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P20749

- BCL3_HUMAN

UniProt

P20749 - BCL3_HUMAN

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Protein
B-cell lymphoma 3 protein
Gene
BCL3, BCL4, D19S37
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. DNA binding Source: Ensembl
  2. protein binding Source: UniProtKB
  3. protein binding, bridging Source: UniProtKB
  4. sequence-specific DNA binding transcription factor activity Source: Ensembl
  5. transcription factor binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  2. I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  3. T-helper 1 type immune response Source: Ensembl
  4. T-helper 2 cell differentiation Source: Ensembl
  5. antimicrobial humoral response Source: Ensembl
  6. cellular response to DNA damage stimulus Source: UniProtKB
  7. defense response to bacterium Source: Ensembl
  8. defense response to protozoan Source: Ensembl
  9. extracellular matrix organization Source: Ensembl
  10. follicular dendritic cell differentiation Source: Ensembl
  11. germinal center formation Source: Ensembl
  12. humoral immune response mediated by circulating immunoglobulin Source: Ensembl
  13. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
  14. maintenance of protein location in nucleus Source: UniProtKB
  15. marginal zone B cell differentiation Source: Ensembl
  16. negative regulation of apoptotic process Source: UniProtKB
  17. negative regulation of interleukin-8 biosynthetic process Source: UniProtKB
  18. negative regulation of transcription, DNA-templated Source: UniProtKB
  19. negative regulation of tumor necrosis factor biosynthetic process Source: Ensembl
  20. positive regulation of interferon-gamma production Source: Ensembl
  21. positive regulation of interleukin-10 biosynthetic process Source: Ensembl
  22. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  23. positive regulation of transcription, DNA-templated Source: UniProtKB
  24. positive regulation of translation Source: UniProtKB
  25. protein import into nucleus, translocation Source: UniProtKB
  26. regulation of DNA binding Source: UniProtKB
  27. regulation of NF-kappaB import into nucleus Source: UniProtKB
  28. regulation of apoptotic process Source: UniProtKB
  29. response to UV-C Source: UniProtKB
  30. response to virus Source: UniProtKB
  31. spleen development Source: Ensembl
  32. transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
B-cell lymphoma 3 protein
Short name:
BCL-3
Alternative name(s):
Proto-oncogene BCL3
Gene namesi
Name:BCL3
Synonyms:BCL4, D19S37
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:998. BCL3.

Subcellular locationi

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

GO - Cellular componenti

  1. Bcl3-Bcl10 complex Source: UniProtKB
  2. Bcl3/NF-kappaB2 complex Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. intercellular bridge Source: HPA
  5. nucleus Source: UniProtKB
  6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  7. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA25310.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454B-cell lymphoma 3 protein
PRO_0000066976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei402 – 4021Phosphoserine; by GSK31 Publication
Modified residuei406 – 4061Phosphoserine; by GSK31 Publication

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP20749.
PaxDbiP20749.
PRIDEiP20749.

PTM databases

PhosphoSiteiP20749.

Expressioni

Gene expression databases

BgeeiP20749.
CleanExiHS_BCL3.
GenevestigatoriP20749.

Organism-specific databases

HPAiCAB002051.
HPA047514.

Interactioni

Subunit structurei

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL10O959993EBI-958997,EBI-958922
CTBP2P565452EBI-958997,EBI-741533
LCKP062393EBI-958997,EBI-1348

Protein-protein interaction databases

BioGridi107074. 42 interactions.
IntActiP20749. 10 interactions.
MINTiMINT-105740.
STRINGi9606.ENSP00000164227.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi138 – 1447
Helixi148 – 16013
Helixi175 – 1817
Helixi185 – 1939
Helixi208 – 2147
Helixi218 – 22710
Helixi245 – 2528
Helixi255 – 2639
Turni273 – 2753
Helixi279 – 2857
Helixi289 – 2979
Helixi312 – 3198
Helixi322 – 3309
Turni345 – 3484
Helixi352 – 3587

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K1AX-ray1.86A127-367[»]
1K1BX-ray1.90A127-367[»]
ProteinModelPortaliP20749.
SMRiP20749. Positions 133-432.

