{PDOC00010}
{PS00010; ASX_HYDROXYL}
{BEGIN}
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* Aspartic acid and asparagine hydroxylation site *
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Post-translational  hydroxylation of aspartic acid or  asparagine [1] to  form
erythro-beta-hydroxyaspartic acid  or erythro-beta-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).

-Consensus pattern: C-x-[DN]-x(4)-[FY]-x-C-x-C
                    [D or N is the hydroxylation site]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: 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.

[ 1] Stenflo J., Ohlin A.-K., Owen W.G., Schneider W.J.
     "beta-Hydroxyaspartic acid or beta-hydroxyasparagine in bovine low
     density lipoprotein receptor and in bovine thrombomodulin."
     J. Biol. Chem. 263:21-24(1988).
     PubMed=2826439

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{END}