Genomes and Genes
Gene Symbol: EPB42
Description: erythrocyte membrane protein band 4.2
Alias: SPH5, P4.2, erythrocyte protein 4.2, erythrocyte surface protein band 4.2
- Associations of protein 4.2 with band 3 and ankyrinYang Su
Department of Physiology and Biophysics, School of Life Sciences, Fudan University, Shanghai 200433, China
Mol Cell Biochem 289:159-66. 2006..2. The proper tertiary structures of these protein 4.2 fragments are essential for protein 4.2-ankyrin interaction. Meanwhile, ankyrin can enhance the interaction between protein 4.2 and CDB3...
- Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3C Korsgren
Department of Biomedical Research, St Elizabeth s Hospital, Boston, Massachusetts 02135
J Biol Chem 263:10212-8. 1988..2 with band 4.1. Our results show that band 4.2 can form multiple associations with red cell membrane proteins and may therefore play an as yet unrecognized structural role on the membrane...
- Absence of CD47 in protein 4.2-deficient hereditary spherocytosis in man: an interaction between the Rh complex and the band 3 complexLesley J Bruce
Department of Biochemistry, University of Bristol, and International Blood Group Reference Laboratory, Bristol, United Kingdom
Blood 100:1878-85. 2002..2 gene (EPB42). The proband's mother was found to be heterozygous for this substitution. Unlike protein 4...
- Akt phosphorylates Tal1 oncoprotein and inhibits its repressor activityAlexey Palamarchuk
Human Cancer Genetics Program, Comprehensive Cancer Center, Ohio State University, Columbus, Ohio 43210, USA
Cancer Res 65:4515-9. 2005..Using luciferase assay, we showed that phosphorylation of Tal1 by Akt decreased repressor activity of Tal1 on EpB42 (P4.2) promoter...
- Red blood cell membrane defectsAchille Iolascon
Institute for Pediatrics, University of Foggia, Viale Pinto, 71100 Foggia, Italy
Rev Clin Exp Hematol 7:22-56. 2003..The mutations of most cases of HS are located in the following genes: ANK1, SPTB, SLC4A1, EPB42 and SPTA1, which encode for ankyrin, spectrin beta-chain, the anion exchanger 1 (band 3), protein 4...
- Variations in Both α-Spectrin (SPTA1) and β-Spectrin ( SPTB ) in a Neonate with Prolonged Jaundice in a Family where Nine Individuals Had Hereditary ElliptocytosisRobert D Christensen
Department of Women and Newborns, Intermountain Healthcare, Salt Lake City, Utah, USA
Neonatology 105:1-4. 2014..In addition, a novel heterozygous mutation was identified in exon 2 of the β-spectrin gene SPTB. No mutations were identified in ANK1 (ankyrin-1), SLC4A1 (band 3), EPB41 (band 4.1), or EPB42 (band 4.2). © 2013 S. Karger AG, Basel.
- Expression of different forms of transglutaminases by immature cells of Helianthus tuberosus sprout apicesSimone Beninati
Department of Biology, II University of Rome Tor Vergata, Via della Ricerca Scientifica, 00173 Rome, Italy
Amino Acids 44:271-83. 2013..great similarities with annotated TGs; in particular, the 75 kDa form was very similar to mammalian inactive EPB42. The 58 kDa form shared a low similarity with other TGs, including a maize sequence of similar molecular mass, ..
- Acute kernicterus in a neonate with O/B blood group incompatibility and a mutation in SLC4A1Robert D Christensen
Women and Newborns Program, Intermountain Healthcare, Salt Lake City, Utah 84403, USA
Pediatrics 132:e531-4. 2013..No mutations were identified in other red cell cytoskeleton genes (ANK1, SPTA1, SPTB, EPB41, EPB42) and the UGT1A1 promoter region was normal...
- Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1)Steven L Ciciotte
The Jackson Laboratory, Bar Harbor, ME 04609, USA
Blood 101:4402-7. 2003....
- Congenital dyserythropoietic anemia type I is caused by mutations in codanin-1Orly Dgany
Pediatric Hematology Laboratory, Felsenstein Research Center, Rabin Medical Center, Petah Tikva, Israel
Am J Hum Genet 71:1467-74. 2002..The specific mechanisms by which codanin-1 underlies normal erythropoiesis remain to be elucidated...
- Molecular basis of red cell membrane disordersJean Delaunay
Service d Hematologie, d Immunologie et de Cytogénétique, Hôpital de Bicêtre Assistance Publique Hôpitaux de Paris, Faculte de Medecine Paris Sud, et INSERM U 473, Le Kremlin Bicetre, France
Acta Haematol 108:210-8. 2002..mutations of most cases of hereditary spherocytosis (HS) are located in the following genes: ANK1, SPTB, SLC4A1, EPB42 and SPTA1, which encode ankyrin, spectrin beta-chain, the anion exchanger 1 (band 3), protein 4...
- ECRG2, a novel candidate of tumor suppressor gene in the esophageal carcinoma, interacts directly with metallothionein 2A and links to apoptosisYongping Cui
Department of Etiology and Carcinogenesis, Cancer Institute, Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100021, PR China
Biochem Biophys Res Commun 302:904-15. 2003..ECRG2 might reduce the function of MT2A on the regulation of cell proliferation and induction of apoptosis. The physical interaction of ECRG2 and MT2A may play an important role in the carcinogenesis of esophageal cancer...
- Evidence that the red cell skeleton protein 4.2 interacts with the Rh membrane complex member CD47Isabelle Mouro-Chanteloup
Institut National de la Santé et de la Recherche Médicale INSERM U76, Institut National de la Transfusion Sanguine, Paris, France
Blood 101:338-44. 2003..2(-) and Rh(null) red cells...
- Using yeast two-hybrid system to identify ECRG2 associated proteins and their possible interactions with ECRG2 geneYong Ping Cui
Department of Etiology and Carcinogenesis, Tumor Hospital, Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100021, China
World J Gastroenterol 9:1892-6. 2003..To identify esophageal cancer related gene2 (ECRG2) associated proteins and their possible interactions with ECRG2 gene...
- Protein 4.2 is critical to CD47-membrane skeleton attachment in human red cellsKris Noel Dahl
Department of Chemical and Biomolecular Engineering and School of Engineering and Applied Science, Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, PA 19104, USA
Blood 103:1131-6. 2004..2 strongly influences CD47 levels as well as the extent of membrane skeleton attachment in the RBC, whereas protein 4.2 affects membrane skeletal attachment of RhAG, Rh, and band 3 to a lesser extent...
- [Molecular mechanism of hereditary spherocytosis]Dzamila M Bogusławska
Uniwersytet Zielonogórski, Instytut Biotechnologii i Ochrony Srodowiska
Pol Merkur Lekarski 20:112-6. 2006..2 (EPB42). Inheritance of HS is usually (75%) autosomal, dominant...
- Protein 4.2: a complex linkerTimothy J Satchwell
University of Bristol, Department of Biochemistry, School of Medical Sciences, University Walk, Bristol, BS8 1TD, UK
Blood Cells Mol Dis 42:201-10. 2009..2 that may represent the active, membrane associated protein 4.2 molecule in red blood cells and also explain the dependence of protein 4.2 on band 3 binding for stability...
- The use of real-time PCR technique in the detection of novel protein 4.2 gene mutations that coexist with thalassaemia alpha in a single patientMonika Maciag
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5A, Warsaw, Poland
Eur J Haematol 83:373-7. 2009..quantification of red cell membrane protein genes in a Polish patient with alpha-thalassaemia trait indicated EPB42 as the gene that could also be involved in anaemia pathogenesis...
- The gene for human erythrocyte protein 4.2 maps to chromosome 15q15V Najfeld
Tumor Cytogenetics Laboratory, Polly Annenberg Levee Hematology Center, Mount Sinai School of Medicine, New York, NY
Am J Hum Genet 50:71-5. 1992..Our results demonstrate that the locus of the P4.2 gene is located within 15q15...
