Human Gene ANK1 (ENST00000265709.14) from GENCODE V44
Description: Homo sapiens ankyrin 1 (ANK1), transcript variant 9, mRNA. (from RefSeq NM_001142446) RefSeq Summary (NM_001142446): 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]. Gencode Transcript: ENST00000265709.14 Gencode Gene: ENSG00000029534.22 Transcript (Including UTRs) Position: hg38 chr8:41,653,225-41,896,741 Size: 243,517 Total Exon Count: 43 Strand: - Coding Region Position: hg38 chr8:41,655,727-41,896,480 Size: 240,754 Coding Exon Count: 43
ID:ANK1_HUMAN DESCRIPTION: RecName: Full=Ankyrin-1; Short=ANK-1; AltName: Full=Ankyrin-R; AltName: Full=Erythrocyte ankyrin; FUNCTION: 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. FUNCTION: Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils. SUBUNIT: Interacts with a number of integral membrane proteins and cytoskeletal proteins. Interacts (via N-terminus) with SPTB/spectrin (beta chain). Interacts (via N-terminus ANK repeats) with SLC4A1/erythrocyte membrane protein band 3 (via cytoplasmic N-terminus). Also interacts with TTN/titin. Isoform Mu17 interacts with OBSCN isoform 3/obscurin. Interacts with HIF1AN. INTERACTION: Q5VST9-3:OBSCN; NbExp=3; IntAct=EBI-941686, EBI-941921; SUBCELLULAR LOCATION: Isoform Er1: Cytoplasm, cytoskeleton. Note=Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane. SUBCELLULAR LOCATION: Isoform Mu17: Membrane. Cytoplasm, myofibril, sarcomere, M line. Note=Colocalizes with OBSCN isoform 3/obscurin at the M line in differentiated skeletal muscle cells. SUBCELLULAR LOCATION: Isoform Mu18: Sarcoplasmic reticulum (Probable). SUBCELLULAR LOCATION: Isoform Mu19: Sarcoplasmic reticulum (Probable). SUBCELLULAR LOCATION: Isoform Mu20: Sarcoplasmic reticulum (Probable). TISSUE SPECIFICITY: Isoform Mu17, isoform Mu18, isoform Mu19 and isoform Mu20 are expressed in skeletal muscle. Isoform Br21 is expressed in brain. DOMAIN: The 55 kDa regulatory domain is involved in regulating binding of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein band 3. DOMAIN: The ANK repeat region forms a spiral around a large central cavity and is involved in binding of ion transporters. DOMAIN: The tandem configuration of the two ZU5 and the UPA domains forms a structural supramodule termed ZZU. ZU5-1 mediates interaction with beta-spectrin, and the ZU5-1/UPA interface is required for ankyrin's function other than binding to spectrin (By similarity). PTM: Regulated by phosphorylation. PTM: Palmitoylated. PTM: Hydroxylated by HIF1AN at several asparagine and 1 aspartate residue within ANK repeat region. Hydroxylation seems to increase the conformational stability of this region and may also modulate protein-protein interactions mediated by the ANK repeat region. DISEASE: Defects in ANK1 are a cause of spherocytosis type 1 (SPH1) [MIM:182900]; also called hereditary spherocytosis type 1 (HS1). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Inheritance can be autosomal dominant or recessive. SIMILARITY: Contains 23 ANK repeats. SIMILARITY: Contains 1 death domain. SIMILARITY: Contains 2 ZU5 domains. SEQUENCE CAUTION: Sequence=AAB47805.1; Type=Erroneous gene model prediction; WEB RESOURCE: Name=Wikipedia; Note=Ankyrin entry; URL="http://en.wikipedia.org/wiki/Ankyrin";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P16157
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006887 exocytosis GO:0006888 ER to Golgi vesicle-mediated transport GO:0007010 cytoskeleton organization GO:0007165 signal transduction GO:0010638 positive regulation of organelle organization GO:0045199 maintenance of epithelial cell apical/basal polarity GO:0072659 protein localization to plasma membrane