We here isolated and characterized a cDNA clone encoding 40-kDa heat-shock protein hsp40 from cDNA expression library of human placenta by immunoscreening with anti-hsp40 antibody. N-terminal amino acid sequence (48 residues) deduced from the base sequence was completely identical to that of hsp40 purified from HeLa cells. Deduced amino acid sequence of the cDNA is homologous to bacterial DnaJ heat-shock protein and its homologues in yeast such as SCJ1, YDJ1(MAS5), SIS1, SEC63 and Zuotin. Nucleotide sequence identity between hsp40 and HDJ1 (another human DnaJ homologue) is more than 98%, suggesting that these two proteins are the same gene product.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|