LH1 ALA667THR
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.	SiMPLOD1-13
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.1999G>A mutation	PLOD1 NM_000302.2:c.1999G>A - NCBI RefSeq NCBI SNP: rs199730384
Mutation type   Current information about the clinical implications of the mutation	Pathogenic
LOVD   Link to Leiden Open Variation Database (LOVD)	c.1999G>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	Giunta et al., 2005 - DOI - PubMed
Notes from publications   A curated excerpt with information about the mutation from the publications found above	Giunta et al. studied 9 patients from 12 unrelated families identifying novel mutations causing Ehlers-Danlos syndrome (EDS VIA). Ala667 and His706Arg mutation are respectively caused by the transitions c.1890G>A and c.2008A>G (c.2117A>G). The authors show that both aminoacids are highly conserved between the three human isoforms (PLOD1, PLOD2, and PLOD3) and across several species (bovine, mouse, rat, chicken, xenopus, fruit fly and C. elegans). The analysis of a control population further identify these mutations as the only responsible for impaired lysyl hydroxylase activity in the two patients under investigation.
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)