Protein 4.2

EPB42
Identifiers
Aliases	EPB42, PA, SPH5, erythrocyte membrane protein band 4.2
External IDs	OMIM: 177070 MGI: 95402 HomoloGene: 93 GeneCards: EPB42
Gene location (Human)
Chr.	Chromosome 15 (human)
End	43,221,018 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	120,867,553 bp
RNA expression pattern
	Top expressed in
	blood; ; bone marrow; ; bone marrow cells; ; monocyte; ; placenta; ; subcutaneous adipose tissue; ; ganglionic eminence; ; gallbladder; ; spleen; ; right lung;
	Top expressed in
	red pulp; ; blood; ; yolk sac; ; body of femur; ; right lobe of liver; ; bone marrow; ; secondary oocyte; ; endocardial cushion; ; proximal tubule; ; Paneth cell;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	structural constituent of cytoskeleton; protein-glutamine gamma-glutamyltransferase activity; protein binding; ATP binding;
Cellular component	cytoplasm; plasma membrane; cytoskeleton; membrane; cortical cytoskeleton;
Biological process	peptide cross-linking; regulation of cell shape; erythrocyte maturation; cytoskeleton organization; cell morphogenesis; hemoglobin metabolic process; spleen development; ion homeostasis; iron ion homeostasis;
	Sources:Amigo / QuickGO
Orthologs
	2038
	13828
	ENSG00000166947
	ENSMUSG00000023216
	P16452
	P49222
	NM_000119; NM_001114134
	NM_013513
	NP_000110; NP_001107606
	NP_038541
	Wikidata
View/Edit Human	View/Edit Mouse

Erythrocyte membrane protein band 4.2 is a protein that in humans is encoded by the EPB42 gene.^[5]^[6] It is part of the red blood cell cytoskeleton.

Erythrocyte membrane protein band 4.2 is an ATP-binding protein which may regulate the association of band 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.^[6]

References

^ a b c GRCh38: Ensembl release 89: ENSG00000166947 – Ensembl, May 2017
^ a b c GRCm38: Ensembl release 89: ENSMUSG00000023216 – 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.
^ 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. S2CID 42065586.
^ a b "Entrez Gene: EPB42 erythrocyte membrane protein band 4.2".

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. doi:10.1182/blood.V79.10.2763.2763. 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. doi:10.1016/S0021-9258(18)42820-7. 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. doi:10.1182/blood.V79.7.1846.1846. 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. Bibcode:1990PNAS...87..955S. 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. doi:10.1182/blood.V77.7.1581.1581. 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. Bibcode:1991PNAS...88.4840K. 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. Bibcode:1990PNAS...87..613K. 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. doi:10.1016/S0021-9258(19)81500-4. 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. doi:10.1042/bj3090677. 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. S2CID 43155950.
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. doi:10.1182/blood.V85.1.250.bloodjournal851250. 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. S2CID 42509283.
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.

External links

band+4.2+protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article on a gene on human chromosome 15 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000166947 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000023216 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1284644-5] 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. S2CID 42065586.

[entrez-6] "Entrez Gene: EPB42 erythrocyte membrane protein band 4.2".

Protein 4.2

See also

References

Further reading

External links