LH1 ASN402ASN
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.	SiMPLOD1-60
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.1206C>T mutation	PLOD1 NM_000302.2:c.1206C>T - NCBI RefSeq NCBI SNP: rs1130529 NCBI ClinVar: 255799
Mutation type   Current information about the clinical implications of the mutation	Benign
LOVD   Link to Leiden Open Variation Database (LOVD)	c.1206C>T
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: 225320 Orphanet: ORPHA:230851 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 does not alter the aminoacid sequence of the enzyme, and therefore is expected to EXIST at the protein level, although no experimental evidence is currently available to support its existence.
References   Publications (and associated links) describing the mutation	Yip et al., 2011 - PubMed
Notes from publications   A curated excerpt with information about the mutation from the publications found above	Mutations annotated (but yet not curated) include c.1206C>[A/C/T], yielding ASN402ASN but also ASN402LYS variants.
Related Entries   A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD1-61: LH1 ASN402LYS (benign) SiMPLOD1-134: LH1 dupl326-585;TYR455THRFS (Pathogenic) SiMPLOD1-320: LH1 delta367-443 (Pathogenic)
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)