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BABAM2 (brain and reproductive organ-expressed (TNFRSF1A modulator))

Written2010-06Yiu-Loon Chui, Kenneth Ka-Ho Lee, John Yeuk-Hon Chan
Department of Chemical Pathology, The Chinese University of Hong Kong, Hong Kong (YLC); School of Biomedical Sciences, The Chinese University of Hong Kong, Hong Kong (KKHL); Key Lab of Regenerative Medicine, Ministry of Education, Jinan University, Guang Zhou, Guang Dong, China (JYHC)

(Note : for Links provided by Atlas : click)


HGNC Alias symbBRCC45
HGNC Alias nameBRCA1/BRCA2-containing complex, subunit 4
HGNC Previous nameBRE
HGNC Previous namebrain and reproductive organ-expressed (TNFRSF1A modulator)
LocusID (NCBI) 9577
Atlas_Id 839
Location 2p23.2  [Link to chromosome band 2p23]
Location_base_pair Starts at 27890615 and ends at 28338900 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping BABAM2.png]
Local_order According to GeneLoc and NCBI Map Viewer, genes flanking BRE are RBKS 2p23.3 (ribokinase) in the minus strand orientation, and RPL23AP34 2p23.2 (ribosomal protein L23a pseudogene 34) in the positive strand orientation.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
BABAM2 (2p23.2)::BABAM2 (2p23.2)BABAM2 (2p23.2)::DPYSL5 (2p23.3)BABAM2 (2p23.2)::EHMT1 (9q34.3)
BABAM2 (2p23.2)::PRKCE (2p21)BABAM2 (2p23.2)::SNX17 (2p23.3)CLIP4 (2p23.2)::BABAM2 (2p23.2)
DYNC1I2 (2q31.1)::BABAM2 (2p23.2)EHMT1 (9q34.3)::BABAM2 (2p23.2)FOSL2 (2p23.2)::BABAM2 (2p23.2)
GALNT14 (2p23.1)::BABAM2 (2p23.2)PLB1 (2p23.2)::BABAM2 (2p23.2)PPP1CB (2p23.2)::BABAM2 (2p23.2)
SLC30A6 (2p22.3)::BABAM2 (2p23.2)


  Generation of the major transcript variant of human BRE. Human BRE gene (not drawn in scale) is consisted of 15 exons, three of which are alternatively spliced. The light green boxes, X - Z, are alternative exons which are not present in the major transcript. The asterisked ATG is the translation start. This transcript encodes the major 383-amino-acid BRE protein isoform 2, that has been studied.
Description The gene spans 448284 bases, telomere to centromere orientation. The first exon is non-coding. In humans, six transcript variants are produced by alternative splicing predominantly at either end of the gene. All human cells examined co-express all of the splice variants, but at different ratios to one another. The major transcript is αa, also known as variant 3 by NCBI nomenclature. This transcript encodes the ubiquitous 383-amino-acid protein, designated by NCBI as protein isoform 2 (NP_954661.1) (Ching et al., 2001). Functions of all minor transcript variants are undetermined. In mice, alternative splicing occurs only at the 5' region of the gene. The major transcript is variant 5 (NCBI nomenclature), which encodes the ubiquitous 383-amino acid protein that is 99% identical to human BRE. The minor transcript variants, unlike the human counterparts, are expressed differentially among tissues. Their functions are undetermined (Ching et al., 2003).
Transcription Exon 1 is non-coding; its flanking sequences are embedded in a CpG island of 1216 bases long. Transcription start varies over the region between 35 to 112 bases upstream of the last base of exon 1, with the most common site at 40 bases upstream. No TATA or CAAT box is located within 150 bases upstream of any of the transcription start sites. BRE mRNA is expressed ubiquitously, and was initially found to be highly expressed in brain, and reproductive organs; hence the name "BRE" (Li et al., 1995). Subsequent screens using human multiple-tissue RNA dot blot and Northern blot revealed highest transcript expression in adrenal and heart (Miao et al., 2001).
Pseudogene No pseudogene found.


