B-cell lymphoma 3 protein - Homo sapiens (Human)

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P20749 (BCL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 135. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
B-cell lymphoma 3 protein
Short name=BCL-3

Alternative name(s):
Proto-oncogene BCL3

Gene names

Name:	BCL3
Synonyms:	BCL4, D19S37

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › perinuclear 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Chromosomal rearrangement
Disease	Proto-oncogene
Domain	ANK repeat Repeat
Molecular function	Activator
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator Inferred from mutant phenotype PubMed 16384933. Source: UniProtKB I-kappaB kinase/NF-kappaB cascade Inferred from direct assay PubMed 8196632. Source: UniProtKB T-helper 1 type immune response Inferred from electronic annotation. Source: Compara T-helper 2 cell differentiation Inferred from electronic annotation. Source: Compara antimicrobial humoral response Inferred from electronic annotation. Source: Compara defense response to bacterium Inferred from electronic annotation. Source: Compara defense response to protozoan Inferred from electronic annotation. Source: Compara extracellular matrix organization Inferred from electronic annotation. Source: Compara follicular dendritic cell differentiation Inferred from electronic annotation. Source: Compara germinal center formation Inferred from electronic annotation. Source: Compara humoral immune response mediated by circulating immunoglobulin Inferred from electronic annotation. Source: Compara 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: Compara 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-dependent Inferred from direct assay PubMed 16306601. Source: UniProtKB negative regulation of tumor necrosis factor biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of interferon-gamma production Inferred from electronic annotation. Source: Compara positive regulation of interleukin-10 biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent 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 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: Compara transcription, DNA-dependent Inferred from direct assay PubMed 16306601. Source: UniProtKB
Cellular_component	Bcl3-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 nucleus Inferred from direct assay PubMed 16280327 PubMed 16306601 PubMed 8196632. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: Compara protein binding, bridging Traceable author statement PubMed 16306601. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL10	O95999	3	EBI-958997,EBI-958922
CTBP2	P56545	2	EBI-958997,EBI-741533

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 454

454

B-cell lymphoma 3 protein

PRO_0000066976

Regions

Repeat

134 – 163

ANK 1

Repeat

171 – 200

ANK 2

Repeat

204 – 235

ANK 3

Repeat

241 – 270

ANK 4

Repeat

275 – 304

ANK 5

Repeat

308 – 337

ANK 6

Repeat

338 – 367

ANK 7

Compositional bias

9 – 120

112

Pro-rich

Compositional bias

365 – 454

Pro/Ser-rich

Amino acid modifications

Modified residue

402

Phosphoserine; by GSK3

Modified residue

406

Phosphoserine; by GSK3 Ref.9

Secondary structure

454

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P20749 [UniParc].

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

454

47,584

        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' referencesShow '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]	"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.
[9]	"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-404 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.

IPI

IPI00791379.

PIR

A34794.

RefSeq

NP_005169.2. NM_005178.4.

UniGene

Hs.31210.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K1A	X-ray	1.86	A	127-367	[»]
1K1B	X-ray	1.90	A	127-367	[»]

ProteinModelPortal

P20749.

SMR

P20749. Positions 133-411.

ModBase

Search...

Protein-protein interaction databases

IntAct

P20749. 3 interactions.

STRING

9606.ENSP00000164227.

PTM databases

PhosphoSite

P20749.

Polymorphism databases

DMDM

294862410.

Proteomic databases

PaxDb

P20749.

PRIDE

P20749.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000164227; ENSP00000164227; ENSG00000069399.

GeneID

602.

KEGG

hsa:602.

UCSC

uc010xxe.2. human.

Organism-specific databases

CTD

602.

GeneCards

GC19P045250.

HGNC

HGNC:998. BCL3.

HPA

CAB002051.

MIM

109560. gene.

neXtProt

NX_P20749.

PharmGKB

PA25310.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOGENOM

HOG000095189.

HOVERGEN

HBG108320.

InParanoid

P20749.

K09258.

OrthoDB

EOG4NCMD1.

Enzyme and pathway databases

Pathway_Interaction_DB

nfkappabatypicalpathway. Atypical NF-kappaB pathway.

Gene expression databases

Bgee

P20749.

CleanEx

HS_BCL3.

Genevestigator

P20749.

GermOnline

ENSG00000069399. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]

Pfam

PF00023. Ank. 4 hits.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 6 hits.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P20749.

GenomeRNAi

602.

NextBio

2447.

SOURCE

Search...

Entry information

Entry name

BCL3_HUMAN

Accession

Primary (citable) accession number: P20749

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	April 20, 2010
Last modified:	May 1, 2013
This is version 135 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 19

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents