| pubmed-article:12383260 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12383260 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:12383260 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:12383260 | lifeskim:mentions | umls-concept:C0031678 | lld:lifeskim |
| pubmed-article:12383260 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:12383260 | lifeskim:mentions | umls-concept:C0070872 | lld:lifeskim |
| pubmed-article:12383260 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:12383260 | pubmed:dateCreated | 2002-10-17 | lld:pubmed |
| pubmed-article:12383260 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12383260 | pubmed:abstractText | Protein histidine phosphorylation in eukaryotes has been sparsely studied compared to protein serine/threonine and tyrosine phosphorylation. In an attempt to rectify this by probing porcine liver cytosol with the phosphohistidine-containing peptide succinyl-Ala-His(P)-Pro-Phe-p-nitroanilide (phosphopeptide I), we observed a phosphatase activity that was insensitive towards okadaic acid and EDTA. This suggested the existence of a phosphohistidine phosphatase different from protein phosphatase 1, 2A and 2C. A 1000-fold purification to apparent homogeneity gave a 14-kDa phosphatase with a specific activity of 3 micro mol.min-1.mg-1 at pH 7.5 with 7 micro m phosphopeptide I as substrate. Partial amino-acid sequence determination of the purified porcine enzyme by MS revealed similarity with a human sequence representing a human chromosome 9 gene of hitherto unknown function. Molecular cloning from a human embryonic kidney cell cDNA-library followed by expression and purification, yielded a protein with a molecular mass of 13 700 Da, and an EDTA-insensitive phosphohistidine phosphatase activity of 9 micro mol.min-1.mg-1 towards phosphopeptide I. No detectable activity was obtained towards a set of phosphoserine-, phosphothreonine-, and phosphotyrosine peptides. Northern blot analysis indicated that the human phosphohistidine phosphatase mRNA was present preferentially in heart and skeletal muscle. These results provide a new tool for studying eukaryotic histidine phosphorylation/dephosphorylation. | lld:pubmed |
| pubmed-article:12383260 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12383260 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12383260 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12383260 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12383260 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12383260 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12383260 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12383260 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12383260 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12383260 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:12383260 | pubmed:author | pubmed-author:OKAKK | lld:pubmed |
| pubmed-article:12383260 | pubmed:author | pubmed-author:GongFengF | lld:pubmed |
| pubmed-article:12383260 | pubmed:author | pubmed-author:LoweLoriL | lld:pubmed |
| pubmed-article:12383260 | pubmed:author | pubmed-author:LiJin-PingJP | lld:pubmed |
| pubmed-article:12383260 | pubmed:author | pubmed-author:PetterssonGun... | lld:pubmed |
| pubmed-article:12383260 | pubmed:author | pubmed-author:ZetterqvistOr... | lld:pubmed |
| pubmed-article:12383260 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12383260 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:12383260 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12383260 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12383260 | pubmed:pagination | 5016-23 | lld:pubmed |
| pubmed-article:12383260 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:meshHeading | pubmed-meshheading:12383260... | lld:pubmed |
| pubmed-article:12383260 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12383260 | pubmed:articleTitle | Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase. | lld:pubmed |
| pubmed-article:12383260 | pubmed:affiliation | Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden. | lld:pubmed |
| pubmed-article:12383260 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12383260 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:29085 | entrezgene:pubmed | pubmed-article:12383260 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:12383260 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12383260 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12383260 | lld:pubmed |
