Human protein S cDNA encodes Phe-16 and Tyr 222 in consensus sequences for the post-translational processing

Hans K.Ploos van Amstel*, A. Linda van der Zanden, Pieter H. Reitsma, Rogier M. Bertina

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

21 Citations (Scopus)

Abstract

Partial cDNAs coding for human protein S were isolated from a pUC9 human liver cDNA library. Together, the overlapping clones span a (partial) 5′-non-coding region, and the complete protein S coding and 3′-untranslated regions. The derived amino acid sequence deviates at five positions from two previously reported protein S sequences. Two of these differences (Phe instead of Leu at position - 16 and Tyr instead of Asp at position 222) are found in regions that are important for the post-translational modification of protein S, the γ-carboxylation of glutamic acid and the hydroxylation of asparagine, respectively.

Original languageEnglish
Pages (from-to)186-190
Number of pages5
JournalFEBS letters
Volume222
Issue number1
DOIs
Publication statusPublished - 28 Sept 1987

Keywords

  • Carboxylation
  • cDNA
  • Hydroxylation
  • Protein S

Fingerprint

Dive into the research topics of 'Human protein S cDNA encodes Phe-16 and Tyr 222 in consensus sequences for the post-translational processing'. Together they form a unique fingerprint.

Cite this