Biology:RHAG
From HandWiki
Revision as of 05:28, 26 April 2022 by imported>MainAI6 (linkage)
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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]
Function
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
RHAG has been shown to interact with ANK1.[4]
See also
References
- ↑ "Organization of the human RH50A gene (RHAG) and evolution of base composition of the RH gene family". Genomics 47 (2): 286–93. Jan 1998. doi:10.1006/geno.1997.5112. PMID 9479501.
- ↑ 2.0 2.1 "Entrez Gene: RHAG Rh-associated glycoprotein". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6005.
- ↑ "Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S". American Journal of Physiology. Cell Physiology 301 (6): C1325-43. Dec 2011. doi:10.1152/ajpcell.00054.2011. PMID 21849667.
- ↑ "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. Jul 2003. doi:10.1074/jbc.M302816200. PMID 12719424.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Further reading
- "The challenge of understanding ammonium homeostasis and the role of the Rh glycoproteins". Transfusion Clinique et Biologique 13 (1–2): 139–46. 2006. doi:10.1016/j.tracli.2006.02.008. PMID 16564724.
- "Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis". Transfusion Clinique et Biologique 13 (1–2): 117–22. 2006. doi:10.1016/j.tracli.2006.03.004. PMID 16574458.
- "Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression". The Biochemical Journal. 287 287 (1): 223–8. Oct 1992. doi:10.1042/bj2870223. PMID 1417776.
- "Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane". The Biochemical Journal 256 (3): 1043–6. Dec 1988. doi:10.1042/bj2561043. PMID 3146980.
- "Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency". Nature Genetics 12 (2): 168–73. Feb 1996. doi:10.1038/ng0296-168. PMID 8563755.
- "The human Rh50 glycoprotein gene. Structural organization and associated splicing defect resulting in Rh(null) disease". The Journal of Biological Chemistry 273 (4): 2207–13. Jan 1998. doi:10.1074/jbc.273.4.2207. PMID 9442063.
- "A novel single missense mutation identified along the RH50 gene in a composite heterozygous Rhnull blood donor of the regulator type". Blood 91 (4): 1458–63. Feb 1998. doi:10.1182/blood.V91.4.1458. PMID 9454778.
- "Identification of 5' flanking sequence of RH50 gene and the core region for erythroid-specific expression". Biochemical and Biophysical Research Communications 243 (1): 233–40. Feb 1998. doi:10.1006/bbrc.1997.8023. PMID 9473510.
- "Rh50 glycoprotein gene and rhnull disease: a silent splice donor is trans to a Gly279-->Glu missense mutation in the conserved transmembrane segment". Blood 92 (5): 1776–84. Sep 1998. doi:10.1182/blood.V92.5.1776. PMID 9716608.
- "Rh-deficiency of the regulator type caused by splicing mutations in the human RH50 gene". Blood 92 (7): 2535–40. Oct 1998. doi:10.1182/blood.V92.7.2535. PMID 9746795.
- "Rhmod syndrome: a family study of the translation-initiator mutation in the Rh50 glycoprotein gene". American Journal of Human Genetics 64 (1): 108–17. Jan 1999. doi:10.1086/302215. PMID 9915949.
- "Molecular basis for Rh(null) syndrome: identification of three new missense mutations in the Rh50 glycoprotein gene". American Journal of Hematology 62 (1): 25–32. Sep 1999. doi:10.1002/(SICI)1096-8652(199909)62:1<25::AID-AJH5>3.0.CO;2-K. PMID 10467273.
- "Cloning and characterization of erythroid-specific DNase I-hypersensitive site in human rhesus-associated glycoprotein gene". The Journal of Biological Chemistry 275 (35): 27324–31. Sep 2000. doi:10.1074/jbc.M003297200. PMID 10862620.
- "The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast". Nature Genetics 26 (3): 341–4. Nov 2000. doi:10.1038/81656. PMID 11062476.
- "Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter". The Journal of Biological Chemistry 277 (15): 12499–502. Apr 2002. doi:10.1074/jbc.C200060200. PMID 11861637.
- "Cell-surface expression of RhD blood group polypeptide is posttranscriptionally regulated by the RhAG glycoprotein". Blood 100 (3): 1038–47. Aug 2002. doi:10.1182/blood.V100.3.1038. PMID 12130520.
- "RhCG is downregulated in oesophageal squamous cell carcinomas, but expressed in multiple squamous epithelia". European Journal of Cancer 38 (14): 1927–36. Sep 2002. doi:10.1016/S0959-8049(02)00190-9. PMID 12204676.
- "Fractional attachment of CD47 (IAP) to the erythrocyte cytoskeleton and visual colocalization with Rh protein complexes". Blood 101 (3): 1194–9. Feb 2003. doi:10.1182/blood-2002-04-1187. PMID 12393442.
External links
- RHCE+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
- RhAG blood group system in the BGMUT blood group antigen gene mutation database
 |  |
