ID GLPB_HUMAN Reviewed; 91 AA. AC P06028; Q0VAF4; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 2. DT 04-NOV-2008, entry version 87. DE RecName: Full=Glycophorin-B; DE AltName: Full=PAS-3; DE AltName: Full=Sialoglycoprotein delta; DE AltName: Full=SS-active sialoglycoprotein; DE AltName: CD_antigen=CD235b; DE Flags: Precursor; GN Name=GYPB; Synonyms=GPB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88016166; PubMed=3477806; RA Siebert P.D., Fukuda M.; RT "Molecular cloning of a human glycophorin B cDNA: nucleotide sequence RT and genomic relationship to glycophorin A."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6735-6739(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-84. RX MEDLINE=89061610; PubMed=3196288; RA Tate C.G., Tanner M.J.A.; RT "Isolation of cDNA clones for human erythrocyte membrane RT sialoglycoproteins alpha and delta."; RL Biochem. J. 254:743-750(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89282822; PubMed=2734312; RA Kudo S., Fukuda M.; RT "Structural organization of glycophorin A and B genes: glycophorin B RT gene 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 [LARGE SCALE MRNA], AND VARIANT SER-84. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-58. RC TISSUE=Blood; RX MEDLINE=91201388; PubMed=2016325; RA Huang C.-H., Blumenfeld O.O.; RT "Molecular genetics of human erythrocyte MiIII and MiVI glycophorins. RT Use of a pseudoexon in construction of two delta-alpha-delta hybrid RT genes resulting in antigenic diversification."; RL J. Biol. Chem. 266:7248-7255(1991). RN [6] RP PROTEIN SEQUENCE OF 20-90. RX MEDLINE=87194779; PubMed=3571235; RA Blanchard D., Dahr W., Hummel M., Latron F., Beyreuther K., RA Cartron J.-P.; RT "Glycophorins B and C from human erythrocyte membranes. Purification RT and sequence analysis."; RL J. Biol. Chem. 262:5808-5811(1987). RN [7] RP PROTEIN SEQUENCE OF 20-90. RX MEDLINE=87246688; PubMed=3595615; RA Dahr W., Beyreuther K., Moulds J., Unger P.; RT "Hybrid glycophorins from human erythrocyte membranes. I. Isolation RT and complete structural analysis of the hybrid sialoglycoprotein from RT Dantu-positive red cells of the N.E. variety."; RL Eur. J. Biochem. 166:31-36(1987). RN [8] RP NUCLEOTIDE SEQUENCE OF 20-45. RX MEDLINE=92305340; 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). CC -!- FUNCTION: This protein is a minor sialoglycoprotein in erythrocyte CC membranes. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: The N-terminal extracellular domain is heavily glycosylated CC on serine and threonine residues (By similarity). CC -!- POLYMORPHISM: Along with GYPA, GYPB is responsible for the MNS CC blood group system. The molecular basis of the S/s blood group CC antigen is a single variation in position 48; Thr-48 corresponds CC to s=MSN4 and Met-48 to S=MNS3. CC -!- SIMILARITY: Belongs to the glycophorin A family. CC -!- WEB RESOURCE: Name=BGMUT; Note=Blood group antigen gene mutation CC database"; CC URL="http://www.ncbi.nlm.nih.gov/projects/mhc/xslcgi.fcgi?cmd=bgmut/systems_info&system=mns"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs 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; BC069310; AAH69310.1; -; mRNA. DR EMBL; BC121077; AAI21078.1; -; mRNA. DR EMBL; BC121078; AAI21079.1; -; mRNA. DR EMBL; M60708; AAC63048.1; -; Genomic_DNA. DR PIR; B33931; B33931. DR RefSeq; NP_002091.2; -. DR UniGene; Hs.654368; -. DR HSSP; P02724; 1AFO. DR GlycoSuiteDB; P06028; -. DR Ensembl; ENSG00000153143; Homo sapiens. DR GeneID; 2994; -. DR KEGG; hsa:2994; -. DR HGNC; HGNC:4703; GYPB. DR MIM; 111740; gene+phenotype. DR PharmGKB; PA29081; -. DR HOVERGEN; P06028; -. DR NextBio; 11866; -. DR CleanEx; HS_GYPB; -. DR GermOnline; ENSG00000153143; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR InterPro; IPR001195; Glycophorin_A_B. DR PANTHER; PTHR13813; Glycophorin_A_B; 1. DR Pfam; PF01102; Glycophorin_A; 1. DR PROSITE; PS00312; GLYCOPHORIN_A; 1. PE 1: Evidence at protein level; KW Blood group antigen; Direct protein sequencing; Glycoprotein; KW Membrane; Polymorphism; Sialic acid; Signal; Transmembrane. FT SIGNAL 1 19 FT CHAIN 20 91 Glycophorin-B. FT /FTId=PRO_0000012136. FT TOPO_DOM 20 59 Extracellular (Potential). FT TRANSMEM 60 81 Potential. FT TOPO_DOM 82 91 Cytoplasmic (Potential). FT VARIANT 48 48 T -> M (in S antigen; dbSNP:rs7683365). FT /FTId=VAR_003192. FT VARIANT 84 84 T -> S (in dbSNP:rs1132783). FT /FTId=VAR_030785. FT CONFLICT 69 69 C -> S (in Ref. 6 and 7). SQ SEQUENCE 91 AA; 9796 MW; F415A64BAA929B7F CRC64; MYGKIIFVLL LSEIVSISAL STTEVAMHTS TSSSVTKSYI SSQTNGETGQ LVHRFTVPAP VVIILIILCV MAGIIGTILL ISYTIRRLIK A //