[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Skeletal muscle; DOI=10.1038/ng0993-66; PubMed=8220427 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1126/science.8235596; PubMed=8235596 [NCBI, ExPASy, EBI, Israel, Japan] 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]. TISSUE=Liver; PubMed=8274740 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1073/pnas.90.11.5262; PubMed=8506375 [NCBI, ExPASy, EBI, Israel, Japan] 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]	FUNCTION, TISSUE SPECIFICITY, PTM, AND MUTAGENESIS OF SER-333 AND SER-343. PubMed=9649500 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	INTERACTION WITH HDAC9. DOI=10.1074/jbc.M212935200; PubMed=12590135 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	INDUCTION, AND TISSUE SPECIFICITY. DOI=10.1016/j.yexcr.2005.12.020; PubMed=16455075 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	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.

Comments

FUNCTION: Transcriptional repressor which is required for germinal center formation and antibody affinity maturation. Probably plays an important role in lymphomagenesis.
SUBUNIT: Interacts with ZBTB7 and BCL6B (By similarity). Interacts with the catalytic domain of HDAC9.
INTERACTION:
P56524:HDAC4; NbExp=1; IntAct=EBI-765407, EBI-308629;
Q9UKV0:HDAC9; NbExp=1; IntAct=EBI-765407, EBI-765444;
Q9UKV0-3:HDAC9; NbExp=1; IntAct=EBI-765407, EBI-765476;
Q9UKV0-7:HDAC9; NbExp=1; IntAct=EBI-765407, EBI-1372717;
Q9ULU4:ZMYND8; NbExp=1; IntAct=EBI-765407, EBI-765834;
SUBCELLULAR LOCATION: Nucleus (By similarity).
TISSUE SPECIFICITY: Expressed in germinal center T and B cells and in primary immature dendritic cells.
INDUCTION: Down-regulated during maturation of dendritic cells by selective stimuli such as LPS, CD40L and zymosan.
PTM: Phosphorylated by MAPK1 in response to antigen receptor activation. Phosphorylation induces its degradation by ubiquitin/proteasome pathway.
DISEASE: Chromosomal aberrations involving BCL6 may be a cause of B-cell non-Hodgkin lymphoma. Translocation t(3;14)(q27;q32); translocation t(3;22)(q27;q11) with immunoglobulin gene regions.
DISEASE: 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: A chromosomal aberration involving BCL6 may be a cause of lymphoma. Translocation t(3;4)(q27;p11) with ARHH/TTF.
SIMILARITY: Contains 1 BTB (POZ) domain.
SIMILARITY: Contains 6 C2H2-type zinc fingers.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/BCL6ID20.html";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z21943; CAA79937.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00115; AAC50054.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S67779; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]

IPI

IPI00012820; -.

PIR

A48752; A48752.
I52586; I52586.

RefSeq

NP_001124317.1; -.
NP_001128210.1; -.
NP_001697.2; -.

UniGene

Hs.478588

3D structure databases

PDB

1R28; X-ray; 2.20 A; A/B=5-129.	[ExPASy / RCSB / EBI]
1R29; X-ray; 1.30 A; A=5-129.	[ExPASy / RCSB / EBI]
1R2B; X-ray; 2.20 A; A/B=5-129.	[ExPASy / RCSB / EBI]
2EN2; NMR; -; A=598-626.	[ExPASy / RCSB / EBI]
2EOS; NMR; -; A=626-654.	[ExPASy / RCSB / EBI]
2YRM; NMR; -; A=515-544.	[ExPASy / RCSB / EBI]
3BIM; X-ray; 2.60 A; A/B/C/D/E/F/G/H=5-129.	[ExPASy / RCSB / EBI]
3E4U; X-ray; 2.10 A; A/B/C/D/E/F=5-129.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1R28; -.
1R29; -.
1R2B; -.
2EN2; -.
2EOS; -.
2YRM; -.
3BIM; -.
3E4U; -.

