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Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity (By similarity). It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (By similarity). The Cul7-RING(FBXW8) complex alone lacks ubiquitination activity and does not promote polyubiquitination and proteasomal degradation of p53/TP53 (By similarity). However it mediates recruitment of p53/TP53 for ubiquitination by neddylated CUL1-RBX1 (By similarity). Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5 (By similarity). The Cul7-RING(FBXW8) complex also mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1 (By similarity). Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) (By similarity). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation (By similarity). Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development (By similarity). While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may have additional functions (By similarity). Probably plays a role in the degradation of proteins involved in endothelial proliferation and/or differentiation (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21572988"}],"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q14999"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21572988"}],"value":"Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1 (PubMed:21572988). Component of the Cul7-RING(FBXW8) complex consisting of CUL7, RBX1, SKP1 and FBXW8 (PubMed:21572988). Within the Cul7-RING(FBXW8) complex interacts with FBXW8 and RBX1, but not with SKP1 (By similarity). Interacts with CUL1 (via the C-terminal domain); the interaction seems to be mediated by FBXW8; it is likely specific to FBXW8, but not other F-box proteins (By similarity). Interacts (via the CPH domain) with p53/TP53; the interaction preferentially involves tetrameric and dimeric p53/TP53; this interaction recruits p53/TP53 for ubiquitination by neddylated CUL1-RBX1 (By similarity). The CUL7-CUL9 heterodimer seems to interact specifically with p53/TP53 (By similarity). Interacts with FBXW8; interaction is mutually exclusive of binding to CUL9 or p53/TP53 (By similarity). Interacts with CUL9; leading to inhibited CUL9 activity (By similarity). Interacts with OBSL1 (By similarity). Interacts (as part of the 3M complex) with HDAC4 and HDAC5; it is negatively regulated by ANKRA2 (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"During mitosis, localizes to the mitotic apparatus. CCDC8 is required for centrosomal location (By similarity). Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21572988"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome","id":"SL-0048"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21572988"}],"value":"Cytoplasm, perinuclear region","id":"SL-0198"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21572988"}],"value":"Golgi apparatus","id":"SL-0132"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q14999"}],"value":"The CPH domain is essential for interaction with p53/TP53"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00330"}],"value":"Belongs to 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