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Q86T24 (KAISO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional regulator Kaiso
Alternative name(s):
Zinc finger and BTB domain-containing protein 33
Gene names
Name:ZBTB33
Synonyms:KAISO, ZNF348
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length672 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.7 Ref.8 Ref.9 Ref.13

Subunit structure

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. Ref.6 Ref.8 Ref.11

Subcellular location

Nucleus. Cytoplasm. Note: Also cytoplasmic in cells grown at high densities. Ref.12

Tissue specificity

Expressed in vascular endothelium. Ref.10

Induction

Induced in vascular endothelium by wounding. This effect is potentiated by prior laminar shear stress, which enhances wound closure. Ref.10

Sequence similarities

Contains 1 BTB (POZ) domain.

Contains 3 C2H2-type zinc fingers.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 672672Transcriptional regulator Kaiso
PRO_0000046988

Regions

Domain32 – 9463BTB
Zinc finger494 – 51623C2H2-type 1
Zinc finger522 – 54423C2H2-type 2
Zinc finger550 – 57324C2H2-type 3
Region1 – 136136Self-association By similarity
Region1 – 103103Interaction with NCOR1
Region454 – 672219Interaction with CTNND1 By similarity
Region514 – 638125Required for DNA-binding By similarity
Motif471 – 48010Nuclear localization signal By similarity

Experimental info

Mutagenesis5521C → R: Abrogates both sequence-specific and methylation-dependent DNA-binding. Ref.9
Sequence conflict401D → Y in CAD91170. Ref.2
Sequence conflict1791E → G in CAD91170. Ref.2
Sequence conflict1891D → DD in CAD91170. Ref.2
Sequence conflict1891D → DD in CAD97963. Ref.2
Sequence conflict1891D → DD in AAH42753. Ref.5
Sequence conflict3621S → Y in CAD91170. Ref.2
Sequence conflict6701E → V in CAD98016. Ref.2

Secondary structure

............................................... 672
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q86T24 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 76D94B4051056DB5

FASTA67274,484
        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 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala, Endometrial tumor and Fetal kidney.
[3]"The DNA sequence of the human X chromosome."
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. expand/collapse author list , 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.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[6]"The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor."
Daniel J.M., Reynolds A.B.
Mol. Cell. Biol. 19:3614-3623(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNND1.
[7]"The p120 catenin partner Kaiso is a DNA methylation-dependent transcriptional repressor."
Prokhortchouk A., Hendrich B., Joergensen H., Ruzov A., Wilm M., Georgiev G., Bird A., Prokhortchouk E.
Genes Dev. 15:1613-1618(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso."
Yoon H.-G., Chan D.W., Reynolds A.B., Qin J., Wong J.
Mol. Cell 12:723-734(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH NCOR1, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Kaiso is a genome-wide repressor of transcription that is essential for amphibian development."
Ruzov A., Dunican D.S., Prokhortchouk A., Pennings S., Stancheva I., Prokhortchouk E., Meehan R.R.
Development 131:6185-6194(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, MUTAGENESIS OF CYS-552.
Tissue: Lung.
[10]"Laminar shear stress differentially modulates gene expression of p120 catenin, Kaiso transcription factor, and vascular endothelial cadherin in human coronary artery endothelial cells."
Kondapalli J., Flozak A.S., Albuquerque M.L.C.
J. Biol. Chem. 279:11417-11424(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[11]"Nuclear import of the BTB/POZ transcriptional regulator Kaiso."
Kelly K.F., Otchere A.A., Graham M., Daniel J.M.
J. Cell Sci. 117:6143-6152(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KPNA2.
[12]"Expression and nuclear location of the transcriptional repressor Kaiso is regulated by the tumor microenvironment."
Soubry A., van Hengel J., Parthoens E., Colpaert C., Van Marck E., Waltregny D., Reynolds A.B., van Roy F.
Cancer Res. 65:2224-2233(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"The catenin p120ctn inhibits Kaiso-mediated transcriptional repression of the beta-catenin/TCF target gene matrilysin."
Spring C.M., Kelly K.F., O'Kelly I., Graham M., Crawford H.C., Daniel J.M.
Exp. Cell Res. 305:253-265(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Crystal structure of human zinc finger and BTB domain containing 33."
Structural genomics consortium (SGC)
Submitted (DEC-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-116.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK312321 mRNA. Translation: BAG35243.1.
AL833856 mRNA. Translation: CAD38715.1.
AL833604 mRNA. Translation: CAD91170.1.
BX538016 mRNA. Translation: CAD97963.1.
BX538101 mRNA. Translation: CAD98016.1.
AC002086 Genomic DNA. Translation: AAB54087.1.
CH471107 Genomic DNA. Translation: EAX11891.1.
BC042753 mRNA. Translation: AAH42753.1.
CCDSCCDS14596.1.
RefSeqNP_001171671.1. NM_001184742.1.
NP_006768.1. NM_006777.3.
UniGeneHs.143604.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LT7NMR-A472-604[»]
3FKCX-ray1.70A1-114[»]
3M4TX-ray2.05A1-122[»]
3M8VX-ray2.70A1-122[»]
4F6MX-ray2.40A472-604[»]
4F6NX-ray2.80A472-604[»]
ProteinModelPortalQ86T24.
SMRQ86T24. Positions 3-117, 481-600.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115327. 13 interactions.
IntActQ86T24. 4 interactions.
STRING9606.ENSP00000314153.

PTM databases

PhosphoSiteQ86T24.

Polymorphism databases

DMDM84029319.

Proteomic databases

MaxQBQ86T24.
PaxDbQ86T24.
PRIDEQ86T24.

Protocols and materials databases

DNASU10009.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326624; ENSP00000314153; ENSG00000177485.
ENST00000557385; ENSP00000450969; ENSG00000177485.
ENST00000599507; ENSP00000471279; ENSG00000269603.
ENST00000602186; ENSP00000470483; ENSG00000269603.
GeneID10009.
KEGGhsa:10009.
UCSCuc004esn.1. human.

Organism-specific databases

CTD10009.
GeneCardsGC0XP119384.
H-InvDBHIX0017022.
HGNCHGNC:16682. ZBTB33.
HPACAB001980.
HPA000755.
HPA005732.
MIM300329. gene.
neXtProtNX_Q86T24.
PharmGKBPA134928604.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283964.
HOGENOMHOG000230932.
HOVERGENHBG079575.
InParanoidQ86T24.
KOK10507.
OMAHSQDPSG.
OrthoDBEOG7WX087.
PhylomeDBQ86T24.
TreeFamTF333100.

Enzyme and pathway databases

SignaLinkQ86T24.

Gene expression databases

BgeeQ86T24.
CleanExHS_ZBTB33.
GenevestigatorQ86T24.

Family and domain databases

Gene3D3.30.160.60. 3 hits.
3.30.710.10. 1 hit.
InterProIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00651. BTB. 1 hit.
[Graphical view]
SMARTSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ86T24.
GeneWikiZBTB33.
GenomeRNAi10009.
NextBio37813.
PROQ86T24.
SOURCESearch...

Entry information

Entry nameKAISO_HUMAN
AccessionPrimary (citable) accession number: Q86T24
Secondary accession number(s): B2R5U6 expand/collapse secondary AC list , O00319, Q7Z361, Q8IVP6, Q8N3P0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: July 9, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM