ID BCL6_HUMAN Reviewed; 706 AA. AC P41182; A7E241; B8PSA7; D3DNV5; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 233. DE RecName: Full=B-cell lymphoma 6 protein; DE Short=BCL-6; DE AltName: Full=B-cell lymphoma 5 protein; DE Short=BCL-5; DE AltName: Full=Protein LAZ-3; DE AltName: Full=Zinc finger and BTB domain-containing protein 27; DE AltName: Full=Zinc finger protein 51; GN Name=BCL6; Synonyms=BCL5, LAZ3, ZBTB27, ZNF51; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Skeletal muscle; RX PubMed=8220427; DOI=10.1038/ng0993-66; RA Kerckaert J.-P., Deweindt C., Tilly H., Quief S., Lecocq G., Bastard C.; RT "LAZ3, a novel zinc-finger encoding gene, is disrupted by recurring RT chromosome 3q27 translocations in human lymphomas."; RL Nat. Genet. 5:66-70(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8235596; DOI=10.1126/science.8235596; RA Ye B.H., Lista F., Lo Coco F., Knowles D.M., Offit K., Chaganti R.S.K., RA Dalla-Favera R.; RT "Alterations of a zinc finger-encoding gene, BCL-6, in diffuse large-cell RT lymphoma."; RL Science 262:747-750(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=8274740; RA Miki T., Kawamata N., Hirosawa S., Aoki N.; RT "Gene involved in the 3q27 translocation associated with B-cell lymphoma, RT BCL5, encodes a Kruppel-like zinc-finger protein."; RL Blood 83:26-32(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8506375; DOI=10.1073/pnas.90.11.5262; RA Baron B.W., Nucifora G., McCabe N., Espinosa R. III, le Beau M.M., RA McKeithan T.W.; RT "Identification of the gene associated with the recurring chromosomal RT translocations t(3;14)(q27;q32) and t(3;22)(q27;q11) in B-cell lymphomas."; RL Proc. Natl. Acad. Sci. U.S.A. 90:5262-5266(1993). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Mao Y., Xiao X., He D., Luo C., Liu C., Lv D.; RT "Discovery of a novel BCL6 transcript and its expression in lung cancer."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-333 AND SER-343, RP MUTAGENESIS OF SER-333 AND SER-343, AND UBIQUITINATION. RX PubMed=9649500; DOI=10.1101/gad.12.13.1953; RA Niu H., Ye B.H., Dalla-Favera R.; RT "Antigen receptor signaling induces MAP kinase-mediated phosphorylation and RT degradation of the BCL-6 transcription factor."; RL Genes Dev. 12:1953-1961(1998). RN [10] RP INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL TRANSLOCATION RP WITH LCP1. RX PubMed=10469447; RX DOI=10.1002/(sici)1098-2264(199910)26:2<97::aid-gcc1>3.3.co;2-0; RA Galiegue-Zouitina S., Quief S., Hildebrand M.P., Denis C., RA Detourmignies L., Lai J.L., Kerckaert J.P.; RT "Nonrandom fusion of L-plastin(LCP1) and LAZ3(BCL6) genes by RT t(3;13)(q27;q14) chromosome translocation in two cases of B-cell non- RT Hodgkin lymphoma."; RL Genes Chromosomes Cancer 26:97-105(1999). RN [11] RP INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL TRANSLOCATION RP WITH IKZF1. RX PubMed=10753856; RA Hosokawa Y., Maeda Y., Ichinohasama R., Miura I., Taniwaki M., Seto M.; RT "The Ikaros gene, a central regulator of lymphoid differentiation, fuses to RT the BCL6 gene as a result of t(3;7)(q27;p12) translocation in a patient RT with diffuse large B-cell lymphoma."; RL Blood 95:2719-2721(2000). RN [12] RP FUNCTION AS TRANSCRIPTIONAL REPRESSOR, AND TISSUE SPECIFICITY. RX PubMed=10981963; DOI=10.1016/s1074-7613(00)00020-0; RA Shaffer A.L., Yu X., He Y., Boldrick J., Chan E.P., Staudt L.M.; RT "BCL-6 represses genes that function in lymphocyte differentiation, RT inflammation, and cell cycle control."; RL Immunity 13:199-212(2000). RN [13] RP FUNCTION AS TRANSCRIPTIONAL REPRESSOR, INVOLVEMENT IN B-CELL NON-HODGKIN RP LYMPHOMA, AND CHROMOSOMAL TRANSLOCATION WITH HISTONE H4. RX PubMed=12414651; RA Kurata M., Maesako Y., Ueda C., Nishikori M., Akasaka T., Uchiyama T., RA Ohno H.; RT "Characterization of t(3;6)(q27;p21) breakpoints in B-cell non-Hodgkin's RT lymphoma and construction of the histone H4/BCL6 fusion gene, leading to RT altered expression of Bcl-6."; RL Cancer Res. 62:6224-6230(2002). RN [14] RP FUNCTION AS TRANSCRIPTIONAL REPRESSOR, ACETYLATION AT LYS-379, RP DEACETYLATION, INTERACTION WITH HDAC2, TISSUE SPECIFICITY, AND MUTAGENESIS RP OF LYS-376; LYS-377 AND LYS-379. RX PubMed=12402037; DOI=10.1038/ng1018; RA Bereshchenko O.R., Gu W., Dalla-Favera R.; RT "Acetylation inactivates the transcriptional repressor BCL6."; RL Nat. Genet. 32:606-613(2002). RN [15] RP INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL TRANSLOCATION RP WITH IL21R. RX PubMed=11821949; DOI=10.1038/sj.onc.1205099; RA Ueda C., Akasaka T., Kurata M., Maesako Y., Nishikori M., Ichinohasama R., RA Imada K., Uchiyama T., Ohno H.; RT "The gene for interleukin-21 receptor is the partner of BCL6 in RT t(3;16)(q27;p11), which is recurrently observed in diffuse large B-cell RT lymphoma."; RL Oncogene 21:368-376(2002). RN [16] RP FUNCTION AS TRANSCRIPTIONAL REPRESSOR, DNA-BINDING, SUBCELLULAR LOCATION, RP INTERACTION WITH HDAC5, AND MUTAGENESIS OF 520-CYS--CYS-523; RP 548-CYS--CYS-551; 576-CYS--CYS-579; 604-CYS--CYS-607; 632-CYS--CYS-635 AND RP 660-CYS--CYS-663. RX PubMed=12504096; DOI=10.1016/s0006-291x(02)02873-5; RA Mascle X., Albagli O., Lemercier C.; RT "Point mutations in BCL6 DNA-binding domain reveal distinct roles for the RT six zinc fingers."; RL Biochem. Biophys. Res. Commun. 