UniProtKB/Swiss-Prot P02724: Variant p.Gly24Glu

Glycophorin-A
Gene: GYPA
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Variant information Variant position:

24 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 Glycine (G) to Glutamate (E) at position 24 (G24E, p.Gly24Glu). 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 glycine (G) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-2 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 N antigen, M(c) antigen and M(g) antigen. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs7687256 [ dbSNP | Ensembl ]

Sequence information Variant position:

24 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:

KIIFVLLLSEIVSISASSTT G VAMHTSTSSSVTKSYISSQT 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                         KIIFVLLLSEIVSIS-------------ASSTTGVAMHTSTSSSVTKSYISSQT

                              KIVIVLLLSGYISTQ---------------------DVTEI

Chimpanzee                    KIIFVLLLSAIVSIS-------------ASSTTEVAMHT-S

Mouse                         STAAVTTSGHSLTTTFHIPSSQHYQEEHSPSLSGSDSLLQI

Pig                           ----------------------------------------T

Horse                         ---------QTIATG-------------SPPIAGTSDLSTI

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	21 – 21	O-linked (GalNAc...) serine
Glycosylation	22 – 22	O-linked (GalNAc...) threonine
Glycosylation	23 – 23	O-linked (GalNAc...) threonine
Glycosylation	29 – 29	O-linked (GalNAc...) threonine
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
Alternative sequence	1 – 26	Missing. In isoform 2.
Alternative sequence	13 – 45	Missing. In isoform 3.

Literature citations
Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta.
Tate C.G.; Tanner M.J.A.;
Biochem. J. 254:743-750(1988)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS N LEU-20 AND GLU-24; Generation and annotation of the DNA sequences of human chromosomes 2 and 4.
Hillier L.W.; Graves T.A.; Fulton R.S.; Fulton L.A.; Pepin K.H.; Minx P.; Wagner-McPherson C.; Layman D.; Wylie K.; Sekhon M.; Becker M.C.; Fewell G.A.; Delehaunty K.D.; Miner T.L.; Nash W.E.; Kremitzki C.; Oddy L.; Du H.; Sun H.; Bradshaw-Cordum H.; Ali J.; Carter J.; Cordes M.; Harris A.; Isak A.; van Brunt A.; Nguyen C.; Du F.; Courtney L.; Kalicki J.; Ozersky P.; Abbott S.; Armstrong J.; Belter E.A.; Caruso L.; Cedroni M.; Cotton M.; Davidson T.; Desai A.; Elliott G.; Erb T.; Fronick C.; Gaige T.; Haakenson W.; Haglund K.; Holmes A.; Harkins R.; Kim K.; Kruchowski S.S.; Strong C.M.; Grewal N.; Goyea E.; Hou S.; Levy A.; Martinka S.; Mead K.; McLellan M.D.; Meyer R.; Randall-Maher J.; Tomlinson C.; Dauphin-Kohlberg S.; Kozlowicz-Reilly A.; Shah N.; Swearengen-Shahid S.; Snider J.; Strong J.T.; Thompson J.; Yoakum M.; Leonard S.; Pearman C.; Trani L.; Radionenko M.; Waligorski J.E.; Wang C.; Rock S.M.; Tin-Wollam A.-M.; Maupin R.; Latreille P.; Wendl M.C.; Yang S.-P.; Pohl C.; Wallis J.W.; Spieth J.; Bieri T.A.; Berkowicz N.; Nelson J.O.; Osborne J.; Ding L.; Meyer R.; Sabo A.; Shotland Y.; Sinha P.; Wohldmann P.E.; Cook L.L.; Hickenbotham M.T.; Eldred J.; Williams D.; Jones T.A.; She X.; Ciccarelli F.D.; Izaurralde E.; Taylor J.; Schmutz J.; Myers R.M.; Cox D.R.; Huang X.; McPherson J.D.; Mardis E.R.; Clifton S.W.; Warren W.C.; Chinwalla A.T.; Eddy S.R.; Marra M.A.; Ovcharenko I.; Furey T.S.; Miller W.; Eichler E.E.; Bork P.; Suyama M.; Torrents D.; Waterston R.H.; Wilson R.K.;
Nature 434:724-731(2005)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANTS N LEU-20 AND GLU-24; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1); VARIANT ALA-13; VARIANTS N LEU-20 AND GLU-24; Mg and Mc: mutations within the amino-terminal region of glycophorin A.
Furthmayr H.; Metaxas M.N.; Metaxas-Buhler M.;
Proc. Natl. Acad. Sci. U.S.A. 78:631-635(1981)
Cited for: PARTIAL PROTEIN SEQUENCE; VARIANT M(C) GLU-24;

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.