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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

Other aliasERR3
ERRG2
FLJ16023
KIAA0832
NR3B3
DKFZp781L1617
LocusID (NCBI) 2104
Atlas_Id 45840
Location 1q41  [Link to chromosome band 1q41]
Location_base_pair Starts at and ends at bp from pter
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
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

ERRgamma directs and maintains the transition to oxidative metabolism in the postnatal heart.
Alaynick WA, Kondo RP, Xie W, He W, Dufour CR, Downes M, Jonker JW, Giles W, Naviaux RK, Gigure V, Evans RM.
Cell Metab. 2007 Jul;6(1):13-24.
PMID 17618853
 
Estrogen-related receptor alpha and estrogen-related receptor gamma associate with unfavorable and favorable biomarkers, respectively, in human breast cancer.
Ariazi EA, Clark GM, Mertz JE.
Cancer Res. 2002 Nov 15;62(22):6510-8.
PMID 12438245
 
Estrogen-related receptors as emerging targets in cancer and metabolic disorders.
Ariazi EA, Jordan VC.
Curr Top Med Chem. 2006;6(3):203-15. (REVIEW)
PMID 16515477
 
Molecular and pharmacological aspects of antiestrogen resistance.
Clarke R, Skaar TC, Bouker KB, Davis N, Lee YR, Welch JN, Leonessa F.
J Steroid Biochem Mol Biol. 2001 Jan-Mar;76(1-5):71-84. (REVIEW)
PMID 11384865
 
Progression of MCF-7 breast cancer cells to antiestrogen-resistant phenotype is accompanied by elevated levels of AP-1 DNA-binding activity.
Dumont JA, Bitonti AJ, Wallace CD, Baumann RJ, Cashman EA, Cross-Doersen DE.
Cell Growth Differ. 1996 Mar;7(3):351-9.
PMID 8838865
 
Expression of estrogen receptor-related receptor isoforms in endometrial carcinoma tissues and its clinical significance.
Gao M, Wei LH, Sun PM, Zhao D, Wang JL, Wang ZQ, Zhao C.
Zhonghua Fu Chan Ke Za Zhi. 2005 Nov;40(11):756-60.
PMID 16324250
 
Transcriptional control of energy homeostasis by the estrogen-related receptors.
Giguere V.
Endocr Rev. 2008 Oct;29(6):677-96. Epub 2008 Jul 29. (REVIEW)
PMID 18664618
 
Development of a coactivator displacement assay for the orphan receptor estrogen-related receptor-gamma using time-resolved fluorescence resonance energy transfer.
Gowda K, Marks BD, Zielinski TK, Ozers MS.
Anal Biochem. 2006 Oct 1;357(1):105-15. Epub 2006 Jul 10.
PMID 16889744
 
Structural basis for the deactivation of the estrogen-related receptor gamma by diethylstilbestrol or 4-hydroxytamoxifen and determinants of selectivity.
Greschik H, Flaig R, Renaud JP, Moras D.
J Biol Chem. 2004 Aug 6;279(32):33639-46. Epub 2004 May 24.
PMID 15161930
 
Coregulators in nuclear estrogen receptor action: from concept to therapeutic targeting.
Hall JM, McDonnell DP.
Mol Interv. 2005 Dec;5(6):343-57. (REVIEW)
PMID 16394250
 
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.
Heard DJ, Norby PL, Holloway J, Vissing H.
Mol Endocrinol. 2000 Mar;14(3):382-92.
PMID 10707956
 
Identification of PNRC2 and TLE1 as activation function-1 cofactors of the orphan nuclear receptor ERRgamma.
Hentschke M, Borgmeyer U.
Biochem Biophys Res Commun. 2003 Dec 26;312(4):975-82.
PMID 14651967
 
Estrogen receptor-related receptors: orphan receptors desperately seeking a ligand.
Horard B, Vanacker JM.
J Mol Endocrinol. 2003 Dec;31(3):349-57. (REVIEW)
PMID 14664699
 
Requirements for transcriptional regulation by the orphan nuclear receptor ERRgamma.
Huppunen J, Wohlfahrt G, Aarnisalo P.
Mol Cell Endocrinol. 2004 Apr 30;219(1-2):151-60.
PMID 15149736
 
Increased activator protein-1 DNA binding and c-Jun NH2-terminal kinase activity in human breast tumors with acquired tamoxifen resistance.
Johnston SR, Lu B, Scott GK, Kushner PJ, Smith IE, Dowsett M, Benz CC.
Clin Cancer Res. 1999 Feb;5(2):251-6.
PMID 10037172
 
A novel estrogen receptor-related protein gamma splice variant lacking a DNA binding domain exon modulates transcriptional activity of a moderate range of nuclear receptors.
Kojo H, Tajima K, Fukagawa M, Isogai T, Nishimura S.
J Steroid Biochem Mol Biol. 2006 Mar;98(4-5):181-92. Epub 2006 Feb 7.
PMID 16460929
 
ERRgamma tethers strongly bisphenol A and 4-alpha-cumylphenol in an induced-fit manner.
Matsushima A, Teramoto T, Okada H, Liu X, Tokunaga T, Kakuta Y, Shimohigashi Y.
Biochem Biophys Res Commun. 2008 Aug 29;373(3):408-13. Epub 2008 Jun 26.
PMID 18582436
 
Identification of novel candidate genes for type 2 diabetes from a genome-wide association scan in the Old Order Amish: evidence for replication from diabetes-related quantitative traits and from independent populations.
Rampersaud E, Damcott CM, Fu M, Shen H, McArdle P, Shi X, Shelton J, Yin J, Chang YP, Ott SH, Zhang L, Zhao Y, Mitchell BD, O'Connell J, Shuldiner AR.
Diabetes. 2007 Dec;56(12):3053-62. Epub 2007 Sep 10.
PMID 17846126
 
