Alternative titles; symbols
HGNC Approved Gene Symbol: ZNF33A
Cytogenetic location: 10p11.1 Genomic coordinates (GRCh38): 10:38,010,489-38,067,834 (from NCBI)
By sequencing clones obtained from a size-fractionated immature myeloid cell line cDNA library, Nomura et al. (1994) cloned ZNF33A, which they designated KIAA0065. The transcript has an Alu element in its 3-prime UTR. The deduced 848-amino acid protein contains a C2H2-type zinc finger domain and shares 93.1% identity with ZNF11B (ZNF33B; 194522) over 374 amino acids. Northern blot analysis detected ZNF33A expression in all tissues examined, with highest expression in skeletal muscle, and lowest expression in testis and colon.
Using ZAK (609479) as bait in a yeast 2-hybrid screen of a heart cDNA library, followed by screening a placenta cDNA library and 5-prime RACE, Yang (2003) cloned ZNF33A, which they designated ZZAPK. The deduced 810-amino acid protein has a calculated molecular mass of 94.3 kD. ZZAPK contains an N-terminal KRAB domain, followed by a 256-amino acid linker region and 16 tandemly repeated Kruppel-type zinc fingers at its C terminus. Northern blot analysis detected variable expression of a major 5.5-kb transcript in all tissues examined.
By immunoprecipitation of cotransfected human embryonic kidney (HEK293) cells, Yang (2003) confirmed direct interaction between epitope-tagged ZZAPK and ZAK. Mutation analysis indicated that the SAM domain of ZAK was required to bind ZZAPK. By coexpression in a rat fibroblast cell line, Yang (2003) determined that ZZAPK countered the effect of ZAK on G2/M cell cycle arrest. When expressed alone, ZZAPK increased entry of cells into S phase. ZZAPK increased expression of cyclin E (CCNE1; 123837) in rat fibroblasts and HEK293 cells. ZZAPK also increased expression of transcription factor E2F (see 189971) and the activity of an E2F-dependent reporter gene.
By a combination of in situ chromosomal hybridization and somatic cell hybrid analysis, Rousseau-Merck et al. (1992) concluded that there are sequences hybridizing to the KOX2 probe at 2 loci, which they called ZNF11A (ZNF33A) and ZNF11B (ZNF33B), that map proximal and distal to a 10q11.2 breakpoint, respectively. They suggested that the 2 ZNF11 loci represent related sequences. Rousseau-Merck et al. (1992) suggested that this cluster of zinc finger protein genes (ZNF11, ZNF22 (194529), and ZNF25 (194528)) is of particular interest since the loci for MEN2A and MEN2B map to this region.
Tunnacliffe et al. (1993) identified 2 related zinc finger gene clusters mapping to the pericentromeric region of chromosome 10. Cluster A contains ZNF11A (ZNF33A) and ZNF37A (616085) and maps to chromosome 10p11.2. Cluster B contains ZNF11B (ZNF33B) and ZNF37B and maps to chromosome 10q11.2. Southern blot analysis indicated that the 2 clusters evolved by duplication of an ancestral gene cluster before the divergence of the human and great ape lineages.
Nomura, N., Nagase, T., Miyajima, N., Sazuka, T., Tanaka, A., Sato, S., Seki, N., Kawarabayasi, Y., Ishikawa, K., Tabata, S. Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1: 223-229, 1994. [PubMed: 7584044] [Full Text: https://doi.org/10.1093/dnares/1.5.223]
Rousseau-Merck, M. F., Tunnacliffe, A., Berger, R., Ponder, B. A. J., Thiesen, H. J. A cluster of expressed zinc finger protein genes in the pericentromeric region of human chromosome 10. Genomics 13: 845-848, 1992. [PubMed: 1639412] [Full Text: https://doi.org/10.1016/0888-7543(92)90166-p]
Tunnacliffe, A., Liu, L., Moore, J. K., Leversha, M. A., Jackson, M. S., Papi, L., Ferguson-Smith, M. A., Thiesen, H.-J., Ponder, B. A. J. Duplicated KOX zinc finger gene clusters flank the centromere of human chromosome 10: evidence for a pericentric inversion during primate evolution. Nucleic Acids Res. 21: 1409-1417, 1993. [PubMed: 8464732] [Full Text: https://doi.org/10.1093/nar/21.6.1409]
Yang, J.-J. A novel zinc finger protein, ZZaPK, interacts with ZAK and stimulates the ZAK-expressing cells re-entering the cell cycle. Biochem. Biophys. Res. Commun. 301: 71-77, 2003. [PubMed: 12535642] [Full Text: https://doi.org/10.1016/s0006-291x(02)02980-7]