ZBTB17

Zinc finger and BTB domain containing 17
Rendering based on PDB 2Q81.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2LVR, 2LVT, 2LVU, 2M0D, 2M0E, 2M0F, 2Q81, 3M52
Identifiers
Symbols	ZBTB17; MIZ-1; ZNF151; ZNF60; pHZ-67
External IDs	OMIM: 604084 MGI: 107410 HomoloGene: 2575 GeneCards: ZBTB17 Gene
Gene Ontology Molecular function • DNA binding • sequence-specific DNA binding transcription factor activity • protein binding • zinc ion binding • metal ion binding Cellular component • nucleoplasm Biological process • gastrulation with mouth forming second • transcription, DNA-dependent • activation of signaling protein activity involved in unfolded protein response • ectoderm development • endoplasmic reticulum unfolded protein response • negative regulation of cell cycle • positive regulation of transcription, DNA-dependent Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7709	22642
Ensembl	ENSG00000116809	ENSMUSG00000006215
UniProt	Q13105	Q60821
RefSeq (mRNA)	NM_001242884	NM_009541
RefSeq (protein)	NP_001229813	NP_033567
Location (UCSC)	Chr 1: 16.27 – 16.3 Mb	Chr 4: 141.44 – 141.47 Mb
PubMed search	[1]	[2]

Zinc finger and BTB domain-containing protein 17 is a protein that in humans is encoded by the ZBTB17 gene.

Interactions

ZBTB17 has been shown to interact with TOPBP1, Host cell factor C1 and Myc.

Further reading

• Lichter P, Bray P, Ried T, et al. (1992). "Clustering of C2-H2 zinc finger motif sequences within telomeric and fragile site regions of human chromosomes.". Genomics 13 (4): 999–1007. doi:10.1016/0888-7543(92)90013-I. PMID 1505991. 
• Bray P, Lichter P, Thiesen HJ, et al. (1991). "Characterization and mapping of human genes encoding zinc finger proteins.". Proc. Natl. Acad. Sci. U.S.A. 88 (21): 9563–7. doi:10.1073/pnas.88.21.9563. PMC 52758. PMID 1946370. 
• Tommerup N, Vissing H (1995). "Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs identify putative candidate genes for developmental and malignant disorders.". Genomics 27 (2): 259–64. doi:10.1006/geno.1995.1040. PMID 7557990. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Wu L, Wu H, Ma L, et al. (1997). "Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA.". Mech. Dev. 65 (1–2): 3–17. doi:10.1016/S0925-4773(97)00032-4. PMID 9256341. 
• Schneider A, Peukert K, Eilers M, Hänel F (1997). "Association of Myc with the zinc-finger protein Miz-1 defines a novel pathway for gene regulation by Myc.". Curr. Top. Microbiol. Immunol. 224: 137–46. PMID 9308237. 
• Peukert K, Staller P, Schneider A, et al. (1997). "An alternative pathway for gene regulation by Myc.". EMBO J. 16 (18): 5672–86. doi:10.1093/emboj/16.18.5672. PMC 1170199. PMID 9312026. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Sui D, Wilson JE (2000). "Interaction of insulin-like growth factor binding protein-4, Miz-1, leptin, lipocalin-type prostaglandin D synthase, and granulin precursor with the N-terminal half of type III hexokinase.". Arch. Biochem. Biophys. 382 (2): 262–74. doi:10.1006/abbi.2000.2019. PMID 11068878. 
• Staller P, Peukert K, Kiermaier A, et al. (2001). "Repression of p15INK4b expression by Myc through association with Miz-1.". Nat. Cell Biol. 3 (4): 392–9. doi:10.1038/35070076. PMID 11283613. 
• Ziegelbauer J, Shan B, Yager D, et al. (2001). "Transcription factor MIZ-1 is regulated via microtubule association.". Mol. Cell 8 (2): 339–49. doi:10.1016/S1097-2765(01)00313-6. PMID 11545736. 
• Tussie-Luna MI, Michel B, Hakre S, Roy AL (2003). "The SUMO ubiquitin-protein isopeptide ligase family member Miz1/PIASxbeta /Siz2 is a transcriptional cofactor for TFII-I.". J. Biol. Chem. 277 (45): 43185–93. doi:10.1074/jbc.M207635200. PMID 12193603. 
• Piluso D, Bilan P, Capone JP (2003). "Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1.". J. Biol. Chem. 277 (48): 46799–808. doi:10.1074/jbc.M206226200. PMID 12244100. 
• Zhang H, Li Z, Viklund EK, Strömblad S (2002). "P21-activated kinase 4 interacts with integrin alpha v beta 5 and regulates alpha v beta 5-mediated cell migration.". J. Cell Biol. 158 (7): 1287–97. doi:10.1083/jcb.200207008. PMC 2173231. PMID 12356872. 
• Herold S, Wanzel M, Beuger V, et al. (2002). "Negative regulation of the mammalian UV response by Myc through association with Miz-1.". Mol. Cell 10 (3): 509–21. doi:10.1016/S1097-2765(02)00633-0. PMID 12408820. 
• Wu S, Cetinkaya C, Munoz-Alonso MJ, et al. (2003). "Myc represses differentiation-induced p21CIP1 expression via Miz-1-dependent interaction with the p21 core promoter.". Oncogene 22 (3): 351–60. doi:10.1038/sj.onc.1206145. PMID 12545156. 
• Bowen H, Lapham A, Phillips E, et al. (2003). "Characterization of the murine Nramp1 promoter: requirements for transactivation by Miz-1.". J. Biol. Chem. 278 (38): 36017–26. doi:10.1074/jbc.M304301200. PMID 12840021. 
• Sakurai T, Itoh K, Higashitsuji H, et al. (2004). "A cleaved form of MAGE-A4 binds to Miz-1 and induces apoptosis in human cells.". J. Biol. Chem. 279 (15): 15505–14. doi:10.1074/jbc.M310437200. PMID 14739298. 
• Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. 

External links

• ZBTB17 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

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