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P04921

- GLPC_HUMAN

UniProt

P04921 - GLPC_HUMAN

Protein

Glycophorin-C

Gene

GYPC

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

    This protein is a minor sialoglycoprotein in human erythrocyte membranes. The blood group Gerbich antigens and receptors for Plasmodium falciparum merozoites are most likely located within the extracellular domain. Glycophorin-C plays an important role in regulating the stability of red cells.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei8 – 81Not glycosylated; in variant Webb antigen

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    Keywords - Molecular functioni

    Blood group antigen

    Keywords - Ligandi

    Sialic acid

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycophorin-C
    Alternative name(s):
    Glycoconnectin
    Glycophorin-D
    Short name:
    GPD
    Glycoprotein beta
    PAS-2'
    Sialoglycoprotein D
    CD_antigen: CD236
    Gene namesi
    Name:GYPC
    Synonyms:GLPC, GPC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4704. GYPC.

    Subcellular locationi

    Cell membrane; Single-pass type III membrane protein
    Note: Linked to the membrane via band 4.1.

    GO - Cellular componenti

    1. cortical cytoskeleton Source: UniProtKB
    2. integral component of plasma membrane Source: ProtInc
    3. membrane Source: UniProtKB
    4. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    MIMi110750. gene+phenotype.
    611162. phenotype.
    Orphaneti98864. Common hereditary elliptocytosis.
    PharmGKBiPA29082.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 128128Glycophorin-CPRO_0000149050Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi3 – 31O-linked (GalNAc...)2 Publications
    Glycosylationi4 – 41O-linked (GalNAc...)2 Publications
    Glycosylationi6 – 61O-linked (GalNAc...)2 Publications
    Glycosylationi8 – 81N-linked (GlcNAc...)1 Publication
    Glycosylationi9 – 91O-linked (GalNAc...)1 Publication
    Glycosylationi10 – 101O-linked (GalNAc...)1 Publication
    Glycosylationi15 – 151O-linked (GalNAc...)2 Publications
    Glycosylationi24 – 241O-linked (GalNAc...)2 Publications
    Glycosylationi26 – 261O-linked (GalNAc...)2 Publications
    Glycosylationi27 – 271O-linked (GalNAc...)2 Publications
    Glycosylationi28 – 281O-linked (GalNAc...)2 Publications
    Glycosylationi31 – 311O-linked (GalNAc...)2 Publications
    Glycosylationi32 – 321O-linked (GalNAc...)2 Publications
    Glycosylationi33 – 331O-linked (GalNAc...)2 Publications
    Glycosylationi42 – 421O-linked (GalNAc...)3 Publications
    Modified residuei104 – 1041Phosphoserine1 Publication

    Post-translational modificationi

    O-glycosylated with core 1 or possibly core 8 glycans.2 Publications

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP04921.
    PRIDEiP04921.

    PTM databases

    PhosphoSiteiP04921.

    Expressioni

    Tissue specificityi

    Glycophorin-C is expressed in erythrocytes. Glycophorin-D and IsoGPC are ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiP04921.
    BgeeiP04921.
    CleanExiHS_GYPC.
    GenevestigatoriP04921.

    Organism-specific databases

    HPAiCAB009445.
    HPA008965.

    Interactioni

    Protein-protein interaction databases

    BioGridi109250. 1 interaction.
    IntActiP04921. 1 interaction.
    MINTiMINT-1527497.
    STRINGi9606.ENSP00000259254.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EJYNMR-B117-126[»]
    ProteinModelPortaliP04921.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04921.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5757ExtracellularAdd
    BLAST
    Topological domaini82 – 12847CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei58 – 8124Helical; Signal-anchor for type III membrane proteinAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycophorin-C family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG146330.
    HOGENOMiHOG000112742.
    HOVERGENiHBG094619.
    InParanoidiP04921.
    KOiK06576.
    OMAiMHTTTIA.
    OrthoDBiEOG7VDXSF.
    PhylomeDBiP04921.
    TreeFamiTF337016.

