Band 4.1

Erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked), also known as EPB41, is a human gene.

PBB_Summary
section_title =
summary_text = 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-spectrin gene (MIM 182860), the beta-spectrin gene (MIM 182870), or the band 3 gene (MIM 109270). [supplied by OMIM] [cite web | title = Entrez Gene: EPB41 erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2035| accessdate = ]

Band 4.1 is a protein associated with the cytoskeleton of the red blood cell.

ee also

* elliptocytosis

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Conboy JG |title=Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells. |journal=Semin. Hematol. |volume=30 |issue= 1 |pages= 58–73 |year= 1993 |pmid= 8434260 |doi=
*cite journal | author=Calinisan V, Gravem D, Chen RP, "et al." |title=New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium. |journal=Front. Biosci. |volume=11 |issue= |pages= 1646–66 |year= 2006 |pmid= 16368544 |doi=
*cite journal | author=Dalla Venezia N, Gilsanz F, Alloisio N, "et al." |title=Homozygous 4.1(-) hereditary elliptocytosis associated with a point mutation in the downstream initiation codon of protein 4.1 gene. |journal=J. Clin. Invest. |volume=90 |issue= 5 |pages= 1713–7 |year= 1992 |pmid= 1430200 |doi=
*cite journal | author=Jöns T, Drenckhahn D |title=Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger. |journal=EMBO J. |volume=11 |issue= 8 |pages= 2863–7 |year= 1992 |pmid= 1639060 |doi=
*cite journal | author=Subrahmanyam G, Bertics PJ, Anderson RA |title=Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 12 |pages= 5222–6 |year= 1991 |pmid= 1647028 |doi=
*cite journal | author=Conboy JG, Chan JY, Chasis JA, "et al." |title=Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1. |journal=J. Biol. Chem. |volume=266 |issue= 13 |pages= 8273–80 |year= 1991 |pmid= 2022644 |doi=
*cite journal | author=Horne WC, Prinz WC, Tang EK |title=Identification of two cAMP-dependent phosphorylation sites on erythrocyte protein 4.1. |journal=Biochim. Biophys. Acta |volume=1055 |issue= 1 |pages= 87–92 |year= 1990 |pmid= 2171679 |doi=
*cite journal | author=Conboy J, Marchesi S, Kim R, "et al." |title=Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. II. Determination of molecular genetic origins of rearrangements. |journal=J. Clin. Invest. |volume=86 |issue= 2 |pages= 524–30 |year= 1990 |pmid= 2384598 |doi=
*cite journal | author=Inaba M, Maede Y |title=O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways. |journal=J. Biol. Chem. |volume=264 |issue= 30 |pages= 18149–55 |year= 1989 |pmid= 2808371 |doi=
*cite journal | author=Korsgren C, Cohen CM |title=Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3. |journal=J. Biol. Chem. |volume=263 |issue= 21 |pages= 10212–8 |year= 1988 |pmid= 2968981 |doi=
*cite journal | author=Conboy JG, Chan J, Mohandas N, Kan YW |title=Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 23 |pages= 9062–5 |year= 1988 |pmid= 3194408 |doi=
*cite journal | author=Tang TK, Leto TL, Marchesi VT, Benz EJ |title=Expression of specific isoforms of protein 4.1 in erythroid and non-erythroid tissues. |journal=Adv. Exp. Med. Biol. |volume=241 |issue= |pages= 81–95 |year= 1989 |pmid= 3223413 |doi=
*cite journal | author=Tang TK, Leto TL, Correas I, "et al." |title=Selective expression of an erythroid-specific isoform of protein 4.1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 11 |pages= 3713–7 |year= 1988 |pmid= 3375238 |doi=
*cite journal | author=Conboy J, Kan YW, Shohet SB, Mohandas N |title=Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 24 |pages= 9512–6 |year= 1987 |pmid= 3467321 |doi=
*cite journal | author=Correas I, Speicher DW, Marchesi VT |title=Structure of the spectrin-actin binding site of erythrocyte protein 4.1. |journal=J. Biol. Chem. |volume=261 |issue= 28 |pages= 13362–6 |year= 1986 |pmid= 3531202 |doi=
*cite journal | author=Tchernia G, Mohandas N, Shohet SB |title=Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability. |journal=J. Clin. Invest. |volume=68 |issue= 2 |pages= 454–60 |year= 1981 |pmid= 6894932 |doi=
*cite journal | author=Schischmanoff PO, Winardi R, Discher DE, "et al." |title=Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding. |journal=J. Biol. Chem. |volume=270 |issue= 36 |pages= 21243–50 |year= 1995 |pmid= 7673158 |doi=
*cite journal | author=Lue RA, Marfatia SM, Branton D, Chishti AH |title=Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 21 |pages= 9818–22 |year= 1994 |pmid= 7937897 |doi=
*cite journal | author=Conboy JG, Chasis JA, Winardi R, "et al." |title=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. |journal=J. Clin. Invest. |volume=91 |issue= 1 |pages= 77–82 |year= 1993 |pmid= 8423235 |doi=

External links

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