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P02724

- GLPA_HUMAN

UniProt

P02724 - GLPA_HUMAN

Protein

Glycophorin-A

Gene

GYPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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).6 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. virus receptor activity Source: UniProtKB-KW

    GO - Biological processi

    1. cytoskeletal anchoring at plasma membrane Source: Ensembl
    2. regulation of response to osmotic stress Source: Ensembl
    3. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Blood group antigen, Host cell receptor for virus entry, Receptor

    Keywords - Biological processi

    Host-virus interaction

    Keywords - Ligandi

    Sialic acid

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycophorin-A
    Alternative name(s):
    MN sialoglycoprotein
    PAS-2
    Sialoglycoprotein alpha
    CD_antigen: CD235a
    Gene namesi
    Name:GYPA
    Synonyms:GPA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:4702. GYPA.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
    Note: Appears to be colocalized with SLC4A1.

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: Ensembl
    4. membrane Source: ProtInc
    5. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi87 – 871F → C: Diminishes dimerization. 1 Publication
    Mutagenesisi88 – 881S → C: Diminishes dimerization. 1 Publication
    Mutagenesisi90 – 901P → C: Diminishes dimerization. 1 Publication
    Mutagenesisi91 – 911E → C: Diminishes dimerization. 1 Publication
    Mutagenesisi94 – 941L → I: Diminishes dimerization. 1 Publication
    Mutagenesisi95 – 951I → A: Diminishes dimerization. 1 Publication
    Mutagenesisi98 – 981G → L: Diminishes dimerization. 1 Publication
    Mutagenesisi102 – 1021G → L: Abolishes dimerization. 1 Publication

    Organism-specific databases

    MIMi111300. gene+phenotype.
    611162. phenotype.
    PharmGKBiPA29080.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 150131Glycophorin-APRO_0000012134Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi21 – 211O-linked (GalNAc...)2 Publications
    Glycosylationi22 – 221O-linked (GalNAc...)2 Publications
    Glycosylationi23 – 231O-linked (GalNAc...)2 Publications
    Glycosylationi29 – 291O-linked (GalNAc...)2 Publications
    Glycosylationi30 – 301O-linked (GalNAc...)2 Publications
    Glycosylationi31 – 311O-linked (GalNAc...)2 Publications
    Glycosylationi32 – 321O-linked (GalNAc...)2 Publications
    Glycosylationi36 – 361O-linked (GalNAc...)1 Publication
    Glycosylationi38 – 381O-linked (GalNAc...)1 Publication
    Glycosylationi41 – 411O-linked (GalNAc...)2 Publications
    Glycosylationi44 – 441O-linked (GalNAc...)2 Publications
    Glycosylationi45 – 451N-linked (GlcNAc...)2 Publications
    Glycosylationi52 – 521O-linked (GalNAc...)1 Publication
    Glycosylationi56 – 561O-linked (GalNAc...)2 Publications
    Glycosylationi63 – 631O-linked (GalNAc...)2 Publications
    Glycosylationi66 – 661O-linked (GalNAc...)2 Publications
    Glycosylationi69 – 691O-linked (GalNAc...)2 Publications

    Post-translational modificationi

    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).5 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP02724.
    PRIDEiP02724.

    PTM databases

    PhosphoSiteiP02724.
    UniCarbKBiP02724.

    Expressioni

    Gene expression databases

    ArrayExpressiP02724.
    BgeeiP02724.
    CleanExiHS_GYPA.
    GenevestigatoriP02724.

    Organism-specific databases

    HPAiCAB002658.
    HPA014811.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with Streptococcus gordonii hsa protein.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-702665,EBI-702665

    Protein-protein interaction databases

    STRINGi9606.ENSP00000354003.

    Structurei

    Secondary structure

    1
    150
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi84 – 863
    Helixi91 – 11727

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AFONMR-A/B81-120[»]
    1MSRmodel-A/B93-110[»]
    2KPENMR-A/B89-117[»]
    2KPFNMR-A/B80-117[»]
    ProteinModelPortaliP02724.
    SMRiP02724. Positions 81-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02724.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 9172ExtracellularAdd
    BLAST
    Topological domaini115 – 15036CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei92 – 11423HelicalAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycophorin A family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG114778.
    HOGENOMiHOG000089933.
    HOVERGENiHBG005850.
    InParanoidiP02724.
    KOiK06575.
    OrthoDBiEOG7ZWD4D.
    PhylomeDBiP02724.
    TreeFamiTF338555.

    Family and domain databases

    InterProiIPR001195. Glycophorin.
    IPR018938. Glycophorin_CS.
    [Graphical view]
    PANTHERiPTHR13813. PTHR13813. 1 hit.
    PIRSFiPIRSF002466. Glycophorin. 1 hit.
    PROSITEiPS00312. GLYCOPHORIN_A. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P02724-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MYGKIIFVLL LSEIVSISAS STTGVAMHTS TSSSVTKSYI SSQTNDTHKR    50
    DTYAATPRAH EVSEISVRTV YPPEEETGER VQLAHHFSEP EITLIIFGVM 100
    AGVIGTILLI SYGIRRLIKK SPSDVKPLPS PDTDVPLSSV EIENPETSDQ 150
    Length:150
    Mass (Da):16,331
    Last modified:September 22, 2009 - v2
    Checksum:i48A5450E22FA99C9
    GO
    Isoform 2 (identifier: P02724-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: Missing.

    Show »
    Length:124
    Mass (Da):13,649
    Checksum:iD257CA020BB42AFD
    GO
    Isoform 3 (identifier: P02724-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         13-45: Missing.

    Show »
    Length:117
    Mass (Da):13,000
    Checksum:i3F1878ED9D7ADB29
    GO

    Sequence cautioni

    The sequence AAA52624.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301S → T AA sequence (PubMed:1059087)Curated
    Sequence conflicti36 – 361T → S AA sequence (PubMed:1059087)Curated
    Sequence conflicti133 – 1331T → R in AAA88044. (PubMed:3456608)Curated

    Polymorphismi

    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.
    GYPA polymorphisms are involved in resistance to malaria [MIMi:611162].

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131E → A.7 Publications
    Corresponds to variant rs4449373 [ dbSNP | Ensembl ].
    VAR_058911
    Natural varianti13 – 131E → G.
    Corresponds to variant rs4449373 [ dbSNP | Ensembl ].
    VAR_059977
    Natural varianti20 – 201S → L in N antigen and M(g) antigen. 3 Publications
    Corresponds to variant rs7682260 [ dbSNP | Ensembl ].
    VAR_003190
    Natural varianti23 – 231T → N in M(g) antigen. 1 Publication
    VAR_058912
    Natural varianti24 – 241G → D.
    Corresponds to variant rs7658293 [ dbSNP | Ensembl ].
    VAR_058913
    Natural varianti24 – 241G → E in N antigen, in M(c) antigen and in M(g) antigen. 4 Publications
    Corresponds to variant rs7687256 [ dbSNP | Ensembl ].
    VAR_003191
    Natural varianti46 – 461D → E in Ny(a) antigen. 1 Publication
    VAR_058914
    Natural varianti47 – 471T → K in ENEH/Hut antigen. 1 Publication
    VAR_058915
    Natural varianti47 – 471T → M in ENEH/Vw antigen. 1 Publication
    VAR_058916
    Natural varianti50 – 501R → W in Or antigen.
    VAR_058917
    Natural varianti66 – 661S → Y in Vr antigen. 1 Publication
    Corresponds to variant rs56077914 [ dbSNP | Ensembl ].
    VAR_058918
    Natural varianti73 – 731P → S in Os(a) antigen. 1 Publication
    VAR_058919
    Natural varianti76 – 761E → K in Ri(a) antigen.
    VAR_058920
    Natural varianti77 – 771T → I in Mt(a) antigen. 1 Publication
    Corresponds to variant rs56172553 [ dbSNP | Ensembl ].
    VAR_058921
    Natural varianti78 – 781G → R in ERIK antigen. 1 Publication
    Corresponds to variant rs1800582 [ dbSNP | Ensembl ].
    VAR_058922
    Natural varianti82 – 821Q → K in ENAV/MARS antigen.
    VAR_058923
    Natural varianti84 – 841A → P in ENEP/HAG antigen. 1 Publication
    VAR_058924

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626Missing in isoform 2. 1 PublicationVSP_047822Add
    BLAST
    Alternative sequencei13 – 4533Missing in isoform 3. CuratedVSP_047823Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12857 mRNA. Translation: AAA88044.1.
    X08054 mRNA. Translation: CAA30843.1.
    M24128
    , M24123, M24134, M24124, M24126, M24127 Genomic DNA. Translation: AAA52768.1.
    X51798 mRNA. Translation: CAA36095.1.
    L31860 mRNA. Translation: AAA88051.1.
    EU338231 mRNA. Translation: ACA96789.1.
    EU338233 mRNA. Translation: ACA96791.1.
    EU338234 mRNA. Translation: ACA96792.1.
    GU347002 mRNA. Translation: ADU25340.1.
    GU347003 mRNA. Translation: ADU25341.1.
    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.
    CCDSiCCDS34069.1. [P02724-1]
    PIRiA33931. A25131.
    RefSeqiNP_002090.4. NM_002099.6.
    UniGeneiHs.434973.

    Genome annotation databases

    EnsembliENST00000324022; ENSP00000324483; ENSG00000170180. [P02724-3]
    ENST00000360771; ENSP00000354003; ENSG00000170180.
    ENST00000535709; ENSP00000445398; ENSG00000170180. [P02724-2]
    GeneIDi2993.
    KEGGihsa:2993.

    Polymorphism databases

    DMDMi259016238.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    dbRBC/BGMUT

    Blood group antigen gene mutation database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12857 mRNA. Translation: AAA88044.1 .
    X08054 mRNA. Translation: CAA30843.1 .
    M24128
    , M24123 , M24134 , M24124 , M24126 , M24127 Genomic DNA. Translation: AAA52768.1 .
    X51798 mRNA. Translation: CAA36095.1 .
    L31860 mRNA. Translation: AAA88051.1 .
    EU338231 mRNA. Translation: ACA96789.1 .
    EU338233 mRNA. Translation: ACA96791.1 .
    EU338234 mRNA. Translation: ACA96792.1 .
    GU347002 mRNA. Translation: ADU25340.1 .
    GU347003 mRNA. Translation: ADU25341.1 .
    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.
    CCDSi CCDS34069.1. [P02724-1 ]
    PIRi A33931. A25131.
    RefSeqi NP_002090.4. NM_002099.6.
    UniGenei Hs.434973.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AFO NMR - A/B 81-120 [» ]
    1MSR model - A/B 93-110 [» ]
    2KPE NMR - A/B 89-117 [» ]
    2KPF NMR - A/B 80-117 [» ]
    ProteinModelPortali P02724.
    SMRi P02724. Positions 81-120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000354003.

    Chemistry

    BindingDBi P02724.
    ChEMBLi CHEMBL5806.

    PTM databases

    PhosphoSitei P02724.
    UniCarbKBi P02724.

    Polymorphism databases

    DMDMi 259016238.

    Proteomic databases

    PaxDbi P02724.
    PRIDEi P02724.

    Protocols and materials databases

    DNASUi 2993.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324022 ; ENSP00000324483 ; ENSG00000170180 . [P02724-3 ]
    ENST00000360771 ; ENSP00000354003 ; ENSG00000170180 .
    ENST00000535709 ; ENSP00000445398 ; ENSG00000170180 . [P02724-2 ]
    GeneIDi 2993.
    KEGGi hsa:2993.

    Organism-specific databases

    CTDi 2993.
    GeneCardsi GC04M145030.
    HGNCi HGNC:4702. GYPA.
    HPAi CAB002658.
    HPA014811.
    MIMi 111300. gene+phenotype.
    611162. phenotype.
    neXtProti NX_P02724.
    PharmGKBi PA29080.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG114778.
    HOGENOMi HOG000089933.
    HOVERGENi HBG005850.
    InParanoidi P02724.
    KOi K06575.
    OrthoDBi EOG7ZWD4D.
    PhylomeDBi P02724.
    TreeFami TF338555.

    Miscellaneous databases

    EvolutionaryTracei P02724.
    GeneWikii GYPA.
    GenomeRNAii 2993.
    NextBioi 11862.
    PROi P02724.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02724.
    Bgeei P02724.
    CleanExi HS_GYPA.
    Genevestigatori P02724.

    Family and domain databases

    InterProi IPR001195. Glycophorin.
    IPR018938. Glycophorin_CS.
    [Graphical view ]
    PANTHERi PTHR13813. PTHR13813. 1 hit.
    PIRSFi PIRSF002466. Glycophorin. 1 hit.
    PROSITEi PS00312. GLYCOPHORIN_A. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-13.
      Tissue: Blood.
    6. "Extensive alternative splicing of glycophorins in Southeast Asian populations."
      Hsu K., Huang S.-Y., Chi N., Lin M.
      Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
      Tissue: Blood.
    7. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-13.
      Tissue: Kidney.
    8. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS N LEU-20 AND GLU-24.
    9. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-13, VARIANTS N LEU-20 AND GLU-24.
      Tissue: Bone marrow and Lung.
    10. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-145 (ISOFORM 1), VARIANT ALA-13.
    11. "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] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-150.
    12. Furthmayr H., Galardy R., Tomita M., Marchesi V.T.
      Submitted (JUN-1977) to the PIR data bank
      Cited for: SEQUENCE REVISION TO 81-120.
    13. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-150.
    14. "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] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, VARIANT M(C) GLU-24.
    15. "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] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, VARIANT M(G) ASN-23.
    16. "Structural studies on human erythrocyte glycoproteins. Alkali-labile oligosaccharides."
      Thomas D.B., Winzler R.J.
      J. Biol. Chem. 244:5943-5946(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    17. "Erythrocytes deficiency in glycophorin resist invasion by the malarial parasite Plasmodium falciparum."
      Pasvol G., Wainscoat J.S., Weatherall D.J.
      Nature 297:64-66(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM, INVOLVEMENT IN RESISTANCE TO MALARIA.
    18. "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] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    19. "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] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    20. "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] [Europe PMC] [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.
    21. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS RECEPTOR FOR PLASMODIUM EBA-175.
    22. "Identification of blood group A and B antigens in human glycophorin."
      Podbielska M., Krotkiewski H.
      Arch. Immunol. Ther. Exp. 48:211-221(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION (AB BLOOD GROUP ANTIGENS).
    23. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LEU-94; ILE-95; GLY-98 AND GLY-102.
    24. "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] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    25. "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] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    26. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF PHE-87; SER-88; PRO-90 AND GLU-91.
    27. "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.
    28. Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
    29. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS RECEPTOR FOR FOR HEPATITIS A VIRUS.
    31. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STREPTOCOCCUS GORDONII HSA PROTEIN.
    32. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    33. "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] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    34. "A transmembrane helix dimer: structure and implications."
      Mackenzie K.R., Prestegard J.H., Engelman D.M.
      Science 276:131-133(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 81-120.
    35. "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] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 93-110.
    36. "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] [Europe PMC] [Abstract]
      Cited for: VARIANT ENEH/VW MET-47.
    37. "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] [Europe PMC] [Abstract]
      Cited for: VARIANT ENEH/HUT ANTIGEN LYS-47.
    38. "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] [Europe PMC] [Abstract]
      Cited for: VARIANT ERIK ARG-78.
    39. "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] [Europe PMC] [Abstract]
      Cited for: VARIANT ENEP/HAG PRO-84.
    40. "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] [Europe PMC] [Abstract]
      Cited for: VARIANTS NY(A) GLU-46 AND OS(A) SER-73.
    41. "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] [Europe PMC] [Abstract]
      Cited for: VARIANTS VR TYR-66 AND MT(A) ILE-77.

    Entry informationi

    Entry nameiGLPA_HUMAN
    AccessioniPrimary (citable) accession number: P02724
    Secondary accession number(s): A8K3E6
    , B8Q182, B8Q185, Q9BS51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 160 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Blood group antigen proteins
      Nomenclature of blood group antigens and list of entries
    2. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    3. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3