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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 |
|---|---|
| ELMs: | MOD_ASX_betaOH_EGF |
| Description: | ASX hydroxylation of some EGF domains. |
| Pattern: | C.([DN]).{4,4}[FY].C.C (Probability: 0.0000000) |
| Present in taxons: | Metazoa |
| Interaction Domain: |
Asp_Arg_Hydrox (PF05118) |
|
| 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. |
4 GO-Terms:
Please cite: ELM - the database of eukaryotic linear motifs (PMID:22110040)