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P20749

- BCL3_HUMAN

UniProt

P20749 - BCL3_HUMAN

Protein

B-cell lymphoma 3 protein

Gene

BCL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (20 Apr 2010)
      Previous versions | rss
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    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.By similarity

    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

    GO - Biological processi

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

    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/NF-kappaB2 complex Source: UniProtKB
    2. Bcl3-Bcl10 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

    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 proteinPRO_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.By similarity
    Activated by phosphorylation.1 Publication

    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.By similarity

    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

    1
    454
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20749.

    Family & Domainsi

    Domains and Repeats

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

    Compositional bias

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

    Sequence similaritiesi

    Contains 7 ANK repeats.PROSITE-ProRule annotation

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 147 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.Curated

    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