Ankyrin 1, Erythrocytic (ANK1)

ANK; SPH1; SPH2; Ankyrin-R

SPN	T932
HGNC	492
MGI	88024
PubMed	8640229
RGD	1309620
UniProt	P16157
Wiki	ANK1_(gene

Ankyrin 1was first discovered in erythrocytes, but since has also been found in brain and muscles.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.

Reference

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Nature 344:36-42(1990) [PubMed] [Europe PMC] [Abstract]

"cDNA sequence for human erythrocyte ankyrin."
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"Structure and organization of the human ankyrin-1 gene. Basis for complexity of pre-mRNA processing."
J. Biol. Chem. 272:19220-19228(1997) [PubMed] [Europe PMC] [Abstract]

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J. Biol. Chem. 286:7648-7660(2011) [PubMed] [Europe PMC] [Abstract]

"The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger."
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"The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin."
J. Biol. Chem. 278:3985-3991(2003) [PubMed] [Europe PMC] [Abstract]

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"Crystal structure of a 12 ANK repeat stack from human ankyrinR."
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"Solution structure of the DEATH domain of ankyrin-1."
Submitted (APR-2008) to the PDB data bank

"Structurally similar but functionally diverse ZU5 domains in human erythrocyte ankyrin."
J. Mol. Biol. 417:336-350(2012) [PubMed] [Europe PMC] [Abstract]

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