BCL6
entrez
604
canonical
uniprot
P41182
canonical
ensembl
ENSG00000113916
resolver
ensp
ENSP00000232014
resolver
ensp
ENSP00000384371
resolver
ensp
ENSP00000479784
resolver
genesymbol
BCL6
resolver
genesymbol_syn
BCL5
resolver
genesymbol_syn
LAZ3
resolver
genesymbol_syn
ZBTB27
resolver
genesymbol_syn
ZNF51
resolver
hgnc
HGNC:1001
resolver
uniprot
A7E241
resolver
uniprot
B5B0A5
resolver
uniprot
B8PSA7
resolver
uniprot
D3DNV5
resolver
uniprot_entry
B5B0A5_HUMAN
resolver
uniprot_entry
BCL6_HUMAN
resolver
uniprot_sec
A7E241
resolver
uniprot_sec
B8PSA7
resolver
uniprot_sec
D3DNV5
resolver
amino_acid_sequence
MASPADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPEGFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASEAEMVSAIKPPREEFLNSRMLMPQDIMAYRGREVVENNLPLRSAPGCESRAFAPSLYSGLSTPPASYSMYSHLPVSSLLFSDEEFRDVRMPVANPFPKERALPCDSARPVPGEYSRPTLEVSPNVCHSNIYSPKETIPEEARSDMHYSVAEGLKPAAPSARNAPYFPCDKASKEEERPSSEDEIALHFEPPNAPLNRKGLVSPQSPQKSDCQPNSPTESCSSKNACILQASGSPPAKSPTDPKACNWKKYKFIVLNSLNQNAKPEGPEQAELGRLSPRAYTAPPACQPPMEPENLDLQSPTKLSASGEDSTIPQASRLNNIVNRSMTGSPRSSSESHSPLYMHPPKCTSCGSQSPQHAEMCLHTAGPTFPEEMGETQSEYSDSSCENGAFFCNECDCRFSEEASLKRHTLQTHSDKPYKCDRCQASFRYKGNLASHKTVHTGEKPYRCNICGAQFNRPANLKTHTRIHSGEKPYKCETCGARFVQVAHLRAHVLIHTGEKPYPCEICGTRFRHLQTLKSHLRIHTGEKPYHCEKCNLHFRHKSQLRLHLRQKHGAITNTKVQYRVSATDLPPELPKAC
uniprot
proteins
disease_involvement
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 (PubMed:10469447, PubMed:10753856, PubMed:11821949, PubMed:12414651). Translocation t(3;14)(q27;q32). Translocation t(3;22)(q27;q11) with immunoglobulin gene regions (PubMed:11821949). Translocation t(3;7)(q27;p12) with IKZF1 gene 5'non-coding region (PubMed:10753856). Translocation t(3;6)(q27;p21) with Histone H4 (PubMed:12414651). Translocation t(3;16)(q27;p11) with IL21R. Translocation t(3;13)(q27;q14) with LCP1 (PubMed:10469447). {ECO:0000269|PubMed:10469447, ECO:0000269|PubMed:10753856, ECO:0000269|PubMed:11821949, ECO:0000269|PubMed:12414651}.; 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.
uniprot
proteins
function
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 immunoglobulin 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}.
