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Background The SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase is a complex of proteins that helps facilitate the ubiquitination of substrates for targeted proteasomal degradation. FBXW11 is F-box containing protein that has 11 WD-repeats and is a substrate recognition component of the SCF complex. FBXW11 recognizes and binds its substrates, including beta-catenin, at phosphorylated sites or Read More …
Background The SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase is a complex of proteins that helps facilitate the ubiquitination of substrates for targeted proteasomal degradation. FBXW7 (F-box/WD repeat-containing protein 7) is an F-box protein component of the SCF complex and is involved in substrate recognition. The F-box domain tethers FBXW7 to the SCF complex by interacting Read More …
Background WDR5 belongs to the WD-repeat protein family and is an important component of various complexes, including SET1/MLL, NuRD, and NSL complex. It interacts with several binding partners via the “WDR5-interacting” (Win) site (e.g. symmetrically dimethylated histone H3R2, MLL1-4, SET1-2) or “WDR5-binding motif” (WBM) site (e.g. c,l,n-MYC, RBBP5). WDR5 emerged as a prime target Read More …
Background Malignant-Brain-Tumor (MBT) protein L3MBTL1 contains three tandem MBT repeats (3xMBT), which interact with mono- and dimethylated lysines of histone H4, H3 and H1.4 resulting in transcriptional repression. The interaction requires conserved aspartic acid (D355) in the second MBT repeat (PMID:17540172, 18408754, 20870725, 18408754). Assay validation Assay measuring the interaction of L3MBTL1 to histone H3 was Read More …
Background HSP70 heat-shock proteins family, including constitutively expressed HSPA8 variant, facilitate correct folding of client proteins and degradation of unfolded clients. To achieve folding or degradation of client proteins, HSP70 cooperates with co-chaperones, which mostly bind to the highly conserved sequence EEVD in the C-terminal domain of HSP70 via their tetratricopeptide repeat (TPR) domain (PMID: Read More …
Background PRMT7 is a type III protein arginine methyltransferase that monomethylates arginine residues mainly within the RXR motif (Fig.1) (PIMID: 24247247). PRMT7 was shown to play an important role in muscle physiology, stem cell biology, and cellular stress response (PIMID: 32409666, 27225728, 26854227). Fig.1. Mammalian PRMTs. There are 9 members and 3 types of the Read More …
Background NSD3 is a member of the NSD (nuclear receptor SET domain- containing) family of H3K36 methyltransferases. It has two isoforms: long -1437 amino acid and short – 645 amino acids, which are derived from alternative splicing of exon 10. In contrast to long isoform, the short isoform lacks the methyltransferase domain and it contains Read More …
Background NSD2 is a member of the NSD (nuclear receptor SET domain- containing) family of H3K36 methyltransferases which contain a conserved catalytic SET domain and several chromatin-associated domains comprising four PHD fingers, two PWWP domains, and an HMG box. NSD2 is implicated in several diseases including Wolf Hirschhorn syndrome and its overexpression or hyperactivity may Read More …
Background Transcriptional coactivators p300 and CBP catalyze the acetylation of lysine residues of a large variety of histone and non-histone proteins (PMID:28426192). p300 and CBP are considered functional homologous proteins that share around 86% amino acid sequence identity in the HAT domain (PIMID:7870179). The upregulation of p300/CBP has been associated with various cancers, indicating an important role in Read More …
Background RFWD3 (E3 ligase RING finger and WD repeat domain-containing protein 3) and RPA2 (Replication protein A2) were shown to functionally interact and participate in replication checkpoint control. At stalled replication forks, the RPA complex binds single-stranded DNA to prevent nucleolytic digestions and also to initiate replication checkpoint signaling by recruitment checkpoint proteins. RFWD3 is Read More …