300:391-396(2003). RN [17] RP INTERACTION WITH HDAC9. RX PubMed=12590135; DOI=10.1074/jbc.m212935200; RA Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M., RA Zelent A.; RT "The histone deacetylase 9 gene encodes multiple protein isoforms."; RL J. Biol. Chem. 278:16059-16072(2003). RN [18] RP FUNCTION IN B-CELL DIFFERENTIATION, INTERACTION WITH NCOR1; NCOR2 AND NURD RP COMPLEX, ACETYLATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-379 AND RP 376-LYS--LYS-379. RX PubMed=15454082; DOI=10.1016/j.cell.2004.09.014; RA Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., RA Wade P.A.; RT "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte RT differentiation."; RL Cell 119:75-86(2004). RN [19] RP FUNCTION AS TP53 TRANSCRIPTIONAL REPRESSOR. RX PubMed=15577913; DOI=10.1038/nature03147; RA Phan R.T., Dalla-Favera R.; RT "The BCL6 proto-oncogene suppresses p53 expression in germinal-centre B- RT cells."; RL Nature 432:635-639(2004). RN [20] RP FUNCTION AS TRANSCRIPTIONAL REPRESSOR, INTERACTION WITH ZBTB17, AND TISSUE RP SPECIFICITY. RX PubMed=16142238; DOI=10.1038/ni1245; RA Phan R.T., Saito M., Basso K., Niu H., Dalla-Favera R.; RT "BCL6 interacts with the transcription factor Miz-1 to suppress the cyclin- RT dependent kinase inhibitor p21 and cell cycle arrest in germinal center B RT cells."; RL Nat. Immunol. 6:1054-1060(2005). RN [21] RP INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=16455075; DOI=10.1016/j.yexcr.2005.12.020; RA Pantano S., Jarrossay D., Saccani S., Bosisio D., Natoli G.; RT "Plastic downregulation of the transcriptional repressor BCL6 during RT maturation of human dendritic cells."; RL Exp. Cell Res. 312:1312-1322(2006). RN [22] RP FUNCTION, PHOSPHORYLATION BY ATM, INDUCTION BY GENOTOXIC STRESS, RP INTERACTION WITH PIN1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP MUTAGENESIS OF THR-190; SER-250 AND SER-260. RX PubMed=17828269; DOI=10.1038/ni1508; RA Phan R.T., Saito M., Kitagawa Y., Means A.R., Dalla-Favera R.; RT "Genotoxic stress regulates expression of the proto-oncogene Bcl6 in RT germinal center B cells."; RL Nat. Immunol. 8:1132-1139(2007). RN [23] RP FUNCTION AS AUTOINHIBITOR, INTERACTION WITH CTBP1; HDAC2 AND NCOR2, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF ASN-21; HIS-116 AND 376-LYS--LYS-379. RX PubMed=18212045; DOI=10.1128/mcb.01400-07; RA Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A., RA Ye B.H.; RT "CtBP is an essential corepressor for BCL6 autoregulation."; RL Mol. Cell. Biol. 28:2175-2186(2008). RN [24] RP FUNCTION IN MIRNA REGULATION, AND SUBCELLULAR LOCATION. RX PubMed=23166356; DOI=10.1084/jem.20121387; RA Basso K., Schneider C., Shen Q., Holmes A.B., Setty M., Leslie C., RA Dalla-Favera R.; RT "BCL6 positively regulates AID and germinal center gene expression via RT repression of miR-155."; RL J. Exp. Med. 209:2455-2465(2012). RN [25] RP FUNCTION, INTERACTION WITH SCF(FBXO11) COMPLEX, UBIQUITINATION, RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX PubMed=22113614; DOI=10.1038/nature10688; RA Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C., di Celle P.F., RA Chapuy B., Shipp M., Chiarle R., Pagano M.; RT "FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B- RT cell lymphomas."; RL Nature 481:90-93(2012). RN [26] RP FUNCTION AS TRANSCRIPTIONAL REPRESSOR, INTERACTION WITH BCOR; HDAC3; NCOR1 RP AND NCOR2, AND DNA-BINDING. RX PubMed=23911289; DOI=10.1016/j.celrep.2013.06.016; RA Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D., RA Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M., RA Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W., RA Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.; RT "A hybrid mechanism of action for BCL6 in B cells defined by formation of RT functionally distinct complexes at enhancers and promoters."; RL Cell Rep. 4:578-588(2013). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [28] RP UBIQUITINATION, AND MUTAGENESIS OF SER-59. RX PubMed=30190310; DOI=10.1126/science.aap8236; RA Mena E.L., Kjolby R.A.S., Saxton R.A., Werner A., Lew B.G., Boyle J.M., RA Harland R., Rape M.; RT "Dimerization quality control ensures neuronal development and survival."; RL Science 362:eaap8236-eaap8236(2018). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 5-129 IN COMPLEX WITH NCOR2. RX PubMed=14690607; DOI=10.1016/s1097-2765(03)00454-4; RA Ahmad K.F., Melnick A., Lax S., Bouchard D., Liu J., Kiang C.L., Mayer S., RA Takahashi S., Licht J.D., Prive G.G.; RT "Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain."; RL Mol. Cell 12:1551-1564(2003). RN [30] RP STRUCTURE BY NMR OF 598-657. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the C2H2 type zinc finger (region 598-654) of human RT B-cell lymphoma 6 protein."; RL Submitted (OCT-2007) to the PDB data bank. RN [31] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 5-129. RX PubMed=19052359; DOI=10.1107/s1744309108036063; RA Stead M.A., Rosbrook G.O., Hadden J.M., Trinh C.H., Carr S.B., Wright S.C.; RT "Structure of the wild-type human BCL6 POZ domain."; RL Acta Crystallogr. F 64:1101-1104(2008). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 5-129 IN COMPLEX WITH BCOR, RP FUNCTION, AND SUBUNIT. RX PubMed=18280243; DOI=10.1016/j.molcel.2007.12.026; RA Ghetu A.F., Corcoran C.M., Cerchietti L., Bardwell V.J., Melnick A., RA Prive G.G.; RT "Structure of a BCOR corepressor peptide in complex with the BCL6 BTB RT domain dimer."; RL Mol. Cell 29:384-391(2008). RN [33] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 5-129 IN COMPLEX WITH INHIBITOR. RX PubMed=20385364; DOI=10.1016/j.ccr.2009.12.050; RA Cerchietti L.C., Ghetu A.F., Zhu X., Da Silva G.F., Zhong S., Matthews M., RA Bunting K.L., Polo J.M., Fares C., Arrowsmith C.H., Yang S.N., Garcia M., RA Coop A., Mackerell A.D. Jr., Prive G.G., Melnick A.; RT "A small-molecule inhibitor of BCL6 kills DLBCL cells in vitro and in RT vivo."; RL Cancer Cell 17:400-411(2010). CC -!