# GYPB

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Protein-coding gene in the species Homo sapiens

GYPB Identifiers Aliases GYPB, CD235b, GPB, GPB.NY, GYPHe.NY, GpMiIII, HGpMiIII, HGpMiVI, HGpMiX, MNS, PAS-3, SS, GYP, glycophorin B (MNS blood group), GYPA External IDs OMIM: 617923; GeneCards: GYPB; OMA:GYPB - orthologs Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q31.21 Start 143,996,104 bp[1] End 144,019,380 bp[1] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in trabecular bone bone marrow bone marrow cell testicle monocyte blood buccal mucosa cell Achilles tendon gonad spleen n/a More reference expression data BioGPS More reference expression data Gene ontology Molecular function protein binding Cellular component integral component of plasma membrane membrane plasma membrane integral component of membrane Biological process leukocyte migration Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 2994 n/a Ensembl ENSG00000250361 n/a UniProt P06028 n/a RefSeq (mRNA) NM_001304382 NM_002100 n/a RefSeq (protein) NP_001291311 NP_002091 n/a Location (UCSC) Chr 4: 144 – 144.02 Mb n/a PubMed search [2] n/a Wikidata View/Edit Human

**Glycophorin B (MNS blood group)** (gene designation **GYPB**) also known as sialoglycoprotein delta and SS-active sialoglycoprotein is a [protein](/source/Protein) which in humans is encoded by the *GYPB* [gene](/source/Gene).[3] GYPB has also recently been designated **CD235b** ([cluster of differentiation](/source/Cluster_of_differentiation) 235b).

## Function

[Glycophorin A](/source/GYPA) (GYPA) and B (GYPB; this protein) are major [sialoglycoproteins](/source/Sialoglycoproteins) of the human [erythrocyte](/source/Erythrocyte) membrane which bear the [antigenic determinants](/source/Epitope) for the MN and Ss [blood groups](/source/MNS_antigen_system) respectively. In addition to the M or N and S or s antigens, that commonly occur in all populations, about 40 related variant phenotypes have been identified. These variants include the Miltenberger (Mi) complex and several isoforms of Stones (Sta); also Dantu, Sat, Henshaw (He or MNS6), Mg and deletion variants Ena, S-s-U- and Mk. Most of these are the result of gene recombinations between GYPA and GYPB.[3]

## Genomics

The gene is located on the long arm of [chromosome 4](/source/Chromosome_4) (4q28-q31) and has 5 exons. It was first sequenced in 1987[4] the peptide sequence of 72 amino acids having been determined earlier that year.

The gene has 97% sequence homology with the glycophorin A gene from the 5' UTR approximately 1 kilobase upstream from the exon encoding the transmembrane regions to the portion of the coding sequence encoding the first 45 amino acids. There is a signal sequence of 19 amino acid residues. The leader peptide differs by one amino acid and the next 26 amino acids are identical. Amino acids 27-55 of glycophorin A are absent from glycophorin B. This section includes an N-glycosylation site. Only O-glycosylation sites are found on glycoprotein B and these are linked via [serine](/source/Serine) or [threonine](/source/Threonine). Residues 80-100 of glycophorin A and 51-71 of glycophorin B are very similar. The intervening residues in contrast differ significantly. The antigenic determinant for the blood group Ss is located at residue 29 where S has a [methionine](/source/Methionine) and s a threonine. This is due to a mutation at nucleotide 143 (C->T). The S antigen is also known as MNS3 and the s antigen as MNS4.

It seems likely that this gene evolved by gene duplication and subsequent mutation of glycophorin A. The transition site from homologous to nonhomologous sequences can be localized within [Alu repeat](/source/Alu_repeat) sequences.

## Molecular biology

There are ~80000 copies of glycophorin B per erythrocyte. Both glycophorin A and B are expressed on the renal endothelium and epithelium.

The first 40 amino acids of the mature protein are extracellular. The next 22 form a transmembrane segment and the remainder are intra cellular.

