LH1 GLY678ARG
SiMPLOD ID   This is the unique identifier for this mutation in the SiMPLOD database. Please use this identifier when linking information described in SiMPLOD about this mutation.	SiMPLOD1-107
Isoenzyme   Follow the links to gather information about the LH1 isoenzyme	Lysyl Hydroxylase 1 (human) - UniProt - Full Info
Nucleotide mutation   Follow the links to explore annotated information about the significance of the PLOD1 c.2032G>A mutation	PLOD1 NM_000302.2:c.2032G>A - NCBI RefSeq NCBI SNP: rs121913551 NCBI ClinVar: 14366
Mutation type   Current information about the clinical implications of the mutation	Conflicting interpretations of pathogenicity
LOVD   Link to Leiden Open Variation Database (LOVD)	c.2032G>A
Disease Phenotype   Annotated information about disease phenotypes associated to this mutation	Kyphoscoliotic Ehlers-Danlos Syndrome (Type VIa) Link1 Link2
Clinical Databases   Link to clinical databases, including OMIM (Online Mendelian Inheritance in Man), Orphanet, ICD-10 (International Statistical Classification of Diseases and Related Health Problems, rev. 10), MeSH (Medical Subject Headings)	OMIM: 225400 Orphanet: ORPHA:1900 ICD-10: Q79.6 MeSH: C536198
Evidence at protein level   Based on available structural and biochemical information, a statement about the existence of an LH enzyme variant bearing the described mutation is provided	This variant MAY EXIST at the protein level, although no experimental evidence is currently available to support its existence.
References   Publications (and associated links) describing the mutation	Ha et al., 1994 - DOI - PubMed Yeowell et al., 2000 - DOI - PubMed Rohrbach et al., 2011 - DOI - PubMed Miller et al., 1979 - DOI - PubMed Dembure et al., 1984 - PubMed Dembure et al., 1987 - DOI - PubMed
Notes from publications   A curated excerpt with information about the mutation from the publications found above	Ha et al. described the Gly678Arg mutation in a patient with Ehlers-Danlos syndrome type VI (EDS VI).The mutation is the responsible (together with Glu532Del) of the patient's decreased lysyl-hydroxylase activity (24% of normal). Gly678Arg mutation was described also by Rohrbach et al. in three patients from the same family (consanguineous parents) with EDS VI. Clinical features are presented.
Related Entries   A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD1-887: LH1 GLY678GLY (SNP)
Last Update   An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure	2021-06-23 08:38:51
The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH1 (generated using the crystal structure of full-length human LH3 as template). You may select a different PDB model file to visualize the mutation(s) using the drop-down menu below (page will refresh): LH1 homology modelLH3 with Fe2+ and 2-OG (PDB 6FXK)