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Q86T24

- KAISO_HUMAN

UniProt

Q86T24 - KAISO_HUMAN

Protein

Transcriptional regulator Kaiso

Gene

ZBTB33

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (20 Dec 2005)
      Previous versions | rss
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    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'. 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 CTNND2.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri494 – 51623C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri522 – 54423C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri550 – 57324C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. methyl-CpG binding Source: UniProt
    3. protein binding Source: UniProt
    4. sequence-specific DNA binding Source: UniProt

    GO - Biological processi

    1. intracellular signal transduction Source: ProtInc
    2. negative regulation of transcription, DNA-templated Source: UniProt
    3. transcription, DNA-templated Source: UniProtKB-KW
    4. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Wnt signaling pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ86T24.

    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, ZNF348
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:16682. ZBTB33.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Also cytoplasmic in cells grown at high densities.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleolus Source: HPA
    3. nucleus Source: HPA
    4. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi552 – 5521C → R: Abrogates both sequence-specific and methylation-dependent DNA-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134928604.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 672672Transcriptional regulator KaisoPRO_0000046988Add
    BLAST

    Proteomic databases

    MaxQBiQ86T24.
    PaxDbiQ86T24.
    PRIDEiQ86T24.

    PTM databases

    PhosphoSiteiQ86T24.

    Expressioni

    Tissue specificityi

    Expressed in vascular endothelium.1 Publication

    Inductioni

    Induced in vascular endothelium by wounding. This effect is potentiated by prior laminar shear stress, which enhances wound closure.1 Publication

    Gene expression databases

    BgeeiQ86T24.
    CleanExiHS_ZBTB33.
    GenevestigatoriQ86T24.

    Organism-specific databases

    HPAiCAB001980.
    HPA000755.
    HPA005732.

    Interactioni

    Subunit structurei

    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.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi115327. 13 interactions.
    IntActiQ86T24. 4 interactions.
    STRINGi9606.ENSP00000314153.

    Structurei

    Secondary structure

    1
    672
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 2714
    Turni28 – 314
    Beta strandi34 – 385
    Beta strandi41 – 455
    Helixi47 – 537
    Helixi55 – 606
    Turni61 – 633
    Beta strandi66 – 705
    Helixi75 – 8511
    Helixi95 – 973
    Helixi98 – 10811
    Helixi111 – 1144
    Beta strandi483 – 4886
    Beta strandi491 – 4966
    Turni497 – 4993
    Beta strandi502 – 5054
    Helixi506 – 51712
    Beta strandi525 – 5284
    Beta strandi530 – 5334
    Helixi534 – 54512
    Beta strandi550 – 5523
    Turni553 – 5553
    Beta strandi558 – 5614
    Helixi562 – 57312
    Beta strandi577 – 5815
    Beta strandi584 – 5863
    Helixi598 – 6014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ86T24.
    SMRiQ86T24. Positions 3-117, 481-600.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86T24.

    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-associationBy similarityAdd
    BLAST
    Regioni1 – 103103Interaction with NCOR1Add
    BLAST
    Regioni454 – 672219Interaction with CTNND1By similarityAdd
    BLAST
    Regioni514 – 638125Required for DNA-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi471 – 48010Nuclear localization signalBy similarity

    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 fingeri494 – 51623C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri522 – 54423C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri550 – 57324C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG283964.
    HOGENOMiHOG000230932.
    HOVERGENiHBG079575.
    InParanoidiQ86T24.
    KOiK10507.
    OMAiHSQDPSG.
    OrthoDBiEOG7WX087.
    PhylomeDBiQ86T24.
    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.

