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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02724: Variant p.Thr77Ile

Glycophorin-A
Gene: GYPA
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Variant information Variant position: help 77 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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: help From Threonine (T) to Isoleucine (I) at position 77 (T77I, p.Thr77Ile). 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: help Change from medium size and polar (T) to medium size and hydrophobic (I) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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).
More information can be found on the following page

Polymorphism: help Along with GYPB, GYPA is responsible for the MNS blood group system [MIM:111300]. The molecular basis of the GPA M/N bloodgroup antigen is a variation at positions 20 and 24. Ser-20 and Gly-24 correspond to M (shown); 'Leu-20' and 'Glu-24' correspond to N.GYPA polymorphisms are involved in resistance to malaria [MIM:611162]. - Additional information on the polymorphism described.
Variant description: help In Mt(a) antigen. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 77 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 150 The length of the canonical sequence.
Location on the sequence: help PRAHEVSEISVRTVYPPEEE T GERVQLAHHFSEPEITLIIF 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         PRAHEVSEISVRTVY---PPEEET-GERVQLAHHFSEPEITLIIF

                              PSTRQDPSGTMYQHL---PDGGQK--ARQQLVHIFSEPVII

Chimpanzee                    PRAHEVSEIYVTTVY---PPEEEN-GEGVQLVHRFSEPEIT

Mouse                         VSTYHTAPTEVSAAFEEQPVSPHIGGMPSPIQHDFPALVMI

Pig                           PSATSPGVMTIKNTT---AVVQKETGVPESYHQDFSHAEIT

Horse                         -------------------------GDGLQLAHDFSQPVIT

Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 20 – 150 Glycophorin-A
Topological domain 20 – 91 Extracellular
Glycosylation 63 – 63 O-linked (GalNAc...) serine
Glycosylation 66 – 66 O-linked (GalNAc...) serine
Glycosylation 69 – 69 O-linked (GalNAc...) threonine
Mutagenesis 87 – 87 F -> C. Diminishes dimerization.
Mutagenesis 88 – 88 S -> C. Diminishes dimerization.
Mutagenesis 90 – 90 P -> C. Diminishes dimerization.
Mutagenesis 91 – 91 E -> C. Diminishes dimerization.
Mutagenesis 94 – 94 L -> I. Diminishes dimerization.
Mutagenesis 95 – 95 I -> A. Diminishes dimerization.



Literature citations
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 TYR-66 AND ILE-77;
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.