Variant position: 42 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 325 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human STSSMGTLPKRVKIVEVGPR DGLQNEKNIVSTPVKIKLIDM
Mouse STSSMGTLPKQVKIVEVGPR DGLQNEKSIVPTPVKIRLIDM
Rat STSSMGTLPKRVKIVEVGPR DGLQNEKSIVPTPVKIKLIDM
Bovine STSSVGTFPKQVKIVEVGPR DGLQNEKNIVPTPVKIKLIDM
Chicken ------AFPQRVKVVEVGPR DGLQNEKSVVPTPVKIRLIDM
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
28 – 325 Hydroxymethylglutaryl-CoA lyase, mitochondrial
33 – 300 Pyruvate carboxyltransferase
41 – 41
42 – 42
48 – 48 N6-acetyllysine; alternate
48 – 48 N6-succinyllysine; alternate
37 – 37 E -> D. Normal activity.
41 – 41 R -> M. Reduced activity, and loss of proton exchange.
42 – 42 D -> AN. Loss of activity, and reduced proton exchange rate.
42 – 45
HMG CoA lyase deficiency: identification of five causal point mutations in codons 41 and 42, including a frequent Saudi Arabian mutation, R41Q.
Mitchell G.A.; Ozand P.T.; Robert M.-F.; Ashmarina L.; Roberts J.; Gibson K.M.; Wanders R.J.; Wang S.; Chevalier I.; Ploechl E.; Miziorko H.;
Am. J. Hum. Genet. 62:295-300(1998)
Cited for: VARIANTS HMGCLD GLN-41; GLU-42; GLY-42 AND HIS-42;
Ten novel HMGCL mutations in 24 patients of different origin with 3-hydroxy-3-methyl-glutaric aciduria.
Menao S.; Lopez-Vinas E.; Mir C.; Puisac B.; Gratacos E.; Arnedo M.; Carrasco P.; Moreno S.; Ramos M.; Gil M.C.; Pie A.; Ribes A.; Perez-Cerda C.; Ugarte M.; Clayton P.T.; Korman S.H.; Serra D.; Asins G.; Ramos F.J.; Gomez-Puertas P.; Hegardt F.G.; Casals N.; Pie J.;
Hum. Mutat. 30:E520-E529(2009)
Cited for: VARIANTS HMGCLD LYS-37; GLY-42; PHE-142; TYR-174; SER-192; PHE-200 AND ARG-233; CHARACTERIZATION OF VARIANTS HMGCLD LYS-37; PHE-142; TYR-174; SER-192 AND PHE-200;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.