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.
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.
C17orf98