ID   KAISO_MOUSE             Reviewed;         671 AA.
AC   Q8BN78; Q8C226; Q9WTZ7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Transcriptional regulator Kaiso;
DE   AltName: Full=Zinc finger and BTB domain-containing protein 33;
GN   Name=Zbtb33; Synonyms=Kaiso;
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], SELF-ASSOCIATION, INTERACTION WITH CTNND1,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=10207085; DOI=10.1128/mcb.19.5.3614;
RA   Daniel J.M., Reynolds A.B.;
RT   "The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc
RT   finger transcription factor.";
RL   Mol. Cell. Biol. 19:3614-3623(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   DNA-BINDING, AND INTERACTION WITH CTNND1.
RX   PubMed=12087177; DOI=10.1093/nar/gkf398;
RA   Daniel J.M., Spring C.M., Crawford H.C., Reynolds A.B., Baig A.;
RT   "The p120(ctn)-binding partner Kaiso is a bi-modal DNA-binding protein that
RT   recognizes both a sequence-specific consensus and methylated CpG
RT   dinucleotides.";
RL   Nucleic Acids Res. 30:2911-2919(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=15138284; DOI=10.1242/jcs.01101;
RA   Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.;
RT   "NLS-dependent nuclear localization of p120ctn is necessary to relieve
RT   Kaiso-mediated transcriptional repression.";
RL   J. Cell Sci. 117:2675-2686(2004).
RN   [5]
RP   ERRATUM OF PUBMED:15138284.
RA   Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.;
RL   J. Cell Sci. 117:3405-3405(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH KPNA2, SUBCELLULAR LOCATION, NUCLEAR
RP   LOCALIZATION SIGNAL, AND MUTAGENESIS OF LYS-472.
RX   PubMed=15564377; DOI=10.1242/jcs.01541;
RA   Kelly K.F., Otchere A.A., Graham M., Daniel J.M.;
RT   "Nuclear import of the BTB/POZ transcriptional regulator Kaiso.";
RL   J. Cell Sci. 117:6143-6152(2004).
RN   [7]
RP   FUNCTION, DNA-BINDING, INTERACTION WITH CTNND2, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=15282317; DOI=10.1128/mcb.24.16.7188-7196.2004;
RA   Rodova M., Kelly K.F., VanSaun M., Daniel J.M., Werle M.J.;
RT   "Regulation of the rapsyn promoter by kaiso and delta-catenin.";
RL   Mol. Cell. Biol. 24:7188-7196(2004).
RN   [8]
RP   FUNCTION.
RX   PubMed=15817151; DOI=10.1016/j.yexcr.2005.01.007;
RA   Spring C.M., Kelly K.F., O'Kelly I., Graham M., Crawford H.C., Daniel J.M.;
RT   "The catenin p120ctn inhibits Kaiso-mediated transcriptional repression of
RT   the beta-catenin/TCF target gene matrilysin.";
RL   Exp. Cell Res. 305:253-265(2005).
RN   [9]
RP   DNA-BINDING.
RX   PubMed=15953356; DOI=10.1111/j.1471-4159.2005.03173.x;
RA   Aranyi T., Faucheux B.A., Khalfallah O., Vodjdani G., Biguet N.F.,
RA   Mallet J., Meloni R.;
RT   "The tissue-specific methylation of the human tyrosine hydroxylase gene
RT   reveals new regulatory elements in the first exon.";
RL   J. Neurochem. 94:129-139(2005).
CC   -!- FUNCTION: Transcriptional regulator with bimodal DNA-binding
CC       specificity. Binds to methylated CpG dinucleotides in the consensus
CC       sequence 5'-CGCG-3' and also binds to the non-methylated consensus
CC       sequence 5'-CTGCNA-3' also known as the consensus kaiso binding site
CC       (KBS). May recruit the N-CoR repressor complex to promote histone
CC       deacetylation and the formation of repressive chromatin structures in
CC       target gene promoters. Contributes to the repression of target genes of
CC       the Wnt signaling pathway. May also activate transcription of a subset
CC       of target genes by the recruitment of CTNND2. Represses expression of
CC       MMP7 in conjunction with transcriptional corepressors CBFA2T3, CBFA2T2
CC       and RUNX1T1 (By similarity). {ECO:0000250|UniProtKB:Q86T24,
CC       ECO:0000269|PubMed:15138284, ECO:0000269|PubMed:15282317,
CC       ECO:0000269|PubMed:15564377, ECO:0000269|PubMed:15817151}.
CC   -!- SUBUNIT: Interacts with NCOR1 (By similarity). Self-associates.
CC       Interacts with CTNND1, and this interaction inhibits binding to both
CC       methylated and non-methylated DNA. Interacts with CTNND2. Interacts
CC       with KPNA2/RCH1, which may mediate nuclear import of this protein.
CC       Interacts with CBFA2T3 (By similarity). {ECO:0000250|UniProtKB:Q86T24,
CC       ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:12087177,
CC       ECO:0000269|PubMed:15282317, ECO:0000269|PubMed:15564377}.
CC   -!- INTERACTION:
CC       Q8BN78; P30999: Ctnnd1; NbExp=3; IntAct=EBI-1216314, EBI-529924;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10207085,
CC       ECO:0000269|PubMed:15282317, ECO:0000269|PubMed:15564377}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC       neuromuscular junctions, skeletal muscle, spleen and testis.
CC       {ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:15282317}.
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DR   EMBL; AF097416; AAD20989.1; -; mRNA.
DR   EMBL; AK087417; BAC39866.1; -; mRNA.
DR   EMBL; AK089423; BAC40875.1; -; mRNA.
DR   CCDS; CCDS30088.1; -.
