UniProtKB/Swiss-Prot P02724: Variant p.Pro73Ser

Glycophorin-A
Gene: GYPA
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Variant information Variant position:

73 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Proline (P) to Serine (S) at position 73 (P73S, p.Pro73Ser). 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:

Change from medium size and hydrophobic (P) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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:

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:

In Os(a) antigen. Any additional useful information about the variant.

Sequence information Variant position:

73 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:

YAATPRAHEVSEISVRTVYP P EEETGERVQLAHHFSEPEIT 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                         YAATPRAHEVSEISVRTVY---PPEEET-GERVQLAHHFSEPEIT

                              SFNTPSTRQDPSGTMYQHL---PDGGQK--ARQQLVHIFSE

Chimpanzee                    YPATPRAHEVSEIYVTTVY---PPEEEN-GEGVQLVHRFSE

Mouse                         PAIHVSTYHTAPTEVSAAFEEQPVSPHIGGMPSPIQHDFPA

Pig                           TAGKPSATSPGVMTIKNTT---AVVQKETGVPESYHQDFSH

Horse                         -----------------------------GDGLQLAHDFSQ

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	20 – 150	Glycophorin-A
Topological domain	20 – 91	Extracellular
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
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.

Literature citations
The low-frequency MNS blood group antigens Ny(a) (MNS18) and Os(a) (MNS38) are associated with GPA amino acid substitutions.
Daniels G.L.; Bruce L.J.; Mawby W.J.; Green C.A.; Petty A.; Okubo Y.; Kornstad L.; Tanner M.J.;
Transfusion 40:555-559(2000)
Cited for: VARIANTS GLU-46 AND SER-73;

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.