ArticleProceedings of the National Academy of Sciences of the United States of America1990
Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 99 citations in OpenAlex.
- The Evolution of Transglutaminases Underlies the Origin and Loss of Cornified Skin Appendages in Vertebrates.Molecular biology and evolution · 2024Article
- Structure, dynamics and assembly of the ankyrin complex on human red blood cell membrane.Nature structural & molecular biology · 2022Article
- Biocatalysis by Transglutaminases: A Review of Biotechnological Applications.Micromachines · 2018Review
- Article
- Cystamine preparations exhibit anticoagulant activity.PloS one · 2015Article
- Plasma factor XIII: understanding the 99%.Blood · 2014Article
- Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis.Molecular biology of the cell · 2012Article
- Investigating the key membrane protein changes during in vitro erythropoiesis of protein 4.2 (-) cells (mutations Chartres 1 and 2).Haematologica · 2010Article
- Antigen specificity of the humoral immune response to Mycoplasma haemofelis infection.Clinical and vaccine immunology : CVI · 2010Article
- Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid alpha-spectrin in a calcium- and calmodulin-dependent manner.The Journal of biological chemistry · 2010Article
- Framework for a protein ontology.BMC bioinformatics · 2007Article
- Interactions of recombinant mouse erythrocyte transglutaminase with membrane skeletal proteins.The Journal of membrane biology · 2007Article
- 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
- Expression of transglutaminase K in normal cervix tissue and cervix carcinomas.The Histochemical journal · 1999Article
- Novel AE1 mutations in recessive distal renal tubular acidosis. Loss-of-function is rescued by glycophorin A.The Journal of clinical investigation · 1998Article
- Molecular basis of bovine red-cell protein 4.2 polymorphism in Japanese black cattle.The Biochemical journal · 1998Article
- Association of a transglutaminase-related antigen with intermediate filaments.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Identification of a band-3 binding site near the N-terminus of erythrocyte membrane protein 4.2.The Biochemical journal · 1995Article
- Protein damage and methylation-mediated repair in the erythrocyte.The Biochemical journal · 1995Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The complete amino acid sequence for human erythrocyte band 4.2 has been derived from the nucleotide sequence of a full-length 2.35-kilobase (kb) cDNA. The 2.35-kb cDNA was isolated from a human reticulocyte cDNA library made in the expression vector lambda gt11. Of the 2348 base pairs (bp), 2073 bp encode 691 amino acids representing 76.9 kDa (the SDS/PAGE molecular mass is 72 kDa). RNA blot analysis of human reticulocyte total RNA gives a message size for band 4.2 of 2.4 kb. The amino acid sequence of band 4.2 has homology with two closely related Ca2(+)-dependent cross-linking proteins, guinea pig liver transglutaminase (protein-glutamine gamma-glutamyltransferase; protein-glutamine: amine gamma-glutamyltransferase, EC 2.3.2.13) (32% identity in a 446-amino acid overlap) and the a subunit of human coagulation factor XIII (27% identity in a 639-amino acid overlap), a transglutaminase that forms intermolecular gamma-glutamyl-epsilon-lysine bonds between fibrin molecules. The region of greatest identity includes a 49-amino acid stretch of band 4.2, which is 69% and 51% identical with guinea pig liver transglutaminase and the a subunit of factor XIII, respectively, within the regions that contain the active sites of these enzymes. Significantly, within the five contiguous consensus residues of the transglutaminase active site, Gly-Gln-Cys-Trp-Val, band 4.2 has an alanine substituted for cysteine (which is apparently essential for activity). Consistent with this active site substitution, erythrocyte membranes or inside-out vesicles, which contain band 4.2, show no evidence of transglutaminase activity by two types of in vitro assay.
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