Variant position: 77 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 150 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 PRAHEVS-------EISVRTVYPPEEE T-GERVQLAHHFSEPEITLIIF
Chimpanzee PRAHEVS-------EIYVTTVYPPEEE N-GEGVQLVHRFSE
Mouse PAIHVSTYHTAPTEVSAAFEEQPVSPH IGGMPSPIQHDFPA
Pig PSATSPG-------VMTIKNTTAVVQK ETGVPESYHQDFSH
Horse PTFTTEQ-----------------DGR EQGDGLQLAHDFSQ
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
20 – 150 Glycophorin-A
20 – 91 Extracellular
63 – 63 O-linked (GalNAc...) serine
66 – 66 O-linked (GalNAc...) serine
69 – 69 O-linked (GalNAc...) threonine
87 – 87 F -> C. Diminishes dimerization.
88 – 88 S -> C. Diminishes dimerization.
90 – 90 P -> C. Diminishes dimerization.
91 – 91 E -> C. Diminishes dimerization.
94 – 94 L -> I. Diminishes dimerization.
95 – 95 I -> A. Diminishes dimerization.
The MNS blood group antigens, Vr (MNS12) and Mt(a) (MNS14), each arise from an amino acid substitution on glycophorin A.
Storry J.R.; Coghlan G.; Poole J.; Figueroa D.; Reid M.E.;
Vox Sang. 78:52-56(2000)
Cited for: VARIANTS VR TYR-66 AND MT(A) ILE-77;
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