    Q86T24-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESRKLISAT DIQYSGSLLN SLNEQRGHGL FCDVTVIVED RKFRAHKNIL    50
    SASSTYFHQL FSVAGQVVEL SFIRAEIFAE ILNYIYSSKI VRVRSDLLDE 100
    LIKSGQLLGV KFIAELGVPL SQVKSISGTA QDGNTEPLPP DSGDKNLVIQ 150
    KSKDEAQDNG ATIMPIITES FSLSAEDYEM KKIIVTDSDD DDDDVIFCSE 200
    ILPTKETLPS NNTVAQVQSN PGPVAISDVA PSASNNSPPL TNITPTQKLP 250
    TPVNQATLSQ TQGSEKLLVS SAPTHLTPNI ILLNQTPLST PPNVSSSLPN 300
    HMPSSINLLV QNQQTPNSAI LTGNKANEEE EEEIIDDDDD TISSSPDSAV 350
    SNTSLVPQAD TSQNTSFDGS LIQKMQIPTL LQEPLSNSLK ISDIITRNTN 400
    DPGVGSKHLM EGQKIITLDT ATEIEGLSTG CKVYANIGED TYDIVIPVKD 450
    DPDEGEARLE NEIPKTSGSE MANKRMKVKH DDHYELIVDG RVYYICIVCK 500
    RSYVCLTSLR RHFNIHSWEK KYPCRYCEKV FPLAEYRTKH EIHHTGERRY 550
    QCLACGKSFI NYQFMSSHIK SVHSQDPSGD SKLYRLHPCR SLQIRQYAYL 600
    SDRSSTIPAM KDDGIGYKVD TGKEPPVGTT TSTQNKPMTW EDIFIQQEND 650
    SIFKQNVTDG STEFEFIIPE SY 672
    Length:672
    Mass (Da):74,484
    Last modified:December 20, 2005 - v2
    Checksum:i76D94B4051056DB5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401D → Y in CAD91170. (PubMed:17974005)Curated
    Sequence conflicti179 – 1791E → G in CAD91170. (PubMed:17974005)Curated
    Sequence conflicti189 – 1891D → DD in CAD91170. (PubMed:17974005)Curated
    Sequence conflicti189 – 1891D → DD in CAD97963. (PubMed:17974005)Curated
    Sequence conflicti189 – 1891D → DD in AAH42753. (PubMed:15489334)Curated
    Sequence conflicti362 – 3621S → Y in CAD91170. (PubMed:17974005)Curated
    Sequence conflicti670 – 6701E → V in CAD98016. (PubMed:17974005)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14596.1.
    RefSeqiNP_001171671.1. NM_001184742.1.
    NP_006768.1. NM_006777.3.
    UniGeneiHs.143604.

    Genome annotation databases

    EnsembliENST00000326624; ENSP00000314153; ENSG00000177485.
    ENST00000557385; ENSP00000450969; ENSG00000177485.
    GeneIDi10009.
    KEGGihsa:10009.
    UCSCiuc004esn.1. human.

    Polymorphism databases

    DMDMi84029319.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14596.1.
    RefSeqi NP_001171671.1. NM_001184742.1.
    NP_006768.1. NM_006777.3.
    UniGenei Hs.143604.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LT7 NMR - A 472-604 [» ]
    3FKC X-ray 1.70 A 1-114 [» ]
    3M4T X-ray 2.05 A 1-122 [» ]
    3M8V X-ray 2.70 A 1-122 [» ]
    4F6M X-ray 2.40 A 472-604 [» ]
    4F6N X-ray 2.80 A 472-604 [» ]
    ProteinModelPortali Q86T24.
    SMRi Q86T24. Positions 3-117, 481-600.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115327. 13 interactions.
    IntActi Q86T24. 4 interactions.
    STRINGi 9606.ENSP00000314153.

    PTM databases

    PhosphoSitei Q86T24.

    Polymorphism databases

    DMDMi 84029319.

    Proteomic databases

    MaxQBi Q86T24.
    PaxDbi Q86T24.
    PRIDEi Q86T24.

    Protocols and materials databases

    DNASUi 10009.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326624 ; ENSP00000314153 ; ENSG00000177485 .
    ENST00000557385 ; ENSP00000450969 ; ENSG00000177485 .
    GeneIDi 10009.
    KEGGi hsa:10009.
    UCSCi uc004esn.1. human.

    Organism-specific databases

    CTDi 10009.
    GeneCardsi GC0XP119384.
    H-InvDB HIX0017022.
    HGNCi HGNC:16682. ZBTB33.
    HPAi CAB001980.
    HPA000755.
    HPA005732.
    MIMi 300329. gene.
    neXtProti NX_Q86T24.
    PharmGKBi PA134928604.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283964.
    HOGENOMi HOG000230932.
    HOVERGENi HBG079575.
    InParanoidi Q86T24.
    KOi K10507.
    OMAi HSQDPSG.
    OrthoDBi EOG7WX087.
    PhylomeDBi Q86T24.
    TreeFami TF333100.

    Enzyme and pathway databases

    SignaLinki Q86T24.

    Miscellaneous databases

    EvolutionaryTracei Q86T24.
    GeneWikii ZBTB33.
    GenomeRNAii 10009.
    NextBioi 37813.
    PROi Q86T24.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q86T24.
    CleanExi HS_ZBTB33.
    Genevestigatori Q86T24.

    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

    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.
      , 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. 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.
      , 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. 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.

    Entry informationi

    Entry nameiKAISO_HUMAN
    AccessioniPrimary (citable) accession number: Q86T24
    Secondary accession number(s): B2R5U6
    , O00319, Q7Z361, Q8IVP6, Q8N3P0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3