page_title: C17orf98
section_title: Motifs and binding sites
hierarchical_section_title: C17orf98 / Protein / Motifs and binding sites
caption_attribution_description: English: Model swiss 3d structure
context_page_description: C17orf98 is a protein which in humans is coded by the gene c17orf98. The protein is derived from Homo sapiens chromosome 17. The C17orf98 gene consists of a 6,302 base sequence. Its mRNA has three exons and no alternative splice sites. The protein has 154 amino acids, with no abnormal amino acid levels. C17orf98 has a domain of unknown function and is 17.6kDa in weight. C17orf98 does not belong to any other families nor does it have any isoforms. The protein has orthologs with high percent similarity in mammals and reptiles. The protein has additional distantly related orthologs across the metazoan kingdom, culminating with the sponge family.
  Like most proteins, C17orf98 is known to be highly expressed in the testes. The protein has also been known to have elevated levels in cancer. The protein has been shown to be expressed in proximity to or within intermediate filaments and the nucleolus. Additionally, c17orf98 has transcription factors which are also active in hematopoietic stem cells, the immune system, and the cardiovascular system, among others. The gene is over-expressed in many cancer types, including kidney renal clear cell carcinoma and lung squamous cell carcinoma.
context_section_description: There are no N-terminal signal peptides. Cleavage motifs were not found. There are no ER membrane retention signals, nor peroxisomal targeting signal. SKL2 is not present, thus a secondary peroxisome signal is not present. There are no vacuolar targeting signals. There are no RNA binding motifs or actinin type actin binding motifs. There are no N-myristoylation pattern or prenylation patterns.
  Kinase finder at Cuckoo determined kinase binding sites for c17orf98. There are many Serine/Threonine, and Tyrosine kinase phosphorylation sites. Serine and Threonine kinase binding sites are the most prevalent above the statistically significant threshold. There are no SUMOylation sites. C17orf98 gene has six sites on the sequence of possible O-GlcNAc sites. Highly conserved O-GlcNAc amino acid sites are 24, 32, 117, and 142. O-GlcNAc post-translational modification occurs on Ser/Thr residues, specifically on oncogenes, tumor suppressors, and proteins involved in growth factor signaling.
  C17orf98 has a Caspase3/7 motif, where either Caspase 3 or 7 would cleave. This supports the idea that C17orf98 is involved in proliferation, as a proapoptotic caspase would want to destroy any protein driving proliferation. The protein also has a motif where peptidyl-prolyl cis-trans isomerase NIMA interacting 1 (Pin1) binds. Pin1 upregulation is involved in cancer and immune disorders. This supports the claim that C17orf98 is involved in cancer, immune cells, and perhaps cancers of the immune system. Additionally, C17orf98 protein has an IBM site, where inhibitors of apoptosis (IAPs) bind. This again supports the idea of C17orf98 being involved in inhibiting apoptosis, and logically, driving cancer. Furthermore, C17orf98 has motifs where GRB2’s SH2 domain binds. GRB2 is an adapter protein involved in the RAS signaling pathway, a pathway that when deregulated drives uncontrolled proliferation.
caption: SWISS-MODEL 3D structure of c17orf98
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