Variant position: 41 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 VSTSSMGTLPKRVKIVEVGP RDGLQNEKNIVSTPVKIKLID
Mouse VSTSSMGTLPKQVKIVEVGP RDGLQNEKSIVPTPVKIRLID
Rat ASTSSMGTLPKRVKIVEVGP RDGLQNEKSIVPTPVKIKLID
Bovine VSTSSVGTFPKQVKIVEVGP RDGLQNEKNIVPTPVKIKLID
Chicken -------AFPQRVKVVEVGP RDGLQNEKSVVPTPVKIRLID
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
42 – 42 Divalent metal cation
41 – 41 Substrate
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.
39 – 41
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;
Mutations underlying 3-hydroxy-3-methylglutaryl CoA lyase deficiency in the Saudi population.
Al-Sayed M.; Imtiaz F.; Alsmadi O.A.; Rashed M.S.; Meyer B.F.;
BMC Med. Genet. 7:86-86(2006)
Cited for: VARIANT HMGCLD GLN-41;
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.