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; OMA:EPB42 - orthologs
Gene location (Human) Chr. Chromosome 15 (human) [1] Band 15q15.2 Start 43,197,227 bp [1] End 43,221,018 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2 E5|2 60.37 cM Start 120,848,372 bp [2] End 120,867,553 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in blood bone marrow bone marrow cell gonad monocyte testicle placenta right testis left testis subcutaneous adipose tissue Top expressed in fetal liver hematopoietic progenitor cell human fetus red pulp blood tibiofemoral joint yolk sac body of femur right lobe of liver genital tubercle bone marrow More reference expression data BioGPS 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 Species Human Mouse Entrez 2038 13828 Ensembl ENSG00000166947 ENSMUSG00000023216 UniProt P16452 P49222 RefSeq (mRNA) NM_000119 NM_001114134 NM_013513 RefSeq (protein) NP_000110 NP_001107606 NP_038541 Location (UCSC) Chr 15: 43.2 – 43.22 Mb Chr 2: 120.85 – 120.87 Mb PubMed search [3] [4]
Wikidata
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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]

See also

• Hereditary elliptocytosis

References

1. GRCh38: Ensembl release 89: ENSG00000166947 – Ensembl, May 2017
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.
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.
6. "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. 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. Bibcode:1988FEBSL.226..291T. 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)