ERRgamma mediates tamoxifen resistance in novel models of invasive lobular breast cancer.
Riggins RB, Lan JP, Zhu Y, Klimach U, Zwart A, Cavalli LR, Haddad BR, Chen L, Gong T, Xuan J, Ethier SP, Clarke R.
Cancer Res. 2008 Nov 1;68(21):8908-17.
PMID 18974135
 
Genetic polymorphisms of estrogen metabolizing enzyme and breast cancer risk in Thai women.
Sangrajrang S, Sato Y, Sakamoto H, Ohnami S, Laird NM, Khuhaprema T, Brennan P, Boffetta P, Yoshida T.
Int J Cancer. 2009 Aug 15;125(4):837-43.
PMID 19415745
 
Deoxyribonucleic acid response element-dependent regulation of transcription by orphan nuclear receptor estrogen receptor-related receptor gamma.
Sanyal S, Matthews J, Bouton D, Kim HJ, Choi HS, Treuter E, Gustafsson JA.
Mol Endocrinol. 2004 Feb;18(2):312-25. Epub 2003 Nov 26.
PMID 14645497
 
Oxidative stress and AP-1 activity in tamoxifen-resistant breast tumors in vivo.
Schiff R, Reddy P, Ahotupa M, Coronado-Heinsohn E, Grim M, Hilsenbeck SG, Lawrence R, Deneke S, Herrera R, Chamness GC, Fuqua SA, Brown PH, Osborne CK.
J Natl Cancer Inst. 2000 Dec 6;92(23):1926-34.
PMID 11106684
 
Expression of estrogen receptor-related receptors, a subfamily of orphan nuclear receptors, as new tumor biomarkers in ovarian cancer cells.
Sun P, Sehouli J, Denkert C, Mustea A, Konsgen D, Koch I, Wei L, Lichtenegger W.
J Mol Med. 2005 Jun;83(6):457-67. Epub 2005 Mar 16.
PMID 15770498
 
Endocrine disruptor bisphenol A strongly binds to human estrogen-related receptor gamma (ERRgamma) with high constitutive activity.
Takayanagi S, Tokunaga T, Liu X, Okada H, Matsushima A, Shimohigashi Y.
Toxicol Lett. 2006 Dec 1;167(2):95-105. Epub 2006 Sep 3.
PMID 17049190
 
Phosphorylation-dependent sumoylation regulates estrogen-related receptor-alpha and -gamma transcriptional activity through a synergy control motif.
Tremblay AM, Wilson BJ, Yang XJ, Giguere V.
Mol Endocrinol. 2008 Mar;22(3):570-84. Epub 2007 Dec 6.
PMID 18063693
 
Phosphorylation-dependent sumoylation of estrogen-related receptor alpha1.
Vu EH, Kraus RJ, Mertz JE.
Biochemistry. 2007 Aug 28;46(34):9795-804. Epub 2007 Aug 4.
PMID 17676930
 
Kaempferol is an estrogen-related receptor alpha and gamma inverse agonist.
Wang J, Fang F, Huang Z, Wang Y, Wong C.
FEBS Lett. 2009 Feb 18;583(4):643-7. Epub 2009 Jan 24.
PMID 19171140
 
GNL3L inhibits activity of estrogen-related receptor gamma by competing for coactivator binding.
Yasumoto H, Meng L, Lin T, Zhu Q, Tsai RY.
J Cell Sci. 2007 Aug 1;120(Pt 15):2532-43. Epub 2007 Jul 10.
PMID 17623774
 
Identification of an agonist ligand for estrogen-related receptors ERRbeta/gamma.
Yu DD, Forman BM.
Bioorg Med Chem Lett. 2005 Mar 1;15(5):1311-3.
PMID 15713377
 
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.
Yu S, Wang X, Ng CF, Chen S, Chan FL.
Cancer Res. 2007 May 15;67(10):4904-14.
PMID 17510420
 
Enhanced NF kappa B and AP-1 transcriptional activity associated with antiestrogen resistant breast cancer.
Zhou Y, Yau C, Gray JW, Chew K, Dairkee SH, Moore DH, Eppenberger U, Eppenberger-Castori S, Benz CC.
BMC Cancer. 2007 Apr 3;7:59.
PMID 17407600
 
Identification and structure-activity relationship of phenolic acyl hydrazones as selective agonists for the estrogen-related orphan nuclear receptors ERRbeta and ERRgamma.
Zuercher WJ, Gaillard S, Orband-Miller LA, Chao EY, Shearer BG, Jones DG, Miller AB, Collins JL, McDonnell DP, Willson TM.
J Med Chem. 2005 May 5;48(9):3107-9.
PMID 15857113
 

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


Other Leukemias implicated (Data extracted from papers in the Atlas) [ 2 ]
  del(1)(q42) ESRRG/ACBD3
del(1)(q42) ESRRG/ACBD3


Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 3 ]
  t(1;1)(q24;q41) ESRRG/ADCY10
t(1;1)(q41;q42) ESRRG/ACBD3
t(1;11)(q41;q13) RNF121/ESRRG


External links

Nomenclature
Cards
AtlasESRRGID45840ch1q41.txt
Aliases
Genomic and cartography
Gene and transcription
RefSeq transcript (Entrez)
RefSeq genomic (Entrez)
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
BioGPS (Tissue expression)2104
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Protein Interaction databases
Ontologies - Pathways
Clinical trials, drugs, therapy
Miscellaneous
canSAR (ICR) (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
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed


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