The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
Accession:
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 Description:
ASX hydroxylation of some EGF domains.
Pattern: C.([DN]).{4,4}[FY].C.C
Pattern Probability: 2.489e-09
Present in taxon: Metazoa
Interaction Domain:
Asp_Arg_Hydrox (PF05118) Aspartyl/Asparaginyl beta-hydroxylase (Stochiometry: 1 : 1)
o See 6 Instances for MOD_ASX_betaOH_EGF
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, and 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 4 GO-Terms:

o 6 Instances for MOD_ASX_betaOH_EGF
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
P00745 PROC
PROC_BOVIN
108 119 RGKCIDGLGGFRCDCAEGWE TP 1 Bos taurus (Cattle)
P00743 F10
FA10_BOVIN
101 112 NQGHCKDGIGDYTCTCAEGF TP 1 Bos taurus (Cattle)
P00742 F10
FA10_HUMAN
101 112 NQGKCKDGLGEYTCTCLEGF TP 1 Homo sapiens (Human)
P22457 F7
FA7_BOVIN
101 112 NGGSCEDQLRSYICFCPDGF TP 1 Bos taurus (Cattle)
P00741 F9
FA9_BOVIN
62 73 GNLERECKEEKCSFEEAREV TP 1 Bos taurus (Cattle)
P00740 F9
FA9_HUMAN
108 119 NGGSCKDDINSYECWCPFGF TP 1 Homo sapiens (Human)
Please cite: ELM 2016-data update and new functionality of the eukaryotic linear motif resource. (PMID:26615199)

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