{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9BTE7","secondaryAccessions":["Q3ZTT2"],"uniProtkbId":"DCNL5_HUMAN","entryAudit":{"firstPublicDate":"2006-10-31","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-06-01","entryVersion":162,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"DCN1-like protein 5"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29958295"}],"value":"DCNL5"}]},"alternativeNames":[{"fullName":{"value":"DCUN1 domain-containing protein 5"}},{"fullName":{"value":"Defective in cullin neddylation protein 1-like protein 5"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24192928"}],"value":"Squamous cell carcinoma-related oncogene 5"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:28409"}],"value":"DCUN1D5"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24192928"}],"value":"SCCRO5"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19617556"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23098533"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23201271"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24192928"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"}],"value":"Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs) (PubMed:19617556, PubMed:23201271, PubMed:26906416). May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth (PubMed:23098533, PubMed:24192928)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23201271"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24192928"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"}],"value":"Part of a complex that contains DCUN1D5, CUL1 and RBX1; this interaction is bridged by CUL1 (PubMed:24192928, PubMed:26906416). 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 (PubMed:23201271, PubMed:24192928, PubMed:26906416). Interacts (via DCUN1 domain) with UBE2M (N-terminally acetylated form) and probably with UBE2F (N-terminally acetylated form) (PubMed:23201271, PubMed:24192928). May also interact with regulators or subunits of cullin-RING ligases such as RBX1, RNF7, ELOB and DDB1; these interactions are bridged by cullins (PubMed:26906416). 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 (PubMed:24192928, PubMed:26906416)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9BTE7","intActId":"EBI-3924013"},"interactantTwo":{"uniProtKBAccession":"Q14204","geneName":"DYNC1H1","intActId":"EBI-356015"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9BTE7","intActId":"EBI-3924013"},"interactantTwo":{"uniProtKBAccession":"O60921","geneName":"HUS1","intActId":"EBI-1056174"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9BTE7","intActId":"EBI-3924013"},"interactantTwo":{"uniProtKBAccession":"Q92876","geneName":"KLK6","intActId":"EBI-2432309"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9BTE7","intActId":"EBI-3924013"},"interactantTwo":{"uniProtKBAccession":"Q8TBB1","geneName":"LNX1","intActId":"EBI-739832"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9BTE7","intActId":"EBI-3924013"},"interactantTwo":{"uniProtKBAccession":"Q9NRD5","geneName":"PICK1","intActId":"EBI-79165"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9BTE7","intActId":"EBI-3924013"},"interactantTwo":{"uniProtKBAccession":"Q58EX7","geneName":"PLEKHG4","intActId":"EBI-949255"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"}],"value":"Subcellular localization is independent of the interaction with cullins"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18445686"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23098533"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18445686"}],"value":"Cytoplasm, cytoskeleton, spindle","id":"SL-0251"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"}],"value":"Weakly expressed in testis, skin and immune tissues (thymus, spleen and lymph nodes)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23098533"}],"value":"Expression is decreased in a time-dependent manner after UVC exposure"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23201271"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24192928"}],"value":"The DCUN1 domain, also known as PONY domain, mediates the interaction with different cullins (PubMed:23201271, PubMed:24192928). The DCUN1 domain mediates the interaction with the N-terminally acetylated NEDD8-conjugating E2s enzyme leading to the NEDD8 transfer from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes; the neddylation efficiency correlates with the DCUN1D5-cullin and DCUN1D5-E2 interaction affinities (PubMed:23201271)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9CXV9"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29958295"}],"value":"Phosphorylation at Ser-41 is independent of cullin's interaction. Phosphorylated in response to both TICAM1 and MYD88 dependent Toll-like receptor (TLR) pathway activation (By similarity). Phosphorylated in response to IL1B stimulation (PubMed:29958295)"}],"commentType":"PTM"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAQ76805.1","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_0000254171"},{"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":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"20068231"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"21406692"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29958295"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Mutagenesis","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":8,"modifier":"EXACT"}},"description":"Affects nucleus localization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"}],"alternativeSequence":{"originalSequence":"KKRK","alternativeSequences":["AAAA"]}},{"type":"Mutagenesis","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"Loss of interaction with CUL1, CUL2, CUL3, CUL4A, CUL5, CAND1 and RBX1; when associated with R-219 and A-225. Does not affect localization at nucleus; when associated with R-219 and A-225.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"Loss of interaction with RBX1, CUL1 and CAND1.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24192928"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"Loss of interaction with RBX1, CUL1 and CAND1. Loss of interaction with CUL1, CUL2, CUL3, CUL4A, CUL5, CAND1 and RBX1; when associated with A-195 and A-225. Does not affect localization at nucleus; when associated with A-195 and A-225.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24192928"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Loss of interaction with CUL1, CUL2, CUL3, CUL4A, CUL5, CAND1 and RBX1; when associated with A-195 and R-219. Does not affect localization at nucleus; when associated with A-195 and R-219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Loss of interaction with RBX1, CUL1, CUL2, CUL3 and CAND1. 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