v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | Protein 4.1 (EPB4.1) is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating physical properties of the membrane, such as mechanical stability and de-formability, by stabilising spectrin-actin interactions [ , , ]. It is required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase []. The protein has been shown to associate with the nuclear mitotic apparatus, the contractile apparatus and tight junctions. Defects in this protein can cause elliptocytosis type 1 and hereditary pyropoikilocytosis.Note: Band 4.1 and Band 7 ( ) proteins refer to human erythrocyte membrane proteins separated by SDS polyacrylamide gels and stained with coomassie blue [ ].This entry represents the N-terminal F1 sub-domain of the FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain found in EPB4.1. This domain is also known as the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). |
| Short Name | EPB4.1_FERM_F1 |