Zinc finger and BTB domain-containing protein 16

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ZBTB16
Protein ZBTB16 PDB 1buo.png
Available structures
PDB Human UniProt search: PDBe RCSB
Identifiers
Aliases ZBTB16, PLZF, ZNF145, zinc finger and BTB domain containing 16
External IDs MGI: 103222 HomoloGene: 21214 GeneCards: 7704
Genetically Related Diseases
Disease Name References
Conduct disorder
RNA expression pattern
PBB GE ZBTB16 205883 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001018011
NM_006006

NM_001033324

RefSeq (protein)

NP_001018011.1
NP_005997.2

n/a

Location (UCSC) Chr 11: 114.06 – 114.25 Mb Chr 9: 48.65 – 48.84 Mb
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Zinc finger and BTB domain-containing protein 16 is a protein that in humans is encoded by the ZBTB16 gene.

Function[edit]

This gene is a member of the Krueppel C2H2-type zinc-finger protein family and encodes a zinc finger transcription factor that contains nine Kruppel-type zinc finger domains at the carboxyl terminus. This protein is located in the nucleus, is involved in cell cycle progression, and interacts with a histone deacetylase. Specific instances of aberrant gene rearrangement at this locus have been associated with acute promyelocytic leukemia (APL)[4] and physiological roles have been identified in mouse Natural Killer T cells[5][6] and gamma-delta T cells.[7] Alternate transcriptional splice variants have been characterized in human.[8][9]

Interactions[edit]

Zinc finger and BTB domain-containing protein 16 has been shown to interact with:

See also[edit]

References[edit]

  1. ^ "chibi.ubc.ca/Gemma/phenotypes.html?phenotypeUrlId=DOID_12995&geneId=171410". 
  2. ^ "Human PubMed Reference:". 
  3. ^ "Mouse PubMed Reference:". 
  4. ^ Chen Z, Brand NJ, Chen A, Chen SJ, Tong JH, Wang ZY, Waxman S, Zelent A (1993). "Fusion between a novel Krüppel-like zinc finger gene and the retinoic acid receptor-alpha locus due to a variant t(11;17) translocation associated with acute promyelocytic leukaemia". The EMBO Journal. 12 (3): 1161–7. PMC 413318free to read. PMID 8384553. 
  5. ^ Kovalovsky D, Uche OU, Eladad S, Hobbs RM, Yi W, Alonzo E, Chua K, Eidson M, et al. (2008). "The BTB-zinc finger transcriptional regulator, PLZF, controls the development of iNKT cell effector functions". Nature Immunology. 9 (9): 1055–64. doi:10.1038/ni.1641. PMC 2662733free to read. PMID 18660811. 
  6. ^ Savage AK, Constantinides MG, Han J, Picard D, Martin E, Li B, Lantz O, Bendelac A (2008). "The transcription factor PLZF (Zbtb16) directs the effector program of the NKT cell lineage". Immunity. 29 (3): 391–403. doi:10.1016/j.immuni.2008.07.011. PMC 2613001free to read. PMID 18703361. 
  7. ^ Kreslavsky T, Savage AK, Hobbs R, Gounari F, Bronson R, Pereira P, Pandolfi PP, Bendelac A, von Boehmer H (2009). "TCR-inducible PLZF transcription factor required for innate phenotype of a subset of γδ T cells with restricted TCR diversity". Proceedings of the National Academy of Sciences of the United States of America. 106 (30): 12453–8. doi:10.1073/pnas.0903895106. PMC 2718370free to read. PMID 19617548. 
  8. ^ Zhang T, Xiong H, Kan LX, Zhang CK, Jiao XF, Fu G, Zhang QH, Lu L, et al. (1999). "Genomic sequence, structural organization, molecular evolution, and aberrant rearrangement of promyelocytic leukemia zinc finger gene". Proceedings of the National Academy of Sciences of the United States of America. 96 (20): 11422–7. doi:10.1073/pnas.96.20.11422. PMC 18049free to read. PMID 10500192. 
  9. ^ "ZBTB16 zinc finger and BTB domain containing 16". Entrez. 4 October 2009. Retrieved 10 October 2009. 
  10. ^ Senbonmatsu T, Saito T, Landon EJ, Watanabe O, Price E, Roberts RL, Imboden H, Fitzgerald TG, et al. "A novel angiotensin II type 2 receptor signaling pathway: possible role in cardiac hypertrophy". EMBO J. 22 (24): 6471–82. doi:10.1093/emboj/cdg637. PMC 291832free to read. PMID 14657020. 
  11. ^ Dhordain P, Albagli O, Honore N, Guidez F, Lantoine D, Schmid M, The HD, Zelent A, Koken MH. "Colocalization and heteromerization between the two human oncogene POZ/zinc finger proteins, LAZ3 (BCL6) and PLZF". Oncogene. 19 (54): 6240–50. doi:10.1038/sj.onc.1203976. PMID 11175338. 
  12. ^ Barna M, Merghoub T, Costoya JA, Ruggero D, Branford M, Bergia A, Samori B, Pandolfi PP. "Plzf mediates transcriptional repression of HoxD gene expression through chromatin remodeling". Dev. Cell. 3 (4): 499–510. doi:10.1016/s1534-5807(02)00289-7. PMID 12408802. 
  13. ^ a b Ward JO, McConnell MJ, Carlile GW, Pandolfi PP, Licht JD, Freedman LP. "The acute promyelocytic leukemia-associated protein, promyelocytic leukemia zinc finger, regulates 1,25-dihydroxyvitamin D(3)-induced monocytic differentiation of U937 cells through a physical interaction with vitamin D(3) receptor". Blood. 98 (12): 3290–300. doi:10.1182/blood.v98.12.3290. PMID 11719366. 
  14. ^ Puccetti E, Obradovic D, Beissert T, Bianchini A, Washburn B, Chiaradonna F, Boehrer S, Hoelzer D, et al. "AML-associated translocation products block vitamin D(3)-induced differentiation by sequestering the vitamin D(3) receptor". Cancer Res. 62 (23): 7050–8. PMID 12460926. 
  15. ^ McLoughlin P, Ehler E, Carlile G, Licht JD, Schäfer BW. "The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein". J. Biol. Chem. 277 (40): 37045–53. doi:10.1074/jbc.M203336200. PMID 12145280. 
  16. ^ Labbaye C, Quaranta MT, Pagliuca A, Militi S, Licht JD, Testa U, Peschle C. "PLZF induces megakaryocytic development, activates Tpo receptor expression and interacts with GATA1 protein". Oncogene. 21 (43): 6669–79. doi:10.1038/sj.onc.1205884. PMID 12242665. 
  17. ^ Tsuzuki S, Enver T. "Interactions of GATA-2 with the promyelocytic leukemia zinc finger (PLZF) protein, its homologue FAZF, and the t(11;17)-generated PLZF-retinoic acid receptor alpha oncoprotein". Blood. 99 (9): 3404–10. doi:10.1182/blood.v99.9.3404. PMID 11964310. 
  18. ^ a b c d Chauchereau A, Mathieu M, de Saintignon J, Ferreira R, Pritchard LL, Mishal Z, Dejean A, Harel-Bellan A. "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene. 23 (54): 8777–84. doi:10.1038/sj.onc.1208128. PMID 15467736. 
  19. ^ a b c David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A. "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene. 16 (19): 2549–56. doi:10.1038/sj.onc.1202043. PMID 9627120. 
  20. ^ a b c Wong CW, Privalsky ML. "Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6". J. Biol. Chem. 273 (42): 27695–702. doi:10.1074/jbc.273.42.27695. PMID 9765306. 
  21. ^ a b Lemercier C, Brocard MP, Puvion-Dutilleul F, Kao HY, Albagli O, Khochbin S. "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". J. Biol. Chem. 277 (24): 22045–52. doi:10.1074/jbc.M201736200. PMID 11929873. 
  22. ^ Nanba D, Mammoto A, Hashimoto K, Higashiyama S. "Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF". J. Cell Biol. 163 (3): 489–502. doi:10.1083/jcb.200303017. PMC 2173632free to read. PMID 14597771. 
  23. ^ Nanba D, Toki F, Higashiyama S. "Roles of charged amino acid residues in the cytoplasmic domain of proHB-EGF". Biochem. Biophys. Res. Commun. 320 (2): 376–82. doi:10.1016/j.bbrc.2004.05.176. PMID 15219838. 
  24. ^ Takahashi S, McConnell MJ, Harigae H, Kaku M, Sasaki T, Melnick AM, Licht JD. "The Flt3 internal tandem duplication mutant inhibits the function of transcriptional repressors by blocking interactions with SMRT". Blood. 103 (12): 4650–8. doi:10.1182/blood-2003-08-2759. PMID 14982881. 
  25. ^ Hong SH, David G, Wong CW, Dejean A, Privalsky ML. "SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF-RARalpha oncoproteins associated with acute promyelocytic leukemia". Proc. Natl. Acad. Sci. U.S.A. 94 (17): 9028–33. doi:10.1073/pnas.94.17.9028. PMC 23013free to read. PMID 9256429. 
  26. ^ Koken MH, Reid A, Quignon F, Chelbi-Alix MK, Davies JM, Kabarowski JH, Zhu J, Dong S, et al. "Leukemia-associated retinoic acid receptor alpha fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies". Proc. Natl. Acad. Sci. U.S.A. 94 (19): 10255–60. doi:10.1073/pnas.94.19.10255. PMC 23349free to read. PMID 9294197. 
  27. ^ Melnick AM, Westendorf JJ, Polinger A, Carlile GW, Arai S, Ball HJ, Lutterbach B, Hiebert SW, Licht JD. "The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is a corepressor for the promyelocytic leukemia zinc finger protein". Mol. Cell. Biol. 20 (6): 2075–86. doi:10.1128/mcb.20.6.2075-2086.2000. PMC 110824free to read. PMID 10688654. 
  28. ^ Melnick A, Carlile GW, McConnell MJ, Polinger A, Hiebert SW, Licht JD. "AML-1/ETO fusion protein is a dominant negative inhibitor of transcriptional repression by the promyelocytic leukemia zinc finger protein". Blood. 96 (12): 3939–47. PMID 11090081. 
  29. ^ Martin PJ, Delmotte MH, Formstecher P, Lefebvre P. "PLZF is a negative regulator of retinoic acid receptor transcriptional activity". Nucl. Recept. 1 (1): 6. doi:10.1186/1478-1336-1-6. PMC 212040free to read. PMID 14521715. 
  30. ^ Hoatlin ME, Zhi Y, Ball H, Silvey K, Melnick A, Stone S, Arai S, Hawe N, et al. "A novel BTB/POZ transcriptional repressor protein interacts with the Fanconi anemia group C protein and PLZF". Blood. 94 (11): 3737–47. PMID 10572087. 

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.