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::2012/11/18::
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::2011/12/14::
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::2012/12/02::
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::2012/11/25::
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::2012/01/07::
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RESULTS [51 .. 101]
From Wikipedia, the free encyclopedia
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Rh-associated glycoprotein
Identifiers
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
Orthologs
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:
49.57 – 49.6 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]

Interactions[edit]

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

See also[edit]

References[edit]

  1. ^ Matassi G, Cherif-Zahar B, Raynal V, Rouger P, Cartron JP (Apr 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, A. K.; Shmukler, B. E.; Vandorpe, D. H.; Rivera, A.; Heneghan, J. F.; Li, X.; Hsu, A.; Karpatkin, M.; O'Neill, A. F.; Bauer, D. E.; Heeney, M. M.; John, K.; Kuypers, F. A.; Gallagher, P. G.; Lux, S. E.; Brugnara, C.; Westhoff, C. M.; Alper, S. L. (2011). "Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S". AJP: Cell Physiology 301 (6): C1325–C1343. doi:10.1152/ajpcell.00054.2011. PMC 3233792. PMID 21849667.  edit
  4. ^ Nicolas, Virginie; Le Van Kim Caroline, Gane Pierre, Birkenmeier Connie, Cartron Jean-Pierre, Colin Yves, Mouro-Chanteloup Isabelle (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". J. Biol. Chem. (United States) 278 (28): 25526–33. doi:10.1074/jbc.M302816200. ISSN 0021-9258. 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.


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