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UniProtKB/Swiss-Prot entry Q86T24


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KAISO_HUMAN
Primary accession number Q86T24
Secondary accession numbers O00319 Q7Z361 Q8IVP6 Q8N3P0
Integrated into Swiss-Prot on December 20, 2005
Sequence was last modified on December 20, 2005 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 53)
Name and origin of the protein
Protein name Transcriptional regulator Kaiso
Synonym Zinc finger and BTB domain-containing protein 33
Gene name
Name: ZBTB33
Synonyms: KAISO, ZNF348
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala, Endometrial tumor, and Fetal kidney;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH CTNND1.
PubMed=10207085 [NCBI, ExPASy, EBI, Israel, Japan]
Daniel J.M., Reynolds A.B.;
"The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor.";
Mol. Cell. Biol. 19:3614-3623(1999).
[5]
FUNCTION, DNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1101/gad.198501; PubMed=11445535 [NCBI, ExPASy, EBI, Israel, Japan]
Prokhortchouk A., Hendrich B., Joergensen H., Ruzov A., Wilm M., Georgiev G., Bird A., Prokhortchouk E.;
"The p120 catenin partner Kaiso is a DNA methylation-dependent transcriptional repressor.";
Genes Dev. 15:1613-1618(2001).
[6]
FUNCTION, DNA-BINDING, INTERACTION WITH NCOR1, AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2003.08.008; PubMed=14527417 [NCBI, ExPASy, EBI, Israel, Japan]
Yoon H.-G., Chan D.W., Reynolds A.B., Qin J., Wong J.;
"N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso.";
Mol. Cell 12:723-734(2003).
[7]
FUNCTION, DNA-BINDING, AND MUTAGENESIS OF CYS-552.
TISSUE=Lung;
DOI=10.1242/dev.01549; PubMed=15548582 [NCBI, ExPASy, EBI, Israel, Japan]
Ruzov A., Dunican D.S., Prokhortchouk A., Pennings S., Stancheva I., Prokhortchouk E., Meehan R.R.;
"Kaiso is a genome-wide repressor of transcription that is essential for amphibian development.";
Development 131:6185-6194(2004).
[8]
TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1074/jbc.M306057200; PubMed=14699141 [NCBI, ExPASy, EBI, Israel, Japan]
Kondapalli J., Flozak A.S., Albuquerque M.L.C.;
"Laminar shear stress differentially modulates gene expression of p120 catenin, Kaiso transcription factor, and vascular endothelial cadherin in human coronary artery endothelial cells.";
J. Biol. Chem. 279:11417-11424(2004).
[9]
INTERACTION WITH KPNA2.
DOI=10.1242/jcs.01541; PubMed=15564377 [NCBI, ExPASy, EBI, Israel, Japan]
Kelly K.F., Otchere A.A., Graham M., Daniel J.M.;
"Nuclear import of the BTB/POZ transcriptional regulator Kaiso.";
J. Cell Sci. 117:6143-6152(2004).
[10]
SUBCELLULAR LOCATION.
DOI=10.1158/0008-5472.CAN-04-2020; PubMed=15781635 [NCBI, ExPASy, EBI, Israel, Japan]
Soubry A., van Hengel J., Parthoens E., Colpaert C., Van Marck E., Waltregny D., Reynolds A.B., van Roy F.;
"Expression and nuclear location of the transcriptional repressor Kaiso is regulated by the tumor microenvironment.";
Cancer Res. 65:2224-2233(2005).
[11]
FUNCTION.
DOI=10.1016/j.yexcr.2005.01.007; PubMed=15817151 [NCBI, ExPASy, EBI, Israel, Japan]
Spring C.M., Kelly K.F., O'Kelly I., Graham M., Crawford H.C., Daniel J.M.;
"The catenin p120ctn inhibits Kaiso-mediated transcriptional repression of the beta-catenin/TCF target gene matrilysin.";
Exp. Cell Res. 305:253-265(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-442, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[13]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-116.
Structural genomics consortium (SGC);
"Crystal structure of human zinc finger and BTB domain containing 33.";
Submitted (DEC-2008) to the PDB data bank.
Comments
  • FUNCTION: Transcriptional regulator with bimodal DNA-binding specificity. Binds to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' and also binds to the non-methylated consensus sequence 5'-CTGCNA-3'. Recruits the N-CoR repressor complex to promote histone deacetylation and the formation of repressive chromatin structures in target gene promoters. May contribute to the repression of target genes of the Wnt signaling pathway. May also activate transcription of a subset of target genes by the recruitment of CTNND2.
  • SUBUNIT: Self-associates. Interacts with CTNND2 (By similarity). Interacts with CTNND1, and this interaction inhibits binding to both methylated and non-methylated DNA. Interacts with NCOR1. Interacts with KPNA2/RCH1, which may mediate nuclear import of this protein.
  • SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Also cytoplasmic in cells grown at high densities.
  • TISSUE SPECIFICITY: Expressed in vascular endothelium.
  • INDUCTION: Induced in vascular endothelium by wounding. This effect is potentiated by prior laminar shear stress, which enhances wound closure.
  • SIMILARITY: Contains 1 BTB (POZ) domain.
  • SIMILARITY: Contains 3 C2H2-type zinc fingers.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL833856; CAD38715.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL833604; CAD91170.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX538016; CAD97963.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX538101; CAD98016.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002086; AAB54087.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC042753; AAH42753.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00465140; -.
RefSeq NP_006768.1; -.
UniGene Hs.143604
3D structure databases
PDB
3FKC; X-ray; 1.70 A; A=1-114.[ExPASy / RCSB / EBI]
PDBsum 3FKC; -.
ModBase Q86T24.
PTM databases
PhosphoSite Q86T24; -.
Organism-specific databases
GeneCards GC0XP119268; -.
H-InvDB HIX0017022; -.
HGNC HGNC:16682; ZBTB33.
GenAtlas ZBTB33.
HPA CAB001980; -.
HPA000755; -.
HPA005732; -.
MIM 300329; gene. [NCBI / EBI]
PharmGKB PA134928604; -.
Gene expression databases
ArrayExpress Q86T24; -.
Bgee Q86T24; -.
CleanEx HS_ZBTB33; -.
GermOnline ENSG00000177485; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005730; Cellular component: nucleolus (inferred from direct assay from HPA).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from HPA).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (traceable author statement from ProtInc).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007242; Biological process: intracellular signaling cascade (traceable author statement from ProtInc).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
GO:0016055; Biological process: Wnt receptor signaling pathway (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000210; BTB/POZ-like.
IPR011333; BTB/POZ_fold.
IPR013069; BTB_POZ.
IPR007087; Znf_C2H2.
IPR015880; Znf_C2H2-like.
Graphical view of domain structure.
Gene3D G3DSA:3.30.710.10; BTB/POZ_fold; 1.
Pfam PF00651; BTB; 1.
PF00096; zf-C2H2; 1.
Pfam graphical view of domain structure.
SMART SM00225; BTB; 1.
SM00355; ZnF_C2H2; 3.
SMART graphical view of domain structure.
PROSITE PS50097; BTB; 1.
PS00028; ZINC_FINGER_C2H2_1; 3.
PS50157; ZINC_FINGER_C2H2_2; 3.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q86T24; -.
Genome annotation databases
Ensembl ENSG00000177485; Homo sapiens. [Contig view]
GeneID 10009; -.
KEGG hsa:10009; -.
Phylogenomic databases
HOGENOM Q86T24; -.
HOVERGEN Q86T24; -.
OMA Q86T24; FIRAEIF.
Other
NextBio 37813; -.
SOURCE ZBTB33; Homo sapiens.
ProtoNet Q86T24.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Repeat; Repressor; Transcription; Transcription regulation; Wnt signaling pathway; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   672  672     Transcriptional regulator Kaiso. PRO_0000046988
DOMAIN   32    94  63     BTB. 
ZN_FING   494   516  23     C2H2-type 1. 
ZN_FING   522   544  23     C2H2-type 2. 
ZN_FING   550   573  24     C2H2-type 3. 
REGION   1   136  136     Self-association (By similarity). 
REGION   1   103  103     Interaction with NCOR1. 
REGION   454   672  219     Interaction with CTNND1 (By similarity). 
REGION   514   638  125     Required for DNA-binding (By similarity). 
MOTIF   471   480  10     Nuclear localization signal (By similarity). 
MOD_RES   442   442        Phosphotyrosine. 
MUTAGEN   552   552        C->R: Abrogates both sequence-specific and methylation-dependent DNA-binding. 
CONFLICT   40    40        D -> Y (in Ref. 1; CAD91170). 
CONFLICT   179   179        E -> G (in Ref. 1; CAD91170). 
CONFLICT   189   189        D -> DD (in Ref. 1; CAD91170/CAD97963 and 3; AAH42753). 
CONFLICT   362   362        S -> Y (in Ref. 1; CAD91170). 
CONFLICT   670   670        E -> V (in Ref. 1; CAD98016). 
Sequence information
Length: 672 AA [This is the length of the unprocessed precursor] Molecular weight: 74484 Da [This is the MW of the unprocessed precursor] CRC64: 76D94B4051056DB5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MESRKLISAT DIQYSGSLLN SLNEQRGHGL FCDVTVIVED RKFRAHKNIL SASSTYFHQL 

