ZBTB17

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

ZBTB17
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2LVR, 2LVT, 2LVU, 2M0D, 2M0E, 2M0F, 2N25, 2N26, 2Q81, 3M52, 4U2M, 4U2N, 5ION
Identifiers
Aliases	ZBTB17, MIZ-1, ZNF151, ZNF60, pHZ-67, zinc finger and BTB domain containing 17
External IDs	OMIM: 604084; MGI: 107410; HomoloGene: 2575; GeneCards: ZBTB17; OMA:ZBTB17 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p36.13 Start 15,941,869 bp End 15,976,132 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4|4 D3 Start 141,171,965 bp End 141,195,241 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve tendon of biceps brachii granulocyte apex of heart right lobe of thyroid gland ganglionic eminence left lobe of thyroid gland upper lobe of left lung spleen ectocervix Top expressed in saccule otic placode otic vesicle ventricular zone plantaris muscle extensor digitorum longus muscle muscle of thigh interventricular septum soleus muscle granulocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA-binding transcription factor activity DNA binding protein binding metal ion binding nucleic acid binding RNA polymerase II cis-regulatory region sequence-specific DNA binding DNA-binding transcription activator activity, RNA polymerase II-specific transcription coactivator binding transcription factor binding DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component nucleus nucleoplasm protein-DNA complex protein-containing complex Biological process positive regulation of transcription, DNA-templated multicellular organism development gastrulation with mouth forming second ectoderm development IRE1-mediated unfolded protein response negative regulation of cell cycle regulation of transcription, DNA-templated transcription, DNA-templated transcription by RNA polymerase II negative regulation of cell population proliferation positive regulation of transcription by RNA polymerase II Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7709 22642 Ensembl ENSG00000116809 ENSMUSG00000006215 UniProt Q13105 Q60821 RefSeq (mRNA) NM_001242884 NM_001287603 NM_001287604 NM_003443 NM_001324137 NM_001324138 NM_009541 NM_001378826 NM_001378827 NM_001378828 RefSeq (protein) NP_001229813 NP_001274532 NP_001274533 NP_001311066 NP_001311067 NP_003434 NP_033567 NP_001365755 NP_001365756 NP_001365757 Location (UCSC) Chr 1: 15.94 – 15.98 Mb Chr 4: 141.17 – 141.2 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Interactions

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

Further reading

• Lichter P, Bray P, Ried T, Dawid IB, Ward DC (Aug 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, Ward DC, Dawid IB (Nov 1991). "Characterization and mapping of human genes encoding zinc finger proteins". Proceedings of the National Academy of Sciences of the United States of America. 88 (21): 9563–7. Bibcode:1991PNAS...88.9563B. doi:10.1073/pnas.88.21.9563. PMC 52758. PMID 1946370.
• Tommerup N, Vissing H (May 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 (Jan 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, Sangiorgi F, Wu N, Bell JR, Lyons GE, Maxson R (Jul 1997). "Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA". Mechanisms of Development. 65 (1–2): 3–17. doi:10.1016/S0925-4773(97)00032-4. PMID 9256341. S2CID 11835268.
• 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". C-Myc in B-Cell Neoplasia. Current Topics in Microbiology and Immunology. Vol. 224. pp. 137–46. doi:10.1007/978-3-642-60801-8_14. ISBN 978-3-642-64560-0. PMID 9308237.
• Peukert K, Staller P, Schneider A, Carmichael G, Hänel F, Eilers M (Sep 1997). "An alternative pathway for gene regulation by Myc". The EMBO Journal. 16 (18): 5672–86. doi:10.1093/emboj/16.18.5672. PMC 1170199. PMID 9312026.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 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 (Oct 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". Archives of Biochemistry and Biophysics. 382 (2): 262–74. doi:10.1006/abbi.2000.2019. PMID 11068878.
• Staller P, Peukert K, Kiermaier A, Seoane J, Lukas J, Karsunky H, Möröy T, Bartek J, Massagué J, Hänel F, Eilers M (Apr 2001). "Repression of p15INK4b expression by Myc through association with Miz-1". Nature Cell Biology. 3 (4): 392–9. doi:10.1038/35070076. PMID 11283613. S2CID 12696178.
• Ziegelbauer J, Shan B, Yager D, Larabell C, Hoffmann B, Tjian R (Aug 2001). "Transcription factor MIZ-1 is regulated via microtubule association". Molecular Cell. 8 (2): 339–49. doi:10.1016/S1097-2765(01)00313-6. PMID 11545736.
• Tussie-Luna MI, Michel B, Hakre S, Roy AL (Nov 2002). "The SUMO ubiquitin-protein isopeptide ligase family member Miz1/PIASxbeta /Siz2 is a transcriptional cofactor for TFII-I". The Journal of Biological Chemistry. 277 (45): 43185–93. doi:10.1074/jbc.M207635200. PMID 12193603.
• Piluso D, Bilan P, Capone JP (Nov 2002). "Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1". The Journal of Biological Chemistry. 277 (48): 46799–808. doi:10.1074/jbc.M206226200. PMID 12244100.
• Zhang H, Li Z, Viklund EK, Strömblad S (Sep 2002). "P21-activated kinase 4 interacts with integrin alpha v beta 5 and regulates alpha v beta 5-mediated cell migration". The Journal of Cell Biology. 158 (7): 1287–97. doi:10.1083/jcb.200207008. PMC 2173231. PMID 12356872.
• Herold S, Wanzel M, Beuger V, Frohme C, Beul D, Hillukkala T, Syvaoja J, Saluz HP, Haenel F, Eilers M (Sep 2002). "Negative regulation of the mammalian UV response by Myc through association with Miz-1". Molecular Cell. 10 (3): 509–21. doi:10.1016/S1097-2765(02)00633-0. PMID 12408820.
• Wu S, Cetinkaya C, Munoz-Alonso MJ, von der Lehr N, Bahram F, Beuger V, Eilers M, Leon J, Larsson LG (Jan 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. S2CID 903258.
• Bowen H, Lapham A, Phillips E, Yeung I, Alter-Koltunoff M, Levi BZ, Perry VH, Mann DA, Barton CH (Sep 2003). "Characterization of the murine Nramp1 promoter: requirements for transactivation by Miz-1". The Journal of Biological Chemistry. 278 (38): 36017–26. doi:10.1074/jbc.M304301200. PMID 12840021.
• Sakurai T, Itoh K, Higashitsuji H, Nagao T, Nonoguchi K, Chiba T, Fujita J (Apr 2004). "A cleaved form of MAGE-A4 binds to Miz-1 and induces apoptosis in human cells". The Journal of Biological Chemistry. 279 (15): 15505–14. doi:10.1074/jbc.M310437200. hdl:2433/147540. PMID 14739298.
• Lehner B, Sanderson CM (Jul 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.

External links

• ZBTB17+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Overview of all the structural information available in the PDB for UniProt: Q13105 (Zinc finger and BTB domain-containing protein 17) at the PDBe-KB.

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