Protein 4.2

Erythrocyte membrane protein band 4.2
Identifiers
Symbols	EPB42 ; PA; SPH5
External IDs	OMIM: 177070 MGI: 95402 HomoloGene: 93 GeneCards: EPB42 Gene
Gene ontology Molecular function • protein-glutamine gamma-glutamyltransferase activity • structural constituent of cytoskeleton • protein binding • ATP binding Cellular component • cytoskeleton • plasma membrane • cortical cytoskeleton Biological process • cell morphogenesis • regulation of cell shape • peptide cross-linking • hemoglobin metabolic process • erythrocyte maturation • spleen development • iron ion homeostasis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2038	13828
Ensembl	ENSG00000166947	ENSMUSG00000023216
UniProt	P16452	P49222
RefSeq (mRNA)	NM_000119	NM_013513
RefSeq (protein)	NP_000110	NP_038541
Location (UCSC)	Chr 15: 43.11 – 43.22 Mb	Chr 2: 121.02 – 121.04 Mb
PubMed search

Erythrocyte membrane protein band 4.2 is a protein that in humans is encoded by the EPB42 gene.^[1][2]

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.^[2]

References

1. White RA, Peters LL, Adkison LR, Korsgren C, Cohen CM, Lux SE (Jun 1993). "The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene". Nat Genet 2 (1): 80–83. doi:10.1038/ng0992-80. PMID 1284644.
2. "Entrez Gene: EPB42 erythrocyte membrane protein band 4.2".

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): 82–86. doi:10.1034/j.1600-0749.2002.1r082.x. PMID 11936273.
• 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): 955–959. doi:10.1073/pnas.87.3.955. PMC 53388. 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. PMC 1682530. 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): 4840–4844. doi:10.1073/pnas.88.11.4840. PMC 51762. 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): 613–617. doi:10.1073/pnas.87.2.613. PMC 53315. 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): 291–296. doi:10.1016/0014-5793(88)81442-X. 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 (2): 677–81. PMC 1135783. 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): 762–770. doi:10.1111/j.1365-2141.1995.tb08413.x. 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): 527–533. doi:10.1111/j.1365-2141.1994.tb05069.x. PMID 7819064.
• Das AK, Bhattacharya R, Kundu M, et al. (1994). "Human erythrocyte membrane protein 4.2 is palmitoylated". Eur. J. Biochem. 224 (2): 575–580. doi:10.1111/j.1432-1033.1994.00575.x. 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. doi:10.1016/0005-2736(93)90156-T. 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): 3001–3006. 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 (2): 505–12. doi:10.1042/0264-6021:3400505. PMC 1220278. PMID 10333496.

See also

• Hereditary elliptocytosis

External links

• band 4.2 protein at the US National Library of Medicine Medical Subject Headings (MeSH)