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B-cell lymphoma 6 protein (BCL-6) (B-cell lymphoma 5 protein) (BCL-5) (Protein LAZ-3) (Zinc finger and BTB domain-containing protein 27) (Zinc finger protein 51)

 BCL6_HUMAN              Reviewed;         706 AA.
P41182; A7E241; B8PSA7; D3DNV5;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
27-SEP-2017, entry version 189.
RecName: Full=B-cell lymphoma 6 protein;
Short=BCL-6;
AltName: Full=B-cell lymphoma 5 protein;
Short=BCL-5;
AltName: Full=Protein LAZ-3;
AltName: Full=Zinc finger and BTB domain-containing protein 27;
AltName: Full=Zinc finger protein 51;
Name=BCL6; Synonyms=BCL5, LAZ3, ZBTB27, ZNF51;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle;
PubMed=8220427; DOI=10.1038/ng0993-66;
Kerckaert J.-P., Deweindt C., Tilly H., Quief S., Lecocq G.,
Bastard C.;
"LAZ3, a novel zinc-finger encoding gene, is disrupted by recurring
chromosome 3q27 translocations in human lymphomas.";
Nat. Genet. 5:66-70(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8235596; DOI=10.1126/science.8235596;
Ye B.H., Lista F., Lo Coco F., Knowles D.M., Offit K.,
Chaganti R.S.K., Dalla-Favera R.;
"Alterations of a zinc finger-encoding gene, BCL-6, in diffuse large-
cell lymphoma.";
Science 262:747-750(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8274740;
Miki T., Kawamata N., Hirosawa S., Aoki N.;
"Gene involved in the 3q27 translocation associated with B-cell
lymphoma, BCL5, encodes a Kruppel-like zinc-finger protein.";
Blood 83:26-32(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8506375; DOI=10.1073/pnas.90.11.5262;
Baron B.W., Nucifora G., McCabe N., Espinosa R. III, le Beau M.M.,
McKeithan T.W.;
"Identification of the gene associated with the recurring chromosomal
translocations t(3;14)(q27;q32) and t(3;22)(q27;q11) in B-cell
lymphomas.";
Proc. Natl. Acad. Sci. U.S.A. 90:5262-5266(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Mao Y., Xiao X., He D., Luo C., Liu C., Lv D.;
"Discovery of a novel BCL6 transcript and its expression in lung
cancer.";
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-333 AND SER-343,
MUTAGENESIS OF SER-333 AND SER-343, AND UBIQUITINATION.
PubMed=9649500; DOI=10.1101/gad.12.13.1953;
Niu H., Ye B.H., Dalla-Favera R.;
"Antigen receptor signaling induces MAP kinase-mediated
phosphorylation and degradation of the BCL-6 transcription factor.";
Genes Dev. 12:1953-1961(1998).
[10]
INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL
TRANSLOCATION WITH LCP1.
PubMed=10469447;
DOI=10.1002/(SICI)1098-2264(199910)26:2<97::AID-GCC1>3.3.CO;2-0;
Galiegue-Zouitina S., Quief S., Hildebrand M.P., Denis C.,
Detourmignies L., Lai J.L., Kerckaert J.P.;
"Nonrandom fusion of L-plastin(LCP1) and LAZ3(BCL6) genes by
t(3;13)(q27;q14) chromosome translocation in two cases of B-cell non-
Hodgkin lymphoma.";
Genes Chromosomes Cancer 26:97-105(1999).
[11]
INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL
TRANSLOCATION WITH IKZF1.
PubMed=10753856;
Hosokawa Y., Maeda Y., Ichinohasama R., Miura I., Taniwaki M.,
Seto M.;
"The Ikaros gene, a central regulator of lymphoid differentiation,
fuses to the BCL6 gene as a result of t(3;7)(q27;p12) translocation in
a patient with diffuse large B-cell lymphoma.";
Blood 95:2719-2721(2000).
[12]
FUNCTION AS TRANSCRIPTIONAL REPRESSOR, AND TISSUE SPECIFICITY.
PubMed=10981963; DOI=10.1016/S1074-7613(00)00020-0;
Shaffer A.L., Yu X., He Y., Boldrick J., Chan E.P., Staudt L.M.;
"BCL-6 represses genes that function in lymphocyte differentiation,
inflammation, and cell cycle control.";
Immunity 13:199-212(2000).
[13]
FUNCTION AS TRANSCRIPTIONAL REPRESSOR, INVOLVEMENT IN B-CELL
NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL TRANSLOCATION WITH HISTONE H4.
PubMed=12414651;
Kurata M., Maesako Y., Ueda C., Nishikori M., Akasaka T., Uchiyama T.,
Ohno H.;
"Characterization of t(3;6)(q27;p21) breakpoints in B-cell non-
Hodgkin's lymphoma and construction of the histone H4/BCL6 fusion
gene, leading to altered expression of Bcl-6.";
Cancer Res. 62:6224-6230(2002).
[14]
FUNCTION AS TRANSCRIPTIONAL REPRESSOR, ACETYLATION AT LYS-379,
DEACETYLATION, INTERACTION WITH HDAC2, TISSUE SPECIFICITY, AND
MUTAGENESIS OF LYS-376; LYS-377 AND LYS-379.
PubMed=12402037; DOI=10.1038/ng1018;
Bereshchenko O.R., Gu W., Dalla-Favera R.;
"Acetylation inactivates the transcriptional repressor BCL6.";
Nat. Genet. 32:606-613(2002).
[15]
INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL
TRANSLOCATION WITH IL21R.
PubMed=11821949; DOI=10.1038/sj.onc.1205099;
Ueda C., Akasaka T., Kurata M., Maesako Y., Nishikori M.,
Ichinohasama R., Imada K., Uchiyama T., Ohno H.;
"The gene for interleukin-21 receptor is the partner of BCL6 in
t(3;16)(q27;p11), which is recurrently observed in diffuse large B-
cell lymphoma.";
Oncogene 21:368-376(2002).
[16]
FUNCTION AS TRANSCRIPTIONAL REPRESSOR, DNA-BINDING, SUBCELLULAR
LOCATION, INTERACTION WITH HDAC5, AND MUTAGENESIS OF 520-CYS--CYS-523;
548-CYS--CYS-551; 576-CYS--CYS-579; 604-CYS--CYS-607; 632-CYS--CYS-635
AND 660-CYS--CYS-663.
PubMed=12504096; DOI=10.1016/S0006-291X(02)02873-5;
Mascle X., Albagli O., Lemercier C.;
"Point mutations in BCL6 DNA-binding domain reveal distinct roles for
the six zinc fingers.";
Biochem. Biophys. Res. Commun. 300:391-396(2003).
[17]
INTERACTION WITH HDAC9.
PubMed=12590135; DOI=10.1074/jbc.M212935200;
Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M.,
Zelent A.;
"The histone deacetylase 9 gene encodes multiple protein isoforms.";
J. Biol. Chem. 278:16059-16072(2003).
[18]
FUNCTION IN B-CELL DIFFERENTIATION, INTERACTION WITH NCOR1; NCOR2 AND
NURD COMPLEX, ACETYLATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
LYS-379 AND 376-LYS--LYS-379.
PubMed=15454082; DOI=10.1016/j.cell.2004.09.014;
Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R.,
Boss J.M., Wade P.A.;
"MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte
differentiation.";
Cell 119:75-86(2004).
[19]
FUNCTION AS TP53 TRANSCRIPTIONAL REPRESSOR.
PubMed=15577913; DOI=10.1038/nature03147;
Phan R.T., Dalla-Favera R.;
"The BCL6 proto-oncogene suppresses p53 expression in germinal-centre
B-cells.";
Nature 432:635-639(2004).
[20]
FUNCTION AS TRANSCRIPTIONAL REPRESSOR, INTERACTION WITH ZBTB17, AND
TISSUE SPECIFICITY.
PubMed=16142238; DOI=10.1038/ni1245;
Phan R.T., Saito M., Basso K., Niu H., Dalla-Favera R.;
"BCL6 interacts with the transcription factor Miz-1 to suppress the
cyclin-dependent kinase inhibitor p21 and cell cycle arrest in
germinal center B cells.";
Nat. Immunol. 6:1054-1060(2005).
[21]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=16455075; DOI=10.1016/j.yexcr.2005.12.020;
Pantano S., Jarrossay D., Saccani S., Bosisio D., Natoli G.;
"Plastic downregulation of the transcriptional repressor BCL6 during
maturation of human dendritic cells.";
Exp. Cell Res. 312:1312-1322(2006).
[22]
FUNCTION, PHOSPHORYLATION BY ATM, INDUCTION BY GENOTOXIC STRESS,
INTERACTION WITH PIN1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF THR-190; SER-250 AND SER-260.
PubMed=17828269; DOI=10.1038/ni1508;
Phan R.T., Saito M., Kitagawa Y., Means A.R., Dalla-Favera R.;
"Genotoxic stress regulates expression of the proto-oncogene Bcl6 in
germinal center B cells.";
Nat. Immunol. 8:1132-1139(2007).
[23]
FUNCTION AS AUTOINHIBITOR, INTERACTION WITH CTBP1; HDAC2 AND NCOR2,
TISSUE SPECIFICITY, AND MUTAGENESIS OF ASN-21; HIS-116 AND
376-LYS--LYS-379.
PubMed=18212045; DOI=10.1128/MCB.01400-07;
Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A.,
Ye B.H.;
"CtBP is an essential corepressor for BCL6 autoregulation.";
Mol. Cell. Biol. 28:2175-2186(2008).
[24]
FUNCTION IN MIRNA REGULATION, AND SUBCELLULAR LOCATION.