## Blood groups

The MNS blood group was the second set of antigens discovered. M and N were identified in 1927 by Landsteiner and Levine. S and s in were described later in 1947

The frequencies of these antigens are

- M: 78% [Caucasian](/source/White_people); 74% [African descent](/source/African_descent)

- N: 72% Caucasian; 75% African descent

- S: 55% Caucasian; 31% African descent

- s: 89% Caucasian; 93% African descent

## Molecular medicine

### Transfusion medicine

The M and N antigens differ at two amino acid residues: the M allele has serine at position 1 (C at nucleotide 2) and glycine at position 5 (G at nucleotide 14) while the N allele has leucine at position 1 (T at nucleotide 2) and glutamate at position 5 (A at nucleotide 14)

Glycophorin B carries the blood group antigens 'N', Ss, and U. Both glycophorin A and B bind the *[Vicia graminea](/source/Vicia_graminea)* anti-N lectin. S and s antigens are not affected by treatment with [trypsin](/source/Trypsin) or [sialidase](/source/Sialidase) but are destroyed or much depressed by treatment with [papain](/source/Papain), [pronase](/source/Pronase) or [alpha-chymotrypsin](/source/Alpha-chymotrypsin).

There are about 40 known variants in the MNS blood group system. These have arisen largely as a result of mutations within the 4 kb region coding for the extracellular domain. These include the antigens Mv, Dantu, Henshaw (He), Orriss (Or), Miltenberger, Raddon (FR) and Stones (Sta). [Chimpanzees](/source/Common_chimpanzee) also have an MN blood antigen system.[5] In chimpanzees M reacts strong but N only weakly.

### Null mutants

Individuals who lack GypB have the phenotype S-s-U-. This may occur at frequencies of 20% in some African pygmies.

In individuals who lack both glycophorin A and B the phenotype has been designated Mk.[6]

### Dantu antigen

The Dantu antigen was described in 1984.[7] The Dantu antigen has an apparent molecular weight of 29 kilodaltons (kDa) and 99 amino acids. The first 39 amino acids of the Dantu antigen are derived from glycophorin B and residues 40-99 are derived from glycophorin A. Dantu is associated with very weak s antigen, a protease-resistant N antigen and either very weak or no U antigen. There are at least three variants: MD, NE and Ph.[8] The Dantu phenotype occurs with a frequency of Dantu phenotype is ~0.005 in American Blacks and < 0.001 in Germans.[9]

### Henshaw antigen

The Henshaw (He) antigen is due to a mutation of the N terminal region. There are three differences in the first three amino acid residues: the usual form has [Tryptophan](/source/Tryptophan)1-Serine-Threonine-Serine-[Glycine](/source/Glycine)5 while Henshaw has [Leucine](/source/Leucine)1-Serine-Threonine-Threonine-[Glutamate](/source/Glutamate)5. This antigen is rare in Caucasians but occurs at a frequency of 2.1% in US and UK of African origin. It occurs at the rate of 7.0% in blacks in [Natal](/source/Natal_(region))[10] and 2.7% in West Africans.[11] At least 3 variants of this antigen have been identified.

### Miltenberger subsystem

The Miltenberger (Mi) subsystem originally consisting of five phenotypes (Mia, Vw, Mur, Hil and Hut)[12] now has 11 recognised phenotypes numbered I to XI (The antigen 'Mur' is named after to the patient the original serum was isolated from - a Mrs Murrel.) The name originally given to this complex refers to the reaction erythrocytes gave to the standard Miltenberger antisera used to test them. The subclasses were based on additional reactions with other standard antisera.

