BCL6B_MOUSE
ID BCL6B_MOUSE Reviewed; 474 AA.
AC O88282; Q8CCJ6;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=B-cell CLL/lymphoma 6 member B protein;
DE AltName: Full=Bcl6-associated zinc finger protein;
GN Name=Bcl6b; Synonyms=Bazf;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP INTERACTION WITH BCL6.
RX PubMed=9632807; DOI=10.1128/mcb.18.7.4235;
RA Okabe S., Fukuda T., Ishibashi K., Kojima S., Okada S., Hatano M.,
RA Ebara M., Saisho H., Tokuhisa T.;
RT "BAZF, a novel Bcl6 homolog, functions as a transcriptional repressor.";
RL Mol. Cell. Biol. 18:4235-4244(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 304-474.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION.
RX PubMed=15314041; DOI=10.1093/intimm/dxh144;
RA Takamori M., Hatano M., Arima M., Sakamoto A., Fujimura L., Hartatik T.,
RA Kuriyama T., Tokuhisa T.;
RT "BAZF is required for activation of naive CD4 T cells by TCR triggering.";
RL Int. Immunol. 16:1439-1449(2004).
CC -!- FUNCTION: Acts as a sequence-specific transcriptional repressor in
CC association with BCL6. Necessary for activation of naive T-cells to
CC antigenic stimulation. May attenuate the regulatory effect of BCL6 on
CC antigenic activation of naive CD4 T-cells by forming a heterodimer with
CC BCL6. {ECO:0000269|PubMed:15314041, ECO:0000269|PubMed:9632807}.
CC -!- SUBUNIT: Associates with BCL6 through the BTB domain.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression found
CC in heart and lung. {ECO:0000269|PubMed:9632807}.
CC -!- INDUCTION: Induced in activated lymphocytes.
CC {ECO:0000269|PubMed:9632807}.
CC -!- DOMAIN: Amino acids 178-210 are essential for repression activity.
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DR EMBL; AB011665; BAA31223.1; -; mRNA.
DR EMBL; AK032647; BAC27970.1; -; mRNA.
DR CCDS; CCDS24939.1; -.
DR RefSeq; NP_031554.1; NM_007528.3.
DR AlphaFoldDB; O88282; -.
DR SMR; O88282; -.
DR BioGRID; 198305; 2.
DR STRING; 10090.ENSMUSP00000000326; -.
DR iPTMnet; O88282; -.
DR PhosphoSitePlus; O88282; -.
DR PaxDb; O88282; -.
DR PRIDE; O88282; -.
DR Antibodypedia; 23875; 82 antibodies from 23 providers.
DR DNASU; 12029; -.
DR Ensembl; ENSMUST00000000326; ENSMUSP00000000326; ENSMUSG00000000317.
DR GeneID; 12029; -.
DR KEGG; mmu:12029; -.
DR UCSC; uc007juc.2; mouse.
DR CTD; 255877; -.
DR MGI; MGI:1278332; Bcl6b.
DR VEuPathDB; HostDB:ENSMUSG00000000317; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159844; -.
DR HOGENOM; CLU_024196_2_0_1; -.
DR InParanoid; O88282; -.
DR OMA; VCGARFN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O88282; -.
DR TreeFam; TF330912; -.
DR BioGRID-ORCS; 12029; 0 hits in 72 CRISPR screens.
DR PRO; PR:O88282; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O88282; protein.
DR Bgee; ENSMUSG00000000317; Expressed in kidney vasculature and 186 other tissues.
DR ExpressionAtlas; O88282; baseline and differential.
DR Genevisible; O88282; MM.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042092; P:type 2 immune response; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..474
FT /note="B-cell CLL/lymphoma 6 member B protein"
FT /id="PRO_0000047101"
FT DOMAIN 38..105
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 323..345
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 351..373
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 379..401
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..429
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 435..458
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 144..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 51339 MW; 94886AB265B018D8 CRC64;
MGSTAAPEGA LGYVREFTRH SSDVLSNLNE LRLRGILTDV TLLVGGQPLR AHKAVLIACS
GFFYSIFRGR AGLGVDVLSL PGGPEARGFA PLLDFMYTSR LRLSPATAPA VLAAATYLQM
EHVVQACHRF IQASYEPLGI SLRPVEVEPP RPPTVAPPGS PRRSEGHPDP PTESRSCSQG
SPSPASPDPK ACNWKKYKFI VLNSQTSQAG SLVGESSGQP CPQARLPSGD EACSSSSSSE
EGTTPGLQSR LSLATTTARF KCGALANNSY LFTPRAQETS LPASKQANPP PGSEFFSCQN
CEAVAGCSSG LELLAPGDED KPYKCQLCRS AFRYKGNLAS HRTVHTGEKP YRCSICGARF
NRPANLKTHS RIHSGEKPYK CETCGSRFVQ VAHLRAHVLI HTGEKPYPCP TCGTRFRHLQ
TLKSHVRIHT GEKPYHCDPC GLHFRHKSQL RLHLRQKHGA ATNTKVRYHI LGGP