- FUNCTION: Transcriptional repressor mainly required for germinal center CC (GC) formation and antibody affinity maturation which has different CC mechanisms of action specific to the lineage and biological functions. CC Forms complexes with different corepressors and histone deacetylases to CC repress the transcriptional expression of different subsets of target CC genes. Represses its target genes by binding directly to the DNA CC sequence 5'-TTCCTAGAA-3' (BCL6-binding site) or indirectly by CC repressing the transcriptional activity of transcription factors. In GC CC B-cells, represses genes that function in differentiation, CC inflammation, apoptosis and cell cycle control, also autoregulates its CC transcriptional expression and up-regulates, indirectly, the expression CC of some genes important for GC reactions, such as AICDA, through the CC repression of microRNAs expression, like miR155. An important function CC is to allow GC B-cells to proliferate very rapidly in response to T- CC cell dependent antigens and tolerate the physiological DNA breaks CC required for immunglobulin class switch recombination and somatic CC hypermutation without inducing a p53/TP53-dependent apoptotic response. CC In follicular helper CD4(+) T-cells (T(FH) cells), promotes the CC expression of T(FH)-related genes but inhibits the differentiation of CC T(H)1, T(H)2 and T(H)17 cells. Also required for the establishment and CC maintenance of immunological memory for both T- and B-cells. Suppresses CC macrophage proliferation through competition with STAT5 for STAT- CC binding motifs binding on certain target genes, such as CCL2 and CCND2. CC In response to genotoxic stress, controls cell cycle arrest in GC B- CC cells in both p53/TP53-dependedent and -independent manners. Besides, CC also controls neurogenesis through the alteration of the composition of CC NOTCH-dependent transcriptional complexes at selective NOTCH targets, CC such as HES5, including the recruitment of the deacetylase SIRT1 and CC resulting in an epigenetic silencing leading to neuronal CC differentiation. {ECO:0000269|PubMed:10981963, CC ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:12414651, CC ECO:0000269|PubMed:12504096, ECO:0000269|PubMed:15454082, CC ECO:0000269|PubMed:15577913, ECO:0000269|PubMed:16142238, CC ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:18212045, CC ECO:0000269|PubMed:18280243, ECO:0000269|PubMed:22113614, CC ECO:0000269|PubMed:23166356, ECO:0000269|PubMed:23911289, CC ECO:0000269|PubMed:9649500}. CC -!- SUBUNIT: Homodimer. Interacts (via BTB domain) with the corepressors CC BCOR, NCOR1 and SMRT/NCOR2; the interactions are direct. Forms CC preferably ternary complexes with BCOR and SMRT/NCOR2 on target gene CC promoters but, on enhancer elements, interacts with SMRT/NCOR2 and CC HDAC3 to repress proximal gene expression. Interacts with histone CC deacetylases HDAC2, HDAC5 and HDAC9 (via the catalytic domain). CC Interacts with ZBTB7 and BCL6B. Interacts with SCF(FBXO11) complex; the CC interaction is independent of phosphorylation and promotes CC ubiquitination. Interacts (when phosphorylated) with PIN1; the CC interaction is required for BCL6 degradation upon genotoxic stress. CC Interacts with ZBTB17; inhibits ZBTB17 transcriptional activity. CC Interacts with CTBP1, autoinhibits its transcriptional expression. CC Interacts with NOTCH1 NCID and SIRT1; leads to a epigenetic repression CC of selective NOTCH1-target genes. Interacts (nor via BTB domain neither CC acetylated) with the NuRD complex components CHD4, HDAC1, MBD3 and CC MTA3; the interaction with MTA3 inhibits BCL6 acetylation and is CC required for BCL6 transpriptional repression. CC {ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:12504096, CC ECO:0000269|PubMed:12590135, ECO:0000269|PubMed:14690607, CC ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:16142238, CC ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:18212045, CC ECO:0000269|PubMed:18280243, ECO:0000269|PubMed:20385364, CC ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23911289}. CC -!- INTERACTION: CC P41182; Q8N9V6-2: ANKRD53; NbExp=3; IntAct=EBI-765407, EBI-13345447; CC P41182; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-765407, EBI-2875665; CC P41182; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-765407, EBI-12811889; CC P41182; P41182: BCL6; NbExp=4; IntAct=EBI-765407, EBI-765407; CC P41182; A8KA13: BCL6B; NbExp=3; IntAct=EBI-765407, EBI-10174813; CC P41182; Q9H2G9: BLZF1; NbExp=4; IntAct=EBI-765407, EBI-2548012; CC P41182; Q6P656: CFAP161; NbExp=3; IntAct=EBI-765407, EBI-11901329; CC P41182; B2RV13: CFAP97D1; NbExp=3; IntAct=EBI-765407, EBI-12870048; CC P41182; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-765407, EBI-743033; CC P41182; Q9NTM9: CUTC; NbExp=3; IntAct=EBI-765407, EBI-714918; CC P41182; Q86XK2: FBXO11; NbExp=9; IntAct=EBI-765407, EBI-1047804; CC P41182; Q08379: GOLGA2; NbExp=5; IntAct=EBI-765407, EBI-618309; CC P41182; P56524: