RNA/RNP complex-1-interacting phosphatase

Definition:

Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. In addition, has phosphatase activity with ATP, ADP and O-methylfluorescein phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA metabolism.

References:

[1]. Rajeshwer Singh Sankhala, et al. Structure of human PIR1, an atypical dual-specificity phosphatase. Biochemistry. 2014 Feb 11;53(5):862-71. [Content Brief]

[2]. Y Yuan, et al. PIR1, a novel phosphatase that exhibits high affinity to RNA . ribonucleoprotein complexes. J Biol Chem. 1998 Aug 7;273(32):20347-53. [Content Brief]

[3]. T Deshpande, et al. Human PIR1 of the protein-tyrosine phosphatase superfamily has RNA 5'-triphosphatase and diphosphatase activities. J Biol Chem. 1999 Jun 4;274(23):16590-4. [Content Brief]

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