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DUSP11
DUSP11, also known as PIR1 or RNA/RNP complex-1-interacting phosphatase, is a nuclear member of the dual specificity phosphatase family. It removes phosphates from the 5' end of RNA, binds RNA directly and is thought to participate in nuclear mRNA metabolism. Browse Assay Genie's current range of DUSP11 research reagents below, or read on for the biology behind the target.
DUSP11 is a phosphatase with RNA 5'-triphosphatase and diphosphatase activities. Despite its place in the dual specificity phosphatase family, it shows only poor protein-tyrosine phosphatase activity. In vitro it also acts on ATP, ADP and O-methylfluorescein phosphate. The protein binds RNA, and UniProt annotates a possible role in nuclear mRNA metabolism.
The DUSP11 gene encodes a protein that belongs to the protein-tyrosine phosphatase family, in the non-receptor class dual specificity subfamily. HGNC places it in the atypical dual specificity phosphatases. Dual specificity phosphatases in general inactivate their target kinases by dephosphorylating both phosphoserine/threonine and phosphotyrosine residues. Many family members negatively regulate the mitogen-activated protein (MAP) kinase superfamily, including MAPK/ERK, SAPK/JNK and p38, which are associated with cellular proliferation and differentiation. Individual family members differ in substrate specificity, tissue distribution, subcellular localisation and the way extracellular stimuli induce their expression.
DUSP11 is localised to the nucleus, including nuclear speckles. It binds directly to RNA and to splicing factors, which supports the suggestion that it contributes to nuclear mRNA metabolism. Its earlier HGNC name, dual specificity phosphatase 11 (RNA/RNP complex 1-interacting), and the alias PIR1 reflect this association with RNA and ribonucleoprotein complexes. Mouse and rat both carry a Dusp11 ortholog.
DUSP11 removes phosphates from the 5' end of RNA and binds RNA, making it a useful subject for studying RNA modification.
DUSP11 binds splicing factors and is suggested to participate in nuclear mRNA metabolism, linking phosphatase activity to RNA handling.
As an atypical dual specificity phosphatase with weak protein-tyrosine activity, DUSP11 helps define how substrate preference varies within the family.
DUSP11 is found in nuclear speckles, so it is relevant to work on the organisation and function of nuclear compartments.
DUSP11 has RNA 5'-triphosphatase and diphosphatase activities and binds RNA. Its protein-tyrosine phosphatase activity is poor. It also acts on ATP, ADP and O-methylfluorescein phosphate in vitro, and it may participate in nuclear mRNA metabolism.
DUSP11 is the HGNC symbol for dual specificity phosphatase 11. UniProt names the protein RNA/RNP complex-1-interacting phosphatase, and PIR1 is a listed alias. The earlier HGNC name was dual specificity phosphatase 11 (RNA/RNP complex 1-interacting).
Yes. Mouse and rat each have an ortholog named Dusp11, so the gene can be studied in common rodent models. Check the datasheet of any product for its validated reactivity before choosing a reagent for a given species.
Other dual specificity phosphatases, including MAP kinase regulators and atypical family members.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O75319; product specifications from Assay Genie datasheets.
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