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 27-MAR-2024, entry version 193. DE RecName: Full=Glycophorin-B {ECO:0000305}; 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 {ECO:0000312|HGNC:HGNC:4703}; 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). RN [14] {ECO:0007744|PDB:8CRT, ECO:0007744|PDB:8CS9, ECO:0007744|PDB:8CSL} RP STRUCTURE BY ELECTRON MICROSCOPY (2.74 ANGSTROMS), FUNCTION, SUBUNIT, RP ANKYRIN-1 COMPLEX IDENTIFICATION, AND INTERACTION WITH RHAG. RX PubMed=35835865; DOI=10.1038/s41594-022-00792-w; RA Vallese F., Kim K., Yen L.Y., Johnston J.D., Noble A.J., Cali T., RA Clarke O.B.; RT "Architecture of the human erythrocyte ankyrin-1 complex."; RL Nat. Struct. Mol. Biol. 29:706-718(2022). CC -!- FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex CC involved in the stability and shape of the erythrocyte membrane. CC {ECO:0000269|PubMed:35835865}. CC -!- SUBUNIT: Component of the ankyrin-1 complex in the erythrocyte, CC composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1 CC (PubMed:35835865). Interacts (via the N-terminal) with RHAG; this CC interaction bridges the (RHAG)2(RHCE) heterotrimer with the SLC4A1 Band CC 3 I dimer complexed with GYPA (PubMed:35835865). CC {ECO:0000269|PubMed:35835865}. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8CRT; EM; 3.00 A; P=1-91. DR PDB; 8CS9; EM; 2.74 A; P=1-91. DR PDB; 8CSL; EM; 25.00 A; P=1-91. DR PDBsum; 8CRT; -. DR PDBsum; 8CS9; -. DR PDBsum; 8CSL; -. DR AlphaFoldDB; P06028; -. DR EMDB; EMD-26958; -. DR EMDB; EMD-26960; -. DR EMDB; EMD-26965; -. 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 GlyCosmos; P06028; 4 sites, 13 glycans. 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; 9606-ENSP00000427690; -. DR PeptideAtlas; P06028; -. DR Pumba; P06028; -. DR Antibodypedia; 45444; 134 antibodies from 18 providers. DR DNASU; 2994; -. DR Ensembl; ENST00000502664.6; ENSP00000427690.1; ENSG00000250361.10. [P06028-1] DR Ensembl; ENST00000513128.5; ENSP00000425244.1; ENSG00000250361.10. [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 AGR; HGNC:4703; -. 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 1095 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 118 other cell types or tissues. DR ExpressionAtlas; P06028; baseline and differential. DR GO; GO:0170014; C:ankyrin-1 complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR Gene3D; 1.20.5.70; -; 1. DR InterPro; IPR001195; Glycophorin. DR InterPro; IPR018938; Glycophorin_CS. DR InterPro; IPR049535; GYPA_B. DR PANTHER; PTHR13813; GLYCOPHORIN; 1. DR PANTHER; PTHR13813:SF2; GLYCOPHORIN-B; 1. DR Pfam; PF01102; Glycophorin_A; 1. DR PROSITE; PS00312; GLYCOPHORIN_A; 1. DR Genevisible; P06028; HS. PE 1: Evidence at protein level; KW 3D-structure; 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" FT HELIX 60..90 FT /evidence="ECO:0007829|PDB:8CRT" SQ SEQUENCE 91 AA; 9782 MW; EF15A64BAA929B7B CRC64; MYGKIIFVLL LSEIVSISAL STTEVAMHTS TSSSVTKSYI SSQTNGETGQ LVHRFTVPAP VVIILIILCV MAGIIGTILL ISYSIRRLIK A //