GLPB_HUMAN
ID GLPB_HUMAN Reviewed; 91 AA.
AC P06028; B8Q174; E2QBW7; Q0VAF4; Q58HE9; Q58HF0; Q58HF1; Q9UCH7;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Glycophorin-B;
DE AltName: Full=PAS-3;
DE AltName: Full=SS-active sialoglycoprotein;
DE AltName: Full=Sialoglycoprotein delta;
DE AltName: CD_antigen=CD235b;
DE Flags: Precursor;
GN Name=GYPB; Synonyms=GPB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-84.
RX PubMed=3477806; DOI=10.1073/pnas.84.19.6735;
RA Siebert P.D., Fukuda M.;
RT "Molecular cloning of a human glycophorin B cDNA: nucleotide sequence and
RT genomic relationship to glycophorin A.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6735-6739(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3196288; DOI=10.1042/bj2540743;
RA Tate C.G., Tanner M.J.A.;
RT "Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins
RT alpha and delta.";
RL Biochem. J. 254:743-750(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-84.
RX PubMed=2734312; DOI=10.1073/pnas.86.12.4619;
RA Kudo S., Fukuda M.;
RT "Structural organization of glycophorin A and B genes: glycophorin B gene
RT evolved by homologous recombination at Alu repeat sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4619-4623(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Blood;
RA Hsu K., Chi N., Lin M.;
RT "Extensive alternative splicing of glycophorins in Southeast Asian
RT populations.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT M(V) SER-22, VARIANTS MIT
RP MET-48 AND HIS-54, VARIANT S(D) ARG-58, AND VARIANT THR-84.
RC TISSUE=Blood;
RX PubMed=11239234; DOI=10.1046/j.1537-2995.2001.41020269.x;
RA Storry J.R., Reid M.E., MacLennan S., Lubenko A., Nortman P.;
RT "The low-incidence MNS antigens M(v), s(D), and Mit arise from single amino
RT acid substitutions on GPB.";
RL Transfusion 41:269-275(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-58.
RC TISSUE=Blood;
RX PubMed=2016325; DOI=10.1016/s0021-9258(20)89637-9;
RA Huang C.-H., Blumenfeld O.O.;
RT "Molecular genetics of human erythrocyte MiIII and MiVI glycophorins. Use
RT of a pseudoexon in construction of two delta-alpha-delta hybrid genes
RT resulting in antigenic diversification.";
RL J. Biol. Chem. 266:7248-7255(1991).
RN [10]
RP PROTEIN SEQUENCE OF 20-90.
RX PubMed=3595615; DOI=10.1111/j.1432-1033.1987.tb13479.x;
RA Dahr W., Beyreuther K., Moulds J., Unger P.;
RT "Hybrid glycophorins from human erythrocyte membranes. I. Isolation and
RT complete structural analysis of the hybrid sialoglycoprotein from Dantu-
RT positive red cells of the N.E. variety.";
RL Eur. J. Biochem. 166:31-36(1987).
RN [11]
RP PROTEIN SEQUENCE OF 20-90.
RX PubMed=3571235; DOI=10.1016/s0021-9258(18)45646-3;
RA Blanchard D., Dahr W., Hummel M., Latron F., Beyreuther K., Cartron J.-P.;
RT "Glycophorins B and C from human erythrocyte membranes. Purification and
RT sequence analysis.";
RL J. Biol. Chem. 262:5808-5811(1987).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-45.
RX PubMed=1611092;
RA Huang C.-H., Spruell P., Moulds J.J., Blumenfeld O.O.;
RT "Molecular basis for the human erythrocyte glycophorin specifying the
RT Miltenberger class I (MiI) phenotype.";
RL Blood 80:257-263(1992).
RN [13]
RP PROTEIN SEQUENCE OF 20-40, AND GLYCOSYLATION AT THR-36 AND SER-38.
