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

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Reviewed, UniProtKB/Swiss-Prot P20749 (BCL3_HUMAN)

Last modified June 16, 2009. Version 94. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
B-cell lymphoma 3-encoded protein
Short name=Protein Bcl-3

Gene names

Name:	BCL3
Synonyms:	BCL4, D19S37

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Could be a transcriptional activating factor. Functions as a form of I-kappa-B specific for NF-kappa-B p50 subunit inhibiting its translocation to the nucleus. 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 and COPS5. Ref.6 Ref.7
Subcellular location	Nucleus.
Post-translational modification	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.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement
Disease	Proto-oncogene
Domain	ANK repeat Repeat
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis Inferred from mutant phenotype. Source: MGI I-kappaB kinase/NF-kappaB cascade Inferred from direct assay. Source: UniProtKB maintenance of protein location in nucleus Non-traceable author statement. Source: UniProtKB negative regulation of apoptosis Inferred from direct assay. Source: UniProtKB negative regulation of interleukin-8 biosynthetic process Inferred from mutant phenotype. Source: UniProtKB negative regulation of transcription Inferred from direct assay. Source: UniProtKB positive regulation of translation Inferred from mutant phenotype. Source: UniProtKB protein import into nucleus, translocation Inferred from mutant phenotype. Source: UniProtKB regulation of DNA binding Inferred from expression pattern. Source: UniProtKB regulation of NF-kappaB import into nucleus Inferred from expression pattern. Source: UniProtKB response to UV-C Inferred from direct assay. Source: UniProtKB response to virus Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Bcl3-Bcl10 complex Inferred from direct assay. Source: UniProtKB Bcl3/NF-kappaB2 complex Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from direct assay. Source: UniProtKB nucleus Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding, bridging Traceable author statement. Source: UniProtKB transcription factor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL10	O95999	2	EBI-958997,EBI-958922

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 446

446

B-cell lymphoma 3-encoded protein

PRO_0000066976

Regions

Repeat

126 – 155

ANK 1

Repeat

163 – 192

ANK 2

Repeat

196 – 227

ANK 3

Repeat

233 – 262

ANK 4

Repeat

267 – 296

ANK 5

Repeat

300 – 329

ANK 6

Repeat

330 – 359

ANK 7

Compositional bias

1 – 112

112

Pro-rich

Compositional bias

357 – 446

Pro/Ser-rich

Amino acid modifications

Modified residue

394

Phosphoserine; by GSK3 Ref.9

Modified residue

398

Phosphoserine; by GSK3 Ref.9

Secondary structure

446

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P20749-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 61A4C35151718F7C
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FASTA

446

46,800

        10         20         30         40         50         60 
MDEGPVDLRT RPKAAGLPGA ALPLRKRPLR APSPEPAAPR GAAGLVVPLD PLRGGCDLPA 

        70         80         90        100        110        120 
VPGPPHGLAR PEALYYPGAL LPLYPTRAMG SPFPLVNLPT PLYPMMCPME HPLSADIAMA 

       130        140        150        160        170        180 
TRADEDGDTP LHIAVVQGNL PAVHRLVNLF QQGGRELDIY NNLRQTPLHL AVITTLPSVV 

       190        200        210        220        230        240 
RLLVTAGASP MALDRHGQTA AHLACEHRSP TCLRALLDSA APGTLDLEAR NYDGLTALHV 

       250        260        270        280        290        300 
AVNTECQETV QLLLERGADI DAVDIKSGRS PLIHAVENNS LSMVQLLLQH GANVNAQMYS 

       310        320        330        340        350        360 
GSSALHSASG RGLLPLVRTL VRSGADSSLK NCHNDTPLMV ARSRRVIDIL RGKATRPAST 

       370        380        390        400        410        420 
SQPDPSPDRS ANTSPESSSR LSSNGLLSAS PSSSPSQSPP RDPPGFPMAP PNFFLPSPSP 

       430        440 
PAFLPFAGVL RGPGRPVPPS PAPGGS

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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: 2180580] [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: 15489334] [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: 7896265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-446. 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: 8453667] [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: 10469655] [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: 10362352] [Abstract] Cited for: INTERACTION WITH COPS5.
[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: 12730195] [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: 11707390] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 119-359.
[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: 15469820] [Abstract] Cited for: PHOSPHORYLATION AT SER-394 AND SER-398.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M31731 Genomic DNA. Translation: AAA51816.1.
M31732 mRNA. Translation: AAA51815.1.
BC064993 mRNA. Translation: AAH64993.1.
U05681, U05822 Genomic DNA. Translation: AAC51348.1.

IPI

IPI00791379.

PIR

A34794.

RefSeq

NP_005169.2.

UniGene

Hs.31210

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K1A	X-ray	1.86	A	119-359	[»]
1K1B	X-ray	1.90	A	119-359	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P20749. 1 interaction.

PTM databases

PhosphoSite

P20749.

Proteomic databases

PRIDE

P20749.

Genome annotation databases

Ensembl

ENSG00000069399. Homo sapiens. [Contig view]

GeneID

602.

KEGG

hsa:602.

Organism-specific databases

GeneCards

GC19P049943.

H-InvDB

HIX0040117.

HGNC

HGNC:998. BCL3.

HPA

CAB002051.

MIM

109560. gene.

PharmGKB

PA25310.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P20749.

HOVERGEN

P20749.

Enzyme and pathway databases

Pathway_Interaction_DB

nfkappabatypicalpathway. Atypical NF-kappaB pathway.

Gene expression databases

ArrayExpress

P20749.

Bgee

P20749.

CleanEx

HS_BCL3.

GermOnline

ENSG00000069399. Homo sapiens.

Family and domain databases

InterPro

IPR002110. ANK.
[Graphical view]

Gene3D

G3DSA:1.25.40.20. ANK. 1 hit.

Pfam

PF00023. Ank. 7 hits.
[Graphical view]

SMART

SM00248. ANK. 6 hits.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

2447.

SOURCE

Search...

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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:	February 1, 1991
Last modified:	June 16, 2009
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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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 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

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents