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ESRRG (estrogen-related receptor gamma)

Written2009-10Rebecca B Riggins
Department of Oncology, Georgetown University, 3970 Reservoir Road NW, E407 Research Bldg, Washington, DC 20057, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_symbol (synonym)NR3B3
Other aliasERR3
ERRG2
FLJ16023
KIAA0832
DKFZp781L1617
HGNC (Hugo) ESRRG
LocusID (NCBI) 2104
Atlas_Id 45840
Location 1q41  [Link to chromosome band 1q41]
Location_base_pair Starts at 216503246 and ends at 217137755 bp from pter ( according to hg19-Feb_2009)  [Mapping ESRRG.png]
Fusion genes
(updated 2016)
ESRRG (1q41) / ACBD3 (1q42.12)ESRRG (1q41) / ADCY10 (1q24.2)ESRRG (1q41) / MT4 (16q12.2)
ESRRG (1q41) / UBA1 (Xp11.23)RNF121 (11q13.4) / ESRRG (1q41)RNF185 (22q12.2) / ESRRG (1q41)
SLC27A5 (19q13.43) / ESRRG (1q41)

DNA/RNA

Description The ESRRG gene encompasses 587 kb of sequence on the minus strand. ERRgamma transcript variant 1 contains 7 exons, while variants 2, 3, and 4 contain 6 exons.
Transcription ERRgamma has 4 coding and 1 (presumed) non-coding transcript variants. ERRgamma transcript variant 1 (NCBI, NM_001438) is the longest isoform, while ERRgamma transcript variant 2 (NM_206594) utilizes an alternate 5' UTR and lacks the first 23 amino acids of the coding sequence of variant 1 (Heard et al., 2000). In 2006, a third splice variant (ERRgamma3, NM_206595) was identified (Kojo et al., 2006). This isoform has 3 novel amino-terminal exons and lacks Exon F, which contains the second zinc-finger binding motif within the DNA binding domain of the receptor. Consequently ERRgamma3 cannot stimulate transcription from an estrogen response element (ERE)-driven reporter construct, although it can modulate the activity of other nuclear receptors, such as estrogen receptors alpha and beta (ERalpha, ERbeta), thyroid hormone receptor (TR), and glucocorticoid receptor (GR) (Kojo et al., 2006). ERRgamma4 (NM_001134285), similar to variant 2, uses an alternate 5' UTR and also encodes a shorter protein isoform than variant 1. ERRgamma5 (NR_024099) is transcribed but presumed to be non-coding.

Protein

Note The domain structure of ERRgamma is typical for a member of the nuclear receptor superfamily. ERRgamma and its family members (ERRalpha and ERRbeta) are most similar to the classical estrogen receptors alpha and beta (ERalpha, ERbeta).
 
  Schematic of ERRgamma domain structure. aa = amino acid, and numbers correspond to the ERRgamma1 isoform; AF1 = activation function-1 ; DBD = DNA binding domain ; LBD = ligand binding domain; (%) denotes amino acid identity to estrogen receptor alpha (ERalpha).
Description AF1: Like most nuclear receptors, the activation function -1 (AF1) domain of ERRgamma participates in the regulation of transcription by the receptor. It is the region to which several coactivators can bind (see below), as well as the site of post-translational modification. Phosphorylation of the family member ERRalpha at serine 19 has recently been shown to direct subsequent SUMOylation at a nearby lysine (residue 14), and that this series of post-translational modifications is in fact inhibitory for receptor transcriptional activity (Vu et al., 2007). While ERRgamma lacks a serine residue in this position, in March of 2008 Tremblay et al. confirmed ERRalpha phosphorylation at serine 19 and reported that ERRgamma transcriptional activity can also be inhibited by SUMOylation of lysine 40 that is directed by phosphorylation of serine 45 (Tremblay et al., 2008). The authors went on to identify protein inhibitor of activated signal transducer and activator of transcription gamma (PIAS4) as a functional E3 ligase for the family member ERRalpha, and hypothesized that PIAS4 and the SUMO-conjugating enzyme Ubc9 are responsible for the modification of ERRgamma as well.

DBD: The greater than 60% identity between the DNA binding domains (DBDs) of ERRgamma and ERalpha (see figure) results in ERRgamma being able to bind the estrogen response element (ERE: AGGTCA...TGACCT). However, ERRgamma also binds to what was originally identified as the consensus sequence for steroidogenic factor 1 (SF1, SFRE: TCAAGGTCA) (Horard and Vanacker, 2003).

LBD: A key difference between ERRgamma and most members of the nuclear receptor superfamily is the regulation of its transcriptional activity. There is only about 23% sequence identity between classical ERalpha and ERRgamma in the ligand binding domain (LBD) (see figure). Therefore, while ERalpha (like most nuclear receptors) is dependent upon ligand for full activation, ERRgamma and the other members of the ERR family exhibit constitutive transcriptional activity. None of the ERR family members are affected by estradiol (E2) stimulation because their LBDs cannot accommodate E2 binding (discussed in Ariazi and Jordan, 2006). However, ERRgamma transcriptional activity at EREs and SFREs can be inhibited by 4-hydroxytamoxifen (4HT) and the synthetic estrogen diethylstilbestrol (Greschik et al., 2002; Greschik et al., 2004; Yu and Forman, 2005). In contrast, 4HT-bound ERRgamma acquires the ability to positively regulate transcription at activator protein-1 (AP1) sites (Huppunen et al., 2004), but the mechanism by which this occurs is not clear. ERRgamma constitutive activity can be enhanced or stabilized by the synthetic agonist GSK4716 (Yu and Forman, 2005; Zuercher et al., 2005), the endocrine disruptor Bisphenol A (BPA) (Matsushima et al., 2007; Takayanagi et al., 2006), and a variant of this compound (4-alpha-cumylphenol) (Matsushima et al., 2008). ERRgamma constitutive activity has also recently been shown to be inhibited by kaempferol, a dietary flavonoid (Wang et al., 2009).

Coactivators/Corepressors: Like other nuclear receptors, ERRgamma transcriptional activity is modulated by binding to other proteins that can serve as coactivators or corepressors. Coactivators and corepressors bind directly to nuclear receptors, most often within the carboxyl-terminal activation function-2 (AF2) domain that participates in ligand-binding but some can exert their effects by binding to the amino-terminal AF1 domain or the flexible hinge region of the receptor (Hall and McDonnell, 2005). Among the coactivators that have been demonstrated to bind and activate ERRgamma are PPARGC1A (also known as PGC-1alpha), TLE1, NCOA1, NCOA2 and, under certain circumstances, NRIP1 (Gowda et al., 2006; Sanyal et al., 2004). PPARGC1A is best known as a coactivator for peroxisome proliferator-activated receptor gamma, but it is also able to enhance ERRgamma activity in an AF1-dependent manner (Hentschke et al., 2002). TLE1 can also enhance ERRgamma activity by binding to its AF1 domain, and the coactivator function of TLE1 in this context is unique because this protein typically functions as a repressor for Drosophila and mammalian high mobility group (HMG) box transcription factors. TLE1 also has no known interactions with classical ERalpha or any other nuclear receptor (Hentschke and Borgmeyer, 2003). In contrast, NCOA1 and NCOA2 are well-known AF2-dependent coactivators of ERalpha and other nuclear receptors, including ERRgamma (reviewed in Hall and McDonnell, 2005).

