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May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BTE7"}],"value":"Part of a complex that contains DCUN1D5, CUL1 and RBX1; this interaction is bridged by CUL1. Interacts (via the DCUN1 domain) with the unneddylated cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5; these interactions promote the cullin neddylation and the identity of the cullin dictates the affinity of the interaction. Interacts (via DCUN1 domain) with UBE2M (N-terminally acetylated form) and probably with UBE2F (N-terminally acetylated form). May also interact with regulators or subunits of cullin-RING ligases such as RBX1, RNF7, ELOB and DDB1; these interactions are bridged by cullins. Interacts with CAND1; this interaction is bridged by cullins and strongly inhibits the neddylation of cullins. These CAND-cullin-DCNL complexes can only be neddylated in the presence of a substrate adapter"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BTE7"}],"value":"Subcellular localization is independent of the interaction with cullins"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29958295"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BTE7"}],"value":"Cytoplasm, cytoskeleton, spindle","id":"SL-0251"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26792857"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"}],"value":"Highly expressed in testis (PubMed:26792857, PubMed:26906416). Lower levels of expression in skin, thymus, spleen, lymph nodes, lung, brain, heart, skeletal muscles, kidney, liver an ovary (PubMed:26792857, PubMed:26906416)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BTE7"}],"value":"The DCUN1 domain, also known as PONY domain, mediates the interaction with different cullins. 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Phosphorylated in response to IL1B stimulation (By similarity)"}],"commentType":"PTM"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"BC020048","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"DCN1-like protein 5","featureId":"PRO_0000254172"},{"type":"Domain","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"DCUN1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00574"}]},{"type":"Modified residue","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Phosphoserine; by 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