Variant position: 333 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 507 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 CIKLILQPSSK-GFKFTLVSC ALSFFLFSFQVHEKSILLVSL
Mouse CIKLTVRPSCK-GFRFTLVSC ALSFFLFSFQVHEKSILLVS
Rat CIKLTVQPSAK-GFRFTLVSC ALSFFLFSFQVHEKSILLVS
Chicken CIKLTVQPSLR-GFKLTLVSC ALSFFLFSFQVHEKSILLVS
Caenorhabditis elegans LLVLFLRPTEK-QFRISLTAT GLSFFLFSFHVHEKTILLAA
Drosophila NVLLFRRRTNV-GFLLALFNT SLAFFLFSFQVHEKTILLTA
Slime mold VYGIKRIPKNKFVFIHSLINS SFSFFLFSFQVHEKTILLVS
Baker's yeast MIMTLLHPKKH-LLPYVLIAC SMSFFLFSFQVHEKTILIPL
Fission yeast CVILFLYPRKR-LLALGFASA SWGFFLFSFQVHEKSVLLPL
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 – 507 Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
324 – 344 Helical
A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic.
Imbach T.; Burda P.; Kuhnert P.; Wevers R.A.; Aebi M.; Berger E.G.; Hennet T.;
Proc. Natl. Acad. Sci. U.S.A. 96:6982-6987(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT CDG1C VAL-333; VARIANT PHE-304;
Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation.
Westphal V.; Murch S.; Kim S.; Srikrishna G.; Winchester B.; Day R.; Freeze H.H.;
Am. J. Pathol. 157:1917-1925(2000)
Cited for: VARIANTS CDG1C HIS-131; ARG-308 AND VAL-333;
Multi-allelic origin of congenital disorder of glycosylation (CDG)-Ic.
Imbach T.; Gruenewald S.; Schenk B.; Burda P.; Schollen E.; Wevers R.A.; Jaeken J.; de Klerk J.B.C.; Berger E.G.; Matthijs G.; Aebi M.; Hennet T.;
Hum. Genet. 106:538-545(2000)
Cited for: VARIANTS CDG1C VAL-333 AND PRO-478; VARIANT PHE-304;
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