Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153.
Nuclear pore complexes represent the channels for the the bi-directional movement of macromolecules between the nucleus and cytoplasm, and are thought to contain upwards of 100 different polypeptide subunits. Many of these subunits belong to a growing family of polypeptides termed nucleoporins which are characterized by the presence of O-linked N-acetylglucosamine moieties and a distinctive pentapeptide repeat (XFXFG). This paper reports the primary structure of hnup153, the human homologue of the rat nucleoporin, nup153, with which it shares 82% amino acid identity. In addition to 33 copies of the XFXFG repeat, hnup153 exhibits four repeats of 37-38 amino acids each containing an apparent 'zinc finger motif'. These zinc fingers are most closely related to those found in the mouse oncoprotein mdm-2 and a product of Drosophila small optic lobes (sol) gene.
McMorrow
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Department of Cell Biology, Harvard Medical School, Boston, MA 02115.
Bastos
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Horton
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Burke
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D000595:Amino Acid Sequence; D001483:Base Sequence; D018076:DNA, Complementary / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics*; D016415:Sequence Alignment
D018076:DNA, Complementary; C079377:NUP153 protein, human; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; C513084:Nup153 protein, mouse; C513083:Nup153 protein, rat