uniprot
proteins
mass_dalton
78846
uniprot
proteins
mutagenesis
MUTAGEN 21; /note="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."; /evidence="ECO:0000269|PubMed:18212045"; MUTAGEN 59; /note="S->A: Abolished ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:30190310"; MUTAGEN 116; /note="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."; /evidence="ECO:0000269|PubMed:18212045"; MUTAGEN 190; /note="T->A: No effect on interaction with PIN1."; /evidence="ECO:0000269|PubMed:17828269"; MUTAGEN 250; /note="S->A: No effect on interaction with PIN1."; /evidence="ECO:0000269|PubMed:17828269"; MUTAGEN 260; /note="S->A: Strongly reduces interaction with PIN1."; /evidence="ECO:0000269|PubMed:17828269"; MUTAGEN 333; /note="S->A: Decrease in phosphorylation by MAPK1."; /evidence="ECO:0000269|PubMed:9649500"; MUTAGEN 343; /note="S->A: Decrease in phosphorylation by MAPK1."; /evidence="ECO:0000269|PubMed:9649500"; MUTAGEN 376..379; /note="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."; /evidence="ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:18212045"; MUTAGEN 376; /note="K->R: No effect on acetylation."; /evidence="ECO:0000269|PubMed:12402037"; MUTAGEN 377; /note="K->R: No effect on acetylation."; /evidence="ECO:0000269|PubMed:12402037"; MUTAGEN 379; /note="K->R: Abolishes acetylation. No effect on interaction with MTA3, NCOR1 and NCOR2."; /evidence="ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:15454082"; MUTAGEN 520..523; /note="CNEC->GNEG: No effect on DNA-binding, nuclear localization, transcriptional repression activity and interaction with HDAC5."; /evidence="ECO:0000269|PubMed:12504096"; MUTAGEN 548..551; /note="CDRC->GDRG: No effect on DNA-binding, nuclear localization, transcriptional repression activity and interaction with HDAC5."; /evidence="ECO:0000269|PubMed:12504096"; MUTAGEN 576..579; /note="CNIC->GNIG: Abolishes DNA-binding and transcriptional repression activity, no effect on nuclear localization and interaction with HDAC5."; /evidence="ECO:0000269|PubMed:12504096"; MUTAGEN 604..607; /note="CETC->GETG: Abolishes DNA-binding and transcriptional repression activity, perturbs nuclear localization. No effect on interaction with HDAC5."; /evidence="ECO:0000269|PubMed:12504096"; MUTAGEN 632..635; /note="CEIC->GEIG: Abolishes DNA-binding and transcriptional repression activity, no effect on nuclear localization and interaction with HDAC5."; /evidence="ECO:0000269|PubMed:12504096"; MUTAGEN 660..663; /note="CEKC->GEKG: Abolishes DNA-binding and transcriptional repression activity, perturbs nuclear localization. No effect on interaction with HDAC5."; /evidence="ECO:0000269|PubMed:12504096
uniprot
proteins
post_translational_modification
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 (PubMed:22113614, PubMed:30190310, PubMed:9649500). Polyubiquitinated by SCF(FBXO11), leading to its degradation by the proteasome (PubMed:22113614). Ubiquitinated by the SCF(FBXL17) complex, leading to its degradation by the proteasome: ubiquitination by the SCF(FBXL17) complex takes place when aberrant BTB domain dimers are formed (PubMed:30190310). {ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:30190310, ECO:0000269|PubMed:9649500}.; 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}.
uniprot
proteins
pubmed
10469447
uniprot
proteins
pubmed
10753856
uniprot
proteins
pubmed
10981963
uniprot
proteins
pubmed
11821949
uniprot
proteins
pubmed
12402037
uniprot
proteins
pubmed
12414651
uniprot
proteins
pubmed
12504096
uniprot
proteins
pubmed
12590135
uniprot
proteins
pubmed
14690607
uniprot
proteins
pubmed
15454082
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15577913
uniprot
proteins
pubmed
16142238
uniprot
proteins
pubmed
16455075
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17828269
uniprot
proteins
pubmed
18212045
uniprot
proteins
pubmed
18280243
uniprot
proteins
pubmed
19052359
uniprot
proteins
pubmed
20385364
uniprot
proteins
pubmed
22113614
uniprot
proteins
pubmed
23166356
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23911289
uniprot
proteins
pubmed
30190310
uniprot
proteins
pubmed
8220427
uniprot
proteins
pubmed
8235596
uniprot
proteins
pubmed
8274740
uniprot
proteins
pubmed
8506375
uniprot
proteins
pubmed
9649500
uniprot
proteins
sequence_length
706
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12504096, ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23166356}.
uniprot
proteins