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http://purl.uniprot.org/citations/11432789http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11432789http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11432789http://www.w3.org/2000/01/rdf-schema#comment"Five putative dual specificity protein phosphatases (DSPs), designated LMW-DSP1, -DSP4, -DSP6, -DSP10, and -DSP11, were cloned with a combination of RT-PCR and cDNA library screening strategies. Sequencing analysis revealed that all lacked the cdc25 homology domain that is conserved in most known DSPs/MAP kinase phosphatases (MKPs). LMW-DSP1 exhibited the highest similarity to plant DSPs. LMW-DSP4 exhibited the highest similarity to human YVH1 and rat GKAP, but its C-terminal region was much shorter than that of the human and rat clones. LMW-DSP6 was found to be identical to recently cloned TMDP, and LMW-DSP11 seemed to be a mouse ortholog of human VHR. LMW-DSP10 was found to have a DSP catalytic-like domain, but the critical cysteine residue for catalytic activity was missing. Recombinant LMW-DSP1, -DSP6, and -DSP11 exhibited obvious and strong activity against an artificial low molecular substrate, para-nitrophenyl phosphate (pNPP). Recombinant LMW-DSP4 exhibited slight but significant activity, whereas no activity was detected for LMW-DSP10. The phosphatase activity of the recombinant LMW-DSPs was inhibited by orthovanadate but not sodium fluoride. However, none of the DSPs could dephosphorylate MAP kinases such as ERK1, p38, and SAPK/JNK in transiently transfected COS7 cells under the conditions used. Northern blot analysis revealed that LMW-DSP1, -DSP6, -DSP10, and -DSP11 were specifically expressed in testis, while LMW-DSP4 was broadly expressed. The testis-specific expression and apparent absence of dephosphorylation action on MAP kinases suggest that LMW-DSP1, -DSP6, -DSP10, and -DSP11 play specific roles in testis. Taken together, it is conceivable that a distinct class of low molecular mass DSPs is present and plays a role in dephosphorylating unknown molecules other than MAP kinases."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a002952"xsd:string
http://purl.uniprot.org/citations/11432789http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a002952"xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/author"Aoki N."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/author"Aoki N."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/author"Aoyama K."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/author"Aoyama K."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/author"Matsuda T."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/author"Matsuda T."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/author"Nagata M."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/author"Nagata M."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/pages"133-140"xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/pages"133-140"xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/title"A growing family of dual specificity phosphatases with low molecular masses."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/title"A growing family of dual specificity phosphatases with low molecular masses."xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/volume"130"xsd:string
http://purl.uniprot.org/citations/11432789http://purl.uniprot.org/core/volume"130"xsd:string
http://purl.uniprot.org/citations/11432789http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11432789
http://purl.uniprot.org/citations/11432789http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11432789