SiMPLOD v. 0.6.2 alpha

LH1 TYR142END

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.
SiMPLOD1-208

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 426T>A mutation
PLOD1 NM_000302.2:426T>A - NCBI RefSeq

Mutation type
  Current information about the clinical implications of the mutation
Uncertain significance

LOVD
  Link to Leiden Open Variation Database (LOVD)
c.426T>A

Disease Phenotype
  Annotated information about disease phenotypes associated to this mutation
Ehlers-Danlos syndrome, cardiovascular phenotype Link1

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
Warning: this variant incorporates a premature truncation of the aminoacid sequence at residue 142, and may result in misfolding and/or complete absence of the enzyme.

This variant is EXTREMELY UNLIKELY to be compatible with a folded LH enzyme. The representation shown in the structure viewer is therefore for mere display purposes and does not refer to an actual predicted existing protein product.

References
  Publications (and associated links) describing the mutation
Yeowell et al., 2000 - DOI - PubMed

Notes from publications
  A curated excerpt with information about the mutation from the publications found above
Screening PLOD1 cDNA in fibroblast from Ehlers-Danlos syndrome type VI (EDS VI) patients Yeowell et al. identified four novel disease causing mutations. Among these, the point mutation c.450T>A (c.426T>A) in exon 4 was predicted to produce the premature termination codon Tyr142end.

Structural Observations
  An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure

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 TYR142END
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.	SiMPLOD1-208
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 426T>A mutation	PLOD1 NM_000302.2:426T>A - NCBI RefSeq
Mutation type Current information about the clinical implications of the mutation	Uncertain significance
LOVD Link to Leiden Open Variation Database (LOVD)	c.426T>A
Disease Phenotype Annotated information about disease phenotypes associated to this mutation	Ehlers-Danlos syndrome, cardiovascular phenotype Link1
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	Warning: this variant incorporates a premature truncation of the aminoacid sequence at residue 142, and may result in misfolding and/or complete absence of the enzyme. This variant is EXTREMELY UNLIKELY to be compatible with a folded LH enzyme. The representation shown in the structure viewer is therefore for mere display purposes and does not refer to an actual predicted existing protein product.
References Publications (and associated links) describing the mutation	Yeowell et al., 2000 - DOI - PubMed
Notes from publications A curated excerpt with information about the mutation from the publications found above	Screening PLOD1 cDNA in fibroblast from Ehlers-Danlos syndrome type VI (EDS VI) patients Yeowell et al. identified four novel disease causing mutations. Among these, the point mutation c.450T>A (c.426T>A) in exon 4 was predicted to produce the premature termination codon Tyr142end.
Structural Observations An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure
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):