Miscellaneous databases

EvolutionaryTraceiP20749.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati134 – 16330ANK 1
Add
BLAST
Repeati171 – 20030ANK 2
Add
BLAST
Repeati204 – 23532ANK 3
Add
BLAST
Repeati241 – 27030ANK 4
Add
BLAST
Repeati275 – 30430ANK 5
Add
BLAST
Repeati308 – 33730ANK 6
Add
BLAST
Repeati338 – 36730ANK 7
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 120112Pro-rich
Add
BLAST
Compositional biasi365 – 45490Pro/Ser-rich
Add
BLAST

Sequence similaritiesi

Contains 7 ANK repeats.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000095189.
HOVERGENiHBG108320.
InParanoidiP20749.
KOiK09258.
OMAiPLYPMMC.
OrthoDBiEOG7W154S.
PhylomeDBiP20749.
TreeFamiTF320166.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 4 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20749-1 [UniParc]FASTAAdd to Basket

« Hide

MPRCPAGAMD EGPVDLRTRP KAAGLPGAAL PLRKRPLRAP SPEPAAPRGA    50
AGLVVPLDPL RGGCDLPAVP GPPHGLARPE ALYYPGALLP LYPTRAMGSP 100
FPLVNLPTPL YPMMCPMEHP LSADIAMATR ADEDGDTPLH IAVVQGNLPA 150
VHRLVNLFQQ GGRELDIYNN LRQTPLHLAV ITTLPSVVRL LVTAGASPMA 200
LDRHGQTAAH LACEHRSPTC LRALLDSAAP GTLDLEARNY DGLTALHVAV 250
NTECQETVQL LLERGADIDA VDIKSGRSPL IHAVENNSLS MVQLLLQHGA 300
NVNAQMYSGS SALHSASGRG LLPLVRTLVR SGADSSLKNC HNDTPLMVAR 350
SRRVIDILRG KATRPASTSQ PDPSPDRSAN TSPESSSRLS SNGLLSASPS 400
SSPSQSPPRD PPGFPMAPPN FFLPSPSPPA FLPFAGVLRG PGRPVPPSPA 450
PGGS 454
Length:454
Mass (Da):47,584
Last modified:April 20, 2010 - v2
Checksum:i385F5320DB72C0E0
GO

Sequence cautioni

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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12642.2.
PIRiA34794.
RefSeqiNP_005169.2. NM_005178.4.
UniGeneiHs.31210.

Genome annotation databases

EnsembliENST00000164227; ENSP00000164227; ENSG00000069399.
GeneIDi602.
KEGGihsa:602.
UCSCiuc010xxe.2. human.

Polymorphism databases

DMDMi294862410.

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS12642.2.
PIRi A34794.
RefSeqi NP_005169.2. NM_005178.4.
UniGenei Hs.31210.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K1A X-ray 1.86 A 127-367 [» ]
1K1B X-ray 1.90 A 127-367 [» ]
ProteinModelPortali P20749.
SMRi P20749. Positions 133-432.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107074. 42 interactions.
IntActi P20749. 10 interactions.
MINTi MINT-105740.
STRINGi 9606.ENSP00000164227.

PTM databases

PhosphoSitei P20749.

Polymorphism databases

DMDMi 294862410.

Proteomic databases

MaxQBi P20749.
PaxDbi P20749.
PRIDEi P20749.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000164227 ; ENSP00000164227 ; ENSG00000069399 .
GeneIDi 602.
KEGGi hsa:602.
UCSCi uc010xxe.2. human.

Organism-specific databases

CTDi 602.
GeneCardsi GC19P045250.
HGNCi HGNC:998. BCL3.
HPAi CAB002051.
HPA047514.
MIMi 109560. gene.
neXtProti NX_P20749.
PharmGKBi PA25310.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOGENOMi HOG000095189.
HOVERGENi HBG108320.
InParanoidi P20749.
KOi K09258.
OMAi PLYPMMC.
OrthoDBi EOG7W154S.
PhylomeDBi P20749.
TreeFami TF320166.

Miscellaneous databases

EvolutionaryTracei P20749.
GeneWikii BCL3.
GenomeRNAii 602.
NextBioi 2447.
PROi P20749.
SOURCEi Search...

Gene expression databases

Bgeei P20749.
CleanExi HS_BCL3.
Genevestigatori P20749.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view ]
Pfami PF00023. Ank. 4 hits.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 6 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PHOSPHORYLATION AT SER-402 AND SER-406.

Entry informationi

Entry nameiBCL3_HUMAN
AccessioniPrimary (citable) accession number: P20749
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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