Abstract
The dyserythropoietic anemia disease is a genetic disorder of erythropoiesis characterized by morphological abnormalities of erythroblasts. This is caused by human gene C15orf41 mutation. The uncharacterized C15orf41 protein is involved in the formation of a functional complex structure. The uncharacterized C15orf41 protein is thermostable, unstable and acidic. This is associated with TPD (Treponema Pallidum) domain (135 to 265 residue position) and three PTM sites such as K50 (Acetylation), T114 (Phosphorylation) and K176 (Ubiquitination). C15orf41 is paralogous to isoform-1 (gi|194018542|) and open reading frame isoform-CRA_c (gi|119612744|) of Homo sapiens located at chromosome 15. It interacts with the human ATP (Adenosine Triphosphate) binding domain 4 (ATPBD4) having similarity score 0.725 as per protein-protein interaction (PPI) network analysis. This data provides valuable insights towards the functional characterization of human gene C15orf41.
Highlights
The human uncharacterized gene C15orf41 is located at chromosome 15 encodes a protein with two predicted helix-turnhelix domains
The high percentage of those amino acids influences the regulation of signaling pathway and protein synthesis independently [24]
The query protein is regarded as the thermostable protein. It means that the query protein C15orf41 is a resistant protein due to the irretrievable changes of physical and chemical structural decay in the high-temperature
Summary
The human uncharacterized gene C15orf is located at chromosome 15 encodes a protein with two predicted helix-turnhelix domains. The structural and functional characteristics of proteins play the significant role in drug design and discovery Investigations of these proteins characteristics experimentally in the wet lab are much laborious, time consuming and costly. The computational/statistical tools of bioinformatics reduce this cost and time significantly to characterize the uncharacterized proteins. These tools are widely used for homology modeling of sequence profiles and predicting the three-dimensional (3D) structure of the targeted protein. An evolutionary characterization of uncharacterized bacterial proteins based on sequence profile analysis by computational approach is more rapid than experimental approach, which is very important for the discovery of drug targets and biological process [9,10]. In this study, an attempt is made to investigate the physiochemical properties and structural and functional characteristics of this protein using computational/statistical bioinformatics tools
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