ModBase

P41182.

Protein-protein interaction databases

IntAct

P41182; 65.

PTM databases

PhosphoSite

P41182; -.

Enzyme and pathway databases

Pathway_Interaction_DB

foxopathway; FoxO family signaling.
il4_2pathway; IL4-mediated signaling events.
hdac_classii_pathway; Signaling events mediated by HDAC Class II.

Organism-specific databases

GC03M188921; -.

HGNC:1001; BCL6.

CAB000307; -.
HPA004899; -.

MIM

109565; gene. [NCBI / EBI]

Orphanet

545; Follicular lymphoma.

PharmGKB

PA25312; -.

Gene expression databases

P41182; -.

P41182; -.

HS_BCL6; -.

ENSG00000113916; Homo sapiens.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0043565;	Molecular function: sequence-specific DNA binding (inferred from direct assay from UniProtKB).
GO:0003700;	Molecular function: transcription factor activity (inferred from mutant phenotype from UniProtKB).
GO:0016564;	Molecular function: transcription repressor activity (inferred from mutant phenotype from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0002903;	Biological process: negative regulation of B cell apoptosis (non-traceable author statement from UniProtKB).
GO:0030308;	Biological process: negative regulation of cell growth (inferred from direct assay from UniProtKB).
GO:0045749;	Biological process: negative regulation of S phase of mitotic cell cycle (non-traceable author statement from UniProtKB).
GO:0000122;	Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
GO:0043065;	Biological process: positive regulation of apoptosis (inferred from direct assay from UniProtKB).
GO:0000060;	Biological process: protein import into nucleus, translocation (inferred from genetic interaction from UniProtKB).
GO:0002634;	Biological process: regulation of germinal center formation (non-traceable author statement from UniProtKB).
GO:0006974;	Biological process: response to DNA damage stimulus (inferred from direct assay from UniProtKB).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000210; BTB/POZ-like.
IPR011333; BTB/POZ_fold.
IPR013069; BTB_POZ.
IPR007087; Znf_C2H2.
IPR015880; Znf_C2H2-like.
IPR013087; Znf_C2H2/integrase_DNA-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.710.10; BTB/POZ_fold; 1.
G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.

Pfam

PF00651; BTB; 1.
PF00096; zf-C2H2; 6.
Pfam graphical view of domain structure.

SMART

SM00225; BTB; 1.
SM00355; ZnF_C2H2; 6.
SMART graphical view of domain structure.

PROSITE

PS50097; BTB; 1.
PS00028; ZINC_FINGER_C2H2_1; 6.
PS50157; ZINC_FINGER_C2H2_2; 6.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P41182; -.

Genome annotation databases

Ensembl

ENSG00000113916; Homo sapiens. [Contig view]

GeneID

604; -.

KEGG

hsa:604; -.

Phylogenomic databases

HOGENOM

P41182; -.

HOVERGEN

P41182; -.

OMA

P41182; QASFRYK.

Other

2453; -.