    Family and domain databases

    InterProiIPR003585. Neurexin-like.
    [Graphical view]
    SMARTiSM00294. 4.1m. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Glycophorin-C (identifier: P04921-1) [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

    MWSTRSPNST AWPLSLEPDP GMASASTTMH TTTIAEPDPG MSGWPDGRME    50
    TSTPTIMDIV VIAGVIAAVA IVLVSLLFVM LRYMYRHKGT YHTNEAKGTE 100
    FAESADAALQ GDPALQDAGD SSRKEYFI 128
    Length:128
    Mass (Da):13,811
    Last modified:August 13, 1987 - v1
    Checksum:iC9C654009A5642D5
    GO
    Isoform Glycophorin-D (identifier: P04921-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: Missing.

    Show »
    Length:107
    Mass (Da):11,499
    Checksum:iB7D025DEF0555290
    GO
    Isoform 3 (identifier: P04921-3) [UniParc]FASTAAdd to Basket

    Also known as: IsoGPC

    The sequence of this isoform differs from the canonical sequence as follows:
         18-36: Missing.

    Show »
    Length:109
    Mass (Da):11,910
    Checksum:i226D848E8D619180
    GO

    Sequence cautioni

    The sequence CAA32093.1 differs from that shown. Reason: Frameshift at position 35.

    Polymorphismi

    GYPC is responsible for the Gerbich blood group system. Deletion of exon 3 in GYPC changes the serologic phenotype of the Gerbich blood group system, resulting in Ge negativity. Ge negative individuals are protected against severe malaria due to erythrocytes resistance to Plasmodium falciparum invasion [MIMi:611162].

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81N → S in Webb (WB) antigen.
    VAR_003193
    Natural varianti14 – 141L → F in Duch (DH(a)) antigen.
    VAR_003194
    Natural varianti23 – 231A → S in Ahonen (AN(a)) antigen.
    VAR_003195
    Natural varianti124 – 1241K → E.1 Publication
    Corresponds to variant rs28370000 [ dbSNP | Ensembl ].
    VAR_021342

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2121Missing in isoform Glycophorin-D. CuratedVSP_001777Add
    BLAST
    Alternative sequencei18 – 3619Missing in isoform 3. 1 PublicationVSP_054790Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11802 mRNA. Translation: AAA60023.1.
    M36284 mRNA. Translation: AAA52625.1.
    X12496 mRNA. Translation: CAA31016.1.
    M28335 mRNA. Translation: AAA52574.1.
    X51973 mRNA. Translation: CAA36235.1.
    AK312032 mRNA. Translation: BAG34969.1.
    AY838876 Genomic DNA. Translation: AAV80423.1.
    AC013474 Genomic DNA. Translation: AAY14660.1.
    BC106051 mRNA. Translation: AAI06052.1.
    BC104246 mRNA. Translation: AAI04247.1.
    BC104247 mRNA. Translation: AAI04248.1.
    X14242 Genomic DNA. Translation: CAA32458.1.
    M29662 Genomic DNA. Translation: AAA52626.1.
    X13890, X13892, X13893 Genomic DNA. Translation: CAA32093.1. Frameshift.
    CCDSiCCDS2136.1. [P04921-1]
    CCDS46402.1. [P04921-3]
    CCDS58724.1. [P04921-2]
    PIRiA92573. GFHUC.
    RefSeqiNP_001243513.1. NM_001256584.1. [P04921-2]
    NP_002092.1. NM_002101.4. [P04921-1]
    NP_058131.1. NM_016815.3. [P04921-3]
    UniGeneiHs.59138.

    Genome annotation databases

    EnsembliENST00000259254; ENSP00000259254; ENSG00000136732. [P04921-1]
    ENST00000356887; ENSP00000349354; ENSG00000136732. [P04921-2]
    ENST00000409836; ENSP00000386904; ENSG00000136732. [P04921-3]
    GeneIDi2995.
    KEGGihsa:2995.
    UCSCiuc002tnq.4. human. [P04921-1]