HDAC4; NbExp=3; IntAct=EBI-765407, EBI-308629; CC P41182; Q9UKV0: HDAC9; NbExp=2; IntAct=EBI-765407, EBI-765444; CC P41182; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-765407, EBI-2125614; CC P41182; Q53G59: KLHL12; NbExp=3; IntAct=EBI-765407, EBI-740929; CC P41182; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-765407, EBI-10693436; CC P41182; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-765407, EBI-11953846; CC P41182; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-765407, EBI-12811111; CC P41182; P0CW20: LIMS4; NbExp=6; IntAct=EBI-765407, EBI-10196832; CC P41182; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-765407, EBI-10302990; CC P41182; Q99471: PFDN5; NbExp=3; IntAct=EBI-765407, EBI-357275; CC P41182; Q8WVV4-1: POF1B; NbExp=3; IntAct=EBI-765407, EBI-11986735; CC P41182; Q8NI37: PPTC7; NbExp=3; IntAct=EBI-765407, EBI-9089276; CC P41182; P28070: PSMB4; NbExp=3; IntAct=EBI-765407, EBI-603350; CC P41182; Q04864-2: REL; NbExp=3; IntAct=EBI-765407, EBI-10829018; CC P41182; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-765407, EBI-747107; CC P41182; Q96LM5: SPMIP2; NbExp=3; IntAct=EBI-765407, EBI-12020542; CC P41182; Q8N865: SPMIP4; NbExp=3; IntAct=EBI-765407, EBI-10174456; CC P41182; Q8NCR6: SPMIP6; NbExp=3; IntAct=EBI-765407, EBI-10269322; CC P41182; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-765407, EBI-750487; CC P41182; Q08117: TLE5; NbExp=3; IntAct=EBI-765407, EBI-717810; CC P41182; Q12888: TP53BP1; NbExp=3; IntAct=EBI-765407, EBI-396540; CC P41182; Q13077: TRAF1; NbExp=5; IntAct=EBI-765407, EBI-359224; CC P41182; Q12933: TRAF2; NbExp=3; IntAct=EBI-765407, EBI-355744; CC P41182; Q96RU7: TRIB3; NbExp=4; IntAct=EBI-765407, EBI-492476; CC P41182; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-765407, EBI-7705033; CC P41182; O15156: ZBTB7B; NbExp=3; IntAct=EBI-765407, EBI-740434; CC P41182; Q9ULU4: ZMYND8; NbExp=3; IntAct=EBI-765407, EBI-765834; CC P41182; O43257: ZNHIT1; NbExp=3; IntAct=EBI-765407, EBI-347522; CC P41182; P45481: Crebbp; Xeno; NbExp=2; IntAct=EBI-765407, EBI-296306; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12504096, CC ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:22113614, CC ECO:0000269|PubMed:23166356}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P41182-1; Sequence=Displayed; CC Name=2; CC IsoId=P41182-2; Sequence=VSP_042709; CC -!- TISSUE SPECIFICITY: Expressed in germinal center T- and B-cells and in CC primary immature dendritic cells. {ECO:0000269|PubMed:10981963, CC ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:15454082, CC ECO:0000269|PubMed:16142238, ECO:0000269|PubMed:16455075, CC ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:18212045, CC ECO:0000269|PubMed:9649500}. CC -!- INDUCTION: Down-regulated during maturation of dendritic cells by CC selective stimuli such as bacterial lipopolysaccharides (LPS), CD40LG CC and zymosan. Protein levels decreases upon genotoxic stress in a CC dose- and time-dependent way. {ECO:0000269|PubMed:16455075, CC ECO:0000269|PubMed:17828269}. CC -!- DOMAIN: The BTB domain mediates homodimerization. Its dimer interface CC mediates peptide binding such as to corepressors BCOR and NCOR2 CC (PubMed:18212045). Interaction with corepressors through the BTB domain CC is needed to facilitate the rapid proliferation and survival of GC B- CC cells but is not involved in the T(FH) formation and BCL6-mediated CC suppression of T(H)2 and T(H)17 differentiationrequired for GC CC formation (By similarity). {ECO:0000250, ECO:0000269|PubMed:18212045}. CC -!- PTM: Phosphorylated by MAPK1 in response to antigen receptor activation CC at Ser-333 and Ser-343. Phosphorylated by ATM in response to genotoxic CC stress. Phosphorylation induces its degradation by ubiquitin/proteasome CC pathway. {ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:22113614, CC ECO:0000269|PubMed:9649500}. CC -!- PTM: Polyubiquitinated (PubMed:9649500, PubMed:22113614, CC PubMed:30190310). Polyubiquitinated by SCF(FBXO11), leading to its CC degradation by the proteasome (PubMed:22113614). Ubiquitinated by the CC SCF(FBXL17) complex, leading to its degradation by the proteasome: CC ubiquitination by the SCF(FBXL17) complex takes place when aberrant BTB CC domain dimers are formed (PubMed:30190310). CC {ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:30190310, CC ECO:0000269|PubMed:9649500}. CC -!- PTM: Acetylated at Lys-379 by EP300 which inhibits the interaction with CC NuRD complex and the transcriptional repressor function. Deacetylated CC by HDAC- and SIR2-dependent pathways. {ECO:0000269|PubMed:12402037, CC ECO:0000269|PubMed:15454082}. CC -!- DISEASE: Note=Chromosomal aberrations involving BCL6 are a cause of B- CC cell non-Hodgkin lymphomas (B-cell NHL), including diffuse large B-cell CC lymphoma and follicular lymphoma. Approximately 40% of diffuse large B- CC cell lymphomas and 5 to 10% of follicular lymphomas are associated with CC chromosomal translocations that deregulate expression of BCL6 by CC juxtaposing heterologous promoters to the BCL6 coding domain CC (PubMed:10469447, PubMed:10753856, PubMed:12414651, PubMed:11821949). CC Translocation t(3;14)(q27;q32). Translocation t(3;22)(q27;q11) with CC immunoglobulin gene regions (PubMed:11821949). Translocation CC t(3;7)(q27;p12) with IKZF1 gene 5'non-coding region (PubMed:10753856). CC Translocation t(3;6)(q27;p21) with Histone H4 (PubMed:12414651). CC Translocation t(3;16)(q27;p11) with IL21R. Translocation CC t(3;13)(q27;q14) with LCP1 (PubMed:10469447). CC {ECO:0000269|PubMed:10469447, ECO:0000269|PubMed:10753856, CC ECO:0000269|PubMed:11821949, ECO:0000269|PubMed:12414651}. CC -!