A widely expressed novel C2H2 zinc-finger protein with multiple consensus phosphorylation sites is conserved in mouse and man.
We have cloned a murine cDNA whose deduced sequence encodes a 455-amino-acid (aa) zinc-finger protein (Zfp), PZf (penta Zf protein). Sequence analysis shows that PZf has multiple phosphorylation consensus sites for casein kinase II and protein kinase C in its N-terminal portion. This region (aa 1 to 197), which does not share significant homology to known aa sequences, has a number of charged (39 Glu, 15 Asp, 23 Lys, 22 Arg) and hydroxyl (20 Ser, 12 Thr) aa. This potentially phosphorylatable region is followed by five C2H2 Zf in the middle of the protein. The Pzf gene is transcribed as a 5-kb mRNA in all murine tissues examined. The human genome also seems to contain one or more Pzf-related genes.
Saotome
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Y
Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, NY 10032.
Winter
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CG
Hirsh
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D
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D016384:Consensus Sequence; D017124:Conserved Sequence; D018076:DNA, Complementary; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D008040:Genetic Linkage; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D010766:Phosphorylation; D012333:RNA, Messenger / Q000235:genetics; D016335:Zinc Fingers
D018076:DNA, Complementary; D004268:DNA-Binding Proteins; D012333:RNA, Messenger