Variant position: 223 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 ALGWRDTWAFVGRKGGPVFG EKHSKSPALSSWGDPVLLKTD
Mouse ALGWRDTWAFVGRKGGPVLG EKHSKSPALSSWGDPVLLKTD
Rat ALGWRDTWAFVGRKGGPVLG EKHSKSPALSSWGDPVLLKTD
Bovine ALGWRDTWAFVGRKGGPVLG EKHSKSPALSSWGDPVLLKTD
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
92 – 288 Carbohydrate-binding stem domain
207 – 207 Carbohydrate
207 – 207 R -> A. Decreased enzyme activity. Impairs protein stability.
220 – 226
Worldwide distribution and broader clinical spectrum of muscle-eye-brain disease.
Taniguchi K.; Kobayashi K.; Saito K.; Yamanouchi H.; Ohnuma A.; Hayashi Y.K.; Manya H.; Jin D.K.; Lee M.; Parano E.; Falsaperla R.; Pavone P.; Coster R.V.; Talim B.; Steinbrecher A.; Straub V.; Nishino I.; Topaloglu H.; Voit T.; Endo T.; Toda T.;
Hum. Mol. Genet. 12:527-534(2003)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS MDDGA3 LYS-223 AND TYR-269; VARIANT VAL-623;
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;
Structure-function analysis of human protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase 1, POMGnT1.
Akasaka-Manya K.; Manya H.; Kobayashi K.; Toda T.; Endo T.;
Biochem. Biophys. Res. Commun. 320:39-44(2004)
Cited for: IDENTIFICATION OF CATALYTIC DOMAIN; CHARACTERIZATION OF VARIANTS MDDGA3 LYS-223 AND TYR-269;
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.