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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02724: Variant p.Arg50Trp

Glycophorin-A
Gene: GYPA
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Variant information Variant position: help 50 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 Arginine (R) to Tryptophan (W) at position 50 (R50W, p.Arg50Trp). 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 large size and basic (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 Or antigen. Any additional useful information about the variant.


Sequence information Variant position: help 50 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 STSSSVTKSYISSQTNDTHK R DTYAATPRAHEVSEISVRTV 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                         STSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTV

                              EIIPHEISSKLPTQAGFISTEDPSFNTPSTRQDPSGTMYQH

Chimpanzee                    -STSSVTKSYISSETSDKHKWDTYPATPRAHEVSEIYVTTV

Mouse                         QITTPVVASTVGNPNQHSATMSTPAIHVSTYHTAPTEVSAA

Pig                           -TETPVTGEQGSATPGNVSNATVTAGKPSATSPGVMTIKNT

Horse                         TITSAATPTFTTEQDGREQ----------------------

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 30 – 30 O-linked (GalNAc...) serine
Glycosylation 31 – 31 O-linked (GalNAc...) threonine
Glycosylation 32 – 32 O-linked (GalNAc...) serine
Glycosylation 36 – 36 O-linked (GalNAc...) threonine
Glycosylation 38 – 38 O-linked (GalNAc...) serine
Glycosylation 41 – 41 O-linked (GalNAc...) serine
Glycosylation 44 – 44 O-linked (GalNAc...) threonine
Glycosylation 45 – 45 N-linked (GlcNAc...) asparagine
Glycosylation 52 – 52 O-linked (GalNAc...) threonine
Glycosylation 56 – 56 O-linked (GalNAc...) threonine
Glycosylation 63 – 63 O-linked (GalNAc...) serine
Glycosylation 66 – 66 O-linked (GalNAc...) serine
Glycosylation 69 – 69 O-linked (GalNAc...) threonine



Literature citations
No reference for the current variant in UniProtKB/Swiss-Prot.
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.