RNA- and DNA-binding proteins are enriched in intrinsic disorder, with many nuclear proteins being IDPs involved in the regulation of transcription and cell signaling, and with many transcription factors being either completely disordered or containing long IDPRs.
Several ion-binding proteins were enriched in our studies (allB, metK, pdxA, araA, leuB, menD, pphA and pykF).
For this, T. brucei ATP-binding proteins were enriched with an ATP-sepharose matrix, and proteins were eluted with one of three different kinase inhibitors (lapatinib, canertinib, and AEE788).
Drebrin, an actin-binding protein, is enriched and clustered in spine heads.
In accordance with this functional role, the cluster's proteins are enriched for translation factor activity and nucleic acid binding.
In addition to known RNA granule, ribosomal, and RNA binding-proteins, the 189 nonribosomal proteins were enriched for several other functional classes.
8 proteins were enriched in the protein translation process.
Second, apart from kinases/phosphatases as previously reported, ion binding proteins are also enriched in sperm, underlying the crucial roles of intracellular ions in post-translational regulation in sperm.
These 196 RNA binding proteins were strongly enriched for protein family domains compiled in the Pfam database that have previously been identified in RNA binding, including the RNA recognition motif, RNA binding domain, zinc finger and K homology domains.
Genes that belong to the category of transport and binding proteins also are enriched in this cluster.