    Polymorphism databases

    DMDMi121407.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    dbRBC/BGMUT

    Blood group antigen gene mutation database

    Wikipedia

    Glycophorin C entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11802 mRNA. Translation: AAA60023.1 .
    M36284 mRNA. Translation: AAA52625.1 .
    X12496 mRNA. Translation: CAA31016.1 .
    M28335 mRNA. Translation: AAA52574.1 .
    X51973 mRNA. Translation: CAA36235.1 .
    AK312032 mRNA. Translation: BAG34969.1 .
    AY838876 Genomic DNA. Translation: AAV80423.1 .
    AC013474 Genomic DNA. Translation: AAY14660.1 .
    BC106051 mRNA. Translation: AAI06052.1 .
    BC104246 mRNA. Translation: AAI04247.1 .
    BC104247 mRNA. Translation: AAI04248.1 .
    X14242 Genomic DNA. Translation: CAA32458.1 .
    M29662 Genomic DNA. Translation: AAA52626.1 .
    X13890 , X13892 , X13893 Genomic DNA. Translation: CAA32093.1 . Frameshift.
    CCDSi CCDS2136.1. [P04921-1 ]
    CCDS46402.1. [P04921-3 ]
    CCDS58724.1. [P04921-2 ]
    PIRi A92573. GFHUC.
    RefSeqi NP_001243513.1. NM_001256584.1. [P04921-2 ]
    NP_002092.1. NM_002101.4. [P04921-1 ]
    NP_058131.1. NM_016815.3. [P04921-3 ]
    UniGenei Hs.59138.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EJY NMR - B 117-126 [» ]
    ProteinModelPortali P04921.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109250. 1 interaction.
    IntActi P04921. 1 interaction.
    MINTi MINT-1527497.
    STRINGi 9606.ENSP00000259254.

    PTM databases

    PhosphoSitei P04921.

    Polymorphism databases

    DMDMi 121407.

    Proteomic databases

    PaxDbi P04921.
    PRIDEi P04921.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259254 ; ENSP00000259254 ; ENSG00000136732 . [P04921-1 ]
    ENST00000356887 ; ENSP00000349354 ; ENSG00000136732 . [P04921-2 ]
    ENST00000409836 ; ENSP00000386904 ; ENSG00000136732 . [P04921-3 ]
    GeneIDi 2995.
    KEGGi hsa:2995.
    UCSCi uc002tnq.4. human. [P04921-1 ]

    Organism-specific databases

    CTDi 2995.
    GeneCardsi GC02P127413.
    HGNCi HGNC:4704. GYPC.
    HPAi CAB009445.
    HPA008965.
    MIMi 110750. gene+phenotype.
    611162. phenotype.
    neXtProti NX_P04921.
    Orphaneti 98864. Common hereditary elliptocytosis.
    PharmGKBi PA29082.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG146330.
    HOGENOMi HOG000112742.
    HOVERGENi HBG094619.
    InParanoidi P04921.
    KOi K06576.
    OMAi MHTTTIA.
    OrthoDBi EOG7VDXSF.
    PhylomeDBi P04921.
    TreeFami TF337016.

    Miscellaneous databases

    EvolutionaryTracei P04921.
    GenomeRNAii 2995.
    NextBioi 11870.
    PROi P04921.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04921.
    Bgeei P04921.
    CleanExi HS_GYPC.
    Genevestigatori P04921.

    Family and domain databases

    InterProi IPR003585. Neurexin-like.
    [Graphical view ]
    SMARTi SM00294. 4.1m. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of cDNA clones and complete amino acid sequence of human erythrocyte glycophorin C."
      Colin Y., Rahuel C., London J., Romeo P.-H., D'Auriol L., Galibert F., Cartron J.-P.
      J. Biol. Chem. 261:229-233(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
    2. "Human erythrocyte membrane sialoglycoprotein beta. The cDNA sequence suggests the absence of a cleaved N-terminal signal sequence."
      High S., Tanner M.J.A.
      Biochem. J. 243:277-280(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
    4. "Gerbich blood group deficiency of the Ge:-1,-2,-3 and Ge:-1,-2,3 types. Immunochemical study and genomic analysis with cDNA probes."
      le van Kim C., Colin Y., Blanchard D., Dahr W., London J., Cartron J.-P.
      Eur. J. Biochem. 165:571-579(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
      Tissue: Liver.
    5. "An ubiquitous isoform of glycophorin C is produced by alternative splicing."
      le van Kim C., Mitjavila M.T., Clerget M., Cartron J.-P., Colin Y.
      Nucleic Acids Res. 18:3076-3076(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
      Tissue: Spleen.
    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.
      , 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 GLYCOPHORIN-C).
    7. SeattleSNPs variation discovery resource
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-124.
    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].
    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 GLYCOPHORIN-C).
    10. "Glycophorins B and C from human erythrocyte membranes. Purification and sequence analysis."
      Blanchard D., Dahr W., Hummel M., Latron F., Beyreuther K., Cartron J.-P.
      J. Biol. Chem. 262:5808-5811(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 49-88.
    11. "Isolation and structural analysis of glycophorin C."
      Dahr W., Humel M., Blanchard D., Beyreuther K., Cartron J.-P.
      Biol. Chem. Hoppe-Seyler 366:777-778(1985)
      Cited for: PROTEIN SEQUENCE OF 1-87.
      Tissue: Blood.
    12. "A revision of the N-terminal structure of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes."
      Dahr W., Beyreuther K.
      Biol. Chem. Hoppe-Seyler 366:1067-1070(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-48.
      Tissue: Blood.
    13. "N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes."
      Dahr W., Beyreuther K., Kordowicz M., Krueger J.
      Eur. J. Biochem. 125:57-62(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 1-48, GLYCOSYLATION AT SER-3; THR-4; SER-6; ASN-8; SER-9; THR-10; SER-15; SER-24; SER-26; THR-27; THR-28; THR-31; THR-32; THR-33 AND SER-42.
      Tissue: Blood.
    14. "Structural homology between glycophorins C and D of human erythrocytes."
      El-Maliki B., Blanchard D., Dahr W., Beyreuther K., Cartron J.-P.
      Eur. J. Biochem. 183:639-643(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-91.
    15. "Structure of the promoter region and tissue specificity of the human glycophorin C gene."
      le van Kim C., Colin Y., Mitjavila M.T., Clerget M., Dubart A., Nakazawa M., Vainchenker W., Cartron J.-P.
      J. Biol. Chem. 264:20407-20414(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    16. "Rearrangements of the red-cell membrane glycophorin C (sialoglycoprotein beta) gene. A further study of alterations in the glycophorin C gene."
      High S., Tanner M.J.A., Macdonald E.N., Anstee D.J.
      Biochem. J. 262:47-54(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-128.
    17. "Human erythrocyte glycophorin C. Gene structure and rearrangement in genetic variants."
      Colin Y., le van Kim C., Tsapis A., Clerget M., D'Auriol L., London J., Galibert F., Cartron J.-P.
      J. Biol. Chem. 264:3773-3780(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE STRUCTURE.
    18. "Plasmodium falciparum erythrocyte invasion through glycophorin C and selection for Gerbich negativity in human populations."
      Maier A.G., Duraisingh M.T., Reeder J.C., Patel S.S., Kazura J.W., Zimmerman P.A., Cowman A.F.
      Nat. Med. 9:87-92(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM, INVOLVEMENT IN PROTECTION AGAINST MALARIA.
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-42, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    21. "Molecular characterization of erythrocyte glycophorin C variants."
      Chang S., Reid M.E., Conboy J., Kan Y.W., Mohandas N.
      Blood 77:644-648(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BLOOD GROUP ANTIGEN WB.
    22. "Point mutation in the glycophorin C gene results in the expression of the blood group antigen Dha."
      King M.J., Avent N.D., Mallinson G., Reid M.E.
      Vox Sang. 63:56-58(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BLOOD GROUP ANTIGEN DH(A).
    23. "A point mutation in the GYPC gene results in the expression of the blood group Ana antigen on glycophorin D but not on glycophorin C: further evidence that glycophorin D is a product of the GYPC gene."
      Daniels G., King M.J., Avent N.D., Khalid G., Reid M.E., Mallinson G., Symthe J., Cedergren B.
      Blood 82:3198-3203(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BLOOD GROUP ANTIGEN AN(A).

    Entry informationi

    Entry nameiGLPC_HUMAN
    AccessioniPrimary (citable) accession number: P04921
    Secondary accession number(s): B2R522, Q53SV9, Q92642
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 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

    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 2
      Human chromosome 2: 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