KAISO_HUMAN
ID KAISO_HUMAN Reviewed; 672 AA.
AC Q86T24; B2R5U6; O00319; Q7Z361; Q8IVP6; Q8N3P0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Transcriptional regulator Kaiso;
DE AltName: Full=Zinc finger and BTB domain-containing protein 33;
GN Name=ZBTB33; Synonyms=KAISO, ZNF348;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala, Endometrial tumor, and Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH CTNND1.
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 [7]
RP FUNCTION, DNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11445535; DOI=10.1101/gad.198501;
RA Prokhortchouk A., Hendrich B., Joergensen H., Ruzov A., Wilm M.,
RA Georgiev G., Bird A., Prokhortchouk E.;
RT "The p120 catenin partner Kaiso is a DNA methylation-dependent
RT transcriptional repressor.";
RL Genes Dev. 15:1613-1618(2001).
RN [8]
RP FUNCTION, DNA-BINDING, INTERACTION WITH NCOR1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14527417; DOI=10.1016/j.molcel.2003.08.008;
RA Yoon H.-G., Chan D.W., Reynolds A.B., Qin J., Wong J.;
RT "N-CoR mediates DNA methylation-dependent repression through a methyl CpG
RT binding protein Kaiso.";
RL Mol. Cell 12:723-734(2003).
RN [9]
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF CYS-552.
RC TISSUE=Lung;
RX PubMed=15548582; DOI=10.1242/dev.01549;
RA Ruzov A., Dunican D.S., Prokhortchouk A., Pennings S., Stancheva I.,
RA Prokhortchouk E., Meehan R.R.;
RT "Kaiso is a genome-wide repressor of transcription that is essential for
RT amphibian development.";
RL Development 131:6185-6194(2004).
RN [10]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14699141; DOI=10.1074/jbc.m306057200;
RA Kondapalli J., Flozak A.S., Albuquerque M.L.C.;
RT "Laminar shear stress differentially modulates gene expression of p120
RT catenin, Kaiso transcription factor, and vascular endothelial cadherin in
RT human coronary artery endothelial cells.";
RL J. Biol. Chem. 279:11417-11424(2004).
RN [11]
RP INTERACTION WITH KPNA2.
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 [12]
RP SUBCELLULAR LOCATION.
RX PubMed=15781635; DOI=10.1158/0008-5472.can-04-2020;
RA Soubry A., van Hengel J., Parthoens E., Colpaert C., Van Marck E.,
RA Waltregny D., Reynolds A.B., van Roy F.;
RT "Expression and nuclear location of the transcriptional repressor Kaiso is
RT regulated by the tumor microenvironment.";
RL Cancer Res. 65:2224-2233(2005).
RN [13]
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 [14]
RP FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND INTERACTION WITH CTNND1.
RX PubMed=16354688; DOI=10.1128/mcb.26.1.169-181.2006;
RA Filion G.J., Zhenilo S., Salozhin S., Yamada D., Prokhortchouk E.,
RA Defossez P.A.;
RT "A family of human zinc finger proteins that bind methylated DNA and
RT repress transcription.";
RL Mol. Cell. Biol. 26:169-181(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP FUNCTION, AND INTERACTION WITH CBFA2T3.
RX PubMed=23251453; DOI=10.1371/journal.pone.0051205;
RA Barrett C.W., Smith J.J., Lu L.C., Markham N., Stengel K.R., Short S.P.,
RA Zhang B., Hunt A.A., Fingleton B.M., Carnahan R.H., Engel M.E., Chen X.,
RA Beauchamp R.D., Wilson K.T., Hiebert S.W., Reynolds A.B., Williams C.S.;
RT "Kaiso directs the transcriptional corepressor MTG16 to the Kaiso binding
RT site in target promoters.";
RL PLoS ONE 7:E51205-E51205(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-449; LYS-479 AND LYS-582, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-151; LYS-153; LYS-390; LYS-407;
RP LYS-414; LYS-449; LYS-465; LYS-474; LYS-479; LYS-539; LYS-570; LYS-582;
RP LYS-611 AND LYS-618, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-116.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human zinc finger and BTB domain containing 33.";
RL Submitted (DEC-2008) to the PDB data bank.
