Human Gene EPB42 (ENST00000441366.7) from GENCODE V44
Description: Homo sapiens erythrocyte membrane protein band 4.2 (EPB42), transcript variant 2, mRNA. (from RefSeq NM_001114134) RefSeq Summary (NM_001114134): 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. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]. Gencode Transcript: ENST00000441366.7 Gencode Gene: ENSG00000166947.15 Transcript (Including UTRs) Position: hg38 chr15:43,197,227-43,221,018 Size: 23,792 Total Exon Count: 13 Strand: - Coding Region Position: hg38 chr15:43,197,302-43,220,825 Size: 23,524 Coding Exon Count: 13
ID:EPB42_HUMAN DESCRIPTION: RecName: Full=Erythrocyte membrane protein band 4.2; Short=Erythrocyte protein 4.2; Short=P4.2; FUNCTION: Probably plays an important role in the regulation of erythrocyte shape and mechanical properties. SUBUNIT: Oligomer. Interacts with the cytoplasmic domain of SLC4A1/band 3 anion transport protein. INTERACTION: P58062:SPINK7; NbExp=3; IntAct=EBI-1182496, EBI-1182445; SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Cytoplasmic surface of erythrocyte membranes. PTM: Both cAMP-dependent kinase (CAPK) and another kinase present in the red-blood cells seem to be able to phosphorylate EPB42. DISEASE: Defects in EPB42 are the cause of spherocytosis type 5 (SPH5) [MIM:612690]; also known as hereditary spherocytosis type 5 (HS5). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Absence of band 4.2 associated with spur or target erythrocytes has also been reported. MISCELLANEOUS: The substitution of an Ala for a Cys in the active site may be responsible for the lack of transglutaminase activity of band 4.2. SIMILARITY: Belongs to the transglutaminase superfamily. Transglutaminase family. SEQUENCE CAUTION: Sequence=AAA36401.1; Type=Frameshift; Positions=335, 340; Sequence=AAA36402.1; Type=Frameshift; Positions=335, 340;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
Pfam Domains: PF00927 - Transglutaminase family, C-terminal ig like domain PF01841 - Transglutaminase-like superfamily PF00868 - Transglutaminase family
ModBase Predicted Comparative 3D Structure on P16452
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.