Expression In fetal and adult human tissues, ERRgamma1 and ERRgamma2 are most highly expressed in the heart, brain, kidney, and skeletal muscle (Heard et al., 2000), while ERRgamma3 expression appears to be restricted to the prostate and adipose tissue (Kojo et al., 2006). Interestingly, in the mouse ERRgamma is also expressed in these tissues but is even more abundant in the brain stem and spinal cord (http://www.nursa.org/10.1621/datasets.02001).
Localisation Endogenous ERRgamma is localized to the nucleus in human breast cancer (Park et al., 2005) and prostate tissue (Yu et al., 2007), and transfected, exogenous ERRgamma is also found in the nucleus of tissue culture cells (Yasumoto et al., 2007).
Function Molecular function: transcription factor activity, steroid hormone receptor activity, steroid binding, protein binding, zinc ion binding.
Biological processes: transcription, positive regulation of transcription (DNA-dependent)..
As a member of the nuclear receptor superfamily, ERRgamma is a transcription factor. In the mouse, homozygous knockout of ERR results in death on or about postnatal day 1 caused by severe cardiac defects (Alaynick et al., 2007). This is due to a key metabolic defect whereby the animals are unable to switch from deriving energy from carbohydrates in utero to lipids as a neonate because ERRgamma controls the transcription of essential genes that regulate oxidative metabolic processes (Giguere, 2008).
Homology ERRgamma is highly conserved among several species. At the amino acid level, human ERRgamma is 100% identical to rat, mouse, and cow ERRgamma, and 99.78% identical to dog and chimpanzee ERRgamma.

Mutations

Germinal Two recent studies have identified single nucleotide polymorphisms (SNPs) in ERRgamma. In a genome-wide association study searching for genes linked to Type 2 diabetes in an Amish population, Rampersaud et al. identified the non-coding rs2818781, which is present in an intron of ERRgamma2 and ERRgamma3 (Rampersaud et al., 2007). The T vs. C allele confers an increased risk for Type 2 diabetes (O.R. 1.61, p=0.003), and is also significantly associated with elevated glucose area under the curve (GAUC), a measure of impaired glucose tolerance collected during the oral glucose tolerance test (OGTT).
Two different SNPs in ERRgamma have been linked to breast cancer risk in a population of Thai women (Sangrajrang et al., 2009). The non-coding rs1857407 is located in an intron of ERRgamma1, ERRgamma2, and ERRgamma3, and heterozygotes for the G vs. A allele have a reduced breast cancer risk (O.R. 0.72, p=0.022). This risk reduction is even more pronounced in post-menopausal women (O.R. 0.69, p=0.043). In contrast, homozygote carriers of the CC (vs. TT) allele of rs945453 have an elevated breast cancer risk (O.R. 1.66, p=0.034), though this shows no significant association with pre- vs. post-menopausal status. This SNP leads to a synonymous change (serine-to-serine) at position 318 for ERRgamma1, and 295 for ERRgamma2, ERRgamma3, and ERRgamma4.

Implicated in

Note
  
Entity Breast cancer
Note In 2002 Ariazi et al. published a study of ERRgamma family expression in 38 breast tumors as compared to normal mammary epithelial cells (MECs) (Ariazi et al., 2002). ERRgamma mRNA expression is nearly 4-fold higher in these tumors than in the MECs and is positively associated with ERalpha and progesterone receptor (PR) expression. It was therefore concluded that the correlation of ERRgamma with ERalpha and PR in breast tumors suggests that ERRgamma expression is an indicator of good prognosis in breast cancer (Ariazi et al., 2002), given that women with ER+/PR+ breast tumors are excellent candidates for adjuvant endocrine therapy with aromatase inhibitors or antiestrogens such as Tamoxifen (TAM).
However, TAM therapy is ineffective in approximately 30% of patients with ER+/PR+ breast tumors, and the majority of women who initially respond to TAM but go on to acquire resistance to this and other endocrine agents do so without complete loss of ERalpha expression (Clarke et al., 2001). Moreover, 4-hydroxytamoxifen (4HT)-bound ERRgamma is known to activate transcription at AP1 sites, and elevated AP1 activity has been linked to TAM resistance in multiple in vitro (Dumont et al., 1996; Zhou et al., 2007) and in vivo (Johnston et al., 1999; Schiff et al., 2000) studies. In light of this, we were intrigued to find that that endogenous expression of ERRgamma is upregulated during the acquisition of TAM resistance by the ER+/PR+ SUM44 breast cancer cell line (Riggins et al., 2008). We subsequently demonstrated that overexpression of ERRgamma confers Tamoxifen (TAM) resistance to this and another ERalpha+ breast cancer cell line, and that ERRgamma-driven AP1 activation plays a dominant role in the resistance phenotype.
  
