- ANK1
Ankyrin 1, erythrocytic, also known as ANK1, is a human
gene .cite journal | author = Lambert S, Yu H, Prchal JT, "et al" | title = cDNA sequence for human erythrocyte ankyrin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 87 | issue = 5 | pages = 1730–4 | year = 1990 | month = March | pmid = 1689849 | pmc = 53556 | doi = | url = http://www.pnas.org/content/87/5/1730.abstract | issn = ] cite web | title = Entrez Gene: ANK1 ankyrin 1, erythrocytic| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=286| accessdate = ]Tissue distribution
The
protein encoded by this gene, Ankyrin 1, is the prototype of theankyrin family, was first discovered inerythrocyte s, but since has also been found in brain and muscles.Genetics
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.
Disease linkage
Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary
spherocytosis .Function
The ANK1 protein belongs to the
ankyrin family that are believed to link the integral membrane proteins to the underlying spectrin-actincytoskeleton 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 conservedspectrin 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 .cite journal | author = Borzok MA, Catino DH, Nicholson JD, Kontrogianni-Konstantopoulos A, Bloch RJ | title = Mapping the binding site on small ankyrin 1 for obscurin | journal = J. Biol. Chem. | volume = 282 | issue = 44 | pages = 32384–96 | year = 2007 | month = November | pmid = 17720975 | doi = 10.1074/jbc.M704089200 | url = | issn = ]ee also
*
Ankyrin References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Bennett V, Baines AJ |title=Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. |journal=Physiol. Rev. |volume=81 |issue= 3 |pages= 1353–92 |year= 2001 |pmid= 11427698 |doi=
*cite journal | author=Bennett V |title=Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues. |journal=Nature |volume=281 |issue= 5732 |pages= 597–9 |year= 1979 |pmid= 492324 |doi=
*cite journal | author=Lambert S, Yu H, Prchal JT, "et al." |title=cDNA sequence for human erythrocyte ankyrin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 5 |pages= 1730–4 |year= 1990 |pmid= 1689849 |doi=
*cite journal | author=Fujimoto T, Lee K, Miwa S, Ogawa K |title=Immunocytochemical localization of fodrin and ankyrin in bovine chromaffin cells in vitro. |journal=J. Histochem. Cytochem. |volume=39 |issue= 11 |pages= 1485–93 |year= 1991 |pmid= 1833445 |doi=
*cite journal | author=Lux SE, John KM, Bennett V |title=Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. |journal=Nature |volume=344 |issue= 6261 |pages= 36–42 |year= 1990 |pmid= 2137557 |doi= 10.1038/344036a0
*cite journal | author=Davis LH, Bennett V |title=Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin. |journal=J. Biol. Chem. |volume=265 |issue= 18 |pages= 10589–96 |year= 1990 |pmid= 2141335 |doi=
*cite journal | author=Korsgren C, Cohen CM |title=Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3. |journal=J. Biol. Chem. |volume=263 |issue= 21 |pages= 10212–8 |year= 1988 |pmid= 2968981 |doi=
*cite journal | author=Cianci CD, Giorgi M, Morrow JS |title=Phosphorylation of ankyrin down-regulates its cooperative interaction with spectrin and protein 3. |journal=J. Cell. Biochem. |volume=37 |issue= 3 |pages= 301–15 |year= 1988 |pmid= 2970468 |doi= 10.1002/jcb.240370305
*cite journal | author=Steiner JP, Bennett V |title=Ankyrin-independent membrane protein-binding sites for brain and erythrocyte spectrin. |journal=J. Biol. Chem. |volume=263 |issue= 28 |pages= 14417–25 |year= 1988 |pmid= 2971657 |doi=
*cite journal | author=Hargreaves WR, Giedd KN, Verkleij A, Branton D |title=Reassociation of ankyrin with band 3 in erythrocyte membranes and in lipid vesicles. |journal=J. Biol. Chem. |volume=255 |issue= 24 |pages= 11965–72 |year= 1981 |pmid= 6449514 |doi=
*cite journal | author=Bourguignon LY, Lokeshwar VB, Chen X, Kerrick WG |title=Hyaluronic acid-induced lymphocyte signal transduction and HA receptor (GP85/CD44)-cytoskeleton interaction. |journal=J. Immunol. |volume=151 |issue= 12 |pages= 6634–44 |year= 1994 |pmid= 7505012 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Morgans CW, Kopito RR |title=Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin. |journal=J. Cell. Sci. |volume=105 ( Pt 4) |issue= |pages= 1137–42 |year= 1993 |pmid= 8227202 |doi=
*cite journal | author=Bourguignon LY, Jin H, Iida N, "et al." |title=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. |journal=J. Biol. Chem. |volume=268 |issue= 10 |pages= 7290–7 |year= 1993 |pmid= 8385102 |doi=
*cite journal | author=Eber SW, Gonzalez JM, Lux ML, "et al." |title=Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis. |journal=Nat. Genet. |volume=13 |issue= 2 |pages= 214–8 |year= 1996 |pmid= 8640229 |doi= 10.1038/ng0696-214
*cite journal | author=Lanfranchi G, Muraro T, Caldara F, "et al." |title=Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization. |journal=Genome Res. |volume=6 |issue= 1 |pages= 35–42 |year= 1996 |pmid= 8681137 |doi=
*cite journal | author=del Giudice EM, Hayette S, Bozon M, "et al." |title=Ankyrin Napoli: a de novo deletional frameshift mutation in exon 16 of ankyrin gene (ANK1) associated with spherocytosis. |journal=Br. J. Haematol. |volume=93 |issue= 4 |pages= 828–34 |year= 1996 |pmid= 8703812 |doi=
*cite journal | author=Zhou D, Birkenmeier CS, Williams MW, "et al." |title=Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated with the sarcoplasmic reticulum of mammalian skeletal muscle. |journal=J. Cell Biol. |volume=136 |issue= 3 |pages= 621–31 |year= 1997 |pmid= 9024692 |doi=
*cite journal | author=Gallagher PG, Tse WT, Scarpa AL, "et al." |title=Structure and organization of the human ankyrin-1 gene. Basis for complexity of pre-mRNA processing. |journal=J. Biol. Chem. |volume=272 |issue= 31 |pages= 19220–8 |year= 1997 |pmid= 9235914 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=External links
*
PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = no
update_citations = yes
Wikimedia Foundation. 2010.
