ANKIB1

Currently, there is limited information available regarding the post-translational modifications of ANKIB1 protein. However, like many other proteins, it is possible that ANKIB1 may undergo modifications such as phosphorylation, ubiquitination, or acetylation, which can regulate its stability, activity, or cellular localization. Further studies are needed to elucidate the post-translational modifications of ANKIB1 protein.

ANKIB1 protein contains multiple ankyrin repeat domains, which are known to mediate protein-protein interactions. Ankyrin repeat domains consist of approximately 33 amino acids and are characterized by a series of repeated structural units that form a helical hairpin structure. These domains are often involved in binding to specific protein partners. The presence of ankyrin repeat domains in ANKIB1 suggests its potential role in protein interactions and signaling.

ANKIB1 has been found to be mutated in a small number of individuals with neurodevelopmental disorders, including intellectual disability and autism spectrum disorder. These findings suggest a potential role for ANKIB1 in normal brain development and function. Further research is needed to fully understand the involvement of ANKIB1 in disease processes.

Mutations in the ANKIB1 gene have been associated with neurodevelopmental disorders, including intellectual disability and autism spectrum disorders. However, these mutations are rare, and more research is needed to establish a clear link between ANKIB1 protein and these diseases.

The specific binding partners or interactors of ANKIB1 protein have not been extensively characterized yet. Further research is required to investigate its protein-protein interactions and identify potential binding partners.

Yes, ANKIB1 has orthologs in various species. For example, in mice, the ANKIB1 protein is referred to as Ankib1. Orthologs of ANKIB1 can be found by conducting comparative genomics analyses across different species. These orthologous proteins may provide insights into the evolutionary conservation and functional roles of ANKIB1.

its potential role in protein-protein interactions suggests that it may participate in signaling cascades by interacting with other signaling molecules. Further research is necessary to uncover the exact signaling pathways in which ANKIB1 protein is involved.

ANKIB1 protein contains ankyrin repeat domains, which are common protein-protein interaction motifs found in many proteins involved in diverse cellular processes. It also possesses an IBR domain, which suggests potential involvement in protein stability and ubiquitin ligase activity.

The specific interacting partners or binding partners of ANKIB1 protein have not been extensively studied. However, as ankyrin repeat domains are known to mediate protein-protein interactions, it is possible that ANKIB1 may interact with other proteins in the cell. Future research may help identify the specific binding partners and elucidate the functional implications of these interactions.

ANKIB1 protein is broadly expressed in various tissues, including the brain, heart, liver, and skeletal muscles.

Although the exact functions of ANKIB1 protein are still not fully understood, its ankyrin repeat domains suggest a potential role in protein-protein interactions and regulation of cellular processes. Additionally, the presence of the IBR domain suggests a possible involvement in protein stability and ubiquitin ligase activity. However, further research is needed to determine its precise functions.

Mutations in the ANKIB1 gene have been identified in a very limited number of cases with neurodevelopmental disorders such as intellectual disability and autism spectrum disorders. However, more research is needed to establish a clear association between ANKIB1 mutations and these conditions.