Variant position: 493 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 660 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 WDWDMWMRMPEQRRGRECII PDVSRSYHFGIVGLNMNGYFH
Mouse WDWDMWMRMPEQRRGRECII PDVSRSYHFGIVGLNMNGYFH
Rat WDWDMWMRMPEQRRGRECII PDVSRSYHFGIVGLNMNGYFH
Bovine WDWDMWMRMPEQRRGRECII PDVSRSYHFGIVGLNMNGYFH
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
1 – 660 Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
59 – 660 Lumenal
300 – 646 Catalytic
500 – 500 Manganese
473 – 473 W -> A. Abolishes in vitro enzyme activity; when associated with A-477.
474 – 474 D -> A. Nearly abolishes enzyme activity.
477 – 477 M -> A. Abolishes in vitro enzyme activity; when associated with A-473.
481 – 481 M -> A. Decreased enzyme activity.
507 – 507 N -> A. Abolishes enzyme activity.
489 – 500
Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1.
Yoshida A.; Kobayashi K.; Manya H.; Taniguchi K.; Kano H.; Mizuno M.; Inazu T.; Mitsuhashi H.; Takahashi S.; Takeuchi M.; Herrmann R.; Straub V.; Talim B.; Voit T.; Topaloglu H.; Toda T.; Endo T.;
Dev. Cell 1:717-724(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); FUNCTION; CATALYTIC ACTIVITY; PATHWAY; SUBCELLULAR LOCATION; TOPOLOGY; BIOPHYSICOCHEMICAL PROPERTIES; TISSUE SPECIFICITY; VARIANTS MDDGA3 ARG-493 AND ASN-550; VARIANT VAL-623; MUTAGENESIS OF 1-MET--ILE-65;
Loss-of-function of an N-acetylglucosaminyltransferase, POMGnT1, in muscle-eye-brain disease.
Manya H.; Sakai K.; Kobayashi K.; Taniguchi K.; Kawakita M.; Toda T.; Endo T.;
Biochem. Biophys. Res. Commun. 306:93-97(2003)
Cited for: CHARACTERIZATION OF VARIANTS MDDGA3 LYS-223; TYR-269 AND ARG-493; CATALYTIC ACTIVITY; COFACTOR;
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.