BCL6; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Activator; Chromosomal rearrangement; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 706`	`706`	`B-cell lymphoma 6 protein.`	`PRO_0000047098`
`DOMAIN`	`32 99`	`68`	`BTB.`
`ZN_FING`	`518 541`	`24`	`C2H2-type 1.`
`ZN_FING`	`546 568`	`23`	`C2H2-type 2.`
`ZN_FING`	`574 596`	`23`	`C2H2-type 3.`
`ZN_FING`	`602 624`	`23`	`C2H2-type 4.`
`ZN_FING`	`630 652`	`23`	`C2H2-type 5.`
`ZN_FING`	`658 681`	`24`	`C2H2-type 6.`
`VARIANT`	`252 252`	`1`	`N -> S (in dbSNP:rs34463990 [NCBI]).`	`VAR_052709`
`VARIANT`	`493 493`	`1`	`A -> T (in dbSNP:rs2229362 [NCBI]).`	`VAR_019970`
`VARIANT`	`676 676`	`1`	`H -> Y (in dbSNP:rs1056936 [NCBI]).`	`VAR_014825`
`MUTAGEN`	`333 333`		`S->A: Decrease in phosphorylation by MAPK1.`
`MUTAGEN`	`343 343`		`S->A: Decrease in phosphorylation by MAPK1.`
`CONFLICT`	`347 347`		`S -> A (in Ref. 2; AAC50054).`
`CONFLICT`	`393 393`		`E -> G (in Ref. 2; AAC50054).`
`CONFLICT`	`498 498`		`P -> A (in Ref. 2; AAC50054).`
`HELIX`	`14 27`	`14`
`STRAND`	`34 38`	`5`
`STRAND`	`41 45`	`5`
`HELIX`	`47 53`	`7`
`HELIX`	`55 61`	`7`
`TURN`	`64 68`	`5`
`STRAND`	`70 73`	`4`
`HELIX`	`80 92`	`13`
`STRAND`	`93 95`	`3`
`TURN`	`99 101`	`3`
`HELIX`	`102 111`	`10`
`HELIX`	`115 126`	`12`
`STRAND`	`521 523`	`3`
`STRAND`	`527 529`	`3`
`HELIX`	`530 540`	`11`
`STRAND`	`601 603`	`3`
`TURN`	`605 607`	`3`
`STRAND`	`610 613`	`4`
`HELIX`	`614 620`	`7`
`HELIX`	`622 625`	`4`
`STRAND`	`633 635`	`3`
`STRAND`	`639 641`	`3`
`HELIX`	`642 648`	`7`
`TURN`	`649 652`	`4`

Sequence information

Length: 706 AA [This is the length of the unprocessed precursor]

Molecular weight: 78846 Da [This is the MW of the unprocessed precursor]

CRC64: E38D83C213DAE2D0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASPADSCIQ FTRHASDVLL NLNRLRSRDI LTDVVIVVSR EQFRAHKTVL MACSGLFYSI 

        70         80         90        100        110        120 
FTDQLKCNLS VINLDPEINP EGFCILLDFM YTSRLNLREG NIMAVMATAM YLQMEHVVDT 

       130        140        150        160        170        180 
CRKFIKASEA EMVSAIKPPR EEFLNSRMLM PQDIMAYRGR EVVENNLPLR SAPGCESRAF 

       190        200        210        220        230        240 
APSLYSGLST PPASYSMYSH LPVSSLLFSD EEFRDVRMPV ANPFPKERAL PCDSARPVPG 

       250        260        270        280        290        300 
EYSRPTLEVS PNVCHSNIYS PKETIPEEAR SDMHYSVAEG LKPAAPSARN APYFPCDKAS 

       310        320        330        340        350        360 
KEEERPSSED EIALHFEPPN APLNRKGLVS PQSPQKSDCQ PNSPTESCSS KNACILQASG 

       370        380        390        400        410        420 
SPPAKSPTDP KACNWKKYKF IVLNSLNQNA KPEGPEQAEL GRLSPRAYTA PPACQPPMEP 

       430        440        450        460        470        480 
ENLDLQSPTK LSASGEDSTI PQASRLNNIV NRSMTGSPRS SSESHSPLYM HPPKCTSCGS 

       490        500        510        520        530        540 
QSPQHAEMCL HTAGPTFPEE MGETQSEYSD SSCENGAFFC NECDCRFSEE ASLKRHTLQT 

       550        560        570        580        590        600 
HSDKPYKCDR CQASFRYKGN LASHKTVHTG EKPYRCNICG AQFNRPANLK THTRIHSGEK 

       610        620        630        640        650        660 
PYKCETCGAR FVQVAHLRAH VLIHTGEKPY PCEICGTRFR HLQTLKSHLR IHTGEKPYHC 

       670        680        690        700 
EKCNLHFRHK SQLRLHLRQK HGAITNTKVQ YRVSATDLPP ELPKAC

P41182 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools