Ankyrin 1, erythrocytic
, also known as ANK1
, is a human gene
encoded by this gene, Ankyrin 1, is the prototype of the ankyrin
family, was first discovered in erythrocytes
, but since has also been found in brain and muscles.
Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described, however, the precise functions of the various isoforms are not known. Alternative polyadenylation accounting for the different sized erythrocytic ankyrin 1 mRNAs, has also been reported. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified.
Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis
The ANK1 protein belongs to the ankyrin
family that are believed to link the integral membrane proteins to the underlying spectrin-actin cytoskeleton
and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin
binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation.
The small ANK1 (sAnk1) protein splice variants makes contacts with obscurin, a giant protein surrounding the contractile apparatus in striated muscle.