Mi-I (Mia), Mi-II(Vw), Mi-VII and Mi-VIII are carried on glycophorin A. Mi-I is due to a mutation at amino acid 28 (threonine to methionine: C->T at nucleotide 83) resulting in a loss of the glycosylation at the asparagine26 residue.[13][14] Mi-II is due to a mutation at amino acid 28 (threonine to [lysine](/source/Lysine):C->A at nucleotide 83). Similar to the case of Mi-I this mutation results in a loss of the glycosylation at the [asparagine](/source/Asparagine)26 residue. This alteration in glycosylation is detectable by the presence of a new 32kDa glycoprotein stainable with PAS.[15] Mi-VII is due to a double mutation in glycophorin A converting an [arginine](/source/Arginine) residue into a threonine residue and a [tyrosine](/source/Tyrosine) residue into a serine at the positions 49 and 52 respectively.[16] The threonine-49 residue is glycosylated. This appears to be the origin of one of the Mi-VII specific antigens (Anek) which is known to lie between residues 40-61 of glycophorin A and comprises sialic acid residue(s) attached to O-glycosidically linked oligosaccharide(s). This also explains the loss of a high frequency antigen ((EnaKT)) found in normal glycophorin A which is located within the residues 46–56. Mi-VIII is due to a mutation at amino acid residue 49 ([arginine](/source/Arginine)->threonine).[17] M-VIII shares the Anek determinant with MiVII.[18] Mi-III, Mi-VI and Mi-X are due to rearrangements of glycophorin A and B in the order GlyA (alpha)-GlyB (delta)-GlyA (alpha).[19] Mil-IX in contrast is a reverse alpha-delta-alpha hybrid gene.[20] Mi-V, MiV(J.L.) and Sta are due to unequal but homologous crossing-over between alpha and delta glycophorin genes.[21] The MiV and MiV(J.L.) genes are arranged in the same 5' alpha-delta 3' frame whereas Sta gene is in a reciprocal 5'delta-alpha 3' configuration.[22]

Although uncommon in Caucasians (0.0098%) and [Japanese](/source/Japan) (0.006%), the frequency of Mi-III is exceptionally high in several [Taiwanese](/source/Taiwan) aboriginal tribes (up to 90%). In contrast its frequency is 2-3% in Han Taiwanese (Minnan). The Mi-III phenotype occurs in 6.28% of Hong Kong Chinese.[23]

Mi-IX (MNS32) occurs with a frequency of 0.43% in [Denmark](/source/Denmark).[24]

### Stone's antigen

Stones (Sta) has been shown to be the product of a hybrid gene of which the 5'-half is derived from the glycophorin B whereas the 3'-half is derived from the glycophorin A. Several isoforms are known. This antigen is now considered to be part of the Miltenberger complex.

### Sat antigen

A related antigen is Sat. This gene has six exons of which exon I to exon IV are identical to the N allele of glycophorin A whereas its 3' portion, including exon V and exon VI, are derived from the glycophorin B gene. The mature protein SAT protein contains 104 amino acid residues.

### Orissa antigen

Orriss (Or) appears to be a mutant of glyphorin A but its precise nature has not yet been determined.[25]

### Transfusion reactions

Both anti-S and anti-s have been implicated in transfusion reactions and haemolytic disease of the newborn. Anti-M although occurring naturally has rarely been implicated in transfusion reactions. Anti-N is not considered to cause transfusion reactions. Severe reactions have been reported with anti-U and anti-Miltenberger. Anti Mi-I (Vw) and Mi-III has been recognised as a cause of haemolytic disease of the newborn.[26] Raddon has been associated with severe transfusion reactions.[27]

## Other areas

Glycophorin B acts as a receptor for erythrocyte binding Ligand (EBl-1) of *[Plasmodium falciparum](/source/Plasmodium_falciparum)* involved in malaria.[28] Both the Dantu and the S-s-U- cells phenotypes have been shown to be protective against *P. falciparum* infection while the Henshaw phenotype is not protective.[29][30]

Influenza A and B bind to glycophorin B.[18]

## References

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1. **[^](#cite_ref-pmid1722368_24-0)** Skov F, Green C, Daniels G, Khalid G, Tippett P (1991). "Miltenberger class IX of the MNS blood group system". *Vox Sang*. **61** (2): 130–6. [doi](/source/Doi_(identifier)):[10.1111/j.1423-0410.1991.tb00258.x](https://doi.org/10.1111%2Fj.1423-0410.1991.tb00258.x). [PMID](/source/PMID_(identifier)) [1722368](https://pubmed.ncbi.nlm.nih.gov/1722368). [S2CID](/source/S2CID_(identifier)) [24337520](https://api.semanticscholar.org/CorpusID:24337520).

