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Q86T24

- KAISO_HUMAN

UniProt

Q86T24 - KAISO_HUMAN

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Protein

Transcriptional regulator Kaiso

Gene

ZBTB33

Organism
Homo sapiens (Human)
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'. 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. 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
Complete GO annotation...

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
Complete GO annotation...

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. 22 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.
GeneTreeiENSGT00760000119269.
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

        10         20         30         40         50
MESRKLISAT DIQYSGSLLN SLNEQRGHGL FCDVTVIVED RKFRAHKNIL
60 70 80 90 100
SASSTYFHQL FSVAGQVVEL SFIRAEIFAE ILNYIYSSKI VRVRSDLLDE
110 120 130 140 150
LIKSGQLLGV KFIAELGVPL SQVKSISGTA QDGNTEPLPP DSGDKNLVIQ
160 170 180 190 200
KSKDEAQDNG ATIMPIITES FSLSAEDYEM KKIIVTDSDD DDDDVIFCSE
210 220 230 240 250
ILPTKETLPS NNTVAQVQSN PGPVAISDVA PSASNNSPPL TNITPTQKLP
260 270 280 290 300
TPVNQATLSQ TQGSEKLLVS SAPTHLTPNI ILLNQTPLST PPNVSSSLPN
310 320 330 340 350
HMPSSINLLV QNQQTPNSAI LTGNKANEEE EEEIIDDDDD TISSSPDSAV
360 370 380 390 400
SNTSLVPQAD TSQNTSFDGS LIQKMQIPTL LQEPLSNSLK ISDIITRNTN
410 420 430 440 450
DPGVGSKHLM EGQKIITLDT ATEIEGLSTG CKVYANIGED TYDIVIPVKD
460 470 480 490 500
DPDEGEARLE NEIPKTSGSE MANKRMKVKH DDHYELIVDG RVYYICIVCK
510 520 530 540 550
RSYVCLTSLR RHFNIHSWEK KYPCRYCEKV FPLAEYRTKH EIHHTGERRY
560 570 580 590 600
QCLACGKSFI NYQFMSSHIK SVHSQDPSGD SKLYRLHPCR SLQIRQYAYL
610 620 630 640 650
SDRSSTIPAM KDDGIGYKVD TGKEPPVGTT TSTQNKPMTW EDIFIQQEND
660 670
SIFKQNVTDG STEFEFIIPE SY
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. 22 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.
GeneTreei ENSGT00760000119269.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 110 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