PubMed=23166356; DOI=10.1084/jem.20121387;
Basso K., Schneider C., Shen Q., Holmes A.B., Setty M., Leslie C.,
Dalla-Favera R.;
"BCL6 positively regulates AID and germinal center gene expression via
repression of miR-155.";
J. Exp. Med. 209:2455-2465(2012).
[25]
FUNCTION, INTERACTION WITH SCF(FBXO11) COMPLEX, UBIQUITINATION,
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=22113614; DOI=10.1038/nature10688;
Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C.,
di Celle P.F., Chapuy B., Shipp M., Chiarle R., Pagano M.;
"FBXO11 targets BCL6 for degradation and is inactivated in diffuse
large B-cell lymphomas.";
Nature 481:90-93(2012).
[26]
FUNCTION AS TRANSCRIPTIONAL REPRESSOR, INTERACTION WITH BCOR; HDAC3;
NCOR1 AND NCOR2, AND DNA-BINDING.
PubMed=23911289; DOI=10.1016/j.celrep.2013.06.016;
Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D.,
Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M.,
Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W.,
Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.;
"A hybrid mechanism of action for BCL6 in B cells defined by formation
of functionally distinct complexes at enhancers and promoters.";
Cell Rep. 4:578-588(2013).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 5-129 IN COMPLEX WITH NCOR2.
PubMed=14690607; DOI=10.1016/S1097-2765(03)00454-4;
Ahmad K.F., Melnick A., Lax S., Bouchard D., Liu J., Kiang C.L.,
Mayer S., Takahashi S., Licht J.D., Prive G.G.;
"Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain.";
Mol. Cell 12:1551-1564(2003).
[29]
STRUCTURE BY NMR OF 598-657.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the C2H2 type zinc finger (region 598-654) of
human B-cell lymphoma 6 protein.";
Submitted (OCT-2007) to the PDB data bank.
[30]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 5-129.
PubMed=19052359; DOI=10.1107/S1744309108036063;
Stead M.A., Rosbrook G.O., Hadden J.M., Trinh C.H., Carr S.B.,
Wright S.C.;
"Structure of the wild-type human BCL6 POZ domain.";
Acta Crystallogr. F 64:1101-1104(2008).
[31]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 5-129 IN COMPLEX WITH BCOR,
FUNCTION, AND SUBUNIT.
PubMed=18280243; DOI=10.1016/j.molcel.2007.12.026;
Ghetu A.F., Corcoran C.M., Cerchietti L., Bardwell V.J., Melnick A.,
Prive G.G.;
"Structure of a BCOR corepressor peptide in complex with the BCL6 BTB
domain dimer.";
Mol. Cell 29:384-391(2008).
[32]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 5-129 IN COMPLEX WITH
INHIBITOR.
PubMed=20385364; DOI=10.1016/j.ccr.2009.12.050;
Cerchietti L.C., Ghetu A.F., Zhu X., Da Silva G.F., Zhong S.,
Matthews M., Bunting K.L., Polo J.M., Fares C., Arrowsmith C.H.,
Yang S.N., Garcia M., Coop A., Mackerell A.D. Jr., Prive G.G.,
Melnick A.;
"A small-molecule inhibitor of BCL6 kills DLBCL cells in vitro and in
vivo.";
Cancer Cell 17:400-411(2010).
-!- FUNCTION: Transcriptional repressor mainly required for germinal
center (GC) formation and antibody affinity maturation which has
different mechanisms of action specific to the lineage and
biological functions. Forms complexes with different corepressors
and histone deacetylases to repress the transcriptional expression
of different subsets of target genes. Represses its target genes
by binding directly to the DNA sequence 5'-TTCCTAGAA-3' (BCL6-
binding site) or indirectly by repressing the transcriptional
activity of transcription factors. In GC B-cells, represses genes
that function in differentiation, inflammation, apoptosis and cell
cycle control, also autoregulates its transcriptional expression
and up-regulates, indirectly, the expression of some genes
important for GC reactions, such as AICDA, through the repression
of microRNAs expression, like miR155. An important function is to
allow GC B-cells to proliferate very rapidly in response to T-cell
dependent antigens and tolerate the physiological DNA breaks
required for immunglobulin class switch recombination and somatic
hypermutation without inducing a p53/TP53-dependent apoptotic
response. In follicular helper CD4(+) T-cells (T(FH) cells),
promotes the expression of T(FH)-related genes but inhibits the
differentiation of T(H)1, T(H)2 and T(H)17 cells. Also required
for the establishment and maintenance of immunological memory for
both T- and B-cells. Suppresses macrophage proliferation through
competition with STAT5 for STAT-binding motifs binding on certain
target genes, such as CCL2 and CCND2. In response to genotoxic
stress, controls cell cycle arrest in GC B-cells in both p53/TP53-
dependedent and -independent manners. Besides, also controls
neurogenesis through the alteration of the composition of NOTCH-
dependent transcriptional complexes at selective NOTCH targets,
such as HES5, including the recruitment of the deacetylase SIRT1
and resulting in an epigenetic silencing leading to neuronal
differentiation. {ECO:0000269|PubMed:10981963,
ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:12414651,
ECO:0000269|PubMed:12504096, ECO:0000269|PubMed:15454082,
ECO:0000269|PubMed:15577913, ECO:0000269|PubMed:16142238,
ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:18212045,
ECO:0000269|PubMed:18280243, ECO:0000269|PubMed:22113614,
ECO:0000269|PubMed:23166356, ECO:0000269|PubMed:23911289,
ECO:0000269|PubMed:9649500}.
