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Details on Person Protein 4.1 purified from mammalian erythrocytes associates ...
| Class:Id | Summation:427179 |
|---|---|
| _displayName | Protein 4.1 purified from mammalian erythrocytes associates ... |
| _timestamp | 2009-06-18 14:34:07 |
| created | [InstanceEdit:427181] Jupe, S, 2009-06-18 |
| literatureReference | [LiteratureReference:427168] Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein |
| text | Protein 4.1 purified from mammalian erythrocytes associates with the N-terminal region of beta-spectrin. Protein 4.1 and glycophorin C form a high-affinity ternary complex in vitro with the membrane-associated guanylate kinase (MAGUK) p55. Protein 4.1 is a substrate for protein kinases A and C, casein kinase II. Phosphorylation results in downregulation of protein 4.1 membrane association and spectrin/actin binding. |
| (summation) | [Reaction:426392] Spectrin binds protein 4.1:Glycophorin-C:p55 complex [Homo sapiens] |
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No pathways have been reviewed or authored by Protein 4.1 purified from mammalian erythrocytes associates ... (427179)
