Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The SCF(FBXO11) complex mediates ubiquitination and degradation of BCL6, thereby playing a role in the germinal center B-cells terminal differentiation toward memory B-cells and plasma cells. The SCF(FBXO11) complex also mediates ubiquitination and degradation of DTL, an important step for the regulation of TGF-beta signaling, cell migration and the timing of the cell-cycle progression and exit. Binds to and neddylates phosphorylated p53/TP53, inhibiting its transcriptional activity. SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53. Protein modification; protein ubiquitination. Component of the SCF(FBXO11) complex consisting of CUL1, RBX1, SKP1 and FBXO11. Interacts with p53/TP53, BCL6 and DTL (when not phosphorylated). Interacts with PRMD1. Isoform 5 is expressed in keratinocytes, fibroblasts and melanocytes. Protein levels increase during G1 and S phases to decline as cells progress through G2 to enter in G1 phase of the next cell cycle. The disease is caused by variants affecting the gene represented in this entry. Defects in FBXO11 may be a cause of diffuse large B-cell lymphoma by allowing the accumulation of BCL6, an oncoprotein that has a critical role in lymphomas. Has been initially named PRMT9 and reported to act as an arginine methyltransferase that can catalyze the formation of omega-N monomethylarginine (MMA) as well as symmetrical and asymmetrical dimethylarginine (sDMA and aDMA), however no further works support these observations (PubMed:16487488). It should not be confused with official PRMT9 (AC Q6P2P2). Intron retention. Truncated N-terminus.