Note BRE is a 383-amino-acid protein of no identifiable functional domain by sequence homology. No crystal structure of BRE is available. This protein has no paralog. The N-terminal region of 333 residues of human BRE, which is conserved among vertebrate orthologs, has been classified as a single unique domain, pfam06113. It has been recently proprosed that BRE contains 2 ubiquitin E2 variant (UEV) domains (Wang et al., 2009).
Description BRE is an evolutionarily highly conserved protein with no homolog within the same species. The major protein isoform is 383 amino-acids long. Based on bioinformatic analysis, BRE was proposed to have two ubiquitin-binding UEV (Ubiquitin E2 variant) domains. One was located in the N-terminal region between residues 30 and 147. The other one, however, could only be located in the isoform encoded by a rare transcript variant 1, as the C-terminal one quarter of the putative domain is encoded by the alternative exon Y (Wang et al., 2009). Thus, it is not clear whether the remaining putative UEV domain sequence from residues 275 to 363 of the major BRE isoform is functional.
Expression BRE is ubiquitously expressed. All mammalian cell lines examined express high levels of BRE. These cell lines include Jurkat, KRC/Y, HeLa, HepG2, HL60, MCF7, NIH3T3, NS0, THP-1, and lymphoblastoid CB14022 cells. Among mouse tissues, the expression levels of BRE detected by Western blot analysis showed the following pattern: lungs = spleen = thymus > adrenal > testis = kidney > brain > heart = liver. Human hepatocytes express little BRE as detected by immumnohistochemistry and Western blot analysis (Chan et al., 2008).
Localisation BRE is located in cytoplasm and nucleus.
Function DNA-repair and anti-apoptosis via regulation of ubiquitination. BRE was shown able to bind K48- and K63-linked polyubiquitin chains (Wang et al., 2009). BRE and its mouse ortholog are expressed in cytosolic and nuclear compartments (Li et al., 2004). In the nucleus, BRE is part of the BRCA1-A complex involved in DNA repair and maintaining G2/M arrest in response to DNA damage. BRCA1-A complex consists of BRCA1, BARD1, Abraxas/Abra1/CCDC98, RAP80, BRCC36, BRE, and MERIT40/NBA1 (Dong et al., 2003; Sobhian et al., 2007; Feng et al., 2009; Shao et al., 2009; Wang et al., 2009). BRE interacts strongly with MERIT40 and is responsible for binding the latter to the complex of Abraxas, RAP80 and BRCC36 (Feng et al., 2009). BRE may also regulate the K63 deubiquitinase activity of BRCC36 (Sobhian et al., 2007). In conjunction with BRCC36, BRE was shown to potentiate the E3 activity of BRCA1-BARD1 complex (Dong et al., 2003). Furthermore, depletion of BRE by siRNA sensitized cells to death induced by ionizing irradiation (Dong et al., 2003; Feng et al., 2009). This protein also forms multiprotein BRISC (Brcc36 isopeptidase complex) in the cytoplasm. BRISC, containing at least 3 proteins, FAM175B/ABRO1, BRCC36 and MERIT40/NBA1, in addition to BRE, specifically cleaves K63-linked polyubiquitin chains (Cooper et al., 2009). It is not known whether such cytosolic complex is responsible for attenuating apoptotic response emanating from the activated death receptors, TNF-R1 and Fas. BRE also binds to the cytoplasmic region of TNF-R1 and Fas, as well as the death-inducing signaling complex (DISC) during apoptotic induction (Gu et al., 1998; Li et al., 2004). The anti-apoptotic role of BRE has been shown by the increased apoptotic response to TNF-alpha of HeLa cell line depleted of BRE by siRNA, and the attenuated response of HeLa and Jurkat to TNF-alpha and anti-Fas agonist antibody by over-expression of the protein. As over-expression of BRE also reduced intrinsic apoptotic response induced by stress-related and genotoxic stimuli, it has been proposed that the death receptor-associating BRE inhibits the recruitment of mitochondrial apoptotic machinery, which is necessary for amplifying the death-receptor-initiated apoptosis of CD95 type II cell types, which include HeLa, Jurkat, and hepatocytes (Scaffidi et al., 1998; Engels et al., 2000). Ectopic expression of BRE in mouse Lewis lung carcinoma cells was shown to promote tumor growth in footpad injection model, but have no effect on cell proliferation in culture condition (Chan et al., 2005). Over-expression of BRE was found in 74% of 123 samples of human hepatocellular carcinoma, and the protein expression level correlated with poor prognosis. Immortalized human cell lines also uniformly express high levels of BRE regardless of the tissue origin of these cell lines. Transgenic expression of BRE in mouse liver attenuated acute fulminant hepatitis induced by anti-Fas antibody, and promoted diethylnitrosamine-induced, but not spontaneous, liver tumors (Chan et al., 2008; Chui et al., 2010). Thus, it is likely that BRE over-expression enhances tumor survival through its anti-apoptotic activity, rather than initiates tumor formation.