DR   RefSeq; NP_001072981.1; NM_001079513.1.
DR   RefSeq; NP_064652.2; NM_020256.2.
DR   AlphaFoldDB; Q8BN78; -.
DR   SMR; Q8BN78; -.
DR   BioGRID; 208181; 8.
DR   IntAct; Q8BN78; 3.
DR   MINT; Q8BN78; -.
DR   STRING; 10090.ENSMUSP00000049983; -.
DR   iPTMnet; Q8BN78; -.
DR   PhosphoSitePlus; Q8BN78; -.
DR   EPD; Q8BN78; -.
DR   MaxQB; Q8BN78; -.
DR   PaxDb; 10090-ENSMUSP00000110795; -.
DR   ProteomicsDB; 263572; -.
DR   Pumba; Q8BN78; -.
DR   Antibodypedia; 401; 248 antibodies from 31 providers.
DR   DNASU; 56805; -.
DR   Ensembl; ENSMUST00000049740.3; ENSMUSP00000049983.3; ENSMUSG00000048047.4.
DR   Ensembl; ENSMUST00000115142.3; ENSMUSP00000110795.3; ENSMUSG00000048047.4.
DR   GeneID; 56805; -.
DR   KEGG; mmu:56805; -.
DR   UCSC; uc009szp.1; mouse.
DR   AGR; MGI:1927290; -.
DR   CTD; 10009; -.
DR   MGI; MGI:1927290; Zbtb33.
DR   VEuPathDB; HostDB:ENSMUSG00000048047; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000157481; -.
DR   InParanoid; Q8BN78; -.
DR   OMA; TELEDHY; -.
DR   OrthoDB; 783166at2759; -.
DR   PhylomeDB; Q8BN78; -.
DR   TreeFam; TF333100; -.
DR   BioGRID-ORCS; 56805; 0 hits in 80 CRISPR screens.
DR   ChiTaRS; Zbtb33; mouse.
DR   PRO; PR:Q8BN78; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q8BN78; Protein.
DR   Bgee; ENSMUSG00000048047; Expressed in medial ganglionic eminence and 221 other cell types or tissues.
DR   ExpressionAtlas; Q8BN78; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008327; F:methyl-CpG binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0006351; P:DNA-templated transcription; ISA:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd18219; BTB_POZ_ZBTB33_KAISO; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
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   PANTHER; PTHR46105; AGAP004733-PA; 1.
DR   PANTHER; PTHR46105:SF7; ZINC FINGER AND BTB DOMAIN-CONTAINING PROTEIN 7C; 1.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
DR   Genevisible; Q8BN78; MM.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Wnt signaling pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..671
FT                   /note="Transcriptional regulator Kaiso"
FT                   /id="PRO_0000046989"
FT   DOMAIN          32..94
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         492..514
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         520..542
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         548..571
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..136
FT                   /note="Self-association"
FT   REGION          1..103
FT                   /note="Interaction with NCOR1"
FT                   /evidence="ECO:0000250"
FT   REGION          127..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..571
FT                   /note="Interaction with CBFA2T3"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   REGION          332..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..671
FT                   /note="Interaction with CTNND1"
FT   REGION          512..637
FT                   /note="Required for DNA-binding"
FT   MOTIF           469..478
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:15564377"
FT   COMPBIAS        127..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         251
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        151
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        153
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        388
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        405
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        412
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        447
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        463
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        472
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        477
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        537
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        568
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        580
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        609
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   CROSSLNK        616
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86T24"
FT   MUTAGEN         472
FT                   /note="K->A: Abrogates nuclear localization."
FT                   /evidence="ECO:0000269|PubMed:15564377"
FT   CONFLICT        441
FT                   /note="D -> N (in Ref. 1; AAD20989)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        451
FT                   /note="D -> H (in Ref. 1; AAD20989)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        640
FT                   /note="E -> K (in Ref. 1; AAD20989)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   671 AA;  74050 MW;  CFD23E0C15B491D1 CRC64;
     MESRKLISAT DIQYSASLLN SLNEQRGHGL FCDVTVIVED RKFRAHRNIL SASSTYFHQL
     FSVAGQVVEL SFIRAEIFAE ILNYIYSSKV VRVRADLLDE LIKSGQLLGV KFIAELGVPL
     SQVKSISGTE QDGTAETLPS SSSDKSLDME KSKDEAQDNG ATVMPIITES FSLSAEDNEM
     KKIIVTDSDD DDDDDVIFCS EILPAKEDLP SNNTATQVQP NPASVAISEV TPCASNNSPP
     VTNITPTQLP TPVNQATLSQ TQGSEELLVS SASTHLTPNI ILLNQAPLTA PPSASSSLPN
     HMSSSVNVLV QNQQTPNSAV LTGNKAEEEE EIIDDDDDII SSSPDSAVSN TSLVPQADNS
     KSTTLDGSLT QKMQIPVLPQ EPPSNSLKIS DVITRNTNDP GLRSKHVMEG QKIITLDTAT
     EIEGLSTGCK VYANIGEDTY DIVIPVKDDP DGGEAKLDNE LPKTSGSEPP NKRMKVKHDD
     HYELIVDGRV YYICIVCKRS YVCLTSLRRH FNIHSWEKKY QCRYCDKVFP LAEYRTKHEI
     HHTGERRYQC LTCGKSFINY QFMSSHIKSV HSQDPSGDSK LYRLHPCKSL QIRQYAYLSN
     KSSAMPVMKD DAVGYKVDAG KEPPVGTTST PPQNKSTFWE DIFIQQENDS IFKQNVTDGS
     TEFEFIIPES Y
//