- DISEASE: Note=A chromosomal aberration involving BCL6 may be a cause of CC a form of B-cell leukemia. Translocation t(3;11)(q27;q23) with CC POU2AF1/OBF1. CC -!- DISEASE: Note=A chromosomal aberration involving BCL6 may be a cause of CC lymphoma. Translocation t(3;4)(q27;p11) with ARHH/TTF. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/20/BCL6"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z21943; CAA79937.1; -; mRNA. DR EMBL; U00115; AAC50054.1; -; mRNA. DR EMBL; S67779; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; EU139066; ABX45135.1; -; mRNA. DR EMBL; AC072022; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78140.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78141.1; -; Genomic_DNA. DR EMBL; BC150184; AAI50185.1; -; mRNA. DR CCDS; CCDS3289.1; -. [P41182-1] DR CCDS; CCDS46975.1; -. [P41182-2] DR PIR; A48752; A48752. DR PIR; I52586; I52586. DR RefSeq; NP_001124317.1; NM_001130845.1. [P41182-1] DR RefSeq; NP_001128210.1; NM_001134738.1. [P41182-2] DR RefSeq; NP_001697.2; NM_001706.4. [P41182-1] DR RefSeq; XP_005247751.1; XM_005247694.3. [P41182-1] DR RefSeq; XP_011511364.1; XM_011513062.2. [P41182-2] DR PDB; 1R28; X-ray; 2.20 A; A/B=5-129. DR PDB; 1R29; X-ray; 1.30 A; A=5-129. DR PDB; 1R2B; X-ray; 2.20 A; A/B=5-129. DR PDB; 2EN2; NMR; -; A=598-626. DR PDB; 2EOS; NMR; -; A=626-654. DR PDB; 2LCE; NMR; -; A=540-602. DR PDB; 2YRM; NMR; -; A=515-544. DR PDB; 3BIM; X-ray; 2.60 A; A/B/C/D/E/F/G/H=5-129. DR PDB; 3E4U; X-ray; 2.10 A; A/B/C/D/E/F=5-129. DR PDB; 3LBZ; X-ray; 2.30 A; A/B=5-129. DR PDB; 4CP3; X-ray; 2.30 A; A/B=9-128. DR PDB; 4U2M; X-ray; 2.23 A; A/B/C/D=5-129. DR PDB; 5H7G; X-ray; 1.85 A; A/B=5-129. DR PDB; 5H7H; X-ray; 1.95 A; A=5-129. DR PDB; 5MW2; X-ray; 2.35 A; A=5-129. DR PDB; 5MW6; X-ray; 1.65 A; A/B=5-129. DR PDB; 5MWD; X-ray; 1.85 A; A=5-129. DR PDB; 5N1X; X-ray; 1.72 A; A=9-128, B/C=7-127, D=9-125. DR PDB; 5N1Z; X-ray; 1.81 A; A=6-128. DR PDB; 5N20; X-ray; 1.38 A; A=6-128. DR PDB; 5N21; X-ray; 1.58 A; A/B=7-128. DR PDB; 5X4M; X-ray; 1.65 A; A=5-129. DR PDB; 5X4N; X-ray; 1.94 A; A=5-129. DR PDB; 5X4O; X-ray; 2.05 A; A=5-129. DR PDB; 5X4P; X-ray; 2.06 A; A=5-129. DR PDB; 5X4Q; X-ray; 2.00 A; A=5-129. DR PDB; 5X9O; X-ray; 1.58 A; A=5-129. DR PDB; 5X9P; X-ray; 1.86 A; A=5-129. DR PDB; 6C3L; X-ray; 1.46 A; A/B=5-129. DR PDB; 6C3N; X-ray; 2.53 A; A/B=1-129. DR PDB; 6CQ1; X-ray; 1.70 A; A/B=1-129. DR PDB; 6EW6; X-ray; 1.39 A; A=6-128. DR PDB; 6EW7; X-ray; 1.60 A; A/B=7-128. DR PDB; 6EW8; X-ray; 1.84 A; A=6-129. DR PDB; 6TBT; X-ray; 1.63 A; A/B=6-129. DR PDB; 6TCJ; X-ray; 2.13 A; A/B=6-129. DR PDB; 6TOF; X-ray; 1.67 A; A=5-129. DR PDB; 6TOG; X-ray; 1.69 A; A=5-129. DR PDB; 6TOH; X-ray; 1.58 A; A=5-129. DR PDB; 6TOI; X-ray; 1.58 A; A=5-129. DR PDB; 6TOJ; X-ray; 1.85 A; A=5-129. DR PDB; 6TOK; X-ray; 1.43 A; A=5-129. DR PDB; 6TOL; X-ray; 1.64 A; A=5-129. DR PDB; 6TOM; X-ray; 1.90 A; A=5-129. DR PDB; 6TON; X-ray; 2.36 A; A=5-129. DR PDB; 6TOO; X-ray; 1.53 A; A=5-129. DR PDB; 6XMX; EM; 3.70 A; A/B/C/D/E/F/G/H=5-360. DR PDB; 6XWF; X-ray; 1.60 A; A=6-129. DR PDB; 6XXS; X-ray; 3.25 A; A/B/E/F=6-129. DR PDB; 6XYX; X-ray; 1.44 A; A/B=6-129. DR PDB; 6XZZ; X-ray; 1.39 A; A=6-129. DR PDB; 6Y17; X-ray; 1.56 A; A/B=6-129. DR PDB; 6ZBU; X-ray; 2.46 A; A/B/E/F/I/J=6-129. DR PDB; 7BDE; X-ray; 2.04 A; A=5-129. DR PDB; 7LWE; X-ray; 1.17 A; A=1-129. DR PDB; 7LWF; X-ray; 1.22 A; A=5-129. DR PDB; 7LWG; X-ray; 1.30 A; A/B=5-129. DR PDB; 7LZQ; X-ray; 1.71 A; A=1-129. DR PDB; 7LZR; X-ray; 1.34 A; A/B/C/D=5-129. DR PDB; 7LZS; X-ray; 1.49 A; A=5-129. DR PDB; 7OKD; X-ray; 1.94 A; A=5-129. DR PDB; 7OKE; X-ray; 1.48 A; A=5-129. DR PDB; 7OKF; X-ray; 1.60 A; A=5-129. DR PDB; 7OKG; X-ray; 1.32 A; A=5-129. DR PDB; 7OKH; X-ray; 1.52 A; A=5-129. DR PDB; 7OKI; X-ray; 1.61 A; A=5-129. DR PDB; 7OKJ; X-ray; 1.43 A; A=5-129. DR PDB; 7OKK; X-ray; 2.05 A; A=5-129. DR PDB; 7OKL; X-ray; 1.20 A; A=5-129. DR PDB; 7OKM; X-ray; 1.48 A; A=5-129. DR PDB; 7Q7R; X-ray; 1.70 A; A=5-129. DR PDB; 7Q7S; X-ray; 1.44 A; A=5-129. DR PDB; 7Q7T; X-ray; 1.46 A; A=5-129. DR PDB; 7Q7U; X-ray; 1.78 A; A=5-129. DR PDB; 7Q7V; X-ray; 1.81 A; A=5-129. DR PDB; 7QK0; X-ray; 1.96 A; A=5-129. DR PDB; 7RUW; X-ray; 1.30 A; A=5-129. DR PDB; 7RUX; X-ray; 1.30 A; A=5-129. DR PDB; 7RUY; X-ray; 1.27 A; A=5-129. DR PDB; 7RUZ; X-ray; 1.62 A; A=5-129. DR PDB; 7RV0; X-ray; 1.45 A; A=5-129. DR PDB; 7RV1; X-ray; 1.17 A; A=5-129. DR PDB; 7RV2; X-ray; 1.29 A; A=5-129. DR PDB; 7RV3; X-ray; 1.35 A; A=5-129. DR PDB; 7RV4; X-ray; 1.25 A; A=5-129. DR PDB; 7RV5; X-ray; 2.21 A; A=5-129. DR PDB; 7RV6; X-ray; 1.68 A; A=5-129. DR PDB; 7RV7; X-ray; 1.63 A; A=5-129. DR PDB; 7RV8; X-ray; 1.25 A; A=5-129. DR PDB; 7RV9; X-ray; 1.50 A; A=5-129. DR PDB; 7T0S; X-ray; 1.86 A; A/B/C=5-129. DR PDB; 7T0T; X-ray; 2.00 A; A/B/C/D/E/F=5-129. DR PDB; 7T0U; X-ray; 1.49 A; A/B/C/D=5-129. DR PDB; 7ZWN; X-ray; 2.05 A; A=5-129. DR PDB; 7ZWO; X-ray; 1.39 A; A=5-129. DR PDB; 7ZWP; X-ray; 1.85 A; A=5-129. DR PDB; 7ZWQ; X-ray; 1.65 A; A=5-129. DR PDB; 7ZWR; X-ray; 1.47 A; A=5-129. DR PDB; 7ZWS; X-ray; 1.53 A; A=5-129. DR PDB; 7ZWT; X-ray; 1.94 A; A=5-129. DR PDB; 7ZWU; X-ray; 1.56 A; A=5-129. DR PDB; 7ZWV; X-ray; 1.52 A; A=5-129. DR PDB; 7ZWW; X-ray; 1.67 