Phosphatase Subfamily DSP11
DSP11 is a metazoan-specific subfamily. Its exact physiological substrate is unknown, but several lines of evidence link this phosphatase to RNA splicing.
DSP11 is found throughout metazoa (unpublished data from gOrtholog).
DSP11 has a single domain, the DSP phosphatase domain. The DSP11 catalytic domain is most closely related to that of RNGTT, and both domains lack the first beta sheet of the domain.
Human DUSP11 is mainly localized to the cell nucleus. It was originally identified as being associated with RNA or ribonucleoprotein complexes. It is therefore called phosphatase that interacts with RNA–ribonucleoprotein complex 1 (PIR1). Its exact physiological substrate is unknown, but several lines of evidence link this phosphatase to RNA splicing . DSP11 prefers to dephosphorylate RNA than phosphoprotein substrates. Its primary function in vivo is supposed to dephosphorylate RNA 5′-ends . This is not surprising given that it is close to another atypical DSP, RNGTT, (RNA guanylyltransferase and 5'-phosphatase). Its function was reviewed in introduction of  in details.
- Chu C, Das K, Tyminski JR, Bauman JD, Guan R, Qiu W, Montelione GT, Arnold E, and Shatkin AJ. Structure of the guanylyltransferase domain of human mRNA capping enzyme. Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10104-8. DOI:10.1073/pnas.1106610108 |
- Deshpande T, Takagi T, Hao L, Buratowski S, and Charbonneau H. 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. DOI:10.1074/jbc.274.23.16590 |
- Ho CK, Lehman K, and Shuman S. An essential surface motif (WAQKW) of yeast RNA triphosphatase mediates formation of the mRNA capping enzyme complex with RNA guanylyltransferase. Nucleic Acids Res. 1999 Dec 15;27(24):4671-8. DOI:10.1093/nar/27.24.4671 |
- Lima CD, Wang LK, and Shuman S. Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus. Cell. 1999 Nov 24;99(5):533-43. DOI:10.1016/s0092-8674(00)81541-x |