BCL3_MOUSE
ID BCL3_MOUSE Reviewed; 448 AA.
AC Q9Z2F6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=B-cell lymphoma 3 protein homolog;
DE Short=BCL-3;
GN Name=Bcl3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=10361130;
RA Richard M., Louahed J., Demoulin J.-B., Renauld J.-C.;
RT "Interleukin-9 regulates NF-kappaB activity through BCL3 gene induction.";
RL Blood 93:4318-4327(1999).
RN [3]
RP FUNCTION, INTERACTION WITH CYLD, AND SUBCELLULAR LOCATION.
RX PubMed=16713561; DOI=10.1016/j.cell.2006.03.041;
RA Massoumi R., Chmielarska K., Hennecke K., Pfeifer A., Fassler R.;
RT "Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent NF-
RT kappaB signaling.";
RL Cell 125:665-677(2006).
RN [4]
RP INTERACTION WITH CYLD.
RX PubMed=19893491; DOI=10.1038/emboj.2009.317;
RA Wickstrom S.A., Masoumi K.C., Khochbin S., Fassler R., Massoumi R.;
RT "CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and
RT increasing the levels of acetylated tubulin.";
RL EMBO J. 29:131-144(2010).
CC -!- FUNCTION: Contributes to the regulation of transcriptional activation
CC of NF-kappa-B target genes. In the cytoplasm, inhibits the nuclear
CC translocation of the NF-kappa-B p50 subunit (By similarity). In the
CC nucleus, acts as transcriptional activator that promotes transcription
CC of NF-kappa-B target genes. Contributes to the regulation of cell
CC proliferation. {ECO:0000250, ECO:0000269|PubMed:16713561}.
CC -!- SUBUNIT: Component of a complex consisting of the NF-kappa-B p52-p52
CC homodimer and BCL3. Component of a complex consisting of the NF-kappa-B
CC p50-p50 homodimer and BCL3. Interacts with N4BP2, COPS5 and PIR (By
CC similarity). Interacts with CYLD. {ECO:0000250,
CC ECO:0000269|PubMed:16713561, ECO:0000269|PubMed:19893491}.
CC -!- INTERACTION:
CC Q9Z2F6; Q80TQ2: Cyld; NbExp=5; IntAct=EBI-943884, EBI-943859;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16713561}. Cytoplasm
CC {ECO:0000269|PubMed:16713561}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16713561}. Note=Ubiquitination via 'Lys-63'-linked
CC ubiquitin chains is required for nuclear accumulation.
CC -!- PTM: Polyubiquitinated. Ubiquitination via 'Lys-63'-linked ubiquitin
CC chains is required for nuclear accumulation. Deubiquitinated by CYLD,
CC which acts on 'Lys-63'-linked ubiquitin chains. Deubiquitination by
CC CYLD prevents nuclear accumulation.
CC -!- PTM: Activated by phosphorylation. {ECO:0000250}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79694.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC149085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC149282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF067774; AAC79694.1; ALT_INIT; mRNA.
DR CCDS; CCDS20914.2; -.
DR RefSeq; NP_291079.2; NM_033601.3.
DR AlphaFoldDB; Q9Z2F6; -.
DR SMR; Q9Z2F6; -.
DR BioGRID; 198326; 1.
DR IntAct; Q9Z2F6; 1.
DR MINT; Q9Z2F6; -.
DR STRING; 10090.ENSMUSP00000113851; -.
DR iPTMnet; Q9Z2F6; -.
DR PhosphoSitePlus; Q9Z2F6; -.
DR EPD; Q9Z2F6; -.
DR MaxQB; Q9Z2F6; -.
DR PaxDb; Q9Z2F6; -.
DR PRIDE; Q9Z2F6; -.
DR ProteomicsDB; 273548; -.
DR Antibodypedia; 3672; 399 antibodies from 41 providers.
DR DNASU; 12051; -.
