UniProtKB/Swiss-Prot P16442 : Variant p.Phe216Ile
Histo-blood group ABO system transferase
Feedback ?
Variant information
Variant position:
216
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:
The variants are classified into three categories: LP/P, LB/B and US.LP/P: likely pathogenic or pathogenic. LB/B: likely benign or benign. US: uncertain significance
Residue change:
216 (F216I, p.Phe216Ile).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:
The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another: Lowest score: -4 (low probability of substitution).Highest score: 11 (high probability of substitution).following page
Polymorphism:
616093 ]. The ABO blood group system is one of the most important blood group systems in transfusion medicine. The ABO blood group involves 3 carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal). There are only 4 amino acid differences between A and B transferases in the catalytic domain, two of which (Leu266Met and Gly268Ala) are primarily responsible for the substrate specificity. The group O phenotype results from variations in ABO that cause a loss of glycosyltransferase activity. The most common group O allele results from a single nucleotide deletion near the 5' end of the gene (NM_020469.2:c.261del) that causes a frameshift and early termination with no active enzyme production (p.Thr88Profs*31).
Additional information on the polymorphism described.
Other resources:
Links to websites of interest for the variant.
Sequence information
Variant position:
216
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:
F RDHVGVEILTPLFGTLHPGF
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 CERRFLSEVDYLVCVDVDMEF RDHVGVEILTPLFGTLHPGF
Mouse SERRFLREVDYLVCADADMKF SDHVGVEILSTFFGTLHPGF
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
Chain
1 – 354 Histo-blood group ABO system transferase
Chain
54 – 354 Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form
Topological domain
54 – 354 Lumenal
Binding site
211 – 211
Binding site
213 – 213
Binding site
233 – 233
Mutagenesis
214 – 214 M -> TV. Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized.
Mutagenesis
234 – 234 P -> S. Altered substrate specificity in group B transferase.
Beta strand
212 – 216
Literature citations
Submission
SeattleSNPs variation discovery resource;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; POLYMORPHISM; VARIANTS ARG-35; PHE-36; HIS-63; SER-74; LEU-156; HIS-161; GLY-176; CYS-199; ILE-216; SER-235; MET-266; ALA-268 AND MET-277;
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.;
Blood 88:2732-2737(1996)
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;
Disclaimer:
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.
