UniProtKB/Swiss-Prot P02724: Variant p.Leu20Ser

Glycophorin-A
Gene: GYPA
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Variant information Variant position:

20 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 Leucine (L) to Serine (S) at position 20 (L20S, p.Leu20Ser). 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 (L) to small size and polar (S) 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; 'Leu-20' and 'Glu-24' correspond to N (shown).GYPA polymorphisms are involved in resistance to malaria [MIM:611162]. - Additional information on the polymorphism described.
Variant description:

In M antigen. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs7682260 [ dbSNP | Ensembl ]

Sequence information Variant position:

20 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:

MYGKIIFVLLLSEIVSISA L STTEVAMHTSTSSSVTKSYI 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                         MYGKIIFVLLLSEIVSIS-------------ASSTTGVAMHTSTSSSVTKSYI

                              MYEKIVIVLLLSGYISTQ---------------------D

Chimpanzee                    MYGKIIFVLLLSAIVSIS-------------ASSTTEVAM

Mouse                         MTESTAAVTTSGHSLTTTFHIPSSQHYQEEHSPSLSGSDS

Pig                           ----------------------------------------

Horse                         ------------QTIATG-------------SPPIAGTSD

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
Alternative sequence	1 – 26	Missing. In isoform 2.
Alternative sequence	13 – 45	Missing. In isoform 3.

Literature citations
Isolation and characterization of human glycophorin A cDNA clones by a synthetic oligonucleotide approach: nucleotide sequence and mRNA structure.
Siebert P.D.; Fukuda M.;
Proc. Natl. Acad. Sci. U.S.A. 83:1665-1669(1986)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS ALA-13; SER-20 AND GLY-24; Structural organization of glycophorin A and B genes: glycophorin B gene evolved by homologous recombination at Alu repeat sequences.
Kudo S.; Fukuda M.;
Proc. Natl. Acad. Sci. U.S.A. 86:4619-4623(1989)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS ALA-13; SER-20 AND GLY-24; The mechanism of production of multiple mRNAs for human glycophorin A.
Jawad K.; Burness T.H.;
Nucleic Acids Res. 18:5829-5836(1990)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS ALA-13; SER-20 AND GLY-24; Characterization of glycophorin A transcripts: control by the common erythroid-specific promoter and alternative usage of different polyadenylation signals.
Kudo S.; Onda M.; Fukuda M.;
J. Biochem. 116:183-192(1994)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS ALA-13; SER-20 AND GLY-24; Complete sequencing and characterization of 21,243 full-length human cDNAs.
Ota T.; Suzuki Y.; Nishikawa T.; Otsuki T.; Sugiyama T.; Irie R.; Wakamatsu A.; Hayashi K.; Sato H.; Nagai K.; Kimura K.; Makita H.; Sekine M.; Obayashi M.; Nishi T.; Shibahara T.; Tanaka T.; Ishii S.; Yamamoto J.; Saito K.; Kawai Y.; Isono Y.; Nakamura Y.; Nagahari K.; Murakami K.; Yasuda T.; Iwayanagi T.; Wagatsuma M.; Shiratori A.; Sudo H.; Hosoiri T.; Kaku Y.; Kodaira H.; Kondo H.; Sugawara M.; Takahashi M.; Kanda K.; Yokoi T.; Furuya T.; Kikkawa E.; Omura Y.; Abe K.; Kamihara K.; Katsuta N.; Sato K.; Tanikawa M.; Yamazaki M.; Ninomiya K.; Ishibashi T.; Yamashita H.; Murakawa K.; Fujimori K.; Tanai H.; Kimata M.; Watanabe M.; Hiraoka S.; Chiba Y.; Ishida S.; Ono Y.; Takiguchi S.; Watanabe S.; Yosida M.; Hotuta T.; Kusano J.; Kanehori K.; Takahashi-Fujii A.; Hara H.; Tanase T.-O.; Nomura Y.; Togiya S.; Komai F.; Hara R.; Takeuchi K.; Arita M.; Imose N.; Musashino K.; Yuuki H.; Oshima A.; Sasaki N.; Aotsuka S.; Yoshikawa Y.; Matsunawa H.; Ichihara T.; Shiohata N.; Sano S.; Moriya S.; Momiyama H.; Satoh N.; Takami S.; Terashima Y.; Suzuki O.; Nakagawa S.; Senoh A.; Mizoguchi H.; Goto Y.; Shimizu F.; Wakebe H.; Hishigaki H.; Watanabe T.; Sugiyama A.; Takemoto M.; Kawakami B.; Yamazaki M.; Watanabe K.; Kumagai A.; Itakura S.; Fukuzumi Y.; Fujimori Y.; Komiyama M.; Tashiro H.; Tanigami A.; Fujiwara T.; Ono T.; Yamada K.; Fujii Y.; Ozaki K.; Hirao M.; Ohmori Y.; Kawabata A.; Hikiji T.; Kobatake N.; Inagaki H.; Ikema Y.; Okamoto S.; Okitani R.; Kawakami T.; Noguchi S.; Itoh T.; Shigeta K.; Senba T.; Matsumura K.; Nakajima Y.; Mizuno T.; Morinaga M.; Sasaki M.; Togashi T.; Oyama M.; Hata H.; Watanabe M.; Komatsu T.; Mizushima-Sugano J.; Satoh T.; Shirai Y.; Takahashi Y.; Nakagawa K.; Okumura K.; Nagase T.; Nomura N.; Kikuchi H.; Masuho Y.; Yamashita R.; Nakai K.; Yada T.; Nakamura Y.; Ohara O.; Isogai T.; Sugano S.;
Nat. Genet. 36:40-45(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1); VARIANTS ALA-13; SER-20 AND GLY-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); VARIANTS ALA-13; SER-20 AND GLY-24; Molecular biological study of the structure and expression of human glycophorin A.
Siebert P.D.; Fukuda M.;
Rev. Fr. Transfus. Immunohematol. 29:251-266(1986)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-145 (ISOFORM 1); VARIANTS ALA-13; SER-20 AND GLY-24; Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
Tomita M.; Marchesi V.T.;
Proc. Natl. Acad. Sci. U.S.A. 72:2964-2968(1975)
Cited for: PROTEIN SEQUENCE OF 20-150; VARIANTS SER-20 AND GLY-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.