Ankyrin Repeat And MYND Domain Containing Protein 1 (ANKMY1)
ZMYND13; TSAL1; Testis-specific ankyrin-like protein 1; Zinc finger MYND domain-containing protein 13
Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network.
ANKMY1 is a 941 amino acid protein that contains seven ANK repeats, three MORN repeats and one MYND-type zinc finger. MORN repeats were first identified in junctophilins, cytoplasmic proteins involved in junctions between the plasma membrane and the ER/SR membrane. The presence of MORN repeats suggests that ANKMY1 may interact with the plasma membrane. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif which may be involved in protein-protein interactions. Three isoforms of ANKMY1 exists due to alternative splicing events.
ANKMY1 is a 941 amino acid protein that contains seven ANK repeats, three MORN repeats and one MYND-type zinc finger. MORN repeats were first identified in junctophilins, cytoplasmic proteins involved in junctions between the plasma membrane and the ER/SR membrane. The presence of MORN repeats suggests that ANKMY1 may interact with the plasma membrane. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif which may be involved in protein-protein interactions. Three isoforms of ANKMY1 exists due to alternative splicing events.
Organism species: Homo sapiens (Human)
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Organism species: Mus musculus (Mouse)
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