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    Cell. 1992 May 1;69(3):551-8.

    Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62.

    Wong G, Müller O, Clark R, Conroy L, Moran MF, Polakis P, McCormick F.

    Department of Molecular Biology, Chiron Corporation, Emeryville, California 94608.

    p62 is a tyrosine phosphoprotein that associates with p21ras GTPase-activating protein (GAP). Purification and cDNA cloning of p62 reveal extensive sequence similarity to a putative hnRNP protein, GRP33. Recombinant human p62 purified from insect Sf9 cells binds to DNA and to mRNA and, like many proteins involved in mRNA processing, recombinant p62 is modified by dimethylation on multiple arginine residues. p62 also binds tightly to p21ras GAP in vitro: this binding depends on phosphorylation of p62 on tyrosine residues and occurs through SH2 regions of GAP. These data suggest that p120-GAP and p62 play a role in some aspect of mRNA processing or utilization and that this role may be regulated by tyrosine phosphorylation, and indirectly, by p21ras.

    PMID: 1374686 [PubMed - indexed for MEDLINE]

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