Protein 4.1
| EPB41 | |||
|---|---|---|---|
Gene ontology | |||
| Molecular function | |||
| Cellular component | |||
| Biological process |
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| Sources:Amigo / QuickGO | |||
| View/Edit Human | View/Edit Mouse |
Protein 4.1, (Erythrocyte membrane protein band 4.1), is a
elliptocytosis or spherocytosis and anemia
of varying severity.
Clinical significance
.JPG)
Elliptocytosis is a hematologic disorder characterized by elliptically shaped erythrocytes and a variable degree of hemolytic anemia. Inherited as an autosomal dominant, elliptocytosis results from mutation in any one of several genes encoding proteins of the red cell membrane skeleton. The form discussed here is the one found in the 1950s to be linked to Rh blood group and more recently shown to be caused by a defect in protein 4.1. 'Rh-unlinked' forms of elliptocytosis are caused by mutation in the alpha-
band 3 gene (MIM 109270) [supplied by OMIM].[5]
Interactions
Protein 4.1 has been shown to
interact
with:
See also
- Elliptocytosis
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000159023 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028906 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Entrez Gene: EPB41 erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked)".
- PMID 11003675.
- PMID 10887144.)
{{cite journal}}: CS1 maint: DOI inactive as of April 2024 (link - PMID 10189366.
- PMID 10874042.
Further reading
- Conboy JG (1993). "Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells". Semin. Hematol. 30 (1): 58–73. PMID 8434260.
- Calinisan V, Gravem D, Chen RP, Brittin S, Mohandas N, Lecomte MC, Gascard P (2006). "New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium". Front. Biosci. 11: 1646–66. S2CID 26325962.
- Dalla Venezia N, Gilsanz F, Alloisio N, Ducluzeau MT, Benz EJ, Delaunay J (1992). "Homozygous 4.1(-) hereditary elliptocytosis associated with a point mutation in the downstream initiation codon of protein 4.1 gene". J. Clin. Invest. 90 (5): 1713–7. PMID 1430200.
- Jöns T, Drenckhahn D (1992). "Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger". EMBO J. 11 (8): 2863–7. PMID 1639060.
- Subrahmanyam G, Bertics PJ, Anderson RA (1991). "Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro". Proc. Natl. Acad. Sci. U.S.A. 88 (12): 5222–6. PMID 1647028.
- Conboy JG, Chan JY, Chasis JA, Kan YW, Mohandas N (1991). "Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1". J. Biol. Chem. 266 (13): 8273–80. PMID 2022644.
- Horne WC, Prinz WC, Tang EK (1990). "Identification of two cAMP-dependent phosphorylation sites on erythrocyte protein 4.1". Biochim. Biophys. Acta. 1055 (1): 87–92. PMID 2171679.
- Conboy J, Marchesi S, Kim R, Agre P, Kan YW, Mohandas N (1990). "Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. II. Determination of molecular genetic origins of rearrangements". J. Clin. Invest. 86 (2): 524–30. PMID 2384598.
- Inaba M, Maede Y (1989). "O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways". J. Biol. Chem. 264 (30): 18149–55. PMID 2808371.
- Korsgren C, Cohen CM (1988). "Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3". J. Biol. Chem. 263 (21): 10212–8. PMID 2968981.
- Conboy JG, Chan J, Mohandas N, Kan YW (1988). "Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells". Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9062–5. PMID 3194408.
- Tang TK, Leto TL, Marchesi VT, Benz EJ (1988). "Expression of Specific Isoforms of Protein 4.1 in Erythroid and Non-Erythroid Tissues". Molecular Biology of Hemopoiesis. Advances in Experimental Medicine and Biology. Vol. 241. pp. 81–95. PMID 3223413.
- Tang TK, Leto TL, Correas I, Alonso MA, Marchesi VT, Benz EJ (1988). "Selective expression of an erythroid-specific isoform of protein 4.1". Proc. Natl. Acad. Sci. U.S.A. 85 (11): 3713–7. PMID 3375238.
- Conboy J, Kan YW, Shohet SB, Mohandas N (1987). "Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton". Proc. Natl. Acad. Sci. U.S.A. 83 (24): 9512–6. PMID 3467321.
- Correas I, Speicher DW, Marchesi VT (1986). "Structure of the spectrin-actin binding site of erythrocyte protein 4.1". J. Biol. Chem. 261 (28): 13362–6. PMID 3531202.
- Tchernia G, Mohandas N, Shohet SB (1981). "Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability". J. Clin. Invest. 68 (2): 454–60. PMID 6894932.
- Schischmanoff PO, Winardi R, Discher DE, Parra MK, Bicknese SE, Witkowska HE, Conboy JG, Mohandas N (1995). "Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding". J. Biol. Chem. 270 (36): 21243–50. PMID 7673158.
- Lue RA, Marfatia SM, Branton D, Chishti AH (1994). "Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1". Proc. Natl. Acad. Sci. U.S.A. 91 (21): 9818–22. PMID 7937897.
- Conboy JG, Chasis JA, Winardi R, Tchernia G, Kan YW, Mohandas N (1993). "An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells". J. Clin. Invest. 91 (1): 77–82. PMID 8423235.
External links
- erythrocyte+membrane+band+4.1+protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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