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). Recruits the N-CoR repressor complex to promote histone
CC deacetylation and the formation of repressive chromatin structures in
CC target gene promoters. May contribute to the repression of target genes
CC of the Wnt signaling pathway. May also activate transcription of a
CC subset of target genes by the recruitment of CTNND2. Represses
CC expression of MMP7 in conjunction with transcriptional corepressors
CC CBFA2T3, CBFA2T2 and RUNX1T1 (PubMed:23251453).
CC {ECO:0000269|PubMed:11445535, ECO:0000269|PubMed:14527417,
CC ECO:0000269|PubMed:15548582, ECO:0000269|PubMed:15817151,
CC ECO:0000269|PubMed:16354688, ECO:0000269|PubMed:23251453}.
CC -!- SUBUNIT: Self-associates. Interacts with CTNND2 (By similarity).
CC Interacts with CTNND1, and this interaction inhibits binding to both
CC methylated and non-methylated DNA. Interacts with NCOR1. Interacts with
CC KPNA2/RCH1, which may mediate nuclear import of this protein. Interacts
CC with CBFA2T3. {ECO:0000250|UniProtKB:Q8BN78,
CC ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:14527417,
CC ECO:0000269|PubMed:15564377, ECO:0000269|PubMed:16354688,
CC ECO:0000269|PubMed:23251453}.
CC -!- INTERACTION:
CC Q86T24; O60716-5: CTNND1; NbExp=3; IntAct=EBI-2515625, EBI-701963;
CC Q86T24; P57764: GSDMD; NbExp=3; IntAct=EBI-2515625, EBI-2798865;
CC Q86T24; P13807: GYS1; NbExp=3; IntAct=EBI-2515625, EBI-740553;
CC Q86T24; Q9BRQ3: NUDT22; NbExp=3; IntAct=EBI-2515625, EBI-10297093;
CC Q86T24; P61956: SUMO2; NbExp=3; IntAct=EBI-2515625, EBI-473220;
CC Q86T24; P55854: SUMO3; NbExp=3; IntAct=EBI-2515625, EBI-474067;
CC Q86T24; Q8N7C3: TRIML2; NbExp=5; IntAct=EBI-2515625, EBI-11059915;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15781635,
CC ECO:0000269|PubMed:16354688}. Cytoplasm {ECO:0000269|PubMed:15781635}.
CC Note=Also cytoplasmic in cells grown at high densities.
CC -!- TISSUE SPECIFICITY: Expressed in vascular endothelium.
CC {ECO:0000269|PubMed:14699141}.
CC -!- INDUCTION: Induced in vascular endothelium by wounding. This effect is
CC potentiated by prior laminar shear stress, which enhances wound
CC closure. {ECO:0000269|PubMed:14699141}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ZBTB33ID43785chXq24.html";
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DR EMBL; AK312321; BAG35243.1; -; mRNA.
DR EMBL; AL833856; CAD38715.1; -; mRNA.
DR EMBL; AL833604; CAD91170.1; -; mRNA.
DR EMBL; BX538016; CAD97963.1; -; mRNA.
DR EMBL; BX538101; CAD98016.1; -; mRNA.
DR EMBL; AC002086; AAB54087.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11891.1; -; Genomic_DNA.
DR EMBL; BC042753; AAH42753.1; -; mRNA.
DR CCDS; CCDS14596.1; -.
DR RefSeq; NP_001171671.1; NM_001184742.1.
DR RefSeq; NP_006768.1; NM_006777.3.
DR PDB; 2LT7; NMR; -; A=472-604.
DR PDB; 3FKC; X-ray; 1.70 A; A=1-114.
DR PDB; 3M4T; X-ray; 2.05 A; A=1-122.
DR PDB; 3M8V; X-ray; 2.70 A; A=1-122.
DR PDB; 4F6M; X-ray; 2.40 A; A=472-604.
DR PDB; 4F6N; X-ray; 2.80 A; A=472-604.
DR PDB; 5VMU; X-ray; 2.35 A; A=471-604.
DR PDB; 5VMV; X-ray; 2.31 A; A=471-604.
DR PDB; 5VMW; X-ray; 2.40 A; A=471-604.