- Investigating the key membrane protein changes during in vitro erythropoiesis of protein 4.2 (-) cells (mutations Chartres 1 and 2)Emile van den Akker
Department of Biochemistry, School of Medical Sciences, University Walk, Bristol, UK
Haematologica 95:1278-86. 2010Protein 4.2 deficiency caused by mutations in the EPB42 gene results in hereditary spherocytosis with characteristic alterations of CD47, CD44 and RhAG...
- Protein 4.2 interaction with hereditary spherocytosis mutants of the cytoplasmic domain of human anion exchanger 1Susan P Bustos
Department of Biochemistry, University of Toronto, ON, Canada
Biochem J 433:313-22. 2011..2 was associated with the cytoskeleton of HEK-293 cells. The present study shows that cytoplasmic HS mutants cause impaired binding of protein 4.2 to AE1, leaving protein 4.2 susceptible to loss during erythrocyte development...
- Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid alpha-spectrin in a calcium- and calmodulin-dependent mannerCatherine Korsgren
Division of Hematology Oncology, Children s Hospital Boston and Dana Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
J Biol Chem 285:4757-70. 2010....
- Mapping of a spectrin-binding domain of human erythrocyte membrane protein 4.2Debabrata Mandal
Department of Chemistry, Bose Institute, 93 1 Acharya, Prafulla Chandra Road, Kolkata 700 009, India
Biochem J 364:841-7. 2002..2 confirmed that these residues are crucial in mediating protein 4.2-spectrin interactions...
- The pallidin (Pldn) gene and the role of SNARE proteins in melanosome biogenesisJuan M Falcon-Perez
Department of Human Genetics, University of California at Los Angeles UCLA School of Medicine, 90095, USA
Pigment Cell Res 15:82-6. 2002..As SNARE proteins mediate fusion of intracellular membranes, pallidin may play a role in membrane fusion events required for melanosome biogenesis...
- Binding of ras p21 to bands 4.2 and 6 of human erythrocyte membranesT Tanimoto
Department of Biochemistry, Kobe University School of Medicine, Japan
FEBS Lett 226:291-6. 1988..2 or 6 protein. These results indicate that v-Ki-ras p21 can bind directly to bands 4.2 and 6 of human erythrocyte membranes as far as tested in an in vitro cell-free system...
- Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2C Korsgren
Department of Biomedical Research, St Elizabeth s Hospital, Boston, MA
Proc Natl Acad Sci U S A 87:613-7. 1990..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...
- Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIIIC Korsgren
Department of Biomedical Research, St Elizabeth s Hospital, Boston, MA 02135
Proc Natl Acad Sci U S A 88:4840-4. 1991..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...
- Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stabilityP S Low
Department of Chemistry, Purdue University, West Lafayette, IN 47907 1393
Blood 77:1581-6. 1991....
- Molecular cloning of human protein 4.2: a major component of the erythrocyte membraneL A Sung
Department of Applied Mechanics, University of California at San Diego, La Jolla 92093
Proc Natl Acad Sci U S A 87:955-9. 1990..Sequence alignment of P4.2 with these two transglutaminases, however, revealed that P4.2 lacks the critical cysteine residue required for the enzymatic crosslinking of substrates...
- An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2NIPPON)E E Bouhassira
Division of Hematology, Albert Einstein College of Medicine Montefiore Medical Center, Bronx, NY 10467
Blood 79:1846-54. 1992..2-deficiency is related to the pathogenesis of the hemolytic anemia in this variant form of recessively inherited spherocytosis...
- Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylatedM A Risinger
Department of Biomedical Research, St Elizabeth s Hospital, Boston, Massachusetts 02135
J Biol Chem 267:5680-5. 1992..Study of myristylation of band 4.2, an abundant normal cellular protein, and its role in membrane binding may produce insights relevant to other myristylated cellular proteins...
- Human erythrocyte protein 4.2: isoform expression, differential splicing, and chromosomal assignmentL A Sung
Department of AMES Bioengineering, University of California, San Diego 92093 0643
Blood 79:2763-70. 1992..4-kilobase (kb) cDNA to human metaphase chromosomes, the gene for P4.2 was mapped to bands q15-q21 of chromosome 15, and it is not linked to the gene for coagulation factor XIIIa (plasma transglutaminase, TGase)...