Homology No homologous protein of BRE found within the same species.


Note According to HapMap genotyped SNP data, there is no SNP polymorphism in any of the coding exons of BRE.
  Copy number polymorphism (CNP) of BRE gene. Regions with CNP are shown in colored boxes. Blue and red indicate copy loss and gain, respectively. Green indicates loss and gain at different segments of the contiguous region. The largest CNP region on the far left spans the first non-coding and the next 3 coding exons (exons 1, 2, 3 and 4) and extends further upstream into the neighboring ribokinase gene. The copy gain variant at the far right spans the alternative exon Z. Data obtained from HapMap.
Germinal According to the current HapMap_rel27 for all the 4 populations (CEU, CHB, JPT and YRI), the number of nucleotide positions in BRE gene with HapMap genotyped SNP is 453. Given the size of BRE gene of 448284 bases long, the number of bases with SNP fits well to the average genome-wide figure of one SNP per 1000 bases (Dutt and Beroukhim, 2007). It is, however, noteworthy that no SNP has been found in any of the coding exons. All of the SNPs, except one located in the 5' UTR, are present in the introns. Two recombination hotspots are located in the introns, one of which is from position 28271535 to 28276573, located between coding exons 7 and 8. The other one is from position 28338948 to 28341210, located between coding exons 10 and 11. Copy number polymorphisms (CNP) involving a large contiguous region of 163295 bases encompassing the first 3 coding exons and the upstream sequence of the neighbouring ribokinase gene and smaller downstream regions have also been identified (see diagram above) (The International HapMap Consortium, 2003).
Somatic One R9L mutation was identified in a lung carcinoma cell line, NIH-H2126, and a synonymous mutation S182S in a clear cell renal cell carcinoma sample, PD2198a.

Implicated in

Entity Hepatocellular carcinoma (HCC)
Note Immunohistochemical analysis, supplemented by immunoblotting, has revealed overexpression of BRE in the tumoral regions of 72% of the 123 human HCC samples examined. Non-tumoral liver regions, cirrhotic or otherwise, expressed little BRE (Chan et al., 2008).
Prognosis The over-expression levels of BRE correlated with poor differentiation of HCC cells and therefore poor prognosis.
Cytogenetics Not determined.
Hybrid/Mutated Gene Not determined.
Abnormal Protein No fusion protein reported.
Oncogenesis The transgenic mouse model with liver-specific over-expression of human BRE showed no enhanced spontaneous tumor development, indicating that BRE over-expression alone is not tumorigenic. These mice, however, showed significant attenuation of liver apoptosis induced by injection anti-Fas agonist antibody. These findings indicate that the over-expression of BRE in HCC is related to the anti-apoptotic activity of the protein which promotes growth of the carcinoma (Chan et al., 2008). Recent work on inducing liver carcinoma to the above transgenic mice by neonatal injection of diethylnitrosamine (DEN) confirmed that BRE over-expression in the liver could only promote growth of the already initiated tumor, rather than on initiating tumor formation. Interestingly, the DEN-induced liver tumors of the non-transgenic controls also showed up-regulation of endogenous BRE, suggesting that the BRE is important in liver carcinogenesis through its anti-apoptotic activity (Chui et al., 2010).