RX PubMed=7681597; DOI=10.1073/pnas.90.6.2495;
RA Nakada H., Inoue M., Numata Y., Tanaka N., Funakoshi I., Fukui S.,
RA Mellors A., Yamashina I.;
RT "Epitopic structure of Tn glycophorin A for an anti-Tn antibody (MLS
RT 128).";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2495-2499(1993).
CC -!- FUNCTION: This protein is a minor sialoglycoprotein in erythrocyte
CC membranes.
CC -!- INTERACTION:
CC P06028; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-10194756, EBI-18053395;
CC P06028; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-10194756, EBI-7545592;
CC P06028; Q99500: S1PR3; NbExp=3; IntAct=EBI-10194756, EBI-10634734;
CC P06028; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-10194756, EBI-741480;
CC P06028; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-10194756, EBI-10173939;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P06028-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P06028-2; Sequence=VSP_047824;
CC -!- PTM: The N-terminal extracellular domain is heavily glycosylated on
CC serine and threonine residues. {ECO:0000269|PubMed:7681597}.
CC -!- POLYMORPHISM: Along with GYPA, GYPB is responsible for the MNS blood
CC group system. The molecular basis of the S/s blood group antigen is a
CC single variation in position 48; Thr-48 corresponds to s=MSN4 and Met-
CC 48 to S=MNS3.
CC -!- SIMILARITY: Belongs to the glycophorin-A family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=mns";
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DR EMBL; J02982; AAA52573.1; -; mRNA.
DR EMBL; X08055; CAB42645.1; -; mRNA.
DR EMBL; M24137; AAA58626.1; -; Genomic_DNA.
DR EMBL; M24130; AAA58626.1; JOINED; Genomic_DNA.
DR EMBL; M24131; AAA58626.1; JOINED; Genomic_DNA.
DR EMBL; M24135; AAA58626.1; JOINED; Genomic_DNA.
DR EMBL; AY950609; AAX53130.1; -; mRNA.
DR EMBL; AY950610; AAX53131.1; -; mRNA.
DR EMBL; AY950611; AAX53132.1; -; mRNA.
DR EMBL; EU338223; ACA96781.1; -; mRNA.
DR EMBL; EU338235; ACA96793.1; -; mRNA.
DR EMBL; AC093890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX05058.1; -; Genomic_DNA.
DR EMBL; BC069310; AAH69310.1; -; mRNA.
DR EMBL; BC121077; AAI21078.1; -; mRNA.
DR EMBL; BC121078; AAI21079.1; -; mRNA.
DR EMBL; M60708; AAC63048.1; -; Genomic_DNA.
DR CCDS; CCDS54809.1; -. [P06028-1]
DR PIR; B33931; B33931.
DR RefSeq; NP_001291311.1; NM_001304382.1.
DR RefSeq; NP_002091.3; NM_002100.5. [P06028-1]
DR AlphaFoldDB; P06028; -.
DR SMR; P06028; -.
DR BioGRID; 109249; 61.
DR IntAct; P06028; 52.
DR STRING; 9606.ENSP00000427690; -.
DR GlyConnect; 188; 4 O-Linked glycans.
DR GlyConnect; 189; 7 O-Linked glycans (1 site).
DR GlyGen; P06028; 5 sites, 13 O-linked glycans (3 sites).
DR iPTMnet; P06028; -.
DR PhosphoSitePlus; P06028; -.
DR BioMuta; GYPB; -.
DR DMDM; 380865467; -.
DR MassIVE; P06028; -.
DR PaxDb; P06028; -.
DR PeptideAtlas; P06028; -.
DR PRIDE; P06028; -.
DR Antibodypedia; 45444; 110 antibodies from 18 providers.
DR DNASU; 2994; -.
DR Ensembl; ENST00000502664.6; ENSP00000427690.1; ENSG00000250361.9. [P06028-1]
DR Ensembl; ENST00000513128.5; ENSP00000425244.1; ENSG00000250361.9. [P06028-2]
DR GeneID; 2994; -.
DR KEGG; hsa:2994; -.
DR MANE-Select; ENST00000502664.6; ENSP00000427690.1; NM_002100.6; NP_002091.4.
