Disease relevance of ZFP161

• Therefore, ZFP161 is a candidate gene by position for the holoprosencephaly type 4 gene, HPE4, which is involved in congenital malformations [1].
• We isolated a cDNA encoding a human homologue of ZF5 (hZF5), which has five Kruppel-like C2H2 type zinc fingers at carboxyl terminus and the BTB/POZ (poxvirus and zinc finger) at the amino terminus, using autoimmune sera from a patient with overlap syndrome (dermatomyositis and scleroderma) [2].

High impact information on ZFP161

• We show that the human zinc finger 5 protein (ZF5) binds specifically to RRS motifs in vitro and in vivo [3].
• The ZiN/POZ domain was shown to mediate ZF5-dependent transcriptional activation and repression [4].
• In the current study, a cyclic amplification and selection of targets (CAST) protocol detected preferred ZF5 binding sites which are highly GC-rich [4].
• The cDNA of the gene termed ZFP161 has an open reading frame of 1347 bp [1].
• Through the use of a panel of somatic cell hybrids for chromosomal assignment and DNAs of somatic cell hybrids containing a deleted chromosome 18 for fine mapping, the human gene ZFP161 was localized to 18p11.21-pter [1].

Biological context of ZFP161

• Novel human BTB/POZ domain-containing zinc finger protein ZNF295 is directly associated with ZFP161 [5].
• We postulated that ZNF295 may be involved in the bi-directional control of gene expression in concert with ZFP161 [5].
• RT-PCR analyses revealed that transfection of ZFP161 induced hDAT mRNA expression in HEK293 cells [6].
• The deduced amino acid sequence of hZF5 is highly homologous to mouse ZF5 (99.3% identity) [2].

Anatomical context of ZFP161

• Immunofluorescence studies revealed that HA-tagged hZF5 transiently expressed in COS-7 cells showed the nuclear dot pattern in the BTB/POZ domain-dependent manner [2].
• The protein is 98% homologous to a murine zinc finger protein, ZF5 (M. Numoto et al., 1993, Nucleic Acids Res. 21: 3767-3775), which is a putative transcriptional repressor of c-myc and exhibits growth-suppressive activity in mouse cell lines [1].
• From these results, we predict that viral protein which mimics host ZF5 antigen triggers self-reactive T cell clones and induces the autoantibody in M6 serum after the destruction of host tissues [7].
• In a reverse transcriptase PCR assay using mouse skeletal muscle RNA, we identified a 827 bp PCR product including the zinc finger domain of ZF5 and the acidic domain of VP16 [8].

Associations of ZFP161 with chemical compounds

• We cloned two novel arginine methylation substrates, ZF5 (zinc finger 5) and p137GPI (GPI-anchor protein p137), which do not possess typical RGG motifs [9].

Analytical, diagnostic and therapeutic context of ZFP161

• The ability of ZFP161 to directly bind HY1 was examined in an electrophoretic mobility shift assay [6].
• Sequence alignment shows that there is a high homology among the deduced amino acid sequences of the rat, mouse and human ZFP161 proteins [10].
• Detection of mouse skeletal muscle-specific product, which includes ZF5 zinc fingers and a VP16 acidic domain, by reverse transcriptase PCR [8].

References