : HomoloGeneATMIN
Homology/Alignments : Family Browser (UCSC)ATMIN
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerATMIN [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)ATMIN
dbVarATMIN
ClinVarATMIN
1000_GenomesATMIN 
Exome Variant ServerATMIN
ExAC (Exome Aggregation Consortium)ATMIN (select the gene name)
Genetic variants : HAPMAP23300
Genomic Variants (DGV)ATMIN [DGVbeta]
DECIPHER (Syndromes)16:81070787-81080951  ENSG00000166454
CONAN: Copy Number AnalysisATMIN 
Mutations
ICGC Data PortalATMIN 
TCGA Data PortalATMIN 
Broad Tumor PortalATMIN
OASIS PortalATMIN [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICATMIN  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDATMIN
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 ATMIN
DgiDB (Drug Gene Interaction Database)ATMIN
DoCM (Curated mutations)ATMIN (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)ATMIN (select a term)
intoGenATMIN
NCG5 (London)ATMIN
Cancer3DATMIN(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM614693   
Orphanet
MedgenATMIN
Genetic Testing Registry ATMIN
NextProtO43313 [Medical]
TSGene23300
GENETestsATMIN
Huge Navigator ATMIN [HugePedia]
snp3D : Map Gene to Disease23300
BioCentury BCIQATMIN
ClinGenATMIN
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD23300
Chemical/Pharm GKB GenePA162377191
Clinical trialATMIN
Miscellaneous
canSAR (ICR)ATMIN (select the gene name)
Probes
Litterature
PubMed16 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineATMIN
EVEXATMIN
GoPubMedATMIN
iHOPATMIN
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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