Protein 4.2

From Wikipedia, the free encyclopedia

Erythrocyte membrane protein band 4.2

Identifiers

EPB42; PA; MGC116735; MGC116737

External IDs

Gene ontology
Molecular Function:	• structural constituent of cytoskeleton • ATP binding
Cellular Component:	• cytoskeleton • plasma membrane
Biological Process:	• regulation of cell shape • peptide cross-linking • erythrocyte maturation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000119 (mRNA)
NP_000110 (protein)

NM_013513 (mRNA)
NP_038541 (protein)

Location

Chr 15: 41.28 - 41.3 Mb

Chr 2: 120.71 - 120.73 Mb

Pubmed search

[1]

[2]

Erythrocyte membrane protein band 4.2, also known as EPB42, is a human gene.^[1]

Protein 4.2 is a cytoskeleton protein found in red blood cells.

Erythrocyte membrane protein band 4.2 is an ATP-binding protein which may regulate the association of protein 3 with ankyrin. It probably has a role in erythrocyte shape and mechanical property regulation. Mutations in the EPB42 gene are associated with recessive spherocytic elliptocytosis and recessively transmitted hereditary hemolytic anemia.^[1]

1 References
2 Further reading
3 See also
4 External links

[edit] References

^ ^a ^b Entrez Gene: EPB42 erythrocyte membrane protein band 4.2.

[edit] Further reading

Falcón-Pérez JM, Dell'Angelica EC (2002). "The pallidin (Pldn) gene and the role of SNARE proteins in melanosome biogenesis.". Pigment Cell Res. 15 (2): 82–6. PMID 11936273.
White RA, Peters LL, Adkison LR, et al. (1993). "The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene.". Nat. Genet. 2 (1): 80–3. doi:10.1038/ng0992-80. PMID 1284644.
Sung LA, Chien S, Fan YS, et al. (1992). "Human erythrocyte protein 4.2: isoform expression, differential splicing, and chromosomal assignment.". Blood 79 (10): 2763–70. PMID 1350227.
Risinger MA, Dotimas EM, Cohen CM (1992). "Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated.". J. Biol. Chem. 267 (8): 5680–5. PMID 1544941.
Bouhassira EE, Schwartz RS, Yawata Y, et al. (1992). "An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2NIPPON).". Blood 79 (7): 1846–54. PMID 1558976.
Sung LA, Chien S, Chang LS, et al. (1990). "Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane.". Proc. Natl. Acad. Sci. U.S.A. 87 (3): 955–9. PMID 1689063.
Najfeld V, Ballard SG, Menninger J, et al. (1992). "The gene for human erythrocyte protein 4.2 maps to chromosome 15q15.". Am. J. Hum. Genet. 50 (1): 71–5. PMID 1729896.
Low PS, Willardson BM, Mohandas N, et al. (1991). "Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability.". Blood 77 (7): 1581–6. PMID 1826225.
Korsgren C, Cohen CM (1991). "Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII.". Proc. Natl. Acad. Sci. U.S.A. 88 (11): 4840–4. PMID 2052563.
Korsgren C, Lawler J, Lambert S, et al. (1990). "Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2.". Proc. Natl. Acad. Sci. U.S.A. 87 (2): 613–7. PMID 2300550.
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.
Tanimoto T, Hoshijima M, Kawata M, et al. (1988). "Binding of ras p21 to bands 4.2 and 6 of human erythrocyte membranes.". FEBS Lett. 226 (2): 291–6. PMID 3276554.
Rybicki AC, Musto S, Schwartz RS (1995). "Identification of a band-3 binding site near the N-terminus of erythrocyte membrane protein 4.2.". Biochem. J. 309 ( Pt 2): 677–81. PMID 7626035.
Hayette S, Morle L, Bozon M, et al. (1995). "A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia.". Br. J. Haematol. 89 (4): 762–70. PMID 7772513.
Hayette S, Dhermy D, dos Santos ME, et al. (1995). "A deletional frameshift mutation in protein 4.2 gene (allele 4.2 Lisboa) associated with hereditary hemolytic anemia.". Blood 85 (1): 250–6. PMID 7803799.
Takaoka Y, Ideguchi H, Matsuda M, et al. (1995). "A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka).". Br. J. Haematol. 88 (3): 527–33. PMID 7819064.
Das AK, Bhattacharya R, Kundu M, et al. (1994). "Human erythrocyte membrane protein 4.2 is palmitoylated.". Eur. J. Biochem. 224 (2): 575–80. PMID 7925374.
Dotimas E, Speicher DW, GuptaRoy B, Cohen CM (1993). "Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2).". Biochim. Biophys. Acta 1148 (1): 19–29. PMID 8499466.
Azim AC, Marfatia SM, Korsgren C, et al. (1996). "Human erythrocyte dematin and protein 4.2 (pallidin) are ATP binding proteins.". Biochemistry 35 (9): 3001–6. doi:10.1021/bi951745y. PMID 8608138.
Bhattacharyya R, Das AK, Moitra PK, et al. (1999). "Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2.". Biochem. J. 340 ( Pt 2): 505–12. PMID 10333496.