-!- SUBUNIT: Homodimer. Interacts (via BTB domain) with the
corepressors BCOR, NCOR1 and SMRT/NCOR2; the interactions are
direct. Forms preferably ternary complexes with BCOR and
SMRT/NCOR2 on target gene promoters but, on enhancer elements,
interacts with SMRT/NCOR2 and HDAC3 to repress proximal gene
expression. Interacts with histone deacetylases HDAC2, HDAC5 and
HDAC9 (via the catalytic domain). Interacts with ZBTB7 and BCL6B.
Interacts with SCF(FBXO11) complex; the interaction is independent
of phosphorylation and promotes ubiquitination. Interacts (when
phosphorylated) with PIN1; the interaction is required for BCL6
degradation upon genotoxic stress. Interacts with ZBTB17; inhibits
ZBTB17 transcriptional activity. Interacts with CTBP1,
autoinhibits its transcriptional expression. Interacts with NOTCH1
NCID and SIRT1; leads to a epigenetic repression of selective
NOTCH1-target genes. Interacts (nor via BTB domain neither
acetylated) with the NuRD complex components CHD4, HDAC1, MBD3 and
MTA3; the interaction with MTA3 inhibits BCL6 acetylation and is
required for BCL6 transpriptional repression.
{ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:12504096,
ECO:0000269|PubMed:12590135, ECO:0000269|PubMed:14690607,
ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:16142238,
ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:18212045,
ECO:0000269|PubMed:18280243, ECO:0000269|PubMed:20385364,
ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23911289}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-765407, EBI-765407;
Q08117:AES; NbExp=3; IntAct=EBI-765407, EBI-717810;
A8KA13:BCL6B; NbExp=3; IntAct=EBI-765407, EBI-10174813;
Q9H2G9:BLZF1; NbExp=3; IntAct=EBI-765407, EBI-2548012;
Q9NTM9:CUTC; NbExp=3; IntAct=EBI-765407, EBI-714918;
Q08379:GOLGA2; NbExp=4; IntAct=EBI-765407, EBI-618309;
P56524:HDAC4; NbExp=3; IntAct=EBI-765407, EBI-308629;
Q9UKV0:HDAC9; NbExp=2; IntAct=EBI-765407, EBI-765444;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-765407, EBI-2125614;
P0CW20:LIMS4; NbExp=3; IntAct=EBI-765407, EBI-10196832;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-765407, EBI-747107;
Q13077:TRAF1; NbExp=5; IntAct=EBI-765407, EBI-359224;
Q96RU7:TRIB3; NbExp=3; IntAct=EBI-765407, EBI-492476;
O15156:ZBTB7B; NbExp=3; IntAct=EBI-765407, EBI-740434;
Q9ULU4:ZMYND8; NbExp=3; IntAct=EBI-765407, EBI-765834;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12504096,
ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:22113614,
ECO:0000269|PubMed:23166356}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P41182-1; Sequence=Displayed;
Name=2;
IsoId=P41182-2; Sequence=VSP_042709;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in germinal center T- and B-cells
and in primary immature dendritic cells.
{ECO:0000269|PubMed:10981963, ECO:0000269|PubMed:12402037,
ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:16142238,
ECO:0000269|PubMed:16455075, ECO:0000269|PubMed:17828269,
ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:9649500}.
-!- INDUCTION: Down-regulated during maturation of dendritic cells by
selective stimuli such as bacterial lipopolysaccharides (LPS),
CD40LG and zymosan. Protein levels decreases upon genotoxic stress
in a dose- and time-dependent way. {ECO:0000269|PubMed:16455075,
ECO:0000269|PubMed:17828269}.
-!- DOMAIN: The BTB domain mediates homodimerization. Its dimer
interface mediates peptide binding such as to corepressors BCOR
and NCOR2 (PubMed:18212045). Interaction with corepressors through
the BTB domain is needed to facilitate the rapid proliferation and
survival of GC B-cells but is not involved in the T(FH) formation
and BCL6-mediated suppression of T(H)2 and T(H)17
differentiationrequired for GC formation (By similarity).
{ECO:0000250, ECO:0000269|PubMed:18212045}.
-!- PTM: Phosphorylated by MAPK1 in response to antigen receptor
activation at Ser-333 and Ser-343. Phosphorylated by ATM in
response to genotoxic stress. Phosphorylation induces its
degradation by ubiquitin/proteasome pathway.
{ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:22113614,
ECO:0000269|PubMed:9649500}.
-!- PTM: Polyubiquitinated. Polyubiquitinated by SCF(FBXO11), leading
to its degradation by the proteasome.
-!- PTM: Acetylated at Lys-379 by EP300 which inhibits the interaction
with NuRD complex and the transcriptional repressor function.
Deacetylated by HDAC- and SIR2-dependent pathways.
{ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:15454082}.
-!- DISEASE: Note=Chromosomal aberrations involving BCL6 are a cause
of B-cell non-Hodgkin lymphomas (B-cell NHL), including diffuse
large B-cell lymphoma and follicular lymphoma. Approximately 40%
of diffuse large B-cell lymphomas and 5 to 10% of follicular
lymphomas are associated with chromosomal translocations that
deregulate expression of BCL6 by juxtaposing heterologous
promoters to the BCL6 coding domain. Translocation
t(3;14)(q27;q32). Translocation t(3;22)(q27;q11) with
immunoglobulin gene regions. Translocation t(3;7)(q27;p12) with
IKZF1 gene 5'non-coding region. Translocation t(3;6)(q27;p21) with
Histone H4. Translocation t(3;16)(q27;p11) with IL21R.
Translocation t(3;13)(q27;q14) with LCP1.
-!- DISEASE: Note=A chromosomal aberration involving BCL6 may be a
cause of a form of B-cell leukemia. Translocation t(3;11)(q27;q23)
with POU2AF1/OBF1.
-!- DISEASE: Note=A chromosomal aberration involving BCL6 may be a
cause of lymphoma. Translocation t(3;4)(q27;p11) with ARHH/TTF.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCL6ID20.html";
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EMBL; Z21943; CAA79937.1; -; mRNA.
EMBL; U00115; AAC50054.1; -; mRNA.
EMBL; S67779; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; EU139066; ABX45135.1; -; mRNA.
EMBL; AC072022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78140.1; -; Genomic_DNA.
EMBL; CH471052; EAW78141.1; -; Genomic_DNA.
EMBL; BC150184; AAI50185.1; -; mRNA.
CCDS; CCDS3289.1; -. [P41182-1]
CCDS; CCDS46975.1; -. [P41182-2]
PIR; A48752; A48752.
PIR; I52586; I52586.
RefSeq; NP_001124317.1; NM_001130845.1. [P41182-1]
RefSeq; NP_001128210.1; NM_001134738.1. [P41182-2]
RefSeq; NP_001697.2; NM_001706.4. [P41182-1]
RefSeq; XP_005247751.1; XM_005247694.3. [P41182-1]
RefSeq; XP_011511364.1; XM_011513062.2. [P41182-2]
UniGene; Hs.478588; -.
PDB; 1R28; X-ray; 2.20 A; A/B=5-129.
PDB; 1R29; X-ray; 1.30 A; A=5-129.
PDB; 1R2B; X-ray; 2.20 A; A/B=5-129.
PDB; 2EN2; NMR; -; A=598-626.
PDB; 2EOS; NMR; -; A=626-654.
PDB; 2LCE; NMR; -; A=540-602.
PDB; 2YRM; NMR; -; A=515-544.
PDB; 3BIM; X-ray; 2.60 A; A/B/C/D/E/F/G/H=5-129.
PDB; 3E4U; X-ray; 2.10 A; A/B/C/D/E/F=5-129.
PDB; 3LBZ; X-ray; 2.30 A; A/B=5-129.
PDB; 4CP3; X-ray; 2.30 A; A/B=9-128.
PDB; 4U2M; X-ray; 2.23 A; A/B/C/D=5-129.
PDB; 5H7G; X-ray; 1.85 A; A/B=5-129.
PDB; 5H7H; X-ray; 1.95 A; A=5-129.
PDB; 5N1X; X-ray; 1.72 A; A=9-128, B/C=7-127, D=9-125.
PDB; 5N1Z; X-ray; 1.81 A; A=6-128.
PDB; 5N20; X-ray; 1.38 A; A=6-128.
PDB; 5N21; X-ray; 1.58 A; A/B=7-128.
PDB; 5X4M; X-ray; 1.65 A; A=5-129.
PDB; 5X4N; X-ray; 1.94 A; A=5-129.
PDB; 5X4O; X-ray; 2.05 A; A=5-129.
PDB; 5X4P; X-ray; 2.06 A; A=5-129.
PDB; 5X4Q; X-ray; 2.00 A; A=5-129.
PDBsum; 1R28; -.
PDBsum; 1R29; -.
PDBsum; 1R2B; -.
PDBsum; 2EN2; -.
PDBsum; 2EOS; -.
PDBsum; 2LCE; -.
PDBsum; 2YRM; -.
PDBsum; 3BIM; -.
PDBsum; 3E4U; -.
PDBsum; 3LBZ; -.
PDBsum; 4CP3; -.
PDBsum; 4U2M; -.
PDBsum; 5H7G; -.
PDBsum; 5H7H; -.
PDBsum; 5N1X; -.
PDBsum; 5N1Z; -.
PDBsum; 5N20; -.
PDBsum; 5N21; -.
PDBsum; 5X4M; -.
PDBsum; 5X4N; -.
PDBsum; 5X4O; -.
PDBsum; 5X4P; -.
PDBsum; 5X4Q; -.
ProteinModelPortal; P41182; -.
SMR; P41182; -.
BioGrid; 107076; 118.
CORUM; P41182; -.
DIP; DIP-2651N; -.
IntAct; P41182; 121.
MINT; MINT-158757; -.
STRING; 9606.ENSP00000232014; -.
iPTMnet; P41182; -.
PhosphoSitePlus; P41182; -.
BioMuta; BCL6; -.
DMDM; 728952; -.
MaxQB; P41182; -.
PaxDb; P41182; -.
PeptideAtlas; P41182; -.
PRIDE; P41182; -.
TopDownProteomics; P41182-2; -. [P41182-2]
Ensembl; ENST00000232014; ENSP00000232014; ENSG00000113916. [P41182-1]
Ensembl; ENST00000406870; ENSP00000384371; ENSG00000113916. [P41182-1]
Ensembl; ENST00000450123; ENSP00000413122; ENSG00000113916. [P41182-2]
Ensembl; ENST00000621333; ENSP00000479784; ENSG00000113916. [P41182-2]
GeneID; 604; -.
KEGG; hsa:604; -.
UCSC; uc003frp.4; human. [P41182-1]
CTD; 604; -.
DisGeNET; 604; -.
EuPathDB; HostDB:ENSG00000113916.17; -.
GeneCards; BCL6; -.
HGNC; HGNC:1001; BCL6.
HPA; CAB000307; -.
HPA; HPA004899; -.
HPA; HPA050645; -.
MalaCards; BCL6; -.
MIM; 109565; gene.
neXtProt; NX_P41182; -.
OpenTargets; ENSG00000113916; -.
Orphanet; 545; Follicular lymphoma.
Orphanet; 98839; Intravascular large B-cell lymphoma.
Orphanet; 98838; Primary mediastinal large B-cell lymphoma.
PharmGKB; PA25312; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00890000139443; -.
HOGENOM; HOG000001556; -.
HOVERGEN; HBG004831; -.
InParanoid; P41182; -.
KO; K15618; -.
OMA; NECDCRF; -.
OrthoDB; EOG091G025U; -.
PhylomeDB; P41182; -.
TreeFam; TF330912; -.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
SIGNOR; P41182; -.
ChiTaRS; BCL6; human.
EvolutionaryTrace; P41182; -.
GeneWiki; BCL6; -.
GenomeRNAi; 604; -.
PRO; PR:P41182; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000113916; -.
CleanEx; HS_BCL6; -.
ExpressionAtlas; P41182; baseline and differential.
Genevisible; P41182; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0001161; F:intronic transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IMP:UniProtKB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IEA:Ensembl.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
GO; GO:0002467; P:germinal center formation; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0002903; P:negative regulation of B cell apoptotic process; NAS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl.
GO; GO:0048294; P:negative regulation of isotype switching to IgE isotypes; IEA:Ensembl.
GO; GO:0032764; P:negative regulation of mast cell cytokine production; IEA:Ensembl.
GO; GO:1903464; P:negative regulation of mitotic cell cycle DNA replication; NAS:UniProtKB.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:Ensembl.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0051272; P:positive regulation of cellular component movement; IEA:Ensembl.
GO; GO:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IMP:BHF-UCL.
GO; GO:0000060; P:protein import into nucleus, translocation; IGI:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0002634; P:regulation of germinal center formation; NAS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
GO; GO:0050776; P:regulation of immune response; NAS:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
GO; GO:0043380; P:regulation of memory T cell differentiation; IEA:Ensembl.
GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0042092; P:type 2 immune response; IBA:GO_Central.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR011333; SKP1/BTB/POZ.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00651; BTB; 1.
SMART; SM00225; BTB; 1.
SMART; SM00355; ZnF_C2H2; 6.
SUPFAM; SSF54695; SSF54695; 1.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS50097; BTB; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Chromosomal rearrangement; Complete proteome; DNA-binding; Immunity;
Inflammatory response; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 706 B-cell lymphoma 6 protein.
/FTId=PRO_0000047098.
DOMAIN 32 99 BTB. {ECO:0000255|PROSITE-
ProRule:PRU00037}.
ZN_FING 518 541 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 546 568 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 574 596 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 602 624 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 630 652 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 658 681 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 376 379 Required for interaction with NuRD
complex and for transcriptional repressor
activity.
MOD_RES 333 333 Phosphoserine; by MAPK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:9649500}.