  
Entity Ovarian cancer
Note In a study of ovarian cancer specimens, normal ovaries, and ovarian cancer cell lines, Sun et al. showed that ERRgamma expression is significantly greater in ovarian cancer relative to normal tissue (Sun et al., 2005). However, patients whose tumors were positive for ERRgamma had significantly improved disease-free survival, and ERRgamma expression was not correlated with serum levels of CA-125, a tumor marker used to monitor ovarian cancer recurrence.
  
  
Entity Endometrial cancer
Note In 2006, Gao et al. reported that ERRgamma mRNA expression was significantly higher in ERalpha-positive endometrial carcinoma than normal endometrial tissues, although patients with ERRgamma-positive tumors had a reduced occurrence of lymph node metastases (Gao et al., 2005).
  
  
Entity Prostate cancer
Note In cell culture models of prostate cancer, stable overexpression of ERRgamma has been shown to inhibit cell proliferation and survival in vitro and in in vivo xenograft tumor models (Yu et al., 2007). This occurs via cell cycle arrest at the G1/S phase transition, which is induced by upregulation of the cell cycle inhibitors p21 and p27. ERRgamma activates transcription at both the p21 and p27 promoters, which may suggest that ERRgamma has tumor suppressor activities in prostate cancer.
  

Bibliography

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Giguere V.
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Development of a coactivator displacement assay for the orphan receptor estrogen-related receptor-gamma using time-resolved fluorescence resonance energy transfer.
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Structural basis for the deactivation of the estrogen-related receptor gamma by diethylstilbestrol or 4-hydroxytamoxifen and determinants of selectivity.
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Human ERRgamma, a third member of the estrogen receptor-related receptor (ERR) subfamily of orphan nuclear receptors: tissue-specific isoforms are expressed during development and in the adult.
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Identification of PNRC2 and TLE1 as activation function-1 cofactors of the orphan nuclear receptor ERRgamma.
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Estrogen receptor-related receptors: orphan receptors desperately seeking a ligand.
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J Mol Endocrinol. 2003 Dec;31(3):349-57. (REVIEW)
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Requirements for transcriptional regulation by the orphan nuclear receptor ERRgamma.
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Increased activator protein-1 DNA binding and c-Jun NH2-terminal kinase activity in human breast tumors with acquired tamoxifen resistance.
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ERRgamma tethers strongly bisphenol A and 4-alpha-cumylphenol in an induced-fit manner.
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ERRgamma mediates tamoxifen resistance in novel models of invasive lobular breast cancer.
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Endocrine disruptor bisphenol A strongly binds to human estrogen-related receptor gamma (ERRgamma) with high constitutive activity.
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ERRgamma suppresses cell proliferation and tumor growth of androgen-sensitive and androgen-insensitive prostate cancer cells and its implication as a therapeutic target for prostate cancer.
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Citation

This paper should be referenced as such :
Riggins, RB
ESRRG (estrogen-related receptor gamma)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(8):753-757.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/ESRRGID45840ch1q41.html


