ArticleProceedings of the National Academy of Sciences of the United States of America1991
Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Development of Highly Efficient UniversalJournal of fungi (Basel, Switzerland) · 2024Article
- Compound heterozygosity for two novel mutations in the erythrocyte protein 4.2 gene causing spherocytosis in a Caucasian patient.British journal of haematology · 2011Article
- Transglutaminase-mediated remodeling of the human erythrocyte membrane skeleton: relevance for erythrocyte diseases with shortened cell lifespan.Advances in enzymology and related areas of molecular biology · 2011Review
- Erythrocyte tropomodulin isoforms with and without the N-terminal actin-binding domain.The Journal of biological chemistry · 2010Article
- Associations of protein 4.2 with band 3 and ankyrin.Molecular and cellular biochemistry · 2006Article
- Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2.The Biochemical journal · 1999Article
- Molecular basis of bovine red-cell protein 4.2 polymorphism in Japanese black cattle.The Biochemical journal · 1998Article
- Localization of the gene for congenital dyserythropoietic anemia type I to a <1-cM interval on chromosome 15q15.1-15.3.American journal of human genetics · 1998Article
- Molecular cloning of mouse erythrocyte protein 4.2: a membrane protein with strong homology with the transglutaminase supergene family.Mammalian genome : official journal of the International Mammalian Genome Society · 1994Article
- Organization and evolution of the human epidermal keratinocyte transglutaminase I gene.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- New nucleotide sequence data on the EMBL File Server.Nucleic acids research · 1991Article
- A deletion polymorphism in the human alpha-2-macroglobulin (A2M) gene.Nucleic acids research · 1991Article
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2 authors.
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Abstract
Human erythrocyte band 4.2 is a major membrane-associated protein with an important, but still undefined, role in erythrocyte survival. We previously sequenced the complete cDNA for band 4.2 and showed that the protein has a strong sequence identity with the transglutaminase family of proteins but lacks transglutaminase activity. Here we have analyzed the genomic organization of band 4.2. The band 4.2 gene is approximately 20 kilobases, consisting of 13 exons and 12 introns. Reticulocytes contain two different sized messages for band 4.2, and our results show that the major, smaller, message is produced by alternative splicing within band 4.2 exon I. The upstream region of the gene has several prospective promoter elements arranged in a pattern similar to that of two other erythroid genes, beta-globin and porphobilinogen deaminase. Alignment of the band 4.2 amino acid sequence with that of the a subunit of human coagulation factor XIII and division of the sequences into exons reveal a remarkable correspondence, and in most cases identity, in the sizes of the paired exons. Moreover, each corresponding intron of the two genes is of an identical splice junction class. These and other similarities suggest that the gene for band 4.2 is closely related to and possibly derived from that for the a subunit of factor XIII and that the proteins may share common structural and functional properties.
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