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)
|
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. |
6 Instances for MOD_ASX_betaOH_EGF
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, Name | Start | End | Subsequence | Logic | #Ev. | Organism | Notes |
---|---|---|---|---|---|---|---|
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-the Eukaryotic Linear Motif resource-2024 update.
(PMID:37962385)
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement