Variant position: 214 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 354 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 DFCERRFLSEVDYLVCVDVD MEFRDHVGVEILTPLFGTLHP
Mouse HFSERRFLREVDYLVCADAD MKFSDHVGVEILSTFFGTLHP
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 – 354 Histo-blood group ABO system transferase
54 – 354 Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form
54 – 354 Lumenal
211 – 211 Manganese
213 – 213 Manganese
233 – 233 Glycoprotein fucosyl-galactosyl group
214 – 214 M -> TV. Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized.
234 – 234 P -> S. Alters substrate specificity of group B transferase.
212 – 216
Molecular genetic analysis of variant phenotypes of the ABO blood group system.
Ogasawara K.; Yabe R.; Uchikawa M.; Saitou N.; Bannai M.; Nakata K.; Takenaka M.; Fujisawa K.; Ishikawa Y.; Juji T.; Tokunaga K.;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354; POLYMORPHISM; VARIANTS LEU-156; GLY-176; ARG-214; ILE-216; ASP-223; SER-235; MET-266; ALA-268; MET-277; ASN-291; GLY-352 AND TRP-352;
Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif.
Persson M.; Letts J.A.; Hosseini-Maaf B.; Borisova S.N.; Palcic M.M.; Evans S.V.; Olsson M.L.;
J. Biol. Chem. 282:9564-9570(2007)
Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 64-354 OF MUTANTS ARG-214 AND THR-214; COFACTOR; CHARACTERIZATION OF VARIANT ARG-214; MUTAGENESIS OF MET-214; CATALYTIC ACTIVITY;
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