BRE is an antiapoptotic protein in vivo and overexpressed in human hepatocellular carcinoma.
Chan BC, Ching AK, To KF, Leung JC, Chen S, Li Q, Lai PB, Tang NL, Shaw PC, Chan JY, James AE, Lai KN, Lim PL, Lee KK, Chui YL.
Oncogene. 2008 Feb 21;27(9):1208-17. Epub 2007 Aug 20.
PMID 17704801
BRE enhances in vivo growth of tumor cells.
Chan BC, Li Q, Chow SK, Ching AK, Liew CT, Lim PL, Lee KK, Chan JY, Chui YL.
Biochem Biophys Res Commun. 2005 Jan 14;326(2):268-73.
PMID 15582573
Expression of a conserved mouse stress-modulating gene, Bre: comparison with the human ortholog.
Ching AK, Li Q, Lim PL, Chan JY, Chui YL.
DNA Cell Biol. 2003 Aug;22(8):497-504.
PMID 14565866
BRE over-expression promotes growth of hepatocellular carcinoma.
Chui YL, Ching AK, Chen S, Yip FP, Rowlands DK, James AE, Lee KK, Chan JY.
Biochem Biophys Res Commun. 2010 Jan 15;391(3):1522-5. Epub 2009 Dec 24.
PMID 20035718
K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1.
Cooper EM, Cutcliffe C, Kristiansen TZ, Pandey A, Pickart CM, Cohen RE.
EMBO J. 2009 Mar 18;28(6):621-31. Epub 2009 Feb 12.
PMID 19214193
Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair.
Dong Y, Hakimi MA, Chen X, Kumaraswamy E, Cooch NS, Godwin AK, Shiekhattar R.
Mol Cell. 2003 Nov;12(5):1087-99.
PMID 14636569
Single nucleotide polymorphism array analysis of cancer.
Dutt A, Beroukhim R.
Curr Opin Oncol. 2007 Jan;19(1):43-9. (REVIEW)
PMID 17133111
Caspase-8/FLICE functions as an executioner caspase in anticancer drug-induced apoptosis.
Engels IH, Stepczynska A, Stroh C, Lauber K, Berg C, Schwenzer R, Wajant H, Janicke RU, Porter AG, Belka C, Gregor M, Sculze-Osthoff K, Wesselborg S.
Oncogene. 2000 Sep 21;19(40):4563-73.
PMID 11030145
MERIT40 facilitates BRCA1 localization and DNA damage repair.
Feng L, Huang J, Chen J.
Genes Dev. 2009 Mar 15;23(6):719-28. Epub 2009 Mar 4.
PMID 19261748
BRE: a modulator of TNF-alpha action.
Gu C, Castellino A, Chan JY, Chao MV.
FASEB J. 1998 Sep;12(12):1101-8.
PMID 9737713
The International HapMap Project.
International HapMap Consortium.
Nature. 2003 Dec 18;426(6968):789-96.
PMID 14685227
Identification of a brain- and reproductive-organs-specific gene responsive to DNA damage and retinoic acid.
Li L, Yoo H, Becker FF, Ali-Osman F, Chan JY.
Biochem Biophys Res Commun. 1995 Jan 17;206(2):764-74.
PMID 7826398
A death receptor-associated anti-apoptotic protein, BRE, inhibits mitochondrial apoptotic pathway.
Li Q, Ching AK, Chan BC, Chow SK, Lim PL, Ho TC, Ip WK, Wong CK, Lam CW, Lee KK, Chan JY, Chui YL.
J Biol Chem. 2004 Dec 10;279(50):52106-16. Epub 2004 Oct 1.
PMID 15465831
Differential expression of a stress-modulating gene, BRE, in the adrenal gland, in adrenal neoplasia, and in abnormal adrenal tissues.
Miao J, Panesar NS, Chan KT, Lai FM, Xia N, Wang Y, Johnson PJ, Chan JY.
