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Q8BN78

- KAISO_MOUSE

UniProt

Q8BN78 - KAISO_MOUSE

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Protein

Transcriptional regulator Kaiso

Gene

Zbtb33

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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'. May recruit the N-CoR repressor complex to promote histone deacetylation and the formation of repressive chromatin structures in target gene promoters. Contributes 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 CTNND2.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri492 – 51423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri520 – 54223C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri548 – 57124C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. methyl-CpG binding Source: Ensembl

GO - Biological processi

  1. negative regulation of transcription, DNA-templated Source: Ensembl
  2. transcription, DNA-templated Source: MGI
  3. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulator Kaiso
Alternative name(s):
Zinc finger and BTB domain-containing protein 33
Gene namesi
Name:Zbtb33
Synonyms:Kaiso
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1927290. Zbtb33.

Subcellular locationi

Nucleus 3 Publications

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. nucleolus Source: Ensembl
  3. nucleus Source: MGI
  4. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi472 – 4721K → A: Abrogates nuclear localization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 671671Transcriptional regulator KaisoPRO_0000046989Add
BLAST

Proteomic databases

MaxQBiQ8BN78.
PRIDEiQ8BN78.

PTM databases

PhosphoSiteiQ8BN78.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, liver, lung, neuromuscular junctions, skeletal muscle, spleen and testis.2 Publications

Gene expression databases

BgeeiQ8BN78.
CleanExiMM_ZBTB33.
ExpressionAtlasiQ8BN78. baseline and differential.
GenevestigatoriQ8BN78.

Interactioni

Subunit structurei

Interacts with NCOR1 (By similarity). Self-associates. Interacts with CTNND1, and this interaction inhibits binding to both methylated and non-methylated DNA. Interacts with CTNND2. Interacts with KPNA2/RCH1, which may mediate nuclear import of this protein.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ctnnd1P309993EBI-1216314,EBI-529924

Protein-protein interaction databases

BioGridi208181. 6 interactions.
IntActiQ8BN78. 2 interactions.
MINTiMINT-89891.

Structurei

3D structure databases

ProteinModelPortaliQ8BN78.
SMRiQ8BN78. Positions 3-117, 479-598.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 9463BTBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 136136Self-associationAdd
BLAST
Regioni1 – 103103Interaction with NCOR1By similarityAdd
BLAST
Regioni452 – 671220Interaction with CTNND1Add
BLAST
Regioni512 – 637126Required for DNA-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi469 – 47810Nuclear localization signal1 Publication

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri492 – 51423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri520 – 54223C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri548 – 57124C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000119269.
HOGENOMiHOG000230932.
HOVERGENiHBG079575.
InParanoidiQ8BN78.
KOiK10507.
OMAiHSQDPSG.
OrthoDBiEOG7WX087.
PhylomeDBiQ8BN78.
TreeFamiTF333100.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
3.30.710.10. 1 hit.
InterProiIPR000210. 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]
PfamiPF00651. BTB. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BN78-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESRKLISAT DIQYSASLLN SLNEQRGHGL FCDVTVIVED RKFRAHRNIL
60 70 80 90 100
SASSTYFHQL FSVAGQVVEL SFIRAEIFAE ILNYIYSSKV VRVRADLLDE
110 120 130 140 150
LIKSGQLLGV KFIAELGVPL SQVKSISGTE QDGTAETLPS SSSDKSLDME
160 170 180 190 200
KSKDEAQDNG ATVMPIITES FSLSAEDNEM KKIIVTDSDD DDDDDVIFCS
210 220 230 240 250
EILPAKEDLP SNNTATQVQP NPASVAISEV TPCASNNSPP VTNITPTQLP
260 270 280 290 300
TPVNQATLSQ TQGSEELLVS SASTHLTPNI ILLNQAPLTA PPSASSSLPN
310 320 330 340 350
HMSSSVNVLV QNQQTPNSAV LTGNKAEEEE EIIDDDDDII SSSPDSAVSN
360 370 380 390 400
TSLVPQADNS KSTTLDGSLT QKMQIPVLPQ EPPSNSLKIS DVITRNTNDP
410 420 430 440 450
GLRSKHVMEG QKIITLDTAT EIEGLSTGCK VYANIGEDTY DIVIPVKDDP
460 470 480 490 500
DGGEAKLDNE LPKTSGSEPP NKRMKVKHDD HYELIVDGRV YYICIVCKRS
510 520 530 540 550
YVCLTSLRRH FNIHSWEKKY QCRYCDKVFP LAEYRTKHEI HHTGERRYQC
560 570 580 590 600
LTCGKSFINY QFMSSHIKSV HSQDPSGDSK LYRLHPCKSL QIRQYAYLSN
610 620 630 640 650
KSSAMPVMKD DAVGYKVDAG KEPPVGTTST PPQNKSTFWE DIFIQQENDS
660 670
IFKQNVTDGS TEFEFIIPES Y
Length:671
Mass (Da):74,050
Last modified:March 1, 2003 - v1
Checksum:iCFD23E0C15B491D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti441 – 4411D → N in AAD20989. (PubMed:10207085)Curated
Sequence conflicti451 – 4511D → H in AAD20989. (PubMed:10207085)Curated
Sequence conflicti640 – 6401E → K in AAD20989. (PubMed:10207085)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF097416 mRNA. Translation: AAD20989.1.
AK087417 mRNA. Translation: BAC39866.1.
AK089423 mRNA. Translation: BAC40875.1.
CCDSiCCDS30088.1.
RefSeqiNP_001072981.1. NM_001079513.1.
NP_064652.2. NM_020256.2.
UniGeneiMm.391248.

