Variant position: 490 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 EKLWDWDMWMRMPEQRRGRE CIIPDVSRSYHFGIVGLNMNG
Mouse EKLWDWDMWMRMPEQRRGRE CIIPDVSRSYHFGIVGLNMNG
Rat EKLWDWDMWMRMPEQRRGRE CIIPDVSRSYHFGIVGLNMNG
Bovine EKLWDWDMWMRMPEQRRGRE CIIPDVSRSYHFGIVGLNMNG
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
421 – 490
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
POMGnT1 mutation and phenotypic spectrum in muscle-eye-brain disease.
Diesen C.; Saarinen A.; Pihko H.; Rosenlew C.; Cormand B.; Dobyns W.B.; Dieguez J.; Valanne L.; Joensuu T.; Lehesjoki A.-E.;
J. Med. Genet. 41:E115-E115(2004)
Cited for: VARIANTS MDDGA3 SER-425 AND TYR-490;
POMGnT1 mutations in congenital muscular dystrophy: genotype-phenotype correlation and expanded clinical spectrum.
Biancheri R.; Bertini E.; Falace A.; Pedemonte M.; Rossi A.; D'Amico A.; Scapolan S.; Bergamino L.; Petrini S.; Cassandrini D.; Broda P.; Manfredi M.; Zara F.; Santorelli F.M.; Minetti C.; Bruno C.;
Arch. Neurol. 63:1491-1495(2006)
Cited for: VARIANTS MDDGA3 ARG-198 AND TYR-490; VARIANT MDDGB3 GLN-311;
Brain involvement in muscular dystrophies with defective dystroglycan glycosylation.
Clement E.; Mercuri E.; Godfrey C.; Smith J.; Robb S.; Kinali M.; Straub V.; Bushby K.; Manzur A.; Talim B.; Cowan F.; Quinlivan R.; Klein A.; Longman C.; McWilliam R.; Topaloglu H.; Mein R.; Abbs S.; North K.; Barkovich A.J.; Rutherford M.; Muntoni F.;
Ann. Neurol. 64:573-582(2008)
Cited for: VARIANTS MDDGA3 PRO-176; HIS-367 AND HIS-427; VARIANT MDDGB3 TYR-490;
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.