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| pubmed-article:8280084 | lifeskim:mentions | umls-concept:C1979930 | lld:lifeskim |
| pubmed-article:8280084 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8280084 | pubmed:dateCreated | 1994-2-7 | lld:pubmed |
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| pubmed-article:8280084 | pubmed:abstractText | The substrate specificity of mitogen-activated protein (MAP) kinase-activated protein kinase-2 (MAPKAP kinase-2) was investigated by using synthetic peptides related to the N-terminus of glycogen synthase. The minimum sequence required for efficient phosphorylation was found to be Xaa-Xaa-Hyd-Xaa-Arg-Xaa-Xaa-Ser-Xaa-Xaa, where Hyd is a bulky hydrophobic residue (Phe > Leu > Val >> Ala), and the peptide Lys-Lys-Phe-Asn-Arg-Thr-Leu-Ser-Val-Ala was phosphorylated with a Km of 9.3 microM and Vmax. of 10 mumol/min per mg. MAPKAP kinase-1 (a homologue of ribosomal protein S6 kinase) also requires an arginine three residues N-terminal to the serine (position n-3), but not a hydrophobic residue at position n-5. Neither MAPKAP kinase-1 nor MAPKAP kinase-2 could tolerate a proline residue at position n + 1, indicating that their specificities do not overlap with that of MAP kinase. The specificity of calmodulin-dependent protein kinase-II resembled that of MAPKAP kinase-2, except that it could tolerate replacement of the arginine by a lysine and the phosphorylation-site serine by a threonine residue. Partial cDNAs encoding MAPKAP kinase-2 were isolated from rabbit and human skeletal muscle and human teratocarcinoma libraries, and Northern-blotting experiments revealed a single 3.3 kb mRNA transcript present at similar levels in six human tissues examined. The catalytic domain was most similar (35-40% identity) to calmodulin-dependent protein kinases II and IV, phosphorylase kinase, putative serine kinase H1 and the C-terminal domain of MAPKAP kinase-1, which form one branch of the protein kinase phylogenetic tree. The sequence N-terminal to the catalytic domain is proline-rich and contains two putative SH3-binding sites. The threonine residue phosphorylated by MAP kinase lies immediately C-terminal to the catalytic domain and is followed by a nuclear localization signal, Lys-Lys-(Xaa)10-Lys-Arg-Arg-Lys-Lys, near the C-terminus. | lld:pubmed |
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| pubmed-article:8280084 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8280084 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8280084 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8280084 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8280084 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8280084 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8280084 | pubmed:author | pubmed-author:CohenPP | lld:pubmed |
| pubmed-article:8280084 | pubmed:author | pubmed-author:CaudwellBB | lld:pubmed |
| pubmed-article:8280084 | pubmed:author | pubmed-author:CohenP TPT | lld:pubmed |
| pubmed-article:8280084 | pubmed:author | pubmed-author:StokoeDD | lld:pubmed |
| pubmed-article:8280084 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8280084 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8280084 | pubmed:volume | 296 ( Pt 3) | lld:pubmed |
| pubmed-article:8280084 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8280084 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8280084 | pubmed:pagination | 843-9 | lld:pubmed |
| pubmed-article:8280084 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8280084 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8280084 | pubmed:articleTitle | The substrate specificity and structure of mitogen-activated protein (MAP) kinase-activated protein kinase-2. | lld:pubmed |
| pubmed-article:8280084 | pubmed:affiliation | Department of Biochemistry, University of Dundee, Scotland, UK. | lld:pubmed |
| pubmed-article:8280084 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8280084 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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