Band 4.1

Erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked)

PDB rendering based on 1gg3.

| Available structures

PDB |  Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
| List of PDB id codes

1gg3​

Identifiers
Symbols|  EPB41 ; 4.1R; EL1; HE
External IDs|  Template:OMIM5 Template:MGI HomoloGene: 44324
| Gene ontology

Molecular function | Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
Cellular component | Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
Biological process | Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species|  Human|  Mouse
Entrez|  n/a|  n/a
Ensembl|  n/a|  n/a
UniProt|  n/a|  n/a
RefSeq (mRNA)|  n/a|  n/a
RefSeq (protein)|  n/a|  n/a
Location (UCSC)|  n/a|  n/a
PubMed search|  n/a|  n/a
A schematic diagram representing the relationships between cytoskeletal molecules as relevant to hereditary elliptocytosis.

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

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][1]

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

## Contents

* 1 See also
* 2 References
* 3 Further reading
* 4 External links

## See also

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* elliptocytosis

## References

[edit | edit source]

1. ↑ "Entrez Gene: EPB41 erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked)".

## Further reading

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* 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; et al. (2006). "New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium". Front. Biosci. 11: 1646–66. PMID 16368544.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Dalla Venezia N, Gilsanz F, Alloisio N; et al. (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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* 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.CS1 maint: Multiple names: authors list (link)
* Conboy JG, Chan JY, Chasis JA; et al. (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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* 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.CS1 maint: Multiple names: authors list (link)
* Conboy J, Marchesi S, Kim R; et al. (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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* 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.CS1 maint: Multiple names: authors list (link)
* Tang TK, Leto TL, Marchesi VT, Benz EJ (1989). "Expression of specific isoforms of protein 4.1 in erythroid and non-erythroid tissues". Adv. Exp. Med. Biol. 241: 81–95. PMID 3223413.CS1 maint: Multiple names: authors list (link)
* Tang TK, Leto TL, Correas I; et al. (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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* 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.CS1 maint: Multiple names: authors list (link)
* 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.CS1 maint: Multiple names: authors list (link)
* 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.CS1 maint: Multiple names: authors list (link)
* Schischmanoff PO, Winardi R, Discher DE; et al. (1995). "Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding". J. Biol. Chem. 270 (36): 21243–50. PMID 7673158.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* 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.CS1 maint: Multiple names: authors list (link)
* Conboy JG, Chasis JA, Winardi R; et al. (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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)

## External links

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* erythrocyte+membrane+band+4.1+protein at the US National Library of Medicine Medical Subject Headings (MeSH)

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