dual specificity phosphatase 11 (RNA/RNP complex 1-interacting), isofo - Protein

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Structure of human PIR1, an atypical dual-specificity phosphatase. [Biochemistry. 2014]
Structure of human PIR1, an atypical dual-specificity phosphatase.
Sankhala RS, Lokareddy RK, Cingolani G. Biochemistry. 2014 Feb 11; 53(5):862-71. Epub 2014 Jan 31.
Human PIR1 of the protein-tyrosine phosphatase superfamily has RNA 5'-triphosphatase and diphosphatase activities. [J Biol Chem. 1999]
Human PIR1 of the protein-tyrosine phosphatase superfamily has RNA 5'-triphosphatase and diphosphatase activities.
Deshpande T, Takagi T, Hao L, Buratowski S, Charbonneau H. J Biol Chem. 1999 Jun 4; 274(23):16590-4.
PIR1, a novel phosphatase that exhibits high affinity to RNA . ribonucleoprotein complexes. [J Biol Chem. 1998]
PIR1, a novel phosphatase that exhibits high affinity to RNA . ribonucleoprotein complexes.
Yuan Y, Li DM, Sun H. J Biol Chem. 1998 Aug 7; 273(32):20347-53.

RefSeq protein isoforms
See 2 reference sequence protein isoforms for the Dusp11 gene.

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