The protein encoded by this gene is localized to the nucleus of endothelial cells and is induced by IL-1 and TNF-alpha stimulation. Studies in rat cardiomyocytes suggest that this gene functions as a transcription factor. Interactions between this protein and the sarcomeric proteins myopalladin and titin suggest that it may also be involved in the myofibrillar stretch-sensor system.
A synthesized peptide derived from human ANKRD20, corresponding to a region within the internal amino acids.
A synthesized peptide derived from human ANKRD26, corresponding to a region within the internal amino acids.
A synthesized peptide derived from human ANKRD27.
A synthesized peptide derived from human ANKRD50.
This gene encodes a protein containing multiple ankyrin repeats and a SAM domain. It is thought that this protein may localize to the proximal region of the primary cilium, and may play a role in renal and cardiovascular development. Mutations in this gene have been shown to cause a form of nephronophthisis (NPHP16), a chronic tubulo-interstitial nephritis.
A synthesized peptide derived from human Ankyrin erythroid, corresponding to a region within the internal amino acids.
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. ANKZF1 (ankyrin repeat and zinc finger domain containing 1), also known as ZNF744, is 726 amino acids in length and lacks a KRAB domain but contains one C2H2-type zinc finger and two ANK repeats. The gene encoding ANKZF1 localizes to chromosome 2.
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