1N11, 2YQF, 2YVI, 3F59, 3KBT, 3KBU, 3UD1, 3UD2
286
11733
ENSG00000029534
ENSMUSG00000031543
P16157
Q02357
NM_020477NM_020478NM_020479NM_020480NM_020481
NM_001277289NM_031158NM_001310436NM_001310437
NP_065210NP_065211NP_065213
NP_001264218NP_001297365NP_001297366NP_112435
Ankyrin 1, also known as ANK-1, and erythrocyte ankyrin, is a protein that in humans is encoded by the ANK1 gene.[5][6]
The protein 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.[6]
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.[6]
Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis.[6]
ANK1 shows altered methylation and expression in Alzheimer's disease.[7][8] A gene expression study of postmortem brains has suggested ANK1 interacts with interferon-γ signalling.[9]
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 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.[6]
The small ANK1 (sAnk1) protein splice variants makes contacts with obscurin, a giant protein surrounding the contractile apparatus in striated muscle.[10]
ANK1 has been shown to interact with T-cell lymphoma invasion and metastasis-inducing protein 1,[11] Titin,[12] RHAG[13] and OBSCN.[14]
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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