DR PDB; 5VMX; X-ray; 2.05 A; A=471-604.
DR PDB; 5VMY; X-ray; 2.00 A; A=471-604.
DR PDB; 5VMZ; X-ray; 2.32 A; A=471-604.
DR PDB; 6DF5; X-ray; 1.82 A; A=471-604.
DR PDB; 6DF8; X-ray; 2.54 A; A=471-604.
DR PDB; 6DF9; X-ray; 2.32 A; A=471-604.
DR PDB; 6DFA; X-ray; 1.91 A; A=471-604.
DR PDB; 6DFB; X-ray; 1.66 A; A=471-604.
DR PDB; 6DFC; X-ray; 1.85 A; A=471-604.
DR PDB; 6V8U; X-ray; 2.10 A; A=471-604.
DR PDBsum; 2LT7; -.
DR PDBsum; 3FKC; -.
DR PDBsum; 3M4T; -.
DR PDBsum; 3M8V; -.
DR PDBsum; 4F6M; -.
DR PDBsum; 4F6N; -.
DR PDBsum; 5VMU; -.
DR PDBsum; 5VMV; -.
DR PDBsum; 5VMW; -.
DR PDBsum; 5VMX; -.
DR PDBsum; 5VMY; -.
DR PDBsum; 5VMZ; -.
DR PDBsum; 6DF5; -.
DR PDBsum; 6DF8; -.
DR PDBsum; 6DF9; -.
DR PDBsum; 6DFA; -.
DR PDBsum; 6DFB; -.
DR PDBsum; 6DFC; -.
DR PDBsum; 6V8U; -.
DR AlphaFoldDB; Q86T24; -.
DR SMR; Q86T24; -.
DR BioGRID; 115327; 85.
DR CORUM; Q86T24; -.
DR IntAct; Q86T24; 42.
DR MINT; Q86T24; -.
DR STRING; 9606.ENSP00000314153; -.
DR iPTMnet; Q86T24; -.
DR PhosphoSitePlus; Q86T24; -.
DR BioMuta; ZBTB33; -.
DR DMDM; 84029319; -.
DR EPD; Q86T24; -.
DR jPOST; Q86T24; -.
DR MassIVE; Q86T24; -.
DR MaxQB; Q86T24; -.
DR PaxDb; Q86T24; -.
DR PeptideAtlas; Q86T24; -.
DR PRIDE; Q86T24; -.
DR ProteomicsDB; 69660; -.
DR Antibodypedia; 401; 217 antibodies from 31 providers.
DR DNASU; 10009; -.
DR Ensembl; ENST00000326624.2; ENSP00000314153.2; ENSG00000177485.7.
DR Ensembl; ENST00000557385.2; ENSP00000450969.1; ENSG00000177485.7.
DR GeneID; 10009; -.
DR KEGG; hsa:10009; -.
DR MANE-Select; ENST00000557385.2; ENSP00000450969.1; NM_001184742.2; NP_001171671.1.
DR UCSC; uc004esn.2; human.
DR CTD; 10009; -.
DR DisGeNET; 10009; -.
DR GeneCards; ZBTB33; -.
DR HGNC; HGNC:16682; ZBTB33.
DR HPA; ENSG00000177485; Low tissue specificity.
DR MIM; 300329; gene.
DR neXtProt; NX_Q86T24; -.
DR OpenTargets; ENSG00000177485; -.
DR PharmGKB; PA134928604; -.
DR VEuPathDB; HostDB:ENSG00000177485; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157481; -.
DR HOGENOM; CLU_024688_0_0_1; -.
DR InParanoid; Q86T24; -.
DR OMA; TELEDHY; -.
DR OrthoDB; 567120at2759; -.
DR PhylomeDB; Q86T24; -.
DR TreeFam; TF333100; -.
DR PathwayCommons; Q86T24; -.
DR SignaLink; Q86T24; -.
DR SIGNOR; Q86T24; -.
DR BioGRID-ORCS; 10009; 10 hits in 765 CRISPR screens.
DR ChiTaRS; ZBTB33; human.
DR EvolutionaryTrace; Q86T24; -.
DR GeneWiki; ZBTB33; -.
DR GenomeRNAi; 10009; -.