A; A=5-129. DR PDB; 7ZWX; X-ray; 1.38 A; A=5-129. DR PDB; 7ZWY; X-ray; 1.65 A; A=5-129. DR PDB; 7ZWZ; X-ray; 1.40 A; A=5-129. DR PDB; 8AS9; X-ray; 3.40 A; A/B=6-129. DR PDB; 8C78; X-ray; 1.80 A; A=5-129. DR PDBsum; 1R28; -. DR PDBsum; 1R29; -. DR PDBsum; 1R2B; -. DR PDBsum; 2EN2; -. DR PDBsum; 2EOS; -. DR PDBsum; 2LCE; -. DR PDBsum; 2YRM; -. DR PDBsum; 3BIM; -. DR PDBsum; 3E4U; -. DR PDBsum; 3LBZ; -. DR PDBsum; 4CP3; -. DR PDBsum; 4U2M; -. DR PDBsum; 5H7G; -. DR PDBsum; 5H7H; -. DR PDBsum; 5MW2; -. DR PDBsum; 5MW6; -. DR PDBsum; 5MWD; -. DR PDBsum; 5N1X; -. DR PDBsum; 5N1Z; -. DR PDBsum; 5N20; -. DR PDBsum; 5N21; -. DR PDBsum; 5X4M; -. DR PDBsum; 5X4N; -. DR PDBsum; 5X4O; -. DR PDBsum; 5X4P; -. DR PDBsum; 5X4Q; -. DR PDBsum; 5X9O; -. DR PDBsum; 5X9P; -. DR PDBsum; 6C3L; -. DR PDBsum; 6C3N; -. DR PDBsum; 6CQ1; -. DR PDBsum; 6EW6; -. DR PDBsum; 6EW7; -. DR PDBsum; 6EW8; -. DR PDBsum; 6TBT; -. DR PDBsum; 6TCJ; -. DR PDBsum; 6TOF; -. DR PDBsum; 6TOG; -. DR PDBsum; 6TOH; -. DR PDBsum; 6TOI; -. DR PDBsum; 6TOJ; -. DR PDBsum; 6TOK; -. DR PDBsum; 6TOL; -. DR PDBsum; 6TOM; -. DR PDBsum; 6TON; -. DR PDBsum; 6TOO; -. DR PDBsum; 6XMX; -. DR PDBsum; 6XWF; -. DR PDBsum; 6XXS; -. DR PDBsum; 6XYX; -. DR PDBsum; 6XZZ; -. DR PDBsum; 6Y17; -. DR PDBsum; 6ZBU; -. DR PDBsum; 7BDE; -. DR PDBsum; 7LWE; -. DR PDBsum; 7LWF; -. DR PDBsum; 7LWG; -. DR PDBsum; 7LZQ; -. DR PDBsum; 7LZR; -. DR PDBsum; 7LZS; -. DR PDBsum; 7OKD; -. DR PDBsum; 7OKE; -. DR PDBsum; 7OKF; -. DR PDBsum; 7OKG; -. DR PDBsum; 7OKH; -. DR PDBsum; 7OKI; -. DR PDBsum; 7OKJ; -. DR PDBsum; 7OKK; -. DR PDBsum; 7OKL; -. DR PDBsum; 7OKM; -. DR PDBsum; 7Q7R; -. DR PDBsum; 7Q7S; -. DR PDBsum; 7Q7T; -. DR PDBsum; 7Q7U; -. DR PDBsum; 7Q7V; -. DR PDBsum; 7QK0; -. DR PDBsum; 7RUW; -. DR PDBsum; 7RUX; -. DR PDBsum; 7RUY; -. DR PDBsum; 7RUZ; -. DR PDBsum; 7RV0; -. DR PDBsum; 7RV1; -. DR PDBsum; 7RV2; -. DR PDBsum; 7RV3; -. DR PDBsum; 7RV4; -. DR PDBsum; 7RV5; -. DR PDBsum; 7RV6; -. DR PDBsum; 7RV7; -. DR PDBsum; 7RV8; -. DR PDBsum; 7RV9; -. DR PDBsum; 7T0S; -. DR PDBsum; 7T0T; -. DR PDBsum; 7T0U; -. DR PDBsum; 7ZWN; -. DR PDBsum; 7ZWO; -. DR PDBsum; 7ZWP; -. DR PDBsum; 7ZWQ; -. DR PDBsum; 7ZWR; -. DR PDBsum; 7ZWS; -. DR PDBsum; 7ZWT; -. DR PDBsum; 7ZWU; -. DR PDBsum; 7ZWV; -. DR PDBsum; 7ZWW; -. DR PDBsum; 7ZWX; -. DR PDBsum; 7ZWY; -. DR PDBsum; 7ZWZ; -. DR PDBsum; 8AS9; -. DR PDBsum; 8C78; -. DR AlphaFoldDB; P41182; -. DR EMDB; EMD-22265; -. DR SMR; P41182; -. DR BioGRID; 107076; 229. DR CORUM; P41182; -. DR DIP; DIP-2651N; -. DR IntAct; P41182; 126. DR MINT; P41182; -. DR STRING; 9606.ENSP00000384371; -. DR BindingDB; P41182; -. DR ChEMBL; CHEMBL4105786; -. DR GuidetoPHARMACOLOGY; 2957; -. DR iPTMnet; P41182; -. DR PhosphoSitePlus; P41182; -. DR BioMuta; BCL6; -. DR DMDM; 728952; -. DR EPD; P41182; -. DR jPOST; P41182; -. DR MassIVE; P41182; -. DR MaxQB; P41182; -. DR PaxDb; 9606-ENSP00000384371; -. DR PeptideAtlas; P41182; -. DR ProteomicsDB; 55413; -. [P41182-1] DR ProteomicsDB; 55414; -. [P41182-2] DR TopDownProteomics; P41182-2; -. [P41182-2] DR Antibodypedia; 1434; 1309 antibodies from 50 providers. DR DNASU; 604; -. DR Ensembl; ENST00000232014.8; ENSP00000232014.4; ENSG00000113916.18. [P41182-1] DR Ensembl; ENST00000406870.7; ENSP00000384371.2; ENSG00000113916.18. [P41182-1] DR Ensembl; ENST00000450123.6; ENSP00000413122.2; ENSG00000113916.18. [P41182-2] DR Ensembl; ENST00000621333.4; ENSP00000479784.1; ENSG00000113916.18. [P41182-2] DR GeneID; 604; -. DR KEGG; hsa:604; -. DR MANE-Select; ENST00000406870.7; ENSP00000384371.2; NM_001706.5; NP_001697.2. DR UCSC; uc003frp.4; human. [P41182-1] DR AGR; HGNC:1001; -. DR CTD; 604; -. DR DisGeNET; 604; -. DR GeneCards; BCL6; -. DR HGNC; HGNC:1001; BCL6. DR HPA; ENSG00000113916; Tissue enhanced (skeletal). DR MalaCards; BCL6; -. DR MIM; 109565; gene. DR neXtProt; NX_P41182; -. DR OpenTargets; ENSG00000113916; -. DR Orphanet; 545; Follicular lymphoma. DR Orphanet; 480541; High grade B-cell lymphoma with MYC and/ or BCL2 and/or BCL6 rearrangement. DR Orphanet; 98839; Intravascular large B-cell lymphoma. DR Orphanet; 98838; Primary mediastinal large B-cell lymphoma. DR PharmGKB; PA25312; -. DR VEuPathDB; HostDB:ENSG00000113916; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000156311; -. DR HOGENOM; CLU_024196_1_0_1; -. DR InParanoid; P41182; -. DR OMA; DARMPMA; -. DR OrthoDB; 5352496at2759; -. DR PhylomeDB; P41182; -. DR TreeFam; TF330912; -. DR PathwayCommons; P41182; -. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain. DR Reactome; R-HSA-9614657; FOXO-mediated transcription of cell death genes. DR SignaLink; P41182; -. DR SIGNOR; P41182; -. DR BioGRID-ORCS; 604; 47 hits in 1225 CRISPR screens. DR ChiTaRS; BCL6; human. DR EvolutionaryTrace; P41182; -. DR GeneWiki; BCL6; -. DR GenomeRNAi; 604; -. DR Pharos; P41182; Tchem. DR PRO; PR:P41182; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P41182; Protein. DR Bgee; ENSG00000113916; Expressed in gastrocnemius and 211 other cell types or tissues. DR ExpressionAtlas; P41182; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0042382; C:paraspeckles; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0001161; F:intronic transcription regulatory region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl. DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl. DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl. DR GO; GO:0048870; P:cell motility; IEA:Ensembl. DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl. DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB. DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl. DR GO; GO:0002467; P:germinal center formation; IEA:Ensembl. DR GO; GO:0031507; P:heterochromatin formation; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0048289; P:isotype switching to IgE isotypes; IEA:Ensembl. DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; NAS:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB. DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl. DR GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0048294; P:negative regulation of isotype switching to IgE isotypes; IEA:Ensembl. DR GO; GO:0070664; P:negative regulation of leukocyte proliferation; IEA:Ensembl. DR GO; GO:0032764; P:negative regulation of mast cell cytokine production; IEA:Ensembl. DR GO; GO:1903464; P:negative regulation of mitotic cell cycle DNA replication; NAS:UniProtKB. DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:Ensembl. DR GO; GO:1900099; P:negative regulation of plasma cell differentiation; IEA:Ensembl. DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl. DR GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0002317; P:plasma cell differentiation; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl. DR GO; GO:2000147; P:positive regulation of cell motility; IEA:Ensembl. DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl. DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IMP:ARUK-UCL. DR GO; GO:0008104; P:protein localization; IEA:Ensembl. DR GO; GO:0021859; P:pyramidal neuron differentiation; IEA:Ensembl. DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central. DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central. DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central. DR GO; GO:0002634; P:regulation of germinal center formation; NAS:UniProtKB. DR GO; GO:0050776; P:regulation of immune response; NAS:UniProtKB. DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central. DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central. DR GO; GO:0043380; P:regulation of memory T cell differentiation; IEA:Ensembl. DR GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl. DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0045064; P:T-helper 2 cell differentiation; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0042092; P:type 2 immune response; IBA:GO_Central. DR CDD; cd18331; BTB_POZ_ZBTB27_BCL6; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6. DR IDEAL; IID00372; -. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24394:SF36; B-CELL CLL_LYMPHOMA 6 (ZINC FINGER PROTEIN 51)-RELATED; 1. DR PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 4. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 6. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. DR Genevisible; P41182; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Chromosomal rearrangement; DNA-binding; Immunity; Inflammatory response; KW Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; KW Repeat; Repressor; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..706 FT /note="B-cell lymphoma 6 protein" FT /id="PRO_0000047098" FT DOMAIN 32..99 FT /note="BTB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037" FT ZN_FING 518..541 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 546..568 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 574..596 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 602..624 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 630..652 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 658..681 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 317..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 376..379 FT /note="Required for interaction with NuRD complex and for FT transcriptional repressor activity" FT REGION 407..467 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 326..349 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 425..467 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 333 FT /note="Phosphoserine; by MAPK1" FT /evidence="ECO:0000269|PubMed:9649500, FT ECO:0007744|PubMed:23186163" FT MOD_RES 343 FT /note="Phosphoserine; by MAPK1" FT /evidence="ECO:0000269|PubMed:9649500" FT MOD_RES 361 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P41183" FT MOD_RES 379 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:12402037" FT MOD_RES 404 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P41183" FT VAR_SEQ 514..569 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_042709" FT VARIANT 252 FT /note="N -> S (in dbSNP:rs34463990)" FT /id="VAR_052709" FT VARIANT 493 FT /note="A -> T (in dbSNP:rs2229362)" FT /id="VAR_019970" FT VARIANT 676 FT /note="H -> Y (in dbSNP:rs1056936)" FT /id="VAR_014825" FT MUTAGEN 21 FT /note="N->K: Abolishes interaction with NCOR2 and HDAC2, no FT effect on interaction with CTBP1 and transcriptional FT autoinhibition; when associated with A-116 and FT 376-Q--Q-379." FT /evidence="ECO:0000269|PubMed:18212045" FT MUTAGEN 59 FT /note="S->A: Abolished ubiquitination by the SCF(FBXL17) FT complex." FT /evidence="ECO:0000269|PubMed:30190310" FT MUTAGEN 116 FT /note="H->A: Abolishes interaction with NCOR2 and HDAC2, no FT effect on interaction with CTBP1 and transcriptional FT autoinhibition; when associated with K-21 and FT 376-Q--Q-379." FT /evidence="ECO:0000269|PubMed:18212045" FT MUTAGEN 190 FT /note="T->A: No effect on interaction with PIN1." FT /evidence="ECO:0000269|PubMed:17828269" FT MUTAGEN 250 FT /note="S->A: No effect on interaction with PIN1." FT /evidence="ECO:0000269|PubMed:17828269" FT MUTAGEN 260 FT /note="S->A: Strongly reduces interaction with PIN1." FT /evidence="ECO:0000269|PubMed:17828269" FT MUTAGEN 333 FT /note="S->A: Decrease in phosphorylation by MAPK1." FT /evidence="ECO:0000269|PubMed:9649500" FT MUTAGEN 343 FT /note="S->A: Decrease in phosphorylation by MAPK1." FT /evidence="ECO:0000269|PubMed:9649500" FT MUTAGEN 376..379 FT /note="KKYK->QQYQ: Abolishes interaction with HDAC2 and FT MTA3 as well as transcriptional repressor and transforming FT activities. Abolishes interaction with NCOR2 and HDAC2, no FT effect on interaction with CTBP1 and transcriptional FT autoinhibition; when associated with K-21 and A-116." FT /evidence="ECO:0000269|PubMed:15454082, FT ECO:0000269|PubMed:18212045" FT MUTAGEN 376 FT /note="K->R: No effect on acetylation." FT /evidence="ECO:0000269|PubMed:12402037" FT MUTAGEN 377 FT /note="K->R: No effect on acetylation." FT /evidence="ECO:0000269|PubMed:12402037" FT MUTAGEN 379 FT /note="K->R: Abolishes acetylation. No effect on FT interaction with MTA3, NCOR1 and NCOR2." FT /evidence="ECO:0000269|PubMed:12402037, FT ECO:0000269|PubMed:15454082" FT MUTAGEN 520..523 FT /note="CNEC->GNEG: No effect on DNA-binding, nuclear FT localization, transcriptional repression activity and FT interaction with HDAC5." FT /evidence="ECO:0000269|PubMed:12504096" FT MUTAGEN 548..551 FT /note="CDRC->GDRG: No effect on DNA-binding, nuclear FT localization, transcriptional repression activity and FT interaction with HDAC5." FT /evidence="ECO:0000269|PubMed:12504096" FT MUTAGEN 576..579 FT /note="CNIC->GNIG: Abolishes DNA-binding and FT transcriptional repression activity, no effect on nuclear FT localization and interaction with HDAC5." FT /evidence="ECO:0000269|PubMed:12504096" FT MUTAGEN 604..607 FT /note="CETC->GETG: Abolishes DNA-binding and FT transcriptional repression activity, perturbs nuclear FT localization. No effect on interaction with HDAC5." FT /evidence="ECO:0000269|PubMed:12504096" FT MUTAGEN 632..635 FT /note="CEIC->GEIG: Abolishes DNA-binding and FT transcriptional repression activity, no effect on nuclear FT localization and interaction with HDAC5." FT /evidence="ECO:0000269|PubMed:12504096" FT MUTAGEN 660..663 FT /note="CEKC->GEKG: Abolishes DNA-binding and FT transcriptional repression activity, perturbs nuclear FT localization. No effect on interaction with HDAC5." FT /evidence="ECO:0000269|PubMed:12504096" FT CONFLICT 347 FT /note="S -> A (in Ref. 2; AAC50054)" FT /evidence="ECO:0000305" FT CONFLICT 393 FT /note="E -> G (in Ref. 2; AAC50054)" FT /evidence="ECO:0000305" FT CONFLICT 498 FT /note="P -> A (in Ref. 2; AAC50054)" FT /evidence="ECO:0000305" FT HELIX 5..7 FT /evidence="ECO:0007829|PDB:7LWE" FT STRAND 8..10 FT /evidence="ECO:0007829|PDB:6C3L" FT HELIX 14..27 FT /evidence="ECO:0007829|PDB:7LWE" FT TURN 29..31 FT /evidence="ECO:0007829|PDB:3E4U" FT STRAND 34..38 FT /evidence="ECO:0007829|PDB:7LWE" FT STRAND 41..45 FT /evidence="ECO:0007829|PDB:7LWE" FT HELIX 47..53 FT /evidence="ECO:0007829|PDB:7LWE" FT HELIX 55..62 FT /evidence="ECO:0007829|PDB:7LWE" FT TURN 64..68 FT /evidence="ECO:0007829|PDB:7LWE" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:7LWE" FT HELIX 80..92 FT /evidence="ECO:0007829|PDB:7LWE" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:7LWG" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:7LWE" FT HELIX 102..112 FT /evidence="ECO:0007829|PDB:7LWE" FT HELIX 115..127 FT /evidence="ECO:0007829|PDB:7LWE" FT STRAND 521..523 FT /evidence="ECO:0007829|PDB:2YRM" FT STRAND 527..529 FT /evidence="ECO:0007829|PDB:2YRM" FT HELIX 530..540 FT /evidence="ECO:0007829|PDB:2YRM" FT HELIX 558..568 FT /evidence="ECO:0007829|PDB:2LCE" FT STRAND 573..575 FT /evidence="ECO:0007829|PDB:2LCE" FT TURN 577..579 FT /evidence="ECO:0007829|PDB:2LCE" FT STRAND 582..584 FT /evidence="ECO:0007829|PDB:2LCE" FT HELIX 586..596 FT /evidence="ECO:0007829|PDB:2LCE" FT STRAND 601..603 FT /evidence="ECO:0007829|PDB:2EN2" FT TURN 605..607 FT /evidence="ECO:0007829|PDB:2EN2" FT STRAND 610..613 FT /evidence="ECO:0007829|PDB:2EN2" FT HELIX 614..620 FT /evidence="ECO:0007829|PDB:2EN2" FT HELIX 622..625 FT /evidence="ECO:0007829|PDB:2EN2" FT STRAND 633..635 FT /evidence="ECO:0007829|PDB:2EOS" FT STRAND 639..641 FT /evidence="ECO:0007829|PDB:2EOS" FT HELIX 642..648 FT /evidence="ECO:0007829|PDB:2EOS" FT TURN 649..652 FT /evidence="ECO:0007829|PDB:2EOS" SQ SEQUENCE 706 AA; 78846 MW; E38D83C213DAE2D0 CRC64; MASPADSCIQ FTRHASDVLL NLNRLRSRDI LTDVVIVVSR EQFRAHKTVL MACSGLFYSI FTDQLKCNLS VINLDPEINP EGFCILLDFM YTSRLNLREG NIMAVMATAM YLQMEHVVDT CRKFIKASEA EMVSAIKPPR EEFLNSRMLM PQDIMAYRGR EVVENNLPLR SAPGCESRAF APSLYSGLST PPASYSMYSH LPVSSLLFSD EEFRDVRMPV ANPFPKERAL PCDSARPVPG EYSRPTLEVS PNVCHSNIYS PKETIPEEAR SDMHYSVAEG LKPAAPSARN APYFPCDKAS KEEERPSSED EIALHFEPPN APLNRKGLVS PQSPQKSDCQ PNSPTESCSS KNACILQASG SPPAKSPTDP KACNWKKYKF IVLNSLNQNA KPEGPEQAEL GRLSPRAYTA PPACQPPMEP ENLDLQSPTK LSASGEDSTI PQASRLNNIV NRSMTGSPRS SSESHSPLYM HPPKCTSCGS QSPQHAEMCL HTAGPTFPEE MGETQSEYSD SSCENGAFFC NECDCRFSEE ASLKRHTLQT HSDKPYKCDR CQASFRYKGN LASHKTVHTG EKPYRCNICG AQFNRPANLK THTRIHSGEK PYKCETCGAR FVQVAHLRAH VLIHTGEKPY PCEICGTRFR HLQTLKSHLR IHTGEKPYHC EKCNLHFRHK SQLRLHLRQK HGAITNTKVQ YRVSATDLPP ELPKAC //