Genome annotation databases

EnsembliENSMUST00000049740; ENSMUSP00000049983; ENSMUSG00000048047.
ENSMUST00000115142; ENSMUSP00000110795; ENSMUSG00000048047.
GeneIDi56805.
KEGGimmu:56805.
UCSCiuc009szp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF097416 mRNA. Translation: AAD20989.1 .
AK087417 mRNA. Translation: BAC39866.1 .
AK089423 mRNA. Translation: BAC40875.1 .
CCDSi CCDS30088.1.
RefSeqi NP_001072981.1. NM_001079513.1.
NP_064652.2. NM_020256.2.
UniGenei Mm.391248.

3D structure databases

ProteinModelPortali Q8BN78.
SMRi Q8BN78. Positions 3-117, 479-598.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208181. 6 interactions.
IntActi Q8BN78. 2 interactions.
MINTi MINT-89891.

PTM databases

PhosphoSitei Q8BN78.

Proteomic databases

MaxQBi Q8BN78.
PRIDEi Q8BN78.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049740 ; ENSMUSP00000049983 ; ENSMUSG00000048047 .
ENSMUST00000115142 ; ENSMUSP00000110795 ; ENSMUSG00000048047 .
GeneIDi 56805.
KEGGi mmu:56805.
UCSCi uc009szp.1. mouse.

Organism-specific databases

CTDi 10009.
MGIi MGI:1927290. Zbtb33.

Phylogenomic databases

eggNOGi COG5048.
GeneTreei ENSGT00760000119269.
HOGENOMi HOG000230932.
HOVERGENi HBG079575.
InParanoidi Q8BN78.
KOi K10507.
OMAi HSQDPSG.
OrthoDBi EOG7WX087.
PhylomeDBi Q8BN78.
TreeFami TF333100.

Miscellaneous databases

ChiTaRSi ZBTB33. mouse.
NextBioi 313351.
PROi Q8BN78.
SOURCEi Search...

Gene expression databases

Bgeei Q8BN78.
CleanExi MM_ZBTB33.
ExpressionAtlasi Q8BN78. baseline and differential.
Genevestigatori Q8BN78.

Family and domain databases

Gene3Di 3.30.160.60. 3 hits.
3.30.710.10. 1 hit.
InterProi IPR000210. 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 ]
Pfami PF00651. BTB. 1 hit.
[Graphical view ]
SMARTi SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
[Graphical view ]
SUPFAMi SSF54695. SSF54695. 1 hit.
PROSITEi PS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], SELF-ASSOCIATION, INTERACTION WITH CTNND1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye.
  3. "The p120(ctn)-binding partner Kaiso is a bi-modal DNA-binding protein that recognizes both a sequence-specific consensus and methylated CpG dinucleotides."
    Daniel J.M., Spring C.M., Crawford H.C., Reynolds A.B., Baig A.
    Nucleic Acids Res. 30:2911-2919(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, INTERACTION WITH CTNND1.
  4. "NLS-dependent nuclear localization of p120ctn is necessary to relieve Kaiso-mediated transcriptional repression."
    Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.
    J. Cell Sci. 117:2675-2686(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Erratum
    Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.
    J. Cell Sci. 117:3405-3405(2004)
  6. "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: FUNCTION, INTERACTION WITH KPNA2, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF LYS-472.
  7. "Regulation of the rapsyn promoter by kaiso and delta-catenin."
    Rodova M., Kelly K.F., VanSaun M., Daniel J.M., Werle M.J.
    Mol. Cell. Biol. 24:7188-7196(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH CTNND2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "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.
  9. "The tissue-specific methylation of the human tyrosine hydroxylase gene reveals new regulatory elements in the first exon."
    Aranyi T., Faucheux B.A., Khalfallah O., Vodjdani G., Biguet N.F., Mallet J., Meloni R.
    J. Neurochem. 94:129-139(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.

Entry informationi

Entry nameiKAISO_MOUSE
AccessioniPrimary (citable) accession number: Q8BN78
Secondary accession number(s): Q8C226, Q9WTZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
Last modified: October 29, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3