GYPA
entrez
2993
canonical
uniprot
P02724
canonical
ensembl
ENSG00000170180
resolver
ensp
ENSP00000324483
resolver
ensp
ENSP00000426130
resolver
ensp
ENSP00000493142
resolver
ensp
ENSP00000494322
resolver
ensp
ENSP00000495922
resolver
ensp
ENSP00000496079
resolver
ensp
ENSP00000764607
resolver
enst
ENST00000512064
resolver
enst
ENST00000642295
resolver
genesymbol
GYPA
resolver
genesymbol_syn
GPA
resolver
genesymbol_syn
MNS
resolver
hgnc
HGNC:4702
resolver
uniprot
A0A0C4DFT7
resolver
uniprot
A0A2R8Y7F9
resolver
uniprot
A8K3E6
resolver
uniprot
B8Q182
resolver
uniprot
B8Q185
resolver
uniprot
E9PD10
resolver
uniprot
Q14419
resolver
uniprot
Q9BS51
resolver
uniprot_entry
A0A2R8Y7F9_HUMAN
resolver
uniprot_entry
E9PD10_HUMAN
resolver
uniprot_entry
GLPA_HUMAN
resolver
uniprot_entry
Q14419_HUMAN
resolver
uniprot_sec
A0A0C4DFT7
resolver
uniprot_sec
A8K3E6
resolver
uniprot_sec
B8Q182
resolver
uniprot_sec
B8Q185
resolver
uniprot_sec
Q9BS51
resolver
amino_acid_sequence
MYGKIIFVLLLSEIVSISALSTTEVAMHTSTSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTVYPPEEETGERVQLAHHFSEPEITLIIFGVMAGVIGTILLISYGIRRLIKKSPSDVKPLPSPDTDVPLSSVEIENPETSDQ
uniprot
proteins
function
FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. {ECO:0000269|PubMed:10926825, ECO:0000269|PubMed:12813056, ECO:0000269|PubMed:14604989, ECO:0000269|PubMed:19438409, ECO:0000269|PubMed:35835865}.; FUNCTION: (Microbial infection) Appears to be a receptor for Hepatitis A virus (HAV). {ECO:0000269|PubMed:15331714}.; FUNCTION: (Microbial infection) Receptor for P.falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. {ECO:0000269|PubMed:8009226}.
uniprot
proteins
mass_dalton
16430
uniprot
proteins
mutagenesis
MUTAGEN 87; /note="F->C: Diminishes dimerization."; /evidence="ECO:0000269|PubMed:12813056"; MUTAGEN 88; /note="S->C: Diminishes dimerization."; /evidence="ECO:0000269|PubMed:12813056"; MUTAGEN 90; /note="P->C: Diminishes dimerization."; /evidence="ECO:0000269|PubMed:12813056"; MUTAGEN 91; /note="E->C: Diminishes dimerization."; /evidence="ECO:0000269|PubMed:12813056"; MUTAGEN 94; /note="L->I: Diminishes dimerization."; /evidence="ECO:0000269|PubMed:10926825"; MUTAGEN 95; /note="I->A: Diminishes dimerization."; /evidence="ECO:0000269|PubMed:10926825"; MUTAGEN 98; /note="G->L: Diminishes dimerization."; /evidence="ECO:0000269|PubMed:10926825"; MUTAGEN 102; /note="G->L: Abolishes dimerization."; /evidence="ECO:0000269|PubMed:10926825
uniprot
proteins
post_translational_modification
PTM: The major O-linked glycan are NeuAc-alpha-(2-3)-Gal-beta-(1-3)-[NeuAc-alpha-(2-6)]-GalNAcOH (about 78 %) and NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH (17 %). Minor O-glycans (5 %) include NeuAc-alpha-(2-3)-Gal-beta-(1-3)-[NeuAc-alpha-(2-6)]-GalNAcOH NeuAc-alpha-(2-8)-NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH. About 1% of all O-linked glycans carry blood group A, B and H determinants. They derive from a type-2 precursor core structure, Gal-beta-(1,3)-GlcNAc-beta-1-R, and the antigens are synthesized by addition of fucose (H antigen-specific) and then N-acetylgalactosamine (A antigen-specific) or galactose (B antigen-specific). Specifically O-linked-glycans are NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)-[Fuc-alpha-(1-2)]-Gal-beta-(3-1)-GalNAc-alpha (about 1%, B antigen-specific) and NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)-[Fuc-alpha-(1-2)]-Gal-beta (1 %, O antigen-, A antigen- and B antigen-specific). {ECO:0000269|PubMed:10912628, ECO:0000269|PubMed:15313217, ECO:0000269|PubMed:3624241, ECO:0000269|PubMed:5350948, ECO:0000269|PubMed:8286855}.
uniprot
proteins
protein_family
Glycophorin A family
uniprot
proteins
pubmed
10354388
uniprot
proteins
pubmed
1059087
uniprot
proteins
pubmed
10729812
uniprot
proteins
pubmed
10827258
uniprot
proteins
pubmed
10912628
uniprot
proteins
pubmed
10926825
uniprot
proteins
pubmed
11313283
uniprot
proteins
pubmed
11402026
uniprot
proteins
pubmed
12813056
uniprot
proteins
pubmed
1421409
uniprot
proteins
pubmed
14604989
uniprot
proteins
pubmed
1463744
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15313217
uniprot
proteins
pubmed
15331714
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
1611092
uniprot
proteins
pubmed
18380804
uniprot
proteins
pubmed
19438409
uniprot
proteins
pubmed
2216775
uniprot
proteins
pubmed
2386609
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25778531
uniprot
proteins
pubmed
2734312
uniprot
proteins
pubmed
3196288
uniprot
proteins
pubmed
3345758
uniprot
proteins
pubmed
3456608
uniprot
proteins
pubmed
35835865
uniprot
proteins
pubmed
3624241
uniprot
proteins
pubmed
3809885
uniprot
proteins
pubmed
5350948
uniprot
proteins
pubmed
6166001
uniprot
proteins
pubmed
6940143
uniprot
proteins
pubmed
7040988
uniprot
proteins
pubmed
7798177
uniprot
proteins
pubmed
8009226
uniprot
proteins
pubmed
8245024
uniprot
proteins
pubmed
8286855
uniprot
proteins
pubmed
8953647
uniprot
proteins
pubmed
9082985
uniprot
proteins
sequence_length
150
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11402026}; Single-pass type I membrane protein {ECO:0000269|PubMed:11402026}. Note=Appears to be colocalized with SLC4A1.
uniprot
proteins
transmembrane_region
TRANSMEM 92..114; /note="Helical
uniprot
proteins