{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q14999","secondaryAccessions":["B4DYZ0","F5H0L1","Q5T654"],"uniProtkbId":"CUL7_HUMAN","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-10-23","entryVersion":223,"sequenceVersion":2},"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":{"value":"Cullin-7"},"shortNames":[{"value":"CUL-7"}]}},"genes":[{"geneName":{"value":"CUL7"},"synonyms":[{"value":"KIAA0076"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12481031"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12904573"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16547496"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17332328"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18498745"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20139075"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21572988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21737058"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24362026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24793695"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24793696"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35982156"}],"value":"Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:12481031, PubMed:12904573, PubMed:21572988, PubMed:21737058, PubMed:24793695, PubMed:35982156). Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity (PubMed:21572988, PubMed:21737058, PubMed:24793695). It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695). The Cul7-RING(FBXW8) complex alone lacks ubiquitination activity and does not promote polyubiquitination and proteasomal degradation of p53/TP53 (PubMed:16547496, PubMed:17332328, PubMed:35982156). However it mediates recruitment of p53/TP53 for ubiquitination by neddylated CUL1-RBX1 (PubMed:35982156). Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5 (PubMed:24793696). The Cul7-RING(FBXW8) complex also mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1 (PubMed:21572988, PubMed:24362026). 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) (PubMed:18498745). 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 (PubMed:24362026). Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development (PubMed:20139075). 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. Probably plays a role in the degradation of proteins involved in endothelial proliferation and/or differentiation"}],"commentType":"FUNCTION"},{"texts":[{"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12481031"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12904573"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15964813"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16547496"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17298945"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17332328"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21572988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21737058"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24362026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24793695"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24793696"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25752541"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35982156"}],"value":"Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1 (PubMed:21572988, PubMed:21737058, PubMed:24793695). Component of the Cul7-RING(FBXW8) complex consisting of CUL7, RBX1, SKP1 and FBXW8 (PubMed:12481031, PubMed:12904573, PubMed:35982156). Within the Cul7-RING(FBXW8) complex interacts with FBXW8 and RBX1, but not with SKP1 (PubMed:16547496, PubMed:35982156). 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 (PubMed:35982156). 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 (PubMed:16547496, PubMed:17298945, PubMed:17332328, PubMed:35982156). The CUL7-CUL9 heterodimer seems to interact specifically with p53/TP53 (PubMed:17332328, PubMed:24793696). Interacts with FBXW8; interaction is mutually exclusive of binding to CUL9 or p53/TP53 (PubMed:17332328, PubMed:21572988, PubMed:24362026). Interacts with CUL9; leading to inhibited CUL9 activity (PubMed:15964813, PubMed:17332328). Interacts with OBSL1 (PubMed:21572988, PubMed:21737058). Interacts (as part of