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BCLAF1 (BCL2-associated transcription factor 1)

Written2011-06John Peter McPherson
Department of Pharmacology, Toxicology, University of Toronto, Toronto, Ontario, M5S 1A8 Canada

(Note : for Links provided by Atlas : click)


HGNC Alias symbKIAA0164
HGNC Alias nameBCLAF1 and THRAP3 family member 1
HGNC Previous nameBCL2-associated transcription factor 1
LocusID (NCBI) 9774
Atlas_Id 43164
Location 6q23.3  [Link to chromosome band 6q23]
Location_base_pair Starts at 136256627 and ends at 136289846 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping BCLAF1.png]
Local_order Orientation on minus strand, flanked by FAM54A and MAP7 (according to GeneLoc and NCBI Map Viewer).
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
AATF (17q12)::BCLAF1 (6q23.3)BCLAF1 (6q23.3)::BCLAF1 (6q23.3)BCLAF1 (6q23.3)::GRM1 (6q24.3)
BCLAF1 (6q23.3)::MAP7 (6q23.3)BCLAF1 (6q23.3)::PSMB1 (6q27)BCLAF1 (6q23.3)::SEMA6A (5q23.1)
BCLAF1 (6q23.3)::ZNF321P (19q13)CST1 (20p11.21)::BCLAF1 (6q23.3)
Note BCLAF1 was originally identified as a protein partner for adenoviral E1B 19K. Forced expression of BCLAF1 causes cell death which is reversed in the presence of anti-apoptotic BCL-2. BCLAF1 was reported to associate in vitro with BCL-2 and BCL2L1. BCLAF1 was also reported to bind DNA and repress transcription. Taken together, these findings suggested a role for BCLAF1 in apoptotic signalling and transcriptional repression (Kasof et al., 1999). Subsequent studies using BCLAF1-depleted or Bclaf1-deficient cells do not reveal a critical role for BCLAF1 in death signalling (Ziegelbauer et al., 2009; McPherson et al., 2009). Recent studies have suggested roles for BCLAF1 in processes of RNA metabolism (Bracken et al., 2008; Sarras et al., 2010), KSHV viral production (Ziegelbauer et al., 2009), lung development and T cell activation (McPherson et al., 2009; Kong et al., 2011).


Description The BCLAF1 gene is composed of 13 exons and spans 32989 bases.
Transcription Two transcripts 5 kb and 3 kb in length are predominantly detected, however additional variant transcripts have been described with alternative promoters, cassette exons and polyadenylation sites.
Pseudogene None identified.


