Recombinant Human Ankyrin-1 (ANK1), partial

1. Our finding suggested that a de novo nonsense mutation in ANK1 may be causative to HS which plays an important role in supplementing the mutational spectrum of the ANK1 and explaining the mechanism of HS. PMID: 29099659
2. ANK1 rs508419-C type 2 diabetes (T2D)-risk allele alters DNA-protein complex binding leading to increased promoter activity and sAnk1 expression; thus, increased sAnk1 expression in skeletal muscle might contribute to T2D susceptibility. PMID: 27121283
3. rs515071 in ANK1 is a novel genetic risk for late-onset Alzheimer's disease susceptibility in Han Chinese. PMID: 26611832
4. The present study demonstrates that ANK1 is aberrantly expressed in pancreatic adenocarcinomas in association with promoter hypomethylation PMID: 27144336
5. Transient Receptor Potential Vanniloid-1 channel (TRPV-1) has a role in the cough reflex and airway expression is increased in patients with chronic cough. The Ankyrin-1 receptor (TRPA-1) is often co-expressed PMID: 29149168
6. Aberrant ANK1 methylation is highly prevalent in lung cancer, discriminate tumors by histology and patients' smoking history, and contributes to miR-486-5p repression. PMID: 28965852
7. Study shows that Ankyrin-1 forms a high-affinity interaction with AE1 tetramers but does not associate with AE1 dimers in erythrocyte membranes. PMID: 27989623
8. ANK1 is up-regulated 4-fold in Alzheimer disease microglia, but not in neurons or astrocytes from the same individuals. PMID: 28700589
9. Two novel mutations in ANK1 (Y216X and E142X) are responsible for hereditary spherocytosis. PMID: 28694211
10. These results suggest that sAnk1 interacts with SLN both directly and in complex with SERCA1 and reduces SLN's inhibitory effect on SERCA1 activity. PMID: 28487373
11. Mutational characteristics of ANK1 and SPTB genes in Korean hereditary spherocytosis have been described. PMID: 26830532
12. Ankyrin-1 is induced to a greater extent than the embedded miRNA following DNA damage. PMID: 27054339
13. analysis of a novel p.Q1772X ANK1 mutation in a Korean family with hereditary spherocytosis [case report of two family members] PMID: 26107955
14. The study reports the refinement for a protein heterodimer complex using limited EPR spectroscopic data and a rigid-body docking algorithm: a three-dimensional model for an ankyrin 1-BND3 complex. PMID: 24758720
15. A novel L1340P mutation in the ANK1 gene is associated with hereditary spherocytosis. PMID: 24903897
16. We identified a differentially methylated region in the ankyrin 1 (ANK1) gene that was associated with neuropathology in the entorhinal cortex, a primary site of Alzheimer disease manifestation. PMID: 25129077
17. ANK1 rs516946 confers impaired insulin release. PMID: 23457408
18. The ankyrin-binding site on band 3 is located near the deoxygenated hemoglobin-binding site, therefore following deoxygenation ankyrin is displaced from band 3. PMID: 23013433
19. A tissue-specific chromatin loop brings NF-E2 and ANK1E into close proximity preventing gene silencing and mutagenesis leading to hereditary spherocytosis. PMID: 22968456
20. results indicate that the ANK1 locus is a new, common susceptibility locus for type 2 diabetes across different ethnic groups PMID: 22456796
21. The interaction of KCTD6 with ankyrin-1 may have implications beyond muscle for hereditary spherocytosis, as KCTD6 is also present in erythrocytes, and erythrocyte ankyrin isoforms contain its mapped minimal binding site. PMID: 22573887
22. Determination of structural models of the complex between the cytoplasmic domain of erythrocyte band 3 and ankyrin-R repeats 13-24. PMID: 21493712
23. The Hereditary Spherocytosis mutation in the human Ankyrin-1 promoter disrupted the binding of the transcription factor TFIID, the major component of the pre-initiation complex. PMID: 21071415
24. cytoskeletal ankyrin family are substrates for FIH-catalyzed hydroxylations PMID: 21177872
25. a region upstream of the promoter is a barrier insulator. The region exhibited functional and structural characteristics of a barrier, including prevention of gene silencing, appropriate chromatin configuration and occupancy by barrier-associated proteins PMID: 21099109
26. Generated a library of more than 16,000 ANK-1 promoters with degenerate sequence around the dinucleotide deletion mutation and cloned the functional promoter sequences. Identified the wild type and three additional sequences, and derived a consensus. PMID: 20479128
27. ankyrin and protein 4.1 are cleaved by native and recombinant falcipain-2 near their C-termini PMID: 12130521
28. interaction of hydrophilic domain with two N-terminal immunoglobulin domains of titin PMID: 12444090
29. identification of ankyrin as a target of spectrin's E2/E3 activity PMID: 15040428
30. The interactions of three protein 4.2-derived recombinant proteins with CDB3 and ankyrin were investigated by using Far-Western blot and pull-down assay. PMID: 16718373
31. off rates of the band 3-ankyrin interaction are sufficiently slow to allow sustained erythrocyte deformation without loss of elasticity PMID: 16762928
32. Allelic and genotypic frequencies were similar in both studied groups for the G199A and Memphis I polymorphismsin Hereditary Spherocytosis among the Mexican population. PMID: 17128827
33. It was shown that the region within beta-spectrin involved in interactions with ankyrin includes a lipid-binding site and binding is inhibited by ankyrin. Our results shows: the ankyrin-sens. lipid-bind. site of beta-spectrin exhibits a helical conform. PMID: 17520478
34. Our results therefore indicate the importance of N-terminal region for lipid-binding activity of the beta-spectrin ankyrin-binding domain and its substantial role in maintaining the spectrin-based skeleton distribution. PMID: 17716929
35. Structural and mutational studies of the binding region on small Ank1 for obscurin suggest that it consists of two ankyrin repeats with very similar structures. PMID: 17720975
36. Ankyrin facilitates intracellular trafficking of alpha1-Na+-K+-ATPase in polarized cells. PMID: 18768923
37. A small muscle-specific isoform of the ANK1 gene, ank1.5, interacts with obscurin. Since ank1.5 is localised on the sarcoplasmic reticulum and obscurin on the myofibrils, these two proteins may provide a molecular link between these subcellular regions. PMID: 12527750

Show More

Hide All

HGNC: 492

OMIM: 182900

KEGG: hsa:286

STRING: 9606.ENSP00000265709

UniGene: Hs.654438