        70         80         90        100        110        120 
FSVAGQVVEL SFIRAEIFAE ILNYIYSSKI VRVRSDLLDE LIKSGQLLGV KFIAELGVPL 

       130        140        150        160        170        180 
SQVKSISGTA QDGNTEPLPP DSGDKNLVIQ KSKDEAQDNG ATIMPIITES FSLSAEDYEM 

       190        200        210        220        230        240 
KKIIVTDSDD DDDDVIFCSE ILPTKETLPS NNTVAQVQSN PGPVAISDVA PSASNNSPPL 

       250        260        270        280        290        300 
TNITPTQKLP TPVNQATLSQ TQGSEKLLVS SAPTHLTPNI ILLNQTPLST PPNVSSSLPN 

       310        320        330        340        350        360 
HMPSSINLLV QNQQTPNSAI LTGNKANEEE EEEIIDDDDD TISSSPDSAV SNTSLVPQAD 

       370        380        390        400        410        420 
TSQNTSFDGS LIQKMQIPTL LQEPLSNSLK ISDIITRNTN DPGVGSKHLM EGQKIITLDT 

       430        440        450        460        470        480 
ATEIEGLSTG CKVYANIGED TYDIVIPVKD DPDEGEARLE NEIPKTSGSE MANKRMKVKH 

       490        500        510        520        530        540 
DDHYELIVDG RVYYICIVCK RSYVCLTSLR RHFNIHSWEK KYPCRYCEKV FPLAEYRTKH 

       550        560        570        580        590        600 
EIHHTGERRY QCLACGKSFI NYQFMSSHIK SVHSQDPSGD SKLYRLHPCR SLQIRQYAYL 

       610        620        630        640        650        660 
SDRSSTIPAM KDDGIGYKVD TGKEPPVGTT TSTQNKPMTW EDIFIQQEND SIFKQNVTDG 

       670 
STEFEFIIPE SY 

Q86T24 in FASTA format

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