MOD_ASX_betaOH_EGF
ELM server details
ELM
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Functional site class:
 ASX EGF hydroxylation
Functional site description:
 Some EGF domains are post translationally hydroxylated at conserved aspartate or asparagine residues, forming erythro-beta-hydroxyaspartic acid or erythro-beta-hydroxyasparagine
ELM(s): MOD_ASX_betaOH_EGF
MOD_ASX_betaOH_EGF description: ASX hydroxylation of some EGF domains.
Pattern: C.[DN].{4}[FY].C.C
Present in taxon(s): Metazoa  
Not represented in taxon(s):

o Abstract

Some EGF(epidermal growth factor)-type domains in extracellular proteins have conserved ASP/ASN residues that are substrates of an endoplasmic reticulum membrane-bound enzyme aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16). The ASX residues are hydroxylated by the enzyme, forming the beta hydroxylated residue. Many blood coagulation factors, the LDL receptor, BMP 1, Thrombomodulin, EGF have the modification. Drosophila proteins involved in development include crumbs, delta, notch, serrate, slit and tolloid. May be restricted to metazoans. The Prosite entry PS00010 lists many modified proteins.

o Selected references

o This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.

Biological Process
  cell differentiation
  development
Cellular Component
  endoplasmic reticulum
  extracellular
Molecular Function

 

o Instances for MOD_ASX_betaOH_EGF

No instances annotated