PROSITE documentation PDOC00010
Aspartic acid and asparagine hydroxylation site


Post-translational hydroxylation of aspartic acid or asparagine [1] to form erythro-β-hydroxyaspartic acid or erythro-β-hydroxyasparagine has been identified in a number of proteins with domains homologous to epidermal growth factor (EGF). Examples of such proteins are the blood coagulation protein factors VII, IX and X, proteins C, S, and Z, the LDL receptor, thrombomodulin, etc. Based on sequence comparisons of the EGF-homology region that contains hydroxylated Asp or Asn, a consensus sequence has been identified that seems to be required by the hydroxylase(s).


This consensus pattern is located in the N-terminal of EGF-like domains, while our EGF-like cysteine pattern signature (see the relevant entry <PDOC00021>) is located in the C-terminal.

Last update:

January 1989 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

ASX_HYDROXYL, PS00010; Aspartic acid and asparagine hydroxylation site  (PATTERN)


1AuthorsStenflo J. Ohlin A.-K. Owen W.G. Schneider W.J.
Titlebeta-Hydroxyaspartic acid or beta-hydroxyasparagine in bovine low density lipoprotein receptor and in bovine thrombomodulin.
SourceJ. Biol. Chem. 263:21-24(1988).
PubMed ID2826439

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