Erythrocyte Membrane Protein Band 4.2 (EPB42)

PA; Erythrocyte Surface Protein Band 4.2

SPN	R632
HGNC	3381
MGI	95402
PubMed	1284644
RGD	1305306
UniProt	P16452
Wiki	EPB42

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.

The deduced 691-amino acid band 4.2 protein has homology with 2 closely related calcium-dependent crosslinking proteins, guinea pig liver transglutaminase and the alpha subunit of human coagulation factor XIII (F13A1). Within the 5 contiguous consensus residues of the transglutaminase active site, band 4.2 has an amino acid substitution which leads to loss of transglutaminase activity.

Reference

"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. 88:4840-4844(1991) [PubMed] [Europe PMC] [Abstract]

"Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2."
Proc. Natl. Acad. Sci. U.S.A. 87:613-617(1990) [PubMed] [Europe PMC] [Abstract]

"Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane."
Proc. Natl. Acad. Sci. U.S.A. 87:955-959(1990) [PubMed] [Europe PMC] [Abstract]

"Analysis of the DNA sequence and duplication history of human chromosome 15."
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated."
J. Biol. Chem. 267:5680-5685(1992) [PubMed] [Europe PMC] [Abstract]

"Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2)."
Biochim. Biophys. Acta 1148:19-29(1993) [PubMed] [Europe PMC] [Abstract]

"An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2 Nippon)."
Blood 79:1846-1854(1992) [PubMed] [Europe PMC] [Abstract]

"A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka)."
Br. J. Haematol. 88:527-533(1994) [PubMed] [Europe PMC] [Abstract]

"A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia."
Br. J. Haematol. 89:762-770(1995) [PubMed] [Europe PMC] [Abstract]

"Band 4.2 Shiga: 317 CGC-->TGC in compound heterozygotes with 142 GCT-->ACT results in band 4.2 deficiency and microspherocytosis."
Br. J. Haematol. 91:333-340(1995) [PubMed] [Europe PMC] [Abstract]

"Band 4.2 Komatsu: 523 GAT-->TAT (175 Asp-->Tyr) in exon 4 of the band 4.2 gene associated with total deficiency of band 4.2, hemolytic anemia with ovalostomatocytosis and marked disruption of the cytoskeletal network."
Int. J. Hematol. 61:165-178(1995) [PubMed] [Europe PMC] [Abstract]

"4.2 Nippon mutation in a non-Japanese patient with hereditary spherocytosis."
Haematologica 84:660-662(1999) [PubMed] [Europe PMC] [Abstract]