Variant position: 223 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 738 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 GLREKLSLNLDHKSRIFQNL NGALDEVVLKFDRNRVRIRNV
Mouse GLREKLKLSLDHKSRIFQNL NGALDEVILKFDQNRVRIRNV
Rat GLREKLKLSLDHKSRIFQNL NGALDEVVLKFDQNRVRIRNV
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
25 – 738 Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
25 – 290 Required for glycosyltransferase activity
208 – 208 L -> I. Reduced glucosyltransferase activity.
Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3.
Scietti L.; Chiapparino A.; De Giorgi F.; Fumagalli M.; Khoriauli L.; Nergadze S.; Basu S.; Olieric V.; Cucca L.; Banushi B.; Profumo A.; Giulotto E.; Gissen P.; Forneris F.;
Nat. Commun. 9:3163-3163(2018)
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-738 IN COMPLEX WITH IRON; 2-OXOGLUTARATE; MANGANESE AND UDP-GLUCOSE; CATALYTIC ACTIVITY; FUNCTION; COFACTOR; SUBUNIT; DOMAIN; GLYCOSYLATION AT ASN-63 AND ASN-548; DISULFIDE BONDS; CHARACTERIZATION OF VARIANT LH3 DEFICIENCY SER-223; MUTAGENESIS OF TRP-75; TYR-114; THR-672; ARG-714 AND LEU-715;
A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene.
Salo A.M.; Cox H.; Farndon P.; Moss C.; Grindulis H.; Risteli M.; Robins S.P.; Myllylae R.;
Am. J. Hum. Genet. 83:495-503(2008)
Cited for: VARIANT LH3 DEFICIENCY SER-223; CHARACTERIZATION OF VARIANT LH3 DEFICIENCY SER-223; CATALYTIC ACTIVITY; FUNCTION;
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