Reviewed,
UniProtKB/Swiss-Prot P02724 (GLPA_HUMAN)
Last modified
October 13, 2009.
Version 111.
History...
Clusters with 100%,
90%,
50% identity |
Documents (8) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Glycophorin-A Alternative name(s): PAS-2 Sialoglycoprotein alpha MN sialoglycoprotein CD_antigen=CD235a | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 150 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | 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. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). Ref.19 Ref.21 Ref.24 Ref.27 Ref.28 Ref.30 |
| Subunit structure | Homodimer. Interacts with Streptococcus gordonii hsa protein. Ref.17 Ref.22 Ref.29 |
| Subcellular location | Cell membrane; Single-pass type I membrane protein. Note: Appears to be colocalized with SLC4A1. Ref.23 |
| Post-translational modification | 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). |
| Polymorphism | Along with GYPB, GYPA is responsible for the MNS blood group system. 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. |
| Miscellaneous | Involved in several unequal homologous recombinations or gene conversion events, predominantly with GYPB and more rarely with GYPE. The resulting fusion proteins are observed in different phenotypes and encode low incidence bloodgroup antigens. |
| Sequence similarities | Belongs to the glycophorin A family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Host-virus interaction |
| Cellular component | Cell membrane Membrane |
| Coding sequence diversity | Polymorphism |
| Domain | Signal Transmembrane |
| Ligand | Sialic acid |
| Molecular function | Blood group antigen |
| PTM | Glycoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Ref.1Traceable author statement. Source: ProtInc plasma membrane Ref.36Traceable author statement. Source: ProtInc |
| Molecular function | identical protein binding Inferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Ref.10 | ||||||||
| Chain | 20 – 150 | 131 | Glycophorin-A | PRO_0000012134 | |||||||
Regions | |||||||||||
| Topological domain | 20 – 91 | 72 | Extracellular | ||||||||
| Transmembrane | 92 – 114 | 23 | |||||||||
| Topological domain | 115 – 150 | 36 | Cytoplasmic | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 21 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 22 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 23 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 29 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 30 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 31 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 32 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 36 | 1 | O-linked (GalNAc...) Ref.18 | ||||||||
| Glycosylation | 38 | 1 | O-linked (GalNAc...) Ref.18 | ||||||||
| Glycosylation | 41 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 44 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 45 | 1 | N-linked (GlcNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 52 | 1 | O-linked (GalNAc...) Ref.18 | ||||||||
| Glycosylation | 56 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 63 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 66 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
| Glycosylation | 69 | 1 | O-linked (GalNAc...) Ref.10 Ref.18 | ||||||||
Natural variations | |||||||||||
| Natural variant | 13 | 1 | E → A: dbSNP rs4449373. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 | VAR_058911 | |||||||
| Natural variant | 13 | 1 | E → G: dbSNP rs4449373. | VAR_059977 | |||||||
| Natural variant | 20 | 1 | S → L in N antigen and M(g) antigen. Ref.8 Ref.2 Ref.7 | VAR_003190 | |||||||
| Natural variant | 23 | 1 | T → N in M(g) antigen. Ref.14 | VAR_058912 | |||||||
| Natural variant | 24 | 1 | G → D: dbSNP rs7658293. | VAR_058913 | |||||||
| Natural variant | 24 | 1 | G → E in N antigen, in M(c) antigen and in M(g) antigen. Ref.8 Ref.2 Ref.7 Ref.13 | VAR_003191 | |||||||
| Natural variant | 46 | 1 | D → E in Ny(a) antigen. Ref.38 | VAR_058914 | |||||||
| Natural variant | 47 | 1 | T → K in ENEH/Hut antigen. Ref.35 | VAR_058915 | |||||||
| Natural variant | 47 | 1 | T → M in ENEH/Vw antigen. Ref.34 | VAR_058916 | |||||||
| Natural variant | 50 | 1 | R → W in Or antigen. | VAR_058917 | |||||||
| Natural variant | 66 | 1 | S → Y in Vr antigen. Ref.39 | VAR_058918 | |||||||
| Natural variant | 73 | 1 | P → S in Os(a) antigen. Ref.38 | VAR_058919 | |||||||
| Natural variant | 76 | 1 | E → K in Ri(a) antigen. | VAR_058920 | |||||||
| Natural variant | 77 | 1 | T → I in Mt(a) antigen. Ref.39 | VAR_058921 | |||||||
| Natural variant | 78 | 1 | G → R in ERIK antigen. Ref.36 | VAR_058922 | |||||||
| Natural variant | 82 | 1 | Q → K in ENAV/MARS antigen. | VAR_058923 | |||||||
| Natural variant | 84 | 1 | A → P in ENEP/HAG antigen. Ref.37 | VAR_058924 | |||||||
Experimental info | |||||||||||
| Mutagenesis | 87 | 1 | F → C: Diminishes dimerization. Ref.24 | ||||||||
| Mutagenesis | 88 | 1 | S → C: Diminishes dimerization. Ref.24 | ||||||||
| Mutagenesis | 90 | 1 | P → C: Diminishes dimerization. Ref.24 | ||||||||
| Mutagenesis | 91 | 1 | E → C: Diminishes dimerization. Ref.24 | ||||||||
| Mutagenesis | 94 | 1 | L → I: Diminishes dimerization. Ref.21 | ||||||||
| Mutagenesis | 95 | 1 | I → A: Diminishes dimerization. Ref.21 | ||||||||
| Mutagenesis | 98 | 1 | G → L: Diminishes dimerization. Ref.21 | ||||||||
| Mutagenesis | 102 | 1 | G → L: Abolishes dimerization. Ref.21 | ||||||||
| Sequence conflict | 30 | 1 | S → T AA sequence Ref.10 | ||||||||
| Sequence conflict | 36 | 1 | T → S AA sequence Ref.10 | ||||||||
| Sequence conflict | 133 | 1 | T → R in AAA88044. Ref.1 | ||||||||
Secondary structure | |||||||||||
Helix Strand Turn | |||||||||||
| Helix | 91 – 117 | 27 | |||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "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) [PubMed: 3456608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-13. |
| [2] | "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) [PubMed: 3196288] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS N LEU-20 AND GLU-24. |
| [3] | "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) [PubMed: 2734312] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-13. |
| [4] | "The mechanism of production of multiple mRNAs for human glycophorin A." Jawad K., Burness T.H. Nucleic Acids Res. 18:5829-5836(1990) [PubMed: 2216775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-13. Tissue: Blood. |
| [5] | "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) [PubMed: 7798177] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-13. Tissue: Blood. |
| [6] | "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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-13. Tissue: Kidney. |
| [7] | "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. Wilson R.K.Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS N LEU-20 AND GLU-24. |
| [8] | "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) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-13, VARIANTS N LEU-20 AND GLU-24. Tissue: Bone marrow and Lung. |
| [9] | "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) [PubMed: 3809885] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-145, VARIANT ALA-13. |
| [10] | "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) [PubMed: 1059087] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-150. |
| [11] | Furthmayr H., Galardy R., Tomita M., Marchesi V.T. Submitted (JUN-1977) to the PIR data bank Cited for: SEQUENCE REVISION TO 81-120. |
| [12] | "Characterization of cDNA clones for human glycophorin A. Use for gene localization and for analysis of normal of glycophorin-A-deficient (Finnish type) genomic DNA." Rahuel C., London J., D'Auriol L., Mattei M.-G., Tournamille C., Skrzynia C., Lebouc Y., Galibert F., Cartron J.-P. Eur. J. Biochem. 172:147-153(1988) [PubMed: 3345758] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-150. |
| [13] | "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) [PubMed: 6166001] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, VARIANT M(C) GLU-24. |
| [14] | "Amino acid and carbohydrate structural variants of glycoprotein products (M-N glycoproteins) of the M-N allelic locus." Blumenfeld O.O., Adamany A.M., Puglia K.V. Proc. Natl. Acad. Sci. U.S.A. 78:747-751(1981) [PubMed: 6940143] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, VARIANT M(G) ASN-23. |
| [15] | "Structural studies on human erythrocyte glycoproteins. Alkali-labile oligosaccharides." Thomas D.B., Winzler R.J. J. Biol. Chem. 244:5943-5946(1969) [PubMed: 5350948] [Abstract] Cited for: GLYCOSYLATION. |
| [16] | "Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins." Fukuda M., Lauffenburger M., Sasaki H., Rogers M.E., Dell A. J. Biol. Chem. 262:11952-11957(1987) [PubMed: 3624241] [Abstract] Cited for: GLYCOSYLATION. |
| [17] | "The glycophorin A transmembrane domain dimer: sequence-specific propensity for a right-handed supercoil of helices." Treutlein H.R., Lemmon M.A., Engelman D.M., Brunger A.T. Biochemistry 31:12726-12732(1992) [PubMed: 1463744] [Abstract] Cited for: SUBUNIT. |
| [18] | "Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A." Pisano A., Redmond J.W., Williams K.L., Gooley A.A. Glycobiology 3:429-435(1993) [PubMed: 8286855] [Abstract] Cited for: GLYCOSYLATION AT SER-21; THR-22; THR-23; THR-29; SER-30; THR-31; SER-32; THR-36; SER-38; SER-41; THR-44; ASN-45; THR-52; THR-56; SER-63; SER-66 AND THR-69, PARTIAL PROTEIN SEQUENCE. |
| [19] | "Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum." Sim B.K., Chitnis C.E., Wasniowska K., Hadley T.J., Miller L.H. Science 264:1941-1944(1994) [PubMed: 8009226] [Abstract] Cited for: FUNCTION AS RECEPTOR FOR PLASMODIUM EBA-175. |
| [20] | "Identification of blood group A and B antigens in human glycophorin." Podbielska M., Krotkiewski H. Arch. Immunol. Ther. Exp. 48:211-221(2000) [PubMed: 10912628] [Abstract] Cited for: GLYCOSYLATION (AB BLOOD GROUP ANTIGENS). |
| [21] | "Red-cell glycophorin A-band 3 interactions associated with the movement of band 3 to the cell surface." Young M.T., Beckmann R., Toye A.M., Tanner M.J. Biochem. J. 350:53-60(2000) [PubMed: 10926825] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LEU-94; ILE-95; GLY-98 AND GLY-102. |
| [22] | "Glycophorin A dimerization and band 3 interaction during erythroid membrane biogenesis: in vivo studies in human glycophorin A transgenic mice." Auffray I., Marfatia S., de Jong K., Lee G., Huang C.H., Paszty C., Tanner M.J., Mohandas N., Chasis J.A. Blood 97:2872-2878(2001) [PubMed: 11313283] [Abstract] Cited for: SUBUNIT. |
| [23] | "In vivo detection of hetero-association of glycophorin-A and its mutants within the membrane." Gerber D., Shai Y. J. Biol. Chem. 276:31229-31232(2001) [PubMed: 11402026] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [24] | "Distinct regions of human glycophorin A enhance human red cell anion exchanger (band 3; AE1) transport function and surface trafficking." Young M.T., Tanner M.J. J. Biol. Chem. 278:32954-32961(2003) [PubMed: 12813056] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PHE-87; SER-88; PRO-90 AND GLU-91. |
| [25] | "The blood group system." Reid M.E., Christine Lomas-Francis C. (In) Reid M.E., Christine Lomas-Francis C. (eds.); The blood group antigen factsbook, pp.29-104, Academic Press, Oxford (2004) Cited for: REVIEW, VARIANTS. |
| [26] | "ABH blood group antigens in O-glycans of human glycophorin A." Podbielska M., Fredriksson S.A., Nilsson B., Lisowska E., Krotkiewski H. Arch. Biochem. Biophys. 429:145-153(2004) [PubMed: 15313217] [Abstract] Cited for: GLYCOSYLATION, MASS SPECTROMETRY. |
| [27] | "Altered structure and anion transport properties of band 3 (AE1, SLC4A1) in human red cells lacking glycophorin A." Bruce L.J., Pan R.J., Cope D.L., Uchikawa M., Gunn R.B., Cherry R.J., Tanner M.J. J. Biol. Chem. 279:2414-2420(2004) [PubMed: 14604989] [Abstract] Cited for: FUNCTION. |
| [28] | "Capsid region involved in hepatitis A virus binding to glycophorin A of the erythrocyte membrane." Sanchez G., Aragones L., Costafreda M.I., Ribes E., Bosch A., Pinto R.M. J. Virol. 78:9807-9813(2004) [PubMed: 15331714] [Abstract] Cited for: FUNCTION AS RECEPTOR FOR FOR HEPATITIS A VIRUS. |
| [29] | "Hsa, an adhesin of Streptococcus gordonii DL1, binds to alpha2-3-linked sialic acid on glycophorin A of the erythrocyte membrane." Yajima A., Urano-Tashiro Y., Shimazu K., Takashima E., Takahashi Y., Konishi K. Microbiol. Immunol. 52:69-77(2008) [PubMed: 18380804] [Abstract] Cited for: INTERACTION WITH STREPTOCOCCUS GORDONII HSA PROTEIN. |
| [30] | "Interaction of anion exchanger 1 and glycophorin A in human erythroleukaemic K562 cells." Pang A.J., Reithmeier R.A. Biochem. J. 421:345-356(2009) [PubMed: 19438409] [Abstract] Cited for: FUNCTION. |
| [31] | "One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla." Dill K., Hu S.H., Berman E., Pavia A.A., Lacombe J.M. J. Protein Chem. 9:129-136(1990) [PubMed: 2386609] [Abstract] Cited for: STRUCTURE BY NMR. |
| [32] | "A transmembrane helix dimer: structure and implications." Mackenzie K.R., Prestegard J.H., Engelman D.M. Science 276:131-133(1997) [PubMed: 9082985] [Abstract] Cited for: STRUCTURE BY NMR OF 81-120. |
| [33] | "Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching." Adams P.D., Engelman D.M., Bruenger A.T. Proteins 26:257-261(1996) [PubMed: 8953647] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 93-110. |
| [34] | "Molecular basis for the human erythrocyte glycophorin specifying the Miltenberger class I (MiI) phenotype." Huang C.-H., Spruell P., Moulds J.J., Blumenfeld O.O. Blood 80:257-263(1992) [PubMed: 1611092] [Abstract] Cited for: VARIANT ENEH/VW MET-47. |
| [35] | "Molecular analysis of human glycophorin MiIX gene shows a silent segment transfer and untemplated mutation resulting from gene conversion via sequence repeats." Huang C.H., Skov F., Daniels G., Tippett P., Blumenfeld O.O. Blood 80:2379-2387(1992) [PubMed: 1421409] [Abstract] Cited for: VARIANT ENEH/HUT ANTIGEN LYS-47. |
| [36] | "Alteration of splice site selection by an exon mutation in the human glycophorin A gene." Huang C.H., Reid M., Daniels G., Blumenfeld O.O. J. Biol. Chem. 268:25902-25908(1993) [PubMed: 8245024] [Abstract] Cited for: VARIANT ERIK ARG-78. |
| [37] | "Glycophorin A mutation Ala65 --> Pro gives rise to a novel pair of MNS alleles ENEP (MNS39) and HAG (MNS41) and altered Wrb expression: direct evidence for GPA/band 3 interaction necessary for normal Wrb expression." Poole J., Banks J., Bruce L.J., Ring S.M., Levene C., Stern H., Overbeeke M.A., Tanner M.J. Transfus. Med. 9:167-174(1999) [PubMed: 10354388] [Abstract] Cited for: VARIANT ENEP/HAG PRO-84. |
| [38] | "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) [PubMed: 10827258] [Abstract] Cited for: VARIANTS NY(A) GLU-46 AND OS(A) SER-73. |
| [39] | "The MNS blood group antigens, Vr (MNS12) and Mt(a) (MNS14), each arise from an amino acid substitution on glycophorin A." Storry J.R., Coghlan G., Poole J., Figueroa D., Reid M.E. Vox Sang. 78:52-56(2000) [PubMed: 10729812] [Abstract] Cited for: VARIANTS VR TYR-66 AND MT(A) ILE-77. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M12857 mRNA. Translation: AAA88044.1. X08054 mRNA. Translation: CAA30843.1. M24128 M24127 Genomic DNA. Translation: AAA52768.1. X51798 mRNA. Translation: CAA36095.1. L31860 mRNA. Translation: AAA88051.1. AK290561 mRNA. Translation: BAF83250.1. AC107223 Genomic DNA. No translation available. BC005319 mRNA. Translation: AAH05319.1. BC013328 mRNA. Translation: AAH13328.1. M36281 mRNA. Translation: AAA52624.1. Different initiation. | |||||||||||||||||||
| IPI | IPI00298800. | ||||||||||||||||||
| PIR | A25131. A33931. | ||||||||||||||||||
| RefSeq | NP_002090.2. | ||||||||||||||||||
| UniGene | Hs.434973 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| |||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P02724. 1 interaction. | ||||||||||||||||||
| STRING | P02724. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| GlycoSuiteDB | P02724. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000283126; ENSP00000283126; ENSG00000170180; Homo sapiens. [Genome view] ENST00000283128; ENSP00000283128; ENSG00000170180; Homo sapiens. [Genome view] ENST00000306959; ENSP00000306419; ENSG00000170180; Homo sapiens. [Genome view] ENST00000324022; ENSP00000324483; ENSG00000170180; Homo sapiens. [Genome view] ENST00000360771; ENSP00000354003; ENSG00000170180; Homo sapiens. [Genome view] ENST00000394119; ENSP00000377677; ENSG00000170180; Homo sapiens. [Genome view] ENST00000429670; ENSP00000394200; ENSG00000170180; Homo sapiens. [Genome view] | ||||||||||||||||||
| GeneID | 2993. | ||||||||||||||||||
| KEGG | hsa:2993. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 2993. | ||||||||||||||||||
| GeneCards | GC04M145249. | ||||||||||||||||||
| H-InvDB | HIX0004534. | ||||||||||||||||||
| HGNC | HGNC:4702. GYPA. | ||||||||||||||||||
| HPA | CAB002658. HPA014811. | ||||||||||||||||||
| MIM | 111300. gene+phenotype. | ||||||||||||||||||
| PharmGKB | PA29080. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | P02724. | ||||||||||||||||||
| HOVERGEN | P02724. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P02724. | ||||||||||||||||||
| Bgee | P02724. | ||||||||||||||||||
| CleanEx | HS_GYPA. | ||||||||||||||||||
| Genevestigator | P02724. | ||||||||||||||||||
| GermOnline | ENSG00000170180. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR001195. Glycophorin. IPR018938. Glycophorin_CS. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR13813. Glycophorin_A_B. 1 hit. | ||||||||||||||||||
| Pfam | PF01102. Glycophorin_A. 1 hit. [Graphical view] | ||||||||||||||||||
| PIRSF | PIRSF002466. Glycophorin. 1 hit. | ||||||||||||||||||
| PROSITE | PS00312. GLYCOPHORIN_A. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | GLPA_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P02724 Secondary accession number(s): A8K3E6, Q9BS51 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Blood group antigen proteins Nomenclature of blood group antigens and list of entries |
| Human cell differentiation molecules CD nomenclature of surface proteins of human leucocytes and list of entries |
| Human chromosome 4 Human chromosome 4: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