DR Ensembl; ENSMUST00000120537; ENSMUSP00000113851; ENSMUSG00000053175.
DR GeneID; 12051; -.
DR KEGG; mmu:12051; -.
DR UCSC; uc009fnk.2; mouse.
DR CTD; 602; -.
DR MGI; MGI:88140; Bcl3.
DR VEuPathDB; HostDB:ENSMUSG00000053175; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000161392; -.
DR HOGENOM; CLU_720685_0_0_1; -.
DR InParanoid; Q9Z2F6; -.
DR OMA; MMCSMEH; -.
DR OrthoDB; 1341288at2759; -.
DR PhylomeDB; Q9Z2F6; -.
DR TreeFam; TF320166; -.
DR BioGRID-ORCS; 12051; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Bcl3; mouse.
DR PRO; PR:Q9Z2F6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z2F6; protein.
DR Bgee; ENSMUSG00000053175; Expressed in lumbar dorsal root ganglion and 122 other tissues.
DR ExpressionAtlas; Q9Z2F6; baseline and differential.
DR Genevisible; Q9Z2F6; MM.
DR GO; GO:0032996; C:Bcl3-Bcl10 complex; ISO:MGI.
DR GO; GO:0033257; C:Bcl3/NF-kappaB2 complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0019730; P:antimicrobial humoral response; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0002268; P:follicular dendritic cell differentiation; IMP:MGI.
DR GO; GO:0002467; P:germinal center formation; IMP:MGI.
DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI.
DR GO; GO:0002315; P:marginal zone B cell differentiation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051101; P:regulation of DNA binding; IEA:Ensembl.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0010225; P:response to UV-C; ISO:MGI.
DR GO; GO:0009615; P:response to virus; ISO:MGI.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR GO; GO:0070231; P:T cell apoptotic process; IMP:MGI.
DR GO; GO:0042088; P:T-helper 1 type immune response; IMP:MGI.
DR GO; GO:0045064; P:T-helper 2 cell differentiation; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
PE 1: Evidence at protein level;
KW Activator; ANK repeat; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..448
FT /note="B-cell lymphoma 3 protein homolog"
FT /id="PRO_0000066977"
FT REPEAT 129..161
FT /note="ANK 1"
FT REPEAT 166..195
FT /note="ANK 2"
FT REPEAT 199..228
FT /note="ANK 3"
FT REPEAT 236..265
FT /note="ANK 4"
FT REPEAT 270..299
FT /note="ANK 5"
FT REPEAT 303..332
FT /note="ANK 6"
FT REPEAT 333..362
FT /note="ANK 7"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20749"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20749"
FT MOD_RES 396
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000250|UniProtKB:P20749"
FT MOD_RES 400
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000250|UniProtKB:P20749"
SQ SEQUENCE 448 AA; 47216 MW; 7665D28BBC3EE194 CRC64;
MPRCPAGAMD EGPVDLRTRP KGTPGAALPL RKRPLRPASP EPATTRSPAG PLDALRSGCD
VPVVPGPPHC VARPEALYYQ GPLMPIYSTP TMAPHFPLLN LPTHPYSMIC PMEHPLSADI
AMATRVDEDG DTPLHIAVVQ NNIAAVYRIL SLFKLGSREV DVHNNLRQTP LHLAVITTLP
DMVRLLVTAG ASPMALDRHG QTAIHLACEH RSPSCLQALL DSATSGSVDL EVRNYEGLTA
LHVAVNTGCQ EAVLLLLERG ADIDAVDIKS GRSPLIHAVE NNSLNMVQLL LLHGANVNAQ
MYSGSSALHS ASGRGLLPLV RTLVRSGADS GLKNCHNDTP LMVARSRRVI DILRGKASRA
ASGSQPEPSP DQSATNSPES SSRLSSNGLQ SSPSSSPSLS PPKDAPGFPA TPQNFFLPTT
STPAFLPFPG VLRGPGRPVP PSPAPGSS