DR UCSC; uc003ijm.2; human. [P06028-1]
DR CTD; 2994; -.
DR DisGeNET; 2994; -.
DR GeneCards; GYPB; -.
DR HGNC; HGNC:4703; GYPB.
DR HPA; ENSG00000250361; Tissue enriched (bone).
DR MalaCards; GYPB; -.
DR MIM; 111740; phenotype.
DR MIM; 617923; gene.
DR neXtProt; NX_P06028; -.
DR OpenTargets; ENSG00000250361; -.
DR PharmGKB; PA29081; -.
DR VEuPathDB; HostDB:ENSG00000250361; -.
DR eggNOG; ENOG502R1BQ; Eukaryota.
DR GeneTree; ENSGT00550000075214; -.
DR HOGENOM; CLU_154690_1_0_1; -.
DR InParanoid; P06028; -.
DR PhylomeDB; P06028; -.
DR TreeFam; TF338555; -.
DR PathwayCommons; P06028; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P06028; -.
DR SIGNOR; P06028; -.
DR BioGRID-ORCS; 2994; 18 hits in 1026 CRISPR screens.
DR ChiTaRS; GYPB; human.
DR GeneWiki; GYPB; -.
DR GenomeRNAi; 2994; -.
DR Pharos; P06028; Tbio.
DR PRO; PR:P06028; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P06028; protein.
DR Bgee; ENSG00000250361; Expressed in trabecular bone tissue and 117 other tissues.
DR ExpressionAtlas; P06028; baseline and differential.
DR Genevisible; P06028; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR InterPro; IPR001195; Glycophorin.
DR InterPro; IPR018938; Glycophorin_CS.
DR PANTHER; PTHR13813; PTHR13813; 2.
DR PROSITE; PS00312; GLYCOPHORIN_A; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Blood group antigen; Cell membrane;
KW Direct protein sequencing; Glycoprotein; Membrane; Reference proteome;
KW Sialic acid; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3571235,
FT ECO:0000269|PubMed:3595615, ECO:0000269|PubMed:7681597"
FT CHAIN 20..91
FT /note="Glycophorin-B"
FT /id="PRO_0000012136"
FT TOPO_DOM 20..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 33
FT /note="Not glycosylated"
FT SITE 34
FT /note="Not glycosylated"
FT CARBOHYD 36
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7681597"
FT CARBOHYD 38
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:7681597"
FT VAR_SEQ 13..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047824"
FT VARIANT 22
FT /note="T -> S (in M(v) antigen; dbSNP:rs199937833)"
FT /evidence="ECO:0000269|PubMed:11239234"
FT /id="VAR_047948"
FT VARIANT 48
FT /note="T -> M (in S antigen and Mit antigen;
FT dbSNP:rs7683365)"
FT /evidence="ECO:0000269|PubMed:11239234"
FT /id="VAR_003192"
FT VARIANT 54
FT /note="R -> H (in Mit antigen; dbSNP:rs370332485)"
FT /evidence="ECO:0000269|PubMed:11239234"
FT /id="VAR_047949"
FT VARIANT 58
FT /note="P -> R (in s(D) antigen; dbSNP:rs374811215)"
FT /evidence="ECO:0000269|PubMed:11239234"
FT /id="VAR_047950"
FT VARIANT 84
FT /note="S -> T (in dbSNP:rs1132783)"
FT /evidence="ECO:0000269|PubMed:11239234,
FT ECO:0000269|PubMed:2734312, ECO:0000269|PubMed:3477806"
FT /id="VAR_030785"
FT CONFLICT 69
FT /note="C -> S (in Ref. 10; AA sequence and 11; AA
FT sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 91 AA; 9782 MW; EF15A64BAA929B7B CRC64;
MYGKIIFVLL LSEIVSISAL STTEVAMHTS TSSSVTKSYI SSQTNGETGQ LVHRFTVPAP
VVIILIILCV MAGIIGTILL ISYSIRRLIK A
