Aliases for ANK1 Gene
External Ids for ANK1 Gene
Previous HGNC Symbols for ANK1 Gene
Previous GeneCards Identifiers for ANK1 Gene
Ankyrins are a family of proteins that 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. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008]
GeneCards Summary for ANK1 Gene
ANK1 (Ankyrin 1, Erythrocytic) is a Protein Coding gene. Diseases associated with ANK1 include hereditary spherocytosis and 8p11.2 deletion syndrome. Among its related pathways are Developmental Biology and Apoptotic Pathways in Synovial Fibroblasts. GO annotations related to this gene include enzyme binding and structural constituent of cytoskeleton. An important paralog of this gene is ANKRD52.
UniProtKB/Swiss-Prot for ANK1 Gene
Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.
Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.