DR Pharos; Q86T24; Tbio.
DR PRO; PR:Q86T24; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q86T24; protein.
DR Bgee; ENSG00000177485; Expressed in secondary oocyte and 186 other tissues.
DR Genevisible; Q86T24; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 3D-structure; Activator; Cytoplasm; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..672
FT /note="Transcriptional regulator Kaiso"
FT /id="PRO_0000046988"
FT DOMAIN 32..94
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 494..516
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..544
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 550..573
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..136
FT /note="Self-association"
FT /evidence="ECO:0000250"
FT REGION 1..103
FT /note="Interaction with NCOR1"
FT /evidence="ECO:0000269|PubMed:14527417"
FT REGION 298..573
FT /note="Interaction with CBFA2T3"
FT /evidence="ECO:0000269|PubMed:23251453"
FT REGION 325..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..672
FT /note="Interaction with CTNND1"
FT /evidence="ECO:0000250"
FT REGION 514..638
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 616..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 471..480
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 329..343
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 407
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 570
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 582
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 611
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 618
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 552
FT /note="C->R: Abrogates both sequence-specific and
FT methylation-dependent DNA-binding."
FT /evidence="ECO:0000269|PubMed:15548582"
FT CONFLICT 40
FT /note="D -> Y (in Ref. 2; CAD91170)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="E -> G (in Ref. 2; CAD91170)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="D -> DD (in Ref. 2; CAD91170/CAD97963 and 5;
FT AAH42753)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="S -> Y (in Ref. 2; CAD91170)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="E -> V (in Ref. 2; CAD98016)"
FT /evidence="ECO:0000305"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:3FKC"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:3FKC"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:3FKC"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:3FKC"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:3FKC"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:3FKC"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3M4T"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3FKC"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:3FKC"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3FKC"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:3FKC"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:3FKC"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:6DFB"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:6DFB"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:6DFB"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:6DFB"
FT HELIX 506..517
FT /evidence="ECO:0007829|PDB:6DFB"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:6DFB"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:6DFB"
FT HELIX 534..545
FT /evidence="ECO:0007829|PDB:6DFB"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:6DFB"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:6DFB"
FT STRAND 558..561
FT /evidence="ECO:0007829|PDB:6DFB"
FT HELIX 562..572
FT /evidence="ECO:0007829|PDB:6DFB"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:6DFB"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:6DFB"
FT HELIX 598..600
FT /evidence="ECO:0007829|PDB:5VMY"
SQ SEQUENCE 672 AA; 74484 MW; 76D94B4051056DB5 CRC64;
MESRKLISAT DIQYSGSLLN SLNEQRGHGL FCDVTVIVED RKFRAHKNIL SASSTYFHQL
FSVAGQVVEL SFIRAEIFAE ILNYIYSSKI VRVRSDLLDE LIKSGQLLGV KFIAELGVPL
SQVKSISGTA QDGNTEPLPP DSGDKNLVIQ KSKDEAQDNG ATIMPIITES FSLSAEDYEM
KKIIVTDSDD DDDDVIFCSE ILPTKETLPS NNTVAQVQSN PGPVAISDVA PSASNNSPPL
TNITPTQKLP TPVNQATLSQ TQGSEKLLVS SAPTHLTPNI ILLNQTPLST PPNVSSSLPN
HMPSSINLLV QNQQTPNSAI LTGNKANEEE EEEIIDDDDD TISSSPDSAV SNTSLVPQAD
TSQNTSFDGS LIQKMQIPTL LQEPLSNSLK ISDIITRNTN DPGVGSKHLM EGQKIITLDT
ATEIEGLSTG CKVYANIGED TYDIVIPVKD DPDEGEARLE NEIPKTSGSE MANKRMKVKH
DDHYELIVDG RVYYICIVCK RSYVCLTSLR RHFNIHSWEK KYPCRYCEKV FPLAEYRTKH
EIHHTGERRY QCLACGKSFI NYQFMSSHIK SVHSQDPSGD SKLYRLHPCR SLQIRQYAYL
SDRSSTIPAM KDDGIGYKVD TGKEPPVGTT TSTQNKPMTW EDIFIQQEND SIFKQNVTDG
STEFEFIIPE SY