External links

Nomenclature
HGNC (Hugo)ESRRG   3474
Cards
AtlasESRRGID45840ch1q41
Entrez_Gene (NCBI)ESRRG  2104  estrogen related receptor gamma
AliasesERR3; ERRgamma; NR3B3
GeneCards (Weizmann)ESRRG
Ensembl hg19 (Hinxton)ENSG00000196482 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000196482 [Gene_View]  chr1:216503246-217137755 [Contig_View]  ESRRG [Vega]
ICGC DataPortalENSG00000196482
TCGA cBioPortalESRRG
AceView (NCBI)ESRRG
Genatlas (Paris)ESRRG
WikiGenes2104
SOURCE (Princeton)ESRRG
Genetics Home Reference (NIH)ESRRG
Genomic and cartography
GoldenPath hg38 (UCSC)ESRRG  -     chr1:216503246-217137755 -  1q41   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)ESRRG  -     1q41   [Description]    (hg19-Feb_2009)
EnsemblESRRG - 1q41 [CytoView hg19]  ESRRG - 1q41 [CytoView hg38]
Mapping of homologs : NCBIESRRG [Mapview hg19]  ESRRG [Mapview hg38]
OMIM602969   
Gene and transcription
Genbank (Entrez)###############################################################################################################################################################################################################################################################
RefSeq transcript (Entrez)NM_001134285 NM_001243505 NM_001243506 NM_001243507 NM_001243509 NM_001243510 NM_001243511 NM_001243512 NM_001243513 NM_001243514 NM_001243515 NM_001243518 NM_001243519 NM_001350122 NM_001350123 NM_001350124 NM_001350125 NM_001438 NM_206594 NM_206595
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)ESRRG
Cluster EST : UnigeneHs.738938 [ NCBI ]
CGAP (NCI)Hs.738938
Alternative Splicing GalleryENSG00000196482
Gene ExpressionESRRG [ NCBI-GEO ]   ESRRG [ EBI - ARRAY_EXPRESS ]   ESRRG [ SEEK ]   ESRRG [ MEM ]
Gene Expression Viewer (FireBrowse)ESRRG [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2104
GTEX Portal (Tissue expression)ESRRG
Protein : pattern, domain, 3D structure
UniProt/SwissProtP62508   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP62508  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP62508
Splice isoforms : SwissVarP62508
PhosPhoSitePlusP62508
Domaine pattern : Prosite (Expaxy)NUCLEAR_REC_DBD_1 (PS00031)    NUCLEAR_REC_DBD_2 (PS51030)   
Domains : Interpro (EBI)Nucl_hrmn_rcpt_lig-bd    Nuclear_hrmn_rcpt    Oest-rel_rcp    Oest_rcpt/oest-rel_rcp    Retinoic_acid_rcpt    Znf_hrmn_rcpt    Znf_NHR/GATA   
Domain families : Pfam (Sanger)Hormone_recep (PF00104)    zf-C4 (PF00105)   
Domain families : Pfam (NCBI)pfam00104    pfam00105   
Domain families : Smart (EMBL)HOLI (SM00430)  ZnF_C4 (SM00399)  
Conserved Domain (NCBI)ESRRG
DMDM Disease mutations2104
Blocks (Seattle)ESRRG
PDB (SRS)1KV6    1TFC    1VJB    2E2R    2EWP    2GP7    2GPO    2GPP    2GPU    2GPV    2P7A    2P7G    2P7Z    2ZAS    2ZBS    2ZKC   
PDB (PDBSum)1KV6    1TFC    1VJB    2E2R    2EWP    2GP7    2GPO    2GPP    2GPU    2GPV    2P7A    2P7G    2P7Z    2ZAS    2ZBS    2ZKC   
PDB (IMB)1KV6    1TFC    1VJB    2E2R    2EWP    2GP7    2GPO    2GPP    2GPU    2GPV    2P7A    2P7G    2P7Z    2ZAS    2ZBS    2ZKC   
PDB (RSDB)1KV6    1TFC    1VJB    2E2R    2EWP    2GP7    2GPO    2GPP    2GPU    2GPV    2P7A    2P7G    2P7Z    2ZAS    2ZBS    2ZKC   
Structural Biology KnowledgeBase1KV6    1TFC    1VJB    2E2R    2EWP    2GP7    2GPO    2GPP    2GPU    2GPV    2P7A    2P7G    2P7Z    2ZAS    2ZBS    2ZKC   
SCOP (Structural Classification of Proteins)1KV6    1TFC    1VJB    2E2R    2EWP    2GP7    2GPO    2GPP    2GPU    2GPV    2P7A    2P7G    2P7Z    2ZAS    2ZBS    2ZKC   
CATH (Classification of proteins structures)1KV6    1TFC    1VJB    2E2R    2EWP    2GP7    2GPO    2GPP    2GPU    2GPV    2P7A    2P7G    2P7Z    2ZAS    2ZBS    2ZKC   
SuperfamilyP62508
Human Protein AtlasENSG00000196482
Peptide AtlasP62508
HPRD04274
IPIIPI00025743   IPI00427737   IPI01010114   IPI00554597   IPI00940244   IPI00947191   IPI00947505   IPI00945135   IPI00946882   
