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P20749 (BCL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
B-cell lymphoma 3 protein

Short name=BCL-3
Alternative name(s):
Proto-oncogene BCL3
Gene names
Name:BCL3
Synonyms:BCL4, D19S37
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contributes to the regulation of transcriptional activation of NF-kappa-B target genes. In the cytoplasm, inhibits the nuclear translocation of the NF-kappa-B p50 subunit. In the nucleus, acts as transcriptional activator that promotes transcription of NF-kappa-B target genes. Contributes to the regulation of cell proliferation By similarity. Ref.4

Subunit structure

Component of a complex consisting of the NF-kappa-B p52-p52 homodimer and BCL3. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Interacts with N4BP2, COPS5 and PIR. Interacts with CYLD By similarity. Ref.4 Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Note: Ubiquitination via 'Lys-63'-linked ubiquitin chains is required for nuclear accumulation By similarity.

Post-translational modification

Polyubiquitinated. Ubiquitination via 'Lys-63'-linked ubiquitin chains is required for nuclear accumulation. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains. Deubiquitination by CYLD prevents nuclear accumulation By similarity.

Activated by phosphorylation.

Involvement in disease

A chromosomal aberration involving BCL3 may be a cause of B-cell chronic lymphocytic leukemia (B-CLL). Translocation t(14;19)(q32;q13.1) with immunoglobulin gene regions.

Sequence similarities

Contains 7 ANK repeats.

Caution

It is uncertain whether Met-1 or Met-9 is the initiator.

Sequence caution

The sequence AAA51815.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA51816.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH64993.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityChromosomal rearrangement
   DiseaseProto-oncogene
   DomainANK repeat
Repeat
   Molecular functionActivator
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype PubMed 16384933. Source: UniProtKB

I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 8196632. Source: UniProtKB

T-helper 1 type immune response

Inferred from electronic annotation. Source: Ensembl

T-helper 2 cell differentiation

Inferred from electronic annotation. Source: Ensembl

antimicrobial humoral response

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 16384933. Source: UniProtKB

defense response to bacterium

Inferred from electronic annotation. Source: Ensembl

defense response to protozoan

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

follicular dendritic cell differentiation

Inferred from electronic annotation. Source: Ensembl

germinal center formation

Inferred from electronic annotation. Source: Ensembl

humoral immune response mediated by circulating immunoglobulin

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from mutant phenotype PubMed 16384933. Source: MGI

maintenance of protein location in nucleus

Non-traceable author statement PubMed 8196632. Source: UniProtKB

marginal zone B cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay PubMed 16384933. Source: UniProtKB

negative regulation of interleukin-8 biosynthetic process

Inferred from mutant phenotype PubMed 16306601. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16306601. Source: UniProtKB

negative regulation of tumor necrosis factor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-10 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16384933. Source: UniProtKB

positive regulation of translation

Inferred from mutant phenotype PubMed 16384933. Source: UniProtKB

protein import into nucleus, translocation

Inferred from mutant phenotype PubMed 16280327. Source: UniProtKB

regulation of DNA binding

Inferred from expression pattern PubMed 9407099. Source: UniProtKB

regulation of NF-kappaB import into nucleus

Inferred from expression pattern PubMed 8196632. Source: UniProtKB

regulation of apoptotic process

Inferred from direct assay PubMed 16732314. Source: UniProtKB

response to UV-C

Inferred from direct assay PubMed 16384933. Source: UniProtKB

response to virus

Inferred from direct assay PubMed 16306601. Source: UniProtKB

spleen development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from direct assay PubMed 16306601. Source: UniProtKB

   Cellular_componentBcl3-Bcl10 complex

Inferred from direct assay PubMed 16280327. Source: UniProtKB

Bcl3/NF-kappaB2 complex

Inferred from direct assay PubMed 9407099. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 11387332. Source: UniProtKB

intercellular bridge

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 16280327PubMed 16306601PubMed 8196632. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay PubMed 16280327. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.6PubMed 16280327PubMed 16306601. Source: UniProtKB

protein binding, bridging

Traceable author statement PubMed 16306601. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Inferred from physical interaction PubMed 11387332PubMed 16108830PubMed 16306601PubMed 8196632. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454B-cell lymphoma 3 protein
PRO_0000066976

Regions

Repeat134 – 16330ANK 1
Repeat171 – 20030ANK 2
Repeat204 – 23532ANK 3
Repeat241 – 27030ANK 4
Repeat275 – 30430ANK 5
Repeat308 – 33730ANK 6
Repeat338 – 36730ANK 7
Compositional bias9 – 120112Pro-rich
Compositional bias365 – 45490Pro/Ser-rich

Amino acid modifications

Modified residue4021Phosphoserine; by GSK3 Ref.10
Modified residue4061Phosphoserine; by GSK3 Ref.10

Secondary structure

............................... 454
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20749 [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: 385F5320DB72C0E0

FASTA45447,584
        10         20         30         40         50         60 
MPRCPAGAMD EGPVDLRTRP KAAGLPGAAL PLRKRPLRAP SPEPAAPRGA AGLVVPLDPL 

