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Gene Review

ZNF2  -  zinc finger protein 2

Homo sapiens

Synonyms: A1-5, ZNF661, Zfp661, Zinc finger protein 2, Zinc finger protein 2.2, ...
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Disease relevance of ZNF2

  • The lone KRAB-A and composite KRAB-AB domains from the human ZNF2 protein were over-expressed as recombinant proteins in E. coli, isolated and purified to homogeneity to investigate their structure to function relationship [1].

High impact information on ZNF2

  • The KRAB-A domain of another zinc finger protein, ZNF2, also has repressor activity [2].
  • In this communication, we report that PDTC inhibits the activation of temperature-sensitive murine p53(Val-135) (TSp53) in the transformed rat embryo fibroblast line, A1-5, as well as wild-type human p53 in the normal diploid fibroblast line, WS1neo [3].
  • Elements A and B and the zinc finger domain are encoded by separate exons in the ZNF2 gene, a human member of this sub-family [4].

Analytical, diagnostic and therapeutic context of ZNF2

  • Five IgG1k mAbs (A1-5) were selected by ELISA and immunoblotting [5].
  • Tryptic peptide analysis revealed heterogeneity in the beta A1-5 and beta A6-16 peptides, each of which eluted as four peaks on reverse phase HPLC [6].


  1. Expression, purification and partial characterization of the Krüppel-associated box (KRAB) from the human ZNF2 protein. Rivieccio, V., Mannini, R., Concilio, L., D'Auria, S., Pedone, C., Grimaldi, G. Protein Pept. Lett. (2005) [Pubmed]
  2. The Krüppel-associated box-A (KRAB-A) domain of zinc finger proteins mediates transcriptional repression. Witzgall, R., O'Leary, E., Leaf, A., Onaldi, D., Bonventre, J.V. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  3. Pyrrolidine dithiocarbamate prevents p53 activation and promotes p53 cysteine residue oxidation. Wu, H.H., Momand, J. J. Biol. Chem. (1998) [Pubmed]
  4. Members of the zinc finger protein gene family sharing a conserved N-terminal module. Rosati, M., Marino, M., Franzè, A., Tramontano, A., Grimaldi, G. Nucleic Acids Res. (1991) [Pubmed]
  5. Human autoantibody-reactive epitopes of SS-B/La are highly conserved in comparison with epitopes recognized by murine monoclonal antibodies. Chan, E.K., Tan, E.M. J. Exp. Med. (1987) [Pubmed]
  6. Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease. Roher, A.E., Lowenson, J.D., Clarke, S., Wolkow, C., Wang, R., Cotter, R.J., Reardon, I.M., Zürcher-Neely, H.A., Heinrikson, R.L., Ball, M.J. J. Biol. Chem. (1993) [Pubmed]
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