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Rh-associated glycoprotein
Symbols RHAG ; CD241; RH2; RH50A; Rh50; Rh50GP; SLC42A1
External IDs OMIM180297 MGI1202713 HomoloGene68045 GeneCards: RHAG Gene
RNA expression pattern
PBB GE RHAG 206145 at tn.png
PBB GE RHAG 206146 s at tn.png
PBB GE RHAG 211254 x at tn.png
More reference expression data
Species Human Mouse
Entrez 6005 19743
Ensembl ENSG00000112077 ENSMUSG00000023926
UniProt Q02094 Q9QUT0
RefSeq (mRNA) NM_000324 NM_011269
RefSeq (protein) NP_000315 NP_035399
Location (UCSC) Chr 6:
49.61 – 49.64 Mb
Chr 17:
40.81 – 40.84 Mb
PubMed search [1] [2]

Rh-associated glycoprotein (RHAG) is an ammonia transporter protein that in humans is encoded by the RHAG gene.[1][2] RHAG has also recently been designated CD241 (cluster of differentiation 241). Mutations in the RHAG gene can cause stomatocytosis.[3]


The Rh blood group antigens (MIM 111700) are associated with human erythrocyte membrane proteins of approximately 30 kD, the so-called Rh30 polypeptides. Heterogeneously glycosylated membrane proteins of 50 and 45 kD, the Rh50 glycoproteins, are coprecipitated with the Rh30 polypeptides on immunoprecipitation with anti-Rh-specific mono- and polyclonal antibodies. The Rh antigens appear to exist as a multisubunit complex of CD47 (MIM 601028), LW (MIM 111250), glycophorin B (MIM 111740), and play a critical role in the Rh50 glycoprotein [supplied by OMIM].[2]


RHAG has been shown to interact with ANK1.[4]

See also[edit]


  1. ^ Matassi G, Chérif-Zahar B, Raynal V, Rouger P, Cartron JP (Jan 1998). "Organization of the human RH50A gene (RHAG) and evolution of base composition of the RH gene family". Genomics 47 (2): 286–93. doi:10.1006/geno.1997.5112. PMID 9479501. 
  2. ^ a b "Entrez Gene: RHAG Rh-associated glycoprotein". 
  3. ^ Stewart AK, Shmukler BE, Vandorpe DH, Rivera A, Heneghan JF, Li X, Hsu A, Karpatkin M, O'Neill AF, Bauer DE, Heeney MM, John K, Kuypers FA, Gallagher PG, Lux SE, Brugnara C, Westhoff CM, Alper SL (Dec 2011). "Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S". American Journal of Physiology. Cell Physiology 301 (6): C1325–43. doi:10.1152/ajpcell.00054.2011. PMC 3233792. PMID 21849667. 
  4. ^ Nicolas V, Le Van Kim C, Gane P, Birkenmeier C, Cartron JP, Colin Y, Mouro-Chanteloup I (Jul 2003). "Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation". The Journal of Biological Chemistry 278 (28): 25526–33. doi:10.1074/jbc.M302816200. PMID 12719424. 

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.