1. **[^](#cite_ref-pmid2442891_25-0)** Bacon JM, Macdonald EB, Young SG, Connell T (1987). "Evidence that the low frequency antigen Orriss is part of the MN blood group system". *Vox Sang*. **52** (4): 330–4. [doi](/source/Doi_(identifier)):[10.1111/j.1423-0410.1987.tb04902.x](https://doi.org/10.1111%2Fj.1423-0410.1987.tb04902.x). [PMID](/source/PMID_(identifier)) [2442891](https://pubmed.ncbi.nlm.nih.gov/2442891). [S2CID](/source/S2CID_(identifier)) [36810910](https://api.semanticscholar.org/CorpusID:36810910).

1. **[^](#cite_ref-pmid2442890_26-0)** Rearden A, Frandson S, Carry JB (1987). "Severe hemolytic disease of the newborn due to anti-Vw and detection of glycophorin A antigens on the Miltenberger I sialoglycoprotein by Western blotting". *Vox Sang*. **52** (4): 318–21. [doi](/source/Doi_(identifier)):[10.1111/j.1423-0410.1987.tb04900.x](https://doi.org/10.1111%2Fj.1423-0410.1987.tb04900.x). [PMID](/source/PMID_(identifier)) [2442890](https://pubmed.ncbi.nlm.nih.gov/2442890). [S2CID](/source/S2CID_(identifier)) [33092281](https://api.semanticscholar.org/CorpusID:33092281).

1. **[^](#cite_ref-pmid7466911_27-0)** Baldwin ML, Barrasso C, Gavin J (1981). "The first example of a Raddon-like antibody as a cause of a transfusion reaction". *Transfusion*. **21** (1): 86–9. [doi](/source/Doi_(identifier)):[10.1046/j.1537-2995.1981.21181127491.x](https://doi.org/10.1046%2Fj.1537-2995.1981.21181127491.x). [PMID](/source/PMID_(identifier)) [7466911](https://pubmed.ncbi.nlm.nih.gov/7466911). [S2CID](/source/S2CID_(identifier)) [39840648](https://api.semanticscholar.org/CorpusID:39840648).

1. **[^](#cite_ref-pmid8078523_28-0)** Dolan SA, Proctor JL, Alling DW, Okubo Y, Wellems TE, Miller LH (March 1994). ["Glycophorin B as an EBA-175 independent Plasmodium falciparum receptor of human erythrocytes"](https://zenodo.org/record/1258369). *Mol. Biochem. Parasitol*. **64** (1): 55–63. [doi](/source/Doi_(identifier)):[10.1016/0166-6851(94)90134-1](https://doi.org/10.1016%2F0166-6851%2894%2990134-1). [PMID](/source/PMID_(identifier)) [8078523](https://pubmed.ncbi.nlm.nih.gov/8078523).

1. **[^](#cite_ref-pmid8112738_29-0)** Field SP, Hempelmann E, Mendelow BV, Fleming AF (February 1994). "Glycophorin variants and Plasmodium falciparum: protective effect of the Dantu phenotype in vitro". *Hum. Genet*. **93** (2): 148–50. [doi](/source/Doi_(identifier)):[10.1007/BF00210600](https://doi.org/10.1007%2FBF00210600). [PMID](/source/PMID_(identifier)) [8112738](https://pubmed.ncbi.nlm.nih.gov/8112738). [S2CID](/source/S2CID_(identifier)) [28191970](https://api.semanticscholar.org/CorpusID:28191970).

1. **[^](#cite_ref-pmid6356506_30-0)** Facer CA (1983). ["Erythrocyte sialoglycoproteins and Plasmodium falciparum invasion"](https://doi.org/10.1016%2F0035-9203%2883%2990130-X). *Trans. R. Soc. Trop. Med. Hyg*. **77** (4): 524–30. [doi](/source/Doi_(identifier)):[10.1016/0035-9203(83)90130-X](https://doi.org/10.1016%2F0035-9203%2883%2990130-X). [PMID](/source/PMID_(identifier)) [6356506](https://pubmed.ncbi.nlm.nih.gov/6356506).

## Further reading

- Blumenfeld OO, Huang CH (1996). ["Molecular genetics of the glycophorin gene family, the antigens for MNSs blood groups: multiple gene rearrangements and modulation of splice site usage result in extensive diversification"](https://doi.org/10.1002%2Fhumu.1380060302). *Hum. Mutat*. **6** (3): 199–209. [doi](/source/Doi_(identifier)):[10.1002/humu.1380060302](https://doi.org/10.1002%2Fhumu.1380060302). [PMID](/source/PMID_(identifier)) [8535438](https://pubmed.ncbi.nlm.nih.gov/8535438). [S2CID](/source/S2CID_(identifier)) [34245274](https://api.semanticscholar.org/CorpusID:34245274).

- Blumenfeld OO, Huang CH (1997). "Molecular genetics of glycophorin MNS variants". *Transfusion Clinique et Biologique*. **4** (4): 357–65. [doi](/source/Doi_(identifier)):[10.1016/s1246-7820(97)80041-9](https://doi.org/10.1016%2Fs1246-7820%2897%2980041-9). [PMID](/source/PMID_(identifier)) [9269716](https://pubmed.ncbi.nlm.nih.gov/9269716).

- Huang CH, Spruell P, Moulds JJ, Blumenfeld OO (1992). ["Molecular basis for the human erythrocyte glycophorin specifying the Miltenberger class I (MiI) phenotype"](https://doi.org/10.1182%2Fblood.V80.1.257.257). *Blood*. **80** (1): 257–63. [doi](/source/Doi_(identifier)):[10.1182/blood.V80.1.257.257](https://doi.org/10.1182%2Fblood.V80.1.257.257). [PMID](/source/PMID_(identifier)) [1611092](https://pubmed.ncbi.nlm.nih.gov/1611092).

- Rearden A, Phan H, Dubnicoff T, et al. (1990). ["Identification of the crossing-over point of a hybrid gene encoding human glycophorin variant Sta. Similarity to the crossing-over point in haptoglobin-related genes"](https://doi.org/10.1016%2FS0021-9258%2819%2938841-6). *J. Biol. Chem*. **265** (16): 9259–63. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(19)38841-6](https://doi.org/10.1016%2FS0021-9258%2819%2938841-6). [PMID](/source/PMID_(identifier)) [1971625](https://pubmed.ncbi.nlm.nih.gov/1971625).

- Huang CH, Blumenfeld OO (1991). ["Identification of recombination events resulting in three hybrid genes encoding human MiV, MiV(J.L.), and Sta glycophorins"](https://doi.org/10.1182%2Fblood.V77.8.1813.1813). *Blood*. **77** (8): 1813–20. [doi](/source/Doi_(identifier)):[10.1182/blood.V77.8.1813.1813](https://doi.org/10.1182%2Fblood.V77.8.1813.1813). [PMID](/source/PMID_(identifier)) [2015404](https://pubmed.ncbi.nlm.nih.gov/2015404).

- Huang CH, Blumenfeld OO (1991). ["Molecular genetics of human erythrocyte MiIII and MiVI glycophorins. Use of a pseudoexon in construction of two delta-alpha-delta hybrid genes resulting in antigenic diversification"](https://doi.org/10.1016%2FS0021-9258%2820%2989637-9). *J. Biol. Chem*. **266** (11): 7248–55. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(20)89637-9](https://doi.org/10.1016%2FS0021-9258%2820%2989637-9). [PMID](/source/PMID_(identifier)) [2016325](https://pubmed.ncbi.nlm.nih.gov/2016325).

- Kudo S, Fukuda M (1990). ["Identification of a novel human glycophorin, glycophorin E, by isolation of genomic clones and complementary DNA clones utilizing polymerase chain reaction"](https://doi.org/10.1016%2FS0021-9258%2819%2940164-6). *J. Biol. Chem*. **265** (2): 1102–10. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(19)40164-6](https://doi.org/10.1016%2FS0021-9258%2819%2940164-6). [PMID](/source/PMID_(identifier)) [2295603](https://pubmed.ncbi.nlm.nih.gov/2295603).