MOD_RES 343 343 Phosphoserine; by MAPK1.
{ECO:0000269|PubMed:9649500}.
MOD_RES 361 361 Phosphoserine.
{ECO:0000250|UniProtKB:P41183}.
MOD_RES 379 379 N6-acetyllysine.
{ECO:0000269|PubMed:12402037}.
MOD_RES 404 404 Phosphoserine.
{ECO:0000250|UniProtKB:P41183}.
VAR_SEQ 514 569 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_042709.
VARIANT 252 252 N -> S (in dbSNP:rs34463990).
/FTId=VAR_052709.
VARIANT 493 493 A -> T (in dbSNP:rs2229362).
/FTId=VAR_019970.
VARIANT 676 676 H -> Y (in dbSNP:rs1056936).
/FTId=VAR_014825.
MUTAGEN 21 21 N->K: Abolishes interaction with NCOR2
and HDAC2, no effect on interaction with
CTBP1 and transcriptional autoinhibition;
when associated with A-116 and 376-Q--Q-
379. {ECO:0000269|PubMed:18212045}.
MUTAGEN 116 116 H->A: Abolishes interaction with NCOR2
and HDAC2, no effect on interaction with
CTBP1 and transcriptional autoinhibition;
when associated with K-21 and 376-Q--Q-
379. {ECO:0000269|PubMed:18212045}.
MUTAGEN 190 190 T->A: No effect on interaction with PIN1.
{ECO:0000269|PubMed:17828269}.
MUTAGEN 250 250 S->A: No effect on interaction with PIN1.
{ECO:0000269|PubMed:17828269}.
MUTAGEN 260 260 S->A: Strongly reduces interaction with
PIN1. {ECO:0000269|PubMed:17828269}.
MUTAGEN 333 333 S->A: Decrease in phosphorylation by
MAPK1. {ECO:0000269|PubMed:9649500}.
MUTAGEN 343 343 S->A: Decrease in phosphorylation by
MAPK1. {ECO:0000269|PubMed:9649500}.
MUTAGEN 376 379 KKYK->QQYQ: Abolishes interaction with
HDAC2 and MTA3 as well as transcriptional
repressor and transforming activities.
Abolishes interaction with NCOR2 and
HDAC2, no effect on interaction with
CTBP1 and transcriptional autoinhibition;
when associated with K-21 and A-116.
{ECO:0000269|PubMed:15454082,
ECO:0000269|PubMed:18212045}.
MUTAGEN 376 376 K->R: No effect on acetylation.
{ECO:0000269|PubMed:12402037}.
MUTAGEN 377 377 K->R: No effect on acetylation.
{ECO:0000269|PubMed:12402037}.
MUTAGEN 379 379 K->R: Abolishes acetylation. No effect on
interaction with MTA3, NCOR1 and NCOR2.
{ECO:0000269|PubMed:12402037,
ECO:0000269|PubMed:15454082}.
MUTAGEN 520 523 CNEC->GNEG: No effect on DNA-binding,
nuclear localization, transcriptional
repression activity and interaction with
HDAC5. {ECO:0000269|PubMed:12504096}.
MUTAGEN 548 551 CDRC->GDRG: No effect on DNA-binding,
nuclear localization, transcriptional
repression activity and interaction with
HDAC5. {ECO:0000269|PubMed:12504096}.
MUTAGEN 576 579 CNIC->GNIG: Abolishes DNA-binding and
transcriptional repression activity, no
effect on nuclear localization and
interaction with HDAC5.
{ECO:0000269|PubMed:12504096}.
MUTAGEN 604 607 CETC->GETG: Abolishes DNA-binding and
transcriptional repression activity,
perturbs nuclear localization. No effect
on interaction with HDAC5.
{ECO:0000269|PubMed:12504096}.
MUTAGEN 632 635 CEIC->GEIG: Abolishes DNA-binding and
transcriptional repression activity, no
effect on nuclear localization and
interaction with HDAC5.
{ECO:0000269|PubMed:12504096}.
MUTAGEN 660 663 CEKC->GEKG: Abolishes DNA-binding and
transcriptional repression activity,
perturbs nuclear localization. No effect
on interaction with HDAC5.
{ECO:0000269|PubMed:12504096}.
CONFLICT 347 347 S -> A (in Ref. 2; AAC50054).
{ECO:0000305}.
CONFLICT 393 393 E -> G (in Ref. 2; AAC50054).
{ECO:0000305}.
CONFLICT 498 498 P -> A (in Ref. 2; AAC50054).
{ECO:0000305}.
STRAND 8 11 {ECO:0000244|PDB:5H7G}.
HELIX 14 27 {ECO:0000244|PDB:1R29}.
TURN 29 31 {ECO:0000244|PDB:3E4U}.
STRAND 34 38 {ECO:0000244|PDB:1R29}.
STRAND 41 45 {ECO:0000244|PDB:1R29}.
HELIX 47 53 {ECO:0000244|PDB:1R29}.
HELIX 55 61 {ECO:0000244|PDB:1R29}.
TURN 64 68 {ECO:0000244|PDB:1R29}.
STRAND 70 73 {ECO:0000244|PDB:1R29}.
HELIX 80 92 {ECO:0000244|PDB:1R29}.
STRAND 93 95 {ECO:0000244|PDB:5H7G}.
TURN 99 101 {ECO:0000244|PDB:1R29}.
HELIX 102 111 {ECO:0000244|PDB:1R29}.
HELIX 115 126 {ECO:0000244|PDB:1R29}.
STRAND 521 523 {ECO:0000244|PDB:2YRM}.
STRAND 527 529 {ECO:0000244|PDB:2YRM}.
HELIX 530 540 {ECO:0000244|PDB:2YRM}.
HELIX 558 568 {ECO:0000244|PDB:2LCE}.
STRAND 573 575 {ECO:0000244|PDB:2LCE}.
TURN 577 579 {ECO:0000244|PDB:2LCE}.
STRAND 582 584 {ECO:0000244|PDB:2LCE}.
HELIX 586 596 {ECO:0000244|PDB:2LCE}.
STRAND 601 603 {ECO:0000244|PDB:2EN2}.
TURN 605 607 {ECO:0000244|PDB:2EN2}.
STRAND 610 613 {ECO:0000244|PDB:2EN2}.
HELIX 614 620 {ECO:0000244|PDB:2EN2}.
HELIX 622 625 {ECO:0000244|PDB:2EN2}.
STRAND 633 635 {ECO:0000244|PDB:2EOS}.
STRAND 639 641 {ECO:0000244|PDB:2EOS}.
HELIX 642 648 {ECO:0000244|PDB:2EOS}.
TURN 649 652 {ECO:0000244|PDB:2EOS}.
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


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EIAAB30258 Homo sapiens,Human,PDCD2,Programmed cell death protein 2,RP8,Zinc finger MYND domain-containing protein 7,Zinc finger protein Rp-8,ZMYND7
EIAAB47295 Cell proliferation-inducing gene 12 protein,Homo sapiens,Human,PIG12,PRD51,Zinc finger and SCAN domain-containing protein 9,Zinc finger protein 193,ZNF193,ZSCAN9
EIAAB47193 Mouse,Mus musculus,SCAN-KRAB-zinc finger protein,Skz1,Zf47,Zfp306,Zfp307,Zfp47,Zfp-47,Zinc finger protein 306,Zinc finger protein 307,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and S
EIAAB47355 Homo sapiens,Human,Neurotrophin receptor-interacting factor homolog,SP2114,Zf2,Zinc finger protein 274,Zinc finger protein HFB101,Zinc finger protein with KRAB and SCAN domains 19,Zinc finger protein
EIAAB29341 Cellular zinc finger anti-NF-kappa-B protein,Homo sapiens,Human,OTU domain-containing protein 7B,OTUD7B,ZA20D1,Zinc finger A20 domain-containing protein 1,Zinc finger protein Cezanne
EIAAB46811 Homo sapiens,Human,PLZF,Promyelocytic leukemia zinc finger protein,ZBTB16,Zinc finger and BTB domain-containing protein 16,Zinc finger protein 145,Zinc finger protein PLZF,ZNF145
EIAAB48061 Homo sapiens,Human,KOX29,Zinc finger and SCAN domain-containing protein 20,Zinc finger protein 31,Zinc finger protein 360,Zinc finger protein KOX29,ZNF31,ZNF360,ZSCAN20
EIAAB47047 Homo sapiens,Human,hZF5,ZBTB14,ZF5,ZFP161,Zfp-161,Zfp-5,Zinc finger and BTB domain-containing protein 14,Zinc finger protein 161 homolog,Zinc finger protein 478,Zinc finger protein 5 homolog,ZNF478
EIAAB47395 C2H2-like zinc finger protein rearranged in thyroid adenomas,Homo sapiens,Human,RITA,Zinc finger protein 331,Zinc finger protein 361,Zinc finger protein 463,ZNF331,ZNF361,ZNF463
EIAAB47878 HDSG1,Heart development-specific gene 1 protein,Homo sapiens,Human,KOX11,Zinc finger protein 18,Zinc finger protein 535,Zinc finger protein KOX11,Zinc finger protein with KRAB and SCAN domains 6,ZKSCA
EIAAB14743 Fez family zinc finger protein 2,FEZF2,FEZL,FKSG36,Forebrain embryonic zinc finger-like protein 2,Homo sapiens,Human,Zinc finger protein 312,Zinc finger protein Fez-like,ZNF312
EIAAB47275 Homo sapiens,Human,Zinc finger protein 167,Zinc finger protein 448,Zinc finger protein 64,Zinc finger protein with KRAB and SCAN domains 7,ZKSCAN7,ZNF167,ZNF448,ZNF64


 

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