- Identification of a band-3 binding site near the N-terminus of erythrocyte membrane protein 4.2A C Rybicki
Albert Einstein College of Medicine Montefiore Medical Center, Division of Hematology, Bronx, NY 10467, USA
Biochem J 309:677-81. 1995..2 tryptic peptides lacking this site. The V63RRGQPFTIILYF site is highly conserved in mouse and human erythrocyte P4.2 as well as between P4.2 and transglutaminase proteins, which are evolutionarily related to P4.2...
- A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemiaS Hayette
CNRS URA 1171, Institut Pasteur de Lyon, France
Br J Haematol 89:762-70. 1995..We infer that the nearly total absence of protein 4.2 in the patients results from imbalance between destruction and synthesis of mutated protein 4.2 prior to its binding to the membrane...
- Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase ZP Grenard
Connective Tissue Biology Laboratories, School of Biosciences, Cardiff University, Cardiff CF10 3US, United Kingdom
J Biol Chem 276:33066-78. 2001..sequence analysis and mapping showed that this locus contained three transglutaminase genes arranged in tandem: EPB42 (band 4.2 protein), TGM5, and a novel gene (TGM7)...
- The pallid gene encodes a novel, syntaxin 13-interacting protein involved in platelet storage pool deficiencyL Huang
Howard Hughes Medical Institute and Department of Medicine, University of California, San Francisco, California 94143 0794, USA
Nat Genet 23:329-32. 1999..Whereas the mocha and pearl SPD mutants have defects in Ap-3, our findings suggest that pa SPD mutants are defective in a more downstream event of vesicle-trafficking: namely, vesicle-docking and fusion...
- Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2R Bhattacharyya
Department of Chemistry, Bose Institute, 93 1 Acharya Prafulla Chandra Road, Calcutta 700 009, India
Biochem J 340:505-12. 1999..2-CDB3 interaction. This is also the first demonstration that palmitoylation serves as a positive modulator of this interaction...
- Human erythrocyte dematin and protein 4.2 (pallidin) are ATP binding proteinsA C Azim
Department of Biomedical Research, Laboratory of Tumor Cell Biology, St Elizabeth s Medical Center, Tufts University School of Medicine, Boston, Massachusetts 02135, USA
Biochemistry 35:3001-6. 1996..2. Although the functional significance of ATP binding is not yet clear, our findings open new perspectives for the function of dematin and protein 4.2 in vivo...
- Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2)E Dotimas
Dept of Biomedical Research, St Elizabeth s Hospital of Boston, MA 02135
Biochim Biophys Acta 1148:19-29. 1993..Our results show that endogenous pallidin on the red-cell membrane is a poor substrate for the kinase, possibly because it is fully phosphorylated, or inaccessible to the kinase...
- Human erythrocyte membrane protein 4.2 is palmitoylatedA K Das
Department of Chemistry, Bose Institute, Calcutta, India
Eur J Biochem 224:575-80. 1994..Protein 4.2 could be depalmitoylated with hydroxylamine, suggesting a thioester linkage. Depalmitoylated protein 4.2 showed significantly decreased binding to protein-4.2-depleted membranes, compared to native protein 4.2...
- A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka)Y Takaoka
Institute of Genetic Information, Kyushu University, Fukuoka, Japan
Br J Haematol 88:527-33. 1994..2 defect...
- A deletional frameshift mutation in protein 4.2 gene (allele 4.2 Lisboa) associated with hereditary hemolytic anemiaS Hayette
CNRS URA 1171, Institut Pasteur de Lyon, France
Blood 85:250-6. 1995..Antibodies to red cell protein 4.2 showed a doublet (72 and 70 kD) both in the controls and the patient. This finding raises an interesting question concerning the relationship between this doublet and erythroid protein 4.2...
- The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) geneR A White
Division of Hematology Oncology, Children s Hospital, Boston, Massachusetts
Nat Genet 2:80-3. 1992..This is the first gene defect to be associated with a platelet storage pool deficiency, and may allow the identification of a novel structure or biological pathway that influences granulogenesis...