- Kudo S, Fukuda M (1989). ["Structural organization of glycophorin A and B genes: glycophorin B gene evolved by homologous recombination at Alu repeat sequences"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC287322). *Proc. Natl. Acad. Sci. U.S.A*. **86** (12): 4619–23. [Bibcode](/source/Bibcode_(identifier)):[1989PNAS...86.4619K](https://ui.adsabs.harvard.edu/abs/1989PNAS...86.4619K). [doi](/source/Doi_(identifier)):[10.1073/pnas.86.12.4619](https://doi.org/10.1073%2Fpnas.86.12.4619). [PMC](/source/PMC_(identifier)) [287322](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC287322). [PMID](/source/PMID_(identifier)) [2734312](https://pubmed.ncbi.nlm.nih.gov/2734312).

- Tate CG, Tanner MJ (1988). ["Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1135146). *Biochem. J*. **254** (3): 743–50. [doi](/source/Doi_(identifier)):[10.1042/bj2540743](https://doi.org/10.1042%2Fbj2540743). [PMC](/source/PMC_(identifier)) [1135146](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1135146). [PMID](/source/PMID_(identifier)) [3196288](https://pubmed.ncbi.nlm.nih.gov/3196288).

- Siebert PD, Fukuda M (1987). ["Molecular cloning of a human glycophorin B cDNA: nucleotide sequence and genomic relationship to glycophorin A."](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC299158) *Proc. Natl. Acad. Sci. U.S.A*. **84** (19): 6735–9. [Bibcode](/source/Bibcode_(identifier)):[1987PNAS...84.6735S](https://ui.adsabs.harvard.edu/abs/1987PNAS...84.6735S). [doi](/source/Doi_(identifier)):[10.1073/pnas.84.19.6735](https://doi.org/10.1073%2Fpnas.84.19.6735). [PMC](/source/PMC_(identifier)) [299158](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC299158). [PMID](/source/PMID_(identifier)) [3477806](https://pubmed.ncbi.nlm.nih.gov/3477806).

- Blanchard D, Dahr W, Hummel M, et al. (1987). ["Glycophorins B and C from human erythrocyte membranes. Purification and sequence analysis"](https://doi.org/10.1016%2FS0021-9258%2818%2945646-3). *J. Biol. Chem*. **262** (12): 5808–11. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(18)45646-3](https://doi.org/10.1016%2FS0021-9258%2818%2945646-3). [PMID](/source/PMID_(identifier)) [3571235](https://pubmed.ncbi.nlm.nih.gov/3571235).

- Dahr W, Beyreuther K, Moulds J, Unger P (1987). ["Hybrid glycophorins from human erythrocyte membranes. I. Isolation and complete structural analysis of the hybrid sialoglycoprotein from Dantu-positive red cells of the N.E. variety"](https://doi.org/10.1111%2Fj.1432-1033.1987.tb13479.x). *Eur. J. Biochem*. **166** (1): 31–6. [doi](/source/Doi_(identifier)):[10.1111/j.1432-1033.1987.tb13479.x](https://doi.org/10.1111%2Fj.1432-1033.1987.tb13479.x). [PMID](/source/PMID_(identifier)) [3595615](https://pubmed.ncbi.nlm.nih.gov/3595615).

- Onda M, Fukuda M (1995). "Detailed physical mapping of the genes encoding glycophorins A, B and E, as revealed by P1 plasmids containing human genomic DNA". *Gene*. **159** (2): 225–30. [doi](/source/Doi_(identifier)):[10.1016/0378-1119(95)00075-H](https://doi.org/10.1016%2F0378-1119%2895%2900075-H). [PMID](/source/PMID_(identifier)) [7622054](https://pubmed.ncbi.nlm.nih.gov/7622054).

