1984
DOI: 10.1093/nar/12.13.5145
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Compilation of published signal sequences

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Cited by 752 publications
(388 citation statements)
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References 290 publications
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“…1 33-39. (The published rat protein sequence substitutes a glutamine for a glutamic acid residue, resulting in nine consecutive uncharged amino acids.) Since nine amino acids are considered to be a minimum signal peptide (33) and since the seven (human) or nine (rat) "hydrophobic" amino acids do not include leucine, isoleucine, valine, or the aromatic amino acids, but are composed exclusively of glycine, alanine, asparagine, proline, and perhaps glutamine, a signal sequence appears to be absent regardless of location.…”
Section: Resultsmentioning
confidence: 99%
“…1 33-39. (The published rat protein sequence substitutes a glutamine for a glutamic acid residue, resulting in nine consecutive uncharged amino acids.) Since nine amino acids are considered to be a minimum signal peptide (33) and since the seven (human) or nine (rat) "hydrophobic" amino acids do not include leucine, isoleucine, valine, or the aromatic amino acids, but are composed exclusively of glycine, alanine, asparagine, proline, and perhaps glutamine, a signal sequence appears to be absent regardless of location.…”
Section: Resultsmentioning
confidence: 99%
“…After the first methionine residue, there is a potential signal sequence with a hydrophobic core of 13 amino acids and a helix-breaking residue, glycine 17 (Watson, 1984). According to the rule established for a potential cleavage site (von Heijne, 1984), a protease could act between amino acid residues 17 and 18.…”
mentioning
confidence: 99%
“…The putative initiation codon ATG was preceded at 6 bp upstream by a potential ribosome-binding sequence (5 0 -AGGAGG-3 0 ) that is homologous to the consensus Shine-Dalgarno sequence.19) The sequences TTGTAT and TATAAT, with a 15-bp spacing, showing certain homology to the consensus promoter sequences of À35 and À10 regions for E. coli 70 factor, TTGACA and TATAAT with a 17-bp spacing, respectively, were identified upstream of the coding region. 20) Amino acid sequence of Xyl43B The deduced protein sequence of Xyl43B did not contain a typical signal peptide sequence conserved in bacterial extracellular proteins, 21) suggesting that Xyn43B is an intracellular enzyme. The deduced protein sequence of Xyl43B was compared with entries in the DDBJ database.…”
Section: Resultsmentioning
confidence: 99%