  Protein domains in BCLAF1L and BCLAF1S isoforms.
Description At least 4 isoforms are generated by alternative splicing. Two predominant BCLAF1 forms were initially described: a longer isoform 920 amino acids in length with a predicted molecular mass of 106 kDa, and a smaller isoform missing 49 amino acids (residues 797-846) with a predicted molecular mass of 101 kDa (Kasof et al., 1999). Residues 110-126 exhibit 88% homology to the bZIP DNA binding domain (Kasof et al., 1999). Residues 522-531 exhibit 80% homology to the Myb DNA binding domain (Kasof et al., 1999). Functional evidence for both of these domains remains to be shown. The N-terminal region (residues 3-161) of BCLAF1 is arginine- and serine-rich (RS domain). The C-terminal region (residues 512-913) is 59% similar to the C-terminal region of thyroid hormone receptor associated protein 3 (THRAP3/TRAP150).
Expression BCLAF1 is ubiquitously expressed, with high steady-state mRNA levels in skeletal muscle, haematopoietic cells, and various other cell lineages (Kasof et al., 1999; McPherson et al., 2009). Steady-state levels of BCLAF1 protein fluctuate in a temporal and cell-lineage dependent fashion during development (McPherson et al., 2009).
Localisation Bclaf1 is concentrated in punctate foci interspersed through the nucleus. In the presence of E19K and conditions which trigger apoptosis, the nuclear distribution of Bclaf1 appears to concentrate at the nuclear periphery or envelope (Kasof et al., 1999; Haraguchi et al., 2004).
Bclaf1 was identified as a protein component of interchromatin granular clusters, subnuclear structures that appear to serve as repositories for pre-mRNA splicing factors (Misteli and Spector, 1998; Sutherland et al., 2001; Saitoh et al., 2004).
Function The exact molecular function of BCLAF1 remains to be defined. BCLAF1 was originally identified as having properties of a death-inducing transcriptional repressor (Kasof et al., 1999). Several subsequent studies have expanded on the link between BCLAF1, transcription and apoptosis. Depletion of BCLAF1 was reported to render cells resistant to ceramide-induced apoptosis (Renert et al., 2009). Protein kinase C delta-mediated transactivation of p53 transcription has been shown to occur through the stimulation of BCLAF1 to co-occupy a core promoter element in the TP53 promoter (Liu et al., 2007). A role for Bclaf1 in lung development and T cell homeostasis was demonstrated in Bclaf1-deficient mice (McPherson et al., 2009). Bclaf1 was shown to be required for the proper spatial and temporal organization of smooth muscle lineage cells during the saccular stage of lung development. Bclaf1 was also shown to be critical for T cell activation. The phenotype of these mice could not be explained by a defect in apoptosis, furthermore Bclaf1-deficient cells displayed no defect in cell death following exposure to various apoptotic stimuli.
Recent studies have implicated BCLAF1 in processes linked to RNA metabolism. BCLAF1 contains an RS domain, a feature of many factors that facilitate pre-mRNA splicing and mRNA processing. BCLAF1 was found to be a component of ribonucleoprotein complexes (Merz et al., 2007; Sarras et al., 2010). Bclaf1-deficient cells were found to exhibit altered preferences for alternative splicing of a model substrate (Sarras et al., 2010). BCLAF1 was found associated with SkIP, TRAP150 and Pinin in a complex known as SNIP1. SNIP1 was found to regulate cyclin D1 mRNA processing by facilitating the recruitment of the RNA processing factor U2AF65 to cyclin D1 mRNA (Bracken et al., 2008).
BCLAF1 has been shown to complex with the RNA export factor TAP/NXF1 (Sarras et al., 2010). This property has also recently been reported for TRAP150, a protein showing structural similarity to BCLAF1 that also is found in ribonucleoprotein complexes (Lee et al., 2010). TRAP150 has been shown to promote pre-mRNA splicing of reporter substrates and promotes mRNA decay in a manner that is independent of nonsense-mediated decay of mRNA (Lee et al., 2010).

Sirt1 has been shown to exert transcriptional control of BCLAF1 at the promoter level (Kong et al., 2011). Sirt1 was found to form a complex with the histone acetyltransferase p300 and NF-kB transcription factor Rel-A, bind the BCLAF1 promoter and suppress BCLAF1 transcription via H3K56 deacetylation (Kong et al., 2011).
BCLAF1 protein levels fluctuate according to cell cycle position, with levels highest during the G1 phase, but lower during S and G2 phases (Bracken et al., 2008). BCLAF1 protein levels also fluctuate in a cell-lineage and temporal manner during differentiation of certain tissues and organs (McPherson et al., 2009).
Several studies have determined that Bclaf1 is extensively phosphorylated, although the functional significance of this modification is unclear. BCLAF1 has been proposed as a substrate of GSK-3 kinase (Linding et al., 2007). Vasopressin action in kidney cells has been reported to simulate BCLAF1 phosphorylation (Hoffert et al., 2006).
BCLAF1 has been shown to be one of the cellular targets for microRNAs (miRNAs) encoded by Kaposi's sarcoma-associated herpesvirus (KSHV). KSHV triggers certain acquired immune deficiency syndrome-related malignancies such as Kaposi's sarcoma, primary effusion lymphoma and variants of multicentric Castleman disease. A miRNA cluster within the KSHV genome is expressed during viral latency. During induction of lytic KSHV growth, inhibition of miRNAs was associated with increased BCLAF1 expression and decreased KSHV virion production (Ziegelbauer et al., 2009).

E1B 19K. By yeast two-hybrid analysis, BCLAF1 was shown to directly interact with adenoviral E1B 19K via a BH3 domain and another region immediately adjacent to BH3 in E1B 19K (Kasof et al., 1999). In vitro binding assays reported BCLAF1 associates with BCL-2 and BCL2L1.
emerin. By yeast-two hybrid analysis and microtiter well binding assays, BCLAF1 was shown to directly interact with emerin, a nuclear membrane protein. Mutations that result in a loss of functional emerin cause X-linked recessive Emery-Dreifuss muscular dystrophy. The residues of emerin required for binding to BCLAF1 mapped to two regions that flank its lamin-binding domain. Two disease-causing mutations in emerin, S54F and Delta95-99, disrupted binding to BCLAF1. BCLAF1 and emerin were observed to co-localize in the vicinity of the nuclear envelope following induction of apoptosis by Fas antibody (Haraguchi et al., 2004).
MAN1. The C-terminal domain of MAN1, a nuclear inner membrane protein that inhibits Smad signaling downstream of transforming growth factor beta, was observed to bind BCLAF1, as well as the transcriptional regulators GCL, and barrier-to-autointegration factor (BAF) (Mansharamani and Wilson, 2005).
Factors that participate in RNA metabolism. BCLAF1 and TRAP150 have been identified to be protein components of ribonucleoprotein complexes that participate in pre-mRNA splicing and other mRNA processing events (Merz et al., 2007; Sarras et al., 2010; Lee et al., 2010). Both BCLAF1 and TRAP150 have been reported to reside in protein complexes that contain the mRNA export factor NXF1/TAP (Sarras et al., 2010; Lee et al., 2010). Both BCLAF1 and TRAP150, together with Pinin and SkIP, have been found in a protein complex that regulates cyclin D1 mRNA stability.

Homology BCLAF1 shares amino acid similarity (48% overall identity) with TRAP150 in their C-terminal domains. Both proteins also contain RS-rich tracts within their N-termini (Lee et al., 2010).


Note BCLAF1 is located at chromosome 6q23 , a region that has been reported to exhibit a high frequency of deletions in tumours, such as lymphomas and leukemias. BCLAF1 has observed to be absent in Raji cells, derived from Burkitt's lymphoma, which has deletions in 6q (Kasof et al., 1999). A role for the loss of BCLAF1 in neoplastic transformation remains to be determined and may be coincidental.

Implicated in

Entity X-linked recessive Emery-Dreifuss muscular dystrophy
Note Bclaf1 has also recently been identified as a binding partner for emerin, a nuclear membrane protein that is mutated in X-linked recessive Emery-Dreifuss muscular dystrophy. Disease mutations in emerin were found to disrupt the interaction of emerin with BCLAF1 (Haraguchi et al., 2004).
Disease Emerin is encoded by the EMD gene located on human X-chromosome, which when mutated, gives rise to the X-linked form of Emery-Dreifuss muscular dystrophy (Bione et al., 1994). Emerin is a lamin A/C binding protein that participates in nuclear envelope mechanics which impact chromosome segregation, gene expression and muscle differentiation (Liu et al., 2003; Frock et al., 2006).
Entity Choroid plexus papillomas
Note Up-regulation of BCLAF1 was observed in seven cases of choroid plexus papilloma cells compared to eight cases of normal choroid plexus epithelial cells (Hasselblatt et al., 2009).
Disease Choroid plexus papillomas are rare intraventricular papillary neoplasms, typically in children and young adults.
Note An association of BCLAF1 single nucleotide polymorphisms (tagSNPs rs797558 and rs703193, P = 0.0097) with NHL was made following genotyping of 441 newly diagnosed NHL cases and 475 frequency-matched controls (Kelly et al., 2010).
Disease Non-Hodgkin's lymphoma refers to several subtypes of lymphoma that are distinct from Hodgkin's lymphoma, such as Mantle cell lymphoma, diffuse large B cell lymphoma and follicular lymphoma (Sawas et al., 2011).
Entity Chondromyxoid fibroma (CMF)
Note No changes in BCLAF1 were found in 43 samples of CMF (Romeo et al., 2010).
Disease Chondromyxoid fibroma (CMF) is an uncommon benign cartilaginous tumor of bone usually occurring in adolescents (Ralph, 1962; Romeo et al., 2009). CMF is associated with recurrent rearrangements of chromosome bands 6p23-25, 6q12-15, and 6q23-27.


Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy.
Bione S, Maestrini E, Rivella S, Mancini M, Regis S, Romeo G, Toniolo D.
Nat Genet. 1994 Dec;8(4):323-7.
PMID 7894480
Regulation of cyclin D1 RNA stability by SNIP1.
Bracken CP, Wall SJ, Barre B, Panov KI, Ajuh PM, Perkins ND.
Cancer Res. 2008 Sep 15;68(18):7621-8.
PMID 18794151
Lamin A/C and emerin are critical for skeletal muscle satellite cell differentiation.
Frock RL, Kudlow BA, Evans AM, Jameson SA, Hauschka SD, Kennedy BK.
Genes Dev. 2006 Feb 15;20(4):486-500.
PMID 16481476
Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy.
Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, Mori C, Wilson KL, Hiraoka Y.
Eur J Biochem. 2004 Mar;271(5):1035-45.
PMID 15009215
TWIST-1 is overexpressed in neoplastic choroid plexus epithelial cells and promotes proliferation and invasion.
Hasselblatt M, Mertsch S, Koos B, Riesmeier B, Stegemann H, Jeibmann A, Tomm M, Schmitz N, Wrede B, Wolff JE, Zheng W, Paulus W.
Cancer Res. 2009 Mar 15;69(6):2219-23. Epub 2009 Mar 10.
PMID 19276370
Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites.
Hoffert JD, Pisitkun T, Wang G, Shen RF, Knepper MA.
Proc Natl Acad Sci U S A. 2006 May 2;103(18):7159-64. Epub 2006 Apr 25.
PMID 16641100
Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins.
Kasof GM, Goyal L, White E.
Mol Cell Biol. 1999 Jun;19(6):4390-404.
PMID 10330179
Germline variation in apoptosis pathway genes and risk of non-Hodgkin's lymphoma.
Kelly JL, Novak AJ, Fredericksen ZS, Liebow M, Ansell SM, Dogan A, Wang AH, Witzig TE, Call TG, Kay NE, Habermann TM, Slager SL, Cerhan JR.
Cancer Epidemiol Biomarkers Prev. 2010 Nov;19(11):2847-58. Epub 2010 Sep 20.
PMID 20855536
The type III histone deacetylase Sirt1 protein suppresses p300-mediated histone H3 lysine 56 acetylation at Bclaf1 promoter to inhibit T cell activation.
Kong S, Kim SJ, Sandal B, Lee SM, Gao B, Zhang DD, Fang D.
J Biol Chem. 2011 May 13;286(19):16967-75. Epub 2011 Mar 22.
PMID 21454709
TRAP150 activates pre-mRNA splicing and promotes nuclear mRNA degradation.
Lee KM, Hsu IaW, Tarn WY.
Nucleic Acids Res. 2010 Jun;38(10):3340-50. Epub 2010 Jan 31.
PMID 20123736
Systematic discovery of in vivo phosphorylation networks.
Linding R, Jensen LJ, Ostheimer GJ, van Vugt MA, Jorgensen C, Miron IM, Diella F, Colwill K, Taylor L, Elder K, Metalnikov P, Nguyen V, Pasculescu A, Jin J, Park JG, Samson LD, Woodgett JR, Russell RB, Bork P, Yaffe MB, Pawson T.
Cell. 2007 Jun 29;129(7):1415-26. Epub 2007 Jun 14.
PMID 17570479
Protein kinase C delta induces transcription of the TP53 tumor suppressor gene by controlling death-promoting factor Btf in the apoptotic response to DNA damage.
Liu H, Lu ZG, Miki Y, Yoshida K.
Mol Cell Biol. 2007 Dec;27(24):8480-91. Epub 2007 Oct 15.
PMID 17938203
MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans.
Liu J, Lee KK, Segura-Totten M, Neufeld E, Wilson KL, Gruenbaum Y.
Proc Natl Acad Sci U S A. 2003 Apr 15;100(8):4598-603. Epub 2003 Apr 8.
PMID 12684533
Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor.
Mansharamani M, Wilson KL.
J Biol Chem. 2005 Apr 8;280(14):13863-70. Epub 2005 Jan 29.
PMID 15681850
Essential role for Bclaf1 in lung development and immune system function.
McPherson JP, Sarras H, Lemmers B, Tamblyn L, Migon E, Matysiak-Zablocki E, Hakem A, Azami SA, Cardoso R, Fish J, Sanchez O, Post M, Hakem R.
Cell Death Differ. 2009 Feb;16(2):331-9. Epub 2008 Nov 14.
PMID 19008920
Protein composition of human mRNPs spliced in vitro and differential requirements for mRNP protein recruitment.
Merz C, Urlaub H, Will CL, Luhrmann R.
RNA. 2007 Jan;13(1):116-28. Epub 2006 Nov 9.
PMID 17095540
The cellular organization of gene expression.
Misteli T, Spector DL.
Curr Opin Cell Biol. 1998 Jun;10(3):323-31. (REVIEW)
PMID 9640532
Chondromyxoid fibroma of bone.
Ralph LL.
J Bone Joint Surg Br. 1962 Feb;44-B:7-24.
PMID 14038586
The proapoptotic C16-ceramide-dependent pathway requires the death-promoting factor Btf in colon adenocarcinoma cells.
Renert AF, Leprince P, Dieu M, Renaut J, Raes M, Bours V, Chapelle JP, Piette J, Merville MP, Fillet M.
J Proteome Res. 2009 Oct;8(10):4810-22.
PMID 19705920
Heterogeneous and complex rearrangements of chromosome arm 6q in chondromyxoid fibroma: delineation of breakpoints and analysis of candidate target genes.
Romeo S, Duim RA, Bridge JA, Mertens F, de Jong D, Dal Cin P, Wijers-Koster PM, Debiec-Rychter M, Sciot R, Rosenberg AE, Szuhai K, Hogendoorn PC.
Am J Pathol. 2010 Sep;177(3):1365-76. Epub 2010 Aug 9.
PMID 20696777
Benign cartilaginous tumors of bone: from morphology to somatic and germ-line genetics.
Romeo S, Hogendoorn PC, Dei Tos AP.
Adv Anat Pathol. 2009 Sep;16(5):307-15. (REVIEW)
PMID 19700940
Proteomic analysis of interchromatin granule clusters.
Saitoh N, Spahr CS, Patterson SD, Bubulya P, Neuwald AF, Spector DL.
Mol Biol Cell. 2004 Aug;15(8):3876-90. Epub 2004 May 28.
PMID 15169873
In search of a function for BCLAF1.
Sarras H, Alizadeh Azami S, McPherson JP.
ScientificWorldJournal. 2010 Jul 20;10:1450-61. (REVIEW)
PMID 20661537
New therapeutic targets and drugs in non-Hodgkin's lymphoma.
Sawas A, Diefenbach C, O'connor OA.
Curr Opin Hematol. 2011 Jul;18(4):280-7.
PMID 21654386
Large-scale identification of mammalian proteins localized to nuclear sub-compartments.
Sutherland HG, Mumford GK, Newton K, Ford LV, Farrall R, Dellaire G, Caceres JF, Bickmore WA.
Hum Mol Genet. 2001 Sep 1;10(18):1995-2011.
PMID 11555636
Tandem array-based expression screens identify host mRNA targets of virus-encoded microRNAs.
Ziegelbauer JM, Sullivan CS, Ganem D.
Nat Genet. 2009 Jan;41(1):130-4. Epub 2008 Dec 21.
PMID 19098914