- Kudo S, Onda M, Fukuda M (1995). ["Characterization of glycophorin A transcripts: control by the common erythroid-specific promoter and alternative usage of different polyadenylation signals"](https://doi.org/10.1093%2Foxfordjournals.jbchem.a124492). *J. Biochem*. **116** (1): 183–92. [doi](/source/Doi_(identifier)):[10.1093/oxfordjournals.jbchem.a124492](https://doi.org/10.1093%2Foxfordjournals.jbchem.a124492). [PMID](/source/PMID_(identifier)) [7798177](https://pubmed.ncbi.nlm.nih.gov/7798177).

- Rahuel C, Elouet JF, Cartron JP (1995). ["Post-transcriptional regulation of the cell surface expression of glycophorins A, B, and E."](https://doi.org/10.1016%2FS0021-9258%2820%2930055-7) *J. Biol. Chem*. **269** (52): 32752–8. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(20)30055-7](https://doi.org/10.1016%2FS0021-9258%2820%2930055-7). [PMID](/source/PMID_(identifier)) [7806496](https://pubmed.ncbi.nlm.nih.gov/7806496).

- Huang CH, Reid ME, Blumenfeld OO (1994). ["Remodeling of the transmembrane segment in human glycophorin by aberrant RNA splicing"](https://doi.org/10.1016%2FS0021-9258%2817%2934131-5). *J. Biol. Chem*. **269** (14): 10804–12. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(17)34131-5](https://doi.org/10.1016%2FS0021-9258%2817%2934131-5). [PMID](/source/PMID_(identifier)) [8144668](https://pubmed.ncbi.nlm.nih.gov/8144668).

- Huang CH, Lomas C, Daniels G, Blumenfeld OO (1994). ["Glycophorin He(Sta) of the human red blood cell membrane is encoded by a complex hybrid gene resulting from two recombinational events"](https://doi.org/10.1182%2Fblood.V83.11.3369.3369). *Blood*. **83** (11): 3369–76. [doi](/source/Doi_(identifier)):[10.1182/blood.V83.11.3369.3369](https://doi.org/10.1182%2Fblood.V83.11.3369.3369). [PMID](/source/PMID_(identifier)) [8193374](https://pubmed.ncbi.nlm.nih.gov/8193374).

- Huang CH, Reid ME, Blumenfeld OO (1993). ["Exon skipping caused by DNA recombination that introduces a defective donor splice site into the human glycophorin A gene"](https://doi.org/10.1016%2FS0021-9258%2818%2953487-6). *J. Biol. Chem*. **268** (7): 4945–52. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(18)53487-6](https://doi.org/10.1016%2FS0021-9258%2818%2953487-6). [PMID](/source/PMID_(identifier)) [8444872](https://pubmed.ncbi.nlm.nih.gov/8444872).

- Cherif-Zahar B, Raynal V, Gane P, et al. (1996). "Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency". *Nat. Genet*. **12** (2): 168–73. [doi](/source/Doi_(identifier)):[10.1038/ng0296-168](https://doi.org/10.1038%2Fng0296-168). [PMID](/source/PMID_(identifier)) [8563755](https://pubmed.ncbi.nlm.nih.gov/8563755). [S2CID](/source/S2CID_(identifier)) [1999844](https://api.semanticscholar.org/CorpusID:1999844).

## External links

- [GYPB+protein,+human](https://meshb.nlm.nih.gov/record/ui?name=GYPB+protein%2C+human) at the U.S. National Library of Medicine [Medical Subject Headings](/source/Medical_Subject_Headings) (MeSH)

*This article incorporates text from the [United States National Library of Medicine](/source/United_States_National_Library_of_Medicine), which is in the [public domain](/source/Public_domain).*

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation) 1–50 CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50 51–100 CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100 101–150 CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150 151–200 CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200 201–250 CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 CD248 CD249 251–300 CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299 301–350 CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350 351–371 CD351 CD352 CD353 CD354 CD355 CD357 CD358 CD360 CD361 CD362 CD363 CD364 CD365 CD366 CD367 CD368 CD369 CD370 CD371 Category Commons

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Adapted from the Wikipedia article [GYPB](https://en.wikipedia.org/wiki/GYPB) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/GYPB?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.