Protein Interaction databases
DIP (DOE-UCLA)P62508
IntAct (EBI)P62508
FunCoupENSG00000196482
BioGRIDESRRG
STRING (EMBL)ESRRG
ZODIACESRRG
Ontologies - Pathways
QuickGOP62508
Ontology : AmiGORNA polymerase II regulatory region sequence-specific DNA binding  transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding  steroid hormone receptor activity  retinoic acid receptor activity  steroid binding  protein binding  nucleoplasm  regulation of transcription, DNA-templated  transcription initiation from RNA polymerase II promoter  zinc ion binding  steroid hormone mediated signaling pathway  positive regulation of transcription, DNA-templated  positive regulation of transcription from RNA polymerase II promoter  retinoic acid receptor signaling pathway  AF-2 domain binding  
Ontology : EGO-EBIRNA polymerase II regulatory region sequence-specific DNA binding  transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding  steroid hormone receptor activity  retinoic acid receptor activity  steroid binding  protein binding  nucleoplasm  regulation of transcription, DNA-templated  transcription initiation from RNA polymerase II promoter  zinc ion binding  steroid hormone mediated signaling pathway  positive regulation of transcription, DNA-templated  positive regulation of transcription from RNA polymerase II promoter  retinoic acid receptor signaling pathway  AF-2 domain binding  
REACTOMEP62508 [protein]
REACTOME PathwaysR-HSA-383280 [pathway]   
NDEx NetworkESRRG
Atlas of Cancer Signalling NetworkESRRG
Wikipedia pathwaysESRRG
Orthology - Evolution
OrthoDB2104
GeneTree (enSembl)ENSG00000196482
Phylogenetic Trees/Animal Genes : TreeFamESRRG
HOVERGENP62508
HOGENOMP62508
Homologs : HomoloGeneESRRG
Homology/Alignments : Family Browser (UCSC)ESRRG
Gene fusions - Rearrangements
Fusion : MitelmanESRRG/ACBD3 [1q41/1q42.12]  
Fusion : MitelmanESRRG/ADCY10 [1q41/1q24.2]  [t(1;1)(q24;q41)]  
Fusion : MitelmanRNF121/ESRRG [11q13.4/1q41]  [t(1;11)(q41;q13)]  
Fusion: TCGAESRRG 1q41 ACBD3 1q42.12 BRCA
Fusion: TCGAESRRG 1q41 ADCY10 1q24.2 BRCA
Fusion: TCGARNF121 11q13.4 ESRRG 1q41 BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerESRRG [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)ESRRG
dbVarESRRG
ClinVarESRRG
1000_GenomesESRRG 
Exome Variant ServerESRRG
ExAC (Exome Aggregation Consortium)ESRRG (select the gene name)
Genetic variants : HAPMAP2104
Genomic Variants (DGV)ESRRG [DGVbeta]
DECIPHERESRRG [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisESRRG 
Mutations
ICGC Data PortalESRRG 
TCGA Data PortalESRRG 
Broad Tumor PortalESRRG
OASIS PortalESRRG [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICESRRG  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDESRRG
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 ESRRG
DgiDB (Drug Gene Interaction Database)ESRRG
DoCM (Curated mutations)ESRRG (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)ESRRG (select a term)
intoGenESRRG
NCG5 (London)ESRRG
Cancer3DESRRG(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM602969   
Orphanet
MedgenESRRG
Genetic Testing Registry ESRRG
NextProtP62508 [Medical]
TSGene2104
GENETestsESRRG
Target ValidationESRRG
Huge Navigator ESRRG [HugePedia]
snp3D : Map Gene to Disease2104
BioCentury BCIQESRRG
ClinGenESRRG
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD2104
Chemical/Pharm GKB GenePA27891
Clinical trialESRRG
Miscellaneous
canSAR (ICR)ESRRG (select the gene name)
Other databaseMutant Mouse Regional Resource Centers (MMRRC)
Other databaseNIEHS Environmental Genome Project SNP Database
Other databaseRCSB Protein Data Bank
Probes
Litterature
PubMed92 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineESRRG
EVEXESRRG
GoPubMedESRRG
iHOPESRRG
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Tue Aug 1 17:25:48 CEST 2017

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