ANK1

From Wikipedia, the free encyclopedia

Ankyrin 1, erythrocytic

PDB rendering based on 1n11.

Available structures: 1n11

Identifiers

Symbol(s)

ANK1; ANK; SPH1; SPH2

External IDs

OMIM: 182900 MGI: 88024 HomoloGene: 55427

Gene ontology
Molecular Function:	• structural constituent of cytoskeleton • cytoskeletal adaptor activity • enzyme binding • spectrin binding
Cellular Component:	• plasma membrane • actin cytoskeleton • basolateral plasma membrane
Biological Process:	• exocytosis • cytoskeleton organization and biogenesis • signal transduction • maintenance of epithelial cell polarity

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000037 (mRNA)
NP_000028 (protein)

XM_981917 (mRNA)
XP_987011 (protein)

Location

Chr 8: 41.63 - 41.87 Mb

Chr 8: 24.44 - 24.62 Mb

Pubmed search

[1]

[2]

Ankyrin 1, erythrocytic, also known as ANK1, is a human gene.^[1]

Ankyrins are a family of proteins 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. 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, 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.^[1]

[edit] See also

Ankyrin

[edit] References

^ ^a ^b Entrez Gene: ANK1 ankyrin 1, erythrocytic.

[edit] Further reading

Bennett V, Baines AJ (2001). "Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues.". Physiol. Rev. 81 (3): 1353-92. PMID 11427698.
Bennett V (1979). "Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues.". Nature 281 (5732): 597-9. PMID 492324.
Lambert S, Yu H, Prchal JT, et al. (1990). "cDNA sequence for human erythrocyte ankyrin.". Proc. Natl. Acad. Sci. U.S.A. 87 (5): 1730-4. PMID 1689849.
Fujimoto T, Lee K, Miwa S, Ogawa K (1991). "Immunocytochemical localization of fodrin and ankyrin in bovine chromaffin cells in vitro.". J. Histochem. Cytochem. 39 (11): 1485-93. PMID 1833445.
Lux SE, John KM, Bennett V (1990). "Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins.". Nature 344 (6261): 36-42. doi:10.1038/344036a0. PMID 2137557.
Davis LH, Bennett V (1990). "Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin.". J. Biol. Chem. 265 (18): 10589-96. PMID 2141335.
Korsgren C, Cohen CM (1988). "Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3.". J. Biol. Chem. 263 (21): 10212-8. PMID 2968981.
Cianci CD, Giorgi M, Morrow JS (1988). "Phosphorylation of ankyrin down-regulates its cooperative interaction with spectrin and protein 3.". J. Cell. Biochem. 37 (3): 301-15. doi:10.1002/jcb.240370305. PMID 2970468.
Steiner JP, Bennett V (1988). "Ankyrin-independent membrane protein-binding sites for brain and erythrocyte spectrin.". J. Biol. Chem. 263 (28): 14417-25. PMID 2971657.
Hargreaves WR, Giedd KN, Verkleij A, Branton D (1981). "Reassociation of ankyrin with band 3 in erythrocyte membranes and in lipid vesicles.". J. Biol. Chem. 255 (24): 11965-72. PMID 6449514.
Bourguignon LY, Lokeshwar VB, Chen X, Kerrick WG (1994). "Hyaluronic acid-induced lymphocyte signal transduction and HA receptor (GP85/CD44)-cytoskeleton interaction.". J. Immunol. 151 (12): 6634-44. PMID 7505012.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
Morgans CW, Kopito RR (1993). "Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin.". J. Cell. Sci. 105 ( Pt 4): 1137-42. PMID 8227202.
Bourguignon LY, Jin H, Iida N, et al. (1993). "The involvement of ankyrin in the regulation of inositol 1,4,5-trisphosphate receptor-mediated internal Ca2+ release from Ca2+ storage vesicles in mouse T-lymphoma cells.". J. Biol. Chem. 268 (10): 7290-7. PMID 8385102.
Eber SW, Gonzalez JM, Lux ML, et al. (1996). "Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis.". Nat. Genet. 13 (2): 214-8. doi:10.1038/ng0696-214. PMID 8640229.
Lanfranchi G, Muraro T, Caldara F, et al. (1996). "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization.". Genome Res. 6 (1): 35-42. PMID 8681137.
del Giudice EM, Hayette S, Bozon M, et al. (1996). "Ankyrin Napoli: a de novo deletional frameshift mutation in exon 16 of ankyrin gene (ANK1) associated with spherocytosis.". Br. J. Haematol. 93 (4): 828-34. PMID 8703812.
Zhou D, Birkenmeier CS, Williams MW, et al. (1997). "Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated with the sarcoplasmic reticulum of mammalian skeletal muscle.". J. Cell Biol. 136 (3): 621-31. PMID 9024692.
Gallagher PG, Tse WT, Scarpa AL, et al. (1997). "Structure and organization of the human ankyrin-1 gene. Basis for complexity of pre-mRNA processing.". J. Biol. Chem. 272 (31): 19220-8. PMID 9235914.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.