This paper should be referenced as such :
McPherson, JP
BCLAF1 (BCL2-associated transcription factor 1)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(12):994-997.
Free journal version : [ pdf ]   [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  B-cell Prolymphocytic Leukemia

External links


HGNC (Hugo)BCLAF1   16863
Entrez_Gene (NCBI)BCLAF1    BCL2 associated transcription factor 1
AliasesBTF; bK211L9.1
GeneCards (Weizmann)BCLAF1
Ensembl hg19 (Hinxton)ENSG00000029363 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000029363 [Gene_View]  ENSG00000029363 [Sequence]  chr6:136256627-136289846 [Contig_View]  BCLAF1 [Vega]
ICGC DataPortalENSG00000029363
Genatlas (Paris)BCLAF1
SOURCE (Princeton)BCLAF1
Genetics Home Reference (NIH)BCLAF1
Genomic and cartography
GoldenPath hg38 (UCSC)BCLAF1  -     chr6:136256627-136289846 -  6q23.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)BCLAF1  -     6q23.3   [Description]    (hg19-Feb_2009)
GoldenPathBCLAF1 - 6q23.3 [CytoView hg19]  BCLAF1 - 6q23.3 [CytoView hg38]
Genome Data Viewer NCBIBCLAF1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF249273 AK303559 AK308870 AK309259 AK315884
RefSeq transcript (Entrez)NM_001077440 NM_001077441 NM_001301038 NM_001363659 NM_001386693 NM_001386694 NM_001386695 NM_001386696 NM_001386697 NM_001386698 NM_001386699 NM_001386700 NM_001386701 NM_001386702 NM_001386703 NM_001386704 NM_014739
Consensus coding sequences : CCDS (NCBI)BCLAF1
Gene ExpressionBCLAF1 [ NCBI-GEO ]   BCLAF1 [ EBI - ARRAY_EXPRESS ]   BCLAF1 [ SEEK ]   BCLAF1 [ MEM ]
Gene Expression Viewer (FireBrowse)BCLAF1 [ Firebrowse - Broad ]
GenevisibleExpression of BCLAF1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)9774
GTEX Portal (Tissue expression)BCLAF1
Human Protein AtlasENSG00000029363-BCLAF1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9NYF8   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9NYF8  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9NYF8
Domains : Interpro (EBI)Bcl-2_assoc_TF1    THRAP3_BCLAF1   
Domain families : Pfam (Sanger)THRAP3_BCLAF1 (PF15440)   
Domain families : Pfam (NCBI)pfam15440   
Conserved Domain (NCBI)BCLAF1
AlphaFold pdb e-kbQ9NYF8   
Human Protein Atlas [tissue]ENSG00000029363-BCLAF1 [tissue]
Protein Interaction databases
IntAct (EBI)Q9NYF8
Ontologies - Pathways
Ontology : AmiGODNA binding  DNA binding  transcription coregulator activity  RNA binding  protein binding  nucleus  nucleoplasm  cytoplasm  apoptotic process  mediator complex  nuclear speck  positive regulation of apoptotic process  regulation of DNA-templated transcription in response to stress  negative regulation of transcription, DNA-templated  negative regulation of transcription, DNA-templated  positive regulation of transcription by RNA polymerase II  positive regulation of DNA-templated transcription, initiation  positive regulation of response to DNA damage stimulus  positive regulation of intrinsic apoptotic signaling pathway  
Ontology : EGO-EBIDNA binding  DNA binding  transcription coregulator activity  RNA binding  protein binding  nucleus  nucleoplasm  cytoplasm  apoptotic process  mediator complex  nuclear speck  positive regulation of apoptotic process  regulation of DNA-templated transcription in response to stress  negative regulation of transcription, DNA-templated  negative regulation of transcription, DNA-templated  positive regulation of transcription by RNA polymerase II  positive regulation of DNA-templated transcription, initiation  positive regulation of response to DNA damage stimulus  positive regulation of intrinsic apoptotic signaling pathway  
NDEx NetworkBCLAF1
Atlas of Cancer Signalling NetworkBCLAF1
Wikipedia pathwaysBCLAF1
Orthology - Evolution
GeneTree (enSembl)ENSG00000029363
Phylogenetic Trees/Animal Genes : TreeFamBCLAF1
Homologs : HomoloGeneBCLAF1
Homology/Alignments : Family Browser (UCSC)BCLAF1
Gene fusions - Rearrangements
Fusion : MitelmanBCLAF1::GRM1 [6q23.3/6q24.3]  
Fusion : MitelmanBCLAF1::MAP7 [6q23.3/6q23.3]  
Fusion : QuiverBCLAF1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerBCLAF1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)BCLAF1
Exome Variant ServerBCLAF1
GNOMAD BrowserENSG00000029363
Varsome BrowserBCLAF1
ACMGBCLAF1 variants
Genomic Variants (DGV)BCLAF1 [DGVbeta]
DECIPHERBCLAF1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisBCLAF1 
ICGC Data PortalBCLAF1 
TCGA Data PortalBCLAF1 
Broad Tumor PortalBCLAF1
OASIS PortalBCLAF1 [ Somatic mutations - Copy number]
Cancer Gene: CensusBCLAF1 
Somatic Mutations in Cancer : COSMICBCLAF1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DBCLAF1
Mutations and Diseases : HGMDBCLAF1
intOGen PortalBCLAF1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)BCLAF1
DoCM (Curated mutations)BCLAF1
CIViC (Clinical Interpretations of Variants in Cancer)BCLAF1
NCG (London)BCLAF1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry BCLAF1
NextProtQ9NYF8 [Medical]
Target ValidationBCLAF1
Huge Navigator BCLAF1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDBCLAF1
Pharm GKB GenePA134868035
Clinical trialBCLAF1
DataMed IndexBCLAF1
Other database
PubMed144 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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