J Histochem Cytochem. 2001 Apr;49(4):491-500.
PMID 11259452
Two CD95 (APO-1/Fas) signaling pathways.
Scaffidi C, Fulda S, Srinivasan A, Friesen C, Li F, Tomaselli KJ, Debatin KM, Krammer PH, Peter ME.
EMBO J. 1998 Mar 16;17(6):1675-87.
PMID 9501089
MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA double-strand breaks.
Shao G, Patterson-Fortin J, Messick TE, Feng D, Shanbhag N, Wang Y, Greenberg RA.
Genes Dev. 2009 Mar 15;23(6):740-54. Epub 2009 Mar 4.
PMID 19261746
RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites.
Sobhian B, Shao G, Lilli DR, Culhane AC, Moreau LA, Xia B, Livingston DM, Greenberg RA.
Science. 2007 May 25;316(5828):1198-202.
PMID 17525341
NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control.
Wang B, Hurov K, Hofmann K, Elledge SJ.
Genes Dev. 2009 Mar 15;23(6):729-39. Epub 2009 Mar 4.
PMID 19261749


This paper should be referenced as such :
Chui, YL ; Lee, KKH ; Chan, JYH
BRE (brain, reproductive organ-expressed (TNFRSF1A modulator))
Atlas Genet Cytogenet Oncol Haematol. 2011;15(3):255-258.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)BABAM2   1106
Entrez_Gene (NCBI)BABAM2    BRISC and BRCA1 A complex member 2
AliasesBRCC4; BRCC45; BRE
GeneCards (Weizmann)BABAM2
Ensembl hg19 (Hinxton)ENSG00000158019 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000158019 [Gene_View]  ENSG00000158019 [Sequence]  chr2:27890615-28338900 [Contig_View]  BABAM2 [Vega]
ICGC DataPortalENSG00000158019
Genatlas (Paris)BABAM2
SOURCE (Princeton)BABAM2
Genetics Home Reference (NIH)BABAM2
Genomic and cartography
GoldenPath hg38 (UCSC)BABAM2  -     chr2:27890615-28338900 +  2p23.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)BABAM2  -     2p23.2   [Description]    (hg19-Feb_2009)
GoldenPathBABAM2 - 2p23.2 [CytoView hg19]  BABAM2 - 2p23.2 [CytoView hg38]
Genome Data Viewer NCBIBABAM2 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF015767 AF420602 AF420603 AF420604 AF420605
RefSeq transcript (Entrez)NM_001261840 NM_001329112 NM_001329113 NM_001329114 NM_001329115 NM_004899 NM_199191 NM_199192 NM_199193 NM_199194
Consensus coding sequences : CCDS (NCBI)BABAM2
Gene ExpressionBABAM2 [ NCBI-GEO ]   BABAM2 [ EBI - ARRAY_EXPRESS ]   BABAM2 [ SEEK ]   BABAM2 [ MEM ]
Gene Expression Viewer (FireBrowse)BABAM2 [ Firebrowse - Broad ]
GenevisibleExpression of BABAM2 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)9577
GTEX Portal (Tissue expression)BABAM2
Human Protein AtlasENSG00000158019-BABAM2 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9NXR7   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9NXR7  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9NXR7
Domains : Interpro (EBI)BRE   
Domain families : Pfam (Sanger)BRE (PF06113)   
Domain families : Pfam (NCBI)pfam06113   
Conserved Domain (NCBI)BABAM2
PDB (RSDB)6H3C    6R8F   
PDB Europe6H3C    6R8F   
PDB (PDBSum)6H3C    6R8F   
PDB (IMB)6H3C    6R8F   
Structural Biology KnowledgeBase6H3C    6R8F   
SCOP (Structural Classification of Proteins)6H3C    6R8F   
CATH (Classification of proteins structures)6H3C    6R8F   
AlphaFold pdb e-kbQ9NXR7   
Human Protein Atlas [tissue]ENSG00000158019-BABAM2 [tissue]
Protein Interaction databases
IntAct (EBI)Q9NXR7
Complex Portal (EBI)Q9NXR7 CPX-4425 BRCA1-A complex
Q9NXR7 CPX-955 BRCC ubiquitin ligase complex
Ontologies - Pathways
Ontology : AmiGOnuclear ubiquitin ligase complex  peroxisome targeting sequence binding  tumor necrosis factor receptor binding  protein binding  nucleus  nucleoplasm  cytoplasm  cytosol  cytosol  double-strand break repair  double-strand break repair  double-strand break repair via nonhomologous end joining  chromatin organization  apoptotic process  cellular response to DNA damage stimulus  mitotic G2 DNA damage checkpoint signaling  signal transduction  response to ionizing radiation  protein deubiquitination  polyubiquitin modification-dependent protein binding  negative regulation of apoptotic process  positive regulation of DNA repair  cell division  BRCA1-A complex  protein K63-linked deubiquitination  BRISC complex  
Ontology : EGO-EBInuclear ubiquitin ligase complex  peroxisome targeting sequence binding  tumor necrosis factor receptor binding  protein binding  nucleus  nucleoplasm  cytoplasm  cytosol  cytosol  double-strand break repair  double-strand break repair  double-strand break repair via nonhomologous end joining  chromatin organization  apoptotic process  cellular response to DNA damage stimulus  mitotic G2 DNA damage checkpoint signaling  signal transduction  response to ionizing radiation  protein deubiquitination  polyubiquitin modification-dependent protein binding  negative regulation of apoptotic process  positive regulation of DNA repair  cell division  BRCA1-A complex  protein K63-linked deubiquitination  BRISC complex  
REACTOMEQ9NXR7 [protein]
REACTOME PathwaysR-HSA-69473 [pathway]   
NDEx NetworkBABAM2
Atlas of Cancer Signalling NetworkBABAM2
Wikipedia pathwaysBABAM2
Orthology - Evolution
GeneTree (enSembl)ENSG00000158019
Phylogenetic Trees/Animal Genes : TreeFamBABAM2
Homologs : HomoloGeneBABAM2
Homology/Alignments : Family Browser (UCSC)BABAM2
Gene fusions - Rearrangements
Fusion : MitelmanBRE::DPYSL5 [2p23.2/2p23.3]  
Fusion : MitelmanBRE::PRKCE [2p23.2/2p21]  
Fusion : MitelmanCLIP4::BRE [2p23.2/2p23.2]  
Fusion : MitelmanDYNC1I2::BRE [2q31.1/2p23.2]  
Fusion : MitelmanFOSL2::BRE [2p23.2/2p23.2]  
Fusion : MitelmanGALNT14::BRE [2p23.1/2p23.2]  
Fusion : MitelmanPLB1::BRE [2p23.2/2p23.2]  
Fusion : MitelmanPPP1CB::BRE [2p23.2/2p23.2]  
Fusion : MitelmanSLC30A6::BRE [2p22.3/2p23.2]  
Fusion : QuiverBABAM2
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerBABAM2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)BABAM2
Exome Variant ServerBABAM2
GNOMAD BrowserENSG00000158019
Varsome BrowserBABAM2
ACMGBABAM2 variants
Genomic Variants (DGV)BABAM2 [DGVbeta]
DECIPHERBABAM2 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisBABAM2 
ICGC Data PortalBABAM2 
TCGA Data PortalBABAM2 
Broad Tumor PortalBABAM2
OASIS PortalBABAM2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICBABAM2  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DBABAM2
Mutations and Diseases : HGMDBABAM2
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)BABAM2
DoCM (Curated mutations)BABAM2
CIViC (Clinical Interpretations of Variants in Cancer)BABAM2
NCG (London)BABAM2
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry BABAM2
NextProtQ9NXR7 [Medical]
Target ValidationBABAM2
Huge Navigator BABAM2 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDBABAM2
Pharm GKB GenePA25419
Clinical trialBABAM2
DataMed IndexBABAM2
Other database
PubMed75 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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