Reviewed, UniProtKB/Swiss-Prot Q86T24 (KAISO_HUMAN)

Names and origin

Protein names

Recommended name:
    Transcriptional regulator Kaiso
Alternative name(s):
    Zinc finger and BTB domain-containing protein 33

Gene names

Name:	ZBTB33
Synonyms:	KAISO, ZNF348

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	672 AA.
Sequence status	Complete.
Protein existence	Evidence 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.8 Ref.6 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Wnt signaling pathway
Cellular component	Cytoplasm Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Ref.6 Traceable author statement. Source: ProtInc regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.6 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 672

672

Transcriptional regulator Kaiso

PRO_0000046988

Regions

Domain

32 – 94

63

BTB

Zinc finger

494 – 516

23

C2H2-type 1

Zinc finger

522 – 544

23

C2H2-type 2

Zinc finger

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

Amino acid modifications

Modified residue

237

1

Phosphoserine Ref.15

Modified residue

442

1

Phosphotyrosine Ref.14

Experimental info

Mutagenesis

552

1

C → R: Abrogates both sequence-specific and methylation-dependent DNA-binding. Ref.9

Sequence conflict

40

1

D → Y in CAD91170. Ref.2

Sequence conflict

179

1

E → G in CAD91170. Ref.2

Sequence conflict

189

1

D → DD in CAD91170. Ref.2

Sequence conflict

189

1

D → DD in CAD97963. Ref.2

Sequence conflict

189

1

D → DD in AAH42753. Ref.5

Sequence conflict

362

1

S → Y in CAD91170. Ref.2

Sequence conflict

670

1

E → V in CAD98016. Ref.2

Secondary structure

1

.

.

.

.

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.

.

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.

.

.

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.

.

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.

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672

Helix Strand Turn

Details...

Helix

18 – 25

8

Beta strand

34 – 38

5

Beta strand

41 – 45

5

Helix

47 – 53

7

Helix

55 – 60

6

Beta strand

67 – 70

4

Beta strand

72 – 74

3

Helix

75 – 85

11

Helix

95 – 97

3

Helix

98 – 103

6

Helix

111 – 114

4

Sequences

	Sequence		Length	Mass (Da)
	Q86T24-1 [UniParc]. Last modified December 20, 2005. Version 2. Checksum: 76D94B4051056DB5	FASTA	672	74,484
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 14702039] [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: 17974005] [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. , 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: 15772651] [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. , 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: 15489334] [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: 10207085] [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: 11445535] [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: 14527417] [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: 15548582] [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: 14699141] [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: 15564377] [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: 15781635] [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: 15817151] [Abstract] Cited for: FUNCTION.
[14]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." 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. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-442, MASS SPECTROMETRY.
[15]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, MASS SPECTROMETRY.
[16]	"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.

IPI

IPI00465140.

RefSeq

NP_006768.1.

UniGene

Hs.143604

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FKC	X-ray	1.70	A	1-114	[»]

SMR

Q86T24. Positions 13-116, 492-573.

ModBase

Search...

Protein-protein interaction databases

STRING

Q86T24.

PTM databases

PhosphoSite

Q86T24.

Proteomic databases

PRIDE

Q86T24.

Genome annotation databases

Ensembl

ENST00000326624; ENSP00000314153; ENSG00000177485; Homo sapiens. [Genome view]

GeneID

10009.

KEGG

hsa:10009.

UCSC

uc004esn.1. human.

Organism-specific databases

CTD

10009.

GeneCards

GC0XP119268.

H-InvDB

HIX0017022.

HGNC

HGNC:16682. ZBTB33.

HPA

CAB001980.
HPA000755.
HPA005732.

MIM

300329. gene.

PharmGKB

PA134928604.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10872.

HOGENOM

HBG714782.

HOVERGEN

Q86T24.

InParanoid

Q86T24.

OMA

LSFIRAE.

OrthoDB

EOG9577RX.

PhylomeDB

Q86T24.

Gene expression databases

ArrayExpress

Q86T24.

Bgee

Q86T24.

CleanEx

HS_ZBTB33.

Genevestigator

Q86T24.

GermOnline

ENSG00000177485. Homo sapiens.

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]

Gene3D

G3DSA:3.30.710.10. BTB/POZ_fold. 1 hit.

Pfam

PF00651. BTB. 1 hit.
[Graphical view]

SMART

SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
[Graphical view]

PROSITE

PS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

37813.

SOURCE

Search...

Entry information

Entry name

KAISO_HUMAN

Accession

Primary (citable) accession number: Q86T24
Secondary accession number(s): B2R5U6 , O00319, Q7Z361, Q8IVP6, Q8N3P0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	January 19, 2010
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.