Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein.
A human homologue of the bacterial DNAJ heatshock protein, HDJ-2, was isolated from a human umbilical vein endothelial cDNA library using a monoclonal antibody which reacts specifically to human endothelial cells and monocytes. This cDNA clone consists of 1469 nucleotides with an open reading frame of 1191 nucleotides. HDJ-2 shares significant homology with Escherichia coli heat shock protein DNAJ, as well as the yeast homologues Sec63, YDJ1, SCJ1 and SIS1. This homology suggests HDJ-2 may be involved in protein folding and/or transport.
Chellaiah
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Department of Surgery and Pathology, Washington University School of Medicine, St. Louis, MO 63110.
Davis
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Mohanakumar
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics*; D001483:Base Sequence; D002352:Carrier Proteins; D003001:Cloning, Molecular; D016384:Consensus Sequence; D004730:Endothelium, Vascular / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D006801:Humans; D008969:Molecular Sequence Data
D001426:Bacterial Proteins; D002352:Carrier Proteins; C107481:DNAJA1 protein, human; C494635:DnaJ protein, E coli; D029968:Escherichia coli Proteins; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins