KAISO_MOUSE
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 03-AUG-2022, entry version 149.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 7.
DR IntAct; Q8BN78; 3.
DR MINT; Q8BN78; -.
DR STRING; 10090.ENSMUSP00000110795; -.
DR iPTMnet; Q8BN78; -.
DR PhosphoSitePlus; Q8BN78; -.
DR EPD; Q8BN78; -.
DR MaxQB; Q8BN78; -.
DR PaxDb; Q8BN78; -.
DR PRIDE; Q8BN78; -.
DR ProteomicsDB; 263572; -.
DR Antibodypedia; 401; 217 antibodies from 31 providers.
DR DNASU; 56805; -.
DR Ensembl; ENSMUST00000049740; ENSMUSP00000049983; ENSMUSG00000048047.
DR Ensembl; ENSMUST00000115142; ENSMUSP00000110795; ENSMUSG00000048047.
DR GeneID; 56805; -.
DR KEGG; mmu:56805; -.
DR UCSC; uc009szp.1; mouse.
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; 567120at2759; -.
DR PhylomeDB; Q8BN78; -.
DR TreeFam; TF333100; -.
DR BioGRID-ORCS; 56805; 0 hits in 74 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 220 other tissues.
DR ExpressionAtlas; Q8BN78; baseline and differential.
DR Genevisible; Q8BN78; MM.
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:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; ISA:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
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