        70         80         90        100        110        120 
RGGCDLPAVP GPPHGLARPE ALYYPGALLP LYPTRAMGSP FPLVNLPTPL YPMMCPMEHP 

       130        140        150        160        170        180 
LSADIAMATR ADEDGDTPLH IAVVQGNLPA VHRLVNLFQQ GGRELDIYNN LRQTPLHLAV 

       190        200        210        220        230        240 
ITTLPSVVRL LVTAGASPMA LDRHGQTAAH LACEHRSPTC LRALLDSAAP GTLDLEARNY 

       250        260        270        280        290        300 
DGLTALHVAV NTECQETVQL LLERGADIDA VDIKSGRSPL IHAVENNSLS MVQLLLQHGA 

       310        320        330        340        350        360 
NVNAQMYSGS SALHSASGRG LLPLVRTLVR SGADSSLKNC HNDTPLMVAR SRRVIDILRG 

       370        380        390        400        410        420 
KATRPASTSQ PDPSPDRSAN TSPESSSRLS SNGLLSASPS SSPSQSPPRD PPGFPMAPPN 

       430        440        450 
FFLPSPSPPA FLPFAGVLRG PGRPVPPSPA PGGS 

« Hide

References

« Hide 'large scale' references
[1]"The candidate proto-oncogene bcl-3 is related to genes implicated in cell lineage determination and cell cycle control."
Ohno H., Takimoto G., McKeithan T.W.
Cell 60:991-997(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[3]"Genomic structure of the candidate proto-oncogene BCL3."
McKeithan T.W., Ohno H., Dickstein J., Hume E.
Genomics 24:120-126(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 87-454.
Tissue: Leukemia.
[4]"The oncoprotein Bcl-3 directly transactivates through kappa B motifs via association with DNA-binding p50B homodimers."
Bours V., Franzoso G., Azarenko V., Park S., Kanno T., Brown K., Siebenlist U.
Cell 72:729-739(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH NFKB2/P52.
[5]"NF-kappaB p105 is a target of IkappaB kinases and controls signal induction of Bcl-3-p50 complexes."
Heissmeyer V., Krappmann D., Wulczyn F.G., Scheidereit C.
EMBO J. 18:4766-4778(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH NFKB1/P50.
[6]"The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators."
Dechend R., Hirano F., Lehmann K., Heissmeyer V., Ansieau S., Wulczyn F.G., Scheidereit C., Leutz A.
Oncogene 18:3316-3323(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COPS5 AND PIR.
[7]"Identification and characterization of BCL-3-binding protein: implications for transcription and DNA repair or recombination."
Watanabe N., Wachi S., Fujita T.
J. Biol. Chem. 278:26102-26110(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH N4BP2.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family."
Michel F., Soler-Lopez M., Petosa C., Cramer P., Siebenlist U., Muller C.W.
EMBO J. 20:6180-6190(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 127-367.
[10]"GSK3-mediated BCL-3 phosphorylation modulates its degradation and its oncogenicity."
Viatour P., Dejardin E., Warnier M., Lair F., Claudio E., Bureau F., Marine J.C., Merville M.P., Maurer U., Green D., Piette J., Siebenlist U., Bours V., Chariot A.
Mol. Cell 16:35-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-402 AND SER-406.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31731 Genomic DNA. Translation: AAA51816.1. Different initiation.
M31732 mRNA. Translation: AAA51815.1. Different initiation.
AC092066 Genomic DNA. No translation available.
BC064993 mRNA. Translation: AAH64993.1. Different initiation.
AH006679 Genomic DNA. Translation: AAC51348.1.
CCDSCCDS12642.2.
PIRA34794.
RefSeqNP_005169.2. NM_005178.4.
UniGeneHs.31210.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K1AX-ray1.86A127-367[»]
1K1BX-ray1.90A127-367[»]
ProteinModelPortalP20749.
SMRP20749. Positions 133-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107074. 42 interactions.
IntActP20749. 10 interactions.
MINTMINT-105740.
STRING9606.ENSP00000164227.

PTM databases

PhosphoSiteP20749.

Polymorphism databases

DMDM294862410.

Proteomic databases

MaxQBP20749.
PaxDbP20749.
PRIDEP20749.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000164227; ENSP00000164227; ENSG00000069399.
GeneID602.
KEGGhsa:602.
UCSCuc010xxe.2. human.

Organism-specific databases

CTD602.
GeneCardsGC19P045250.
HGNCHGNC:998. BCL3.
HPACAB002051.
HPA047514.
MIM109560. gene.
neXtProtNX_P20749.
PharmGKBPA25310.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000095189.
HOVERGENHBG108320.
InParanoidP20749.
KOK09258.
OMAPLYPMMC.
OrthoDBEOG7W154S.
PhylomeDBP20749.
TreeFamTF320166.

Gene expression databases

BgeeP20749.
CleanExHS_BCL3.
GenevestigatorP20749.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamPF00023. Ank. 4 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20749.
GeneWikiBCL3.
GenomeRNAi602.
NextBio2447.
PROP20749.
SOURCESearch...

Entry information

Entry nameBCL3_HUMAN
AccessionPrimary (citable) accession number: P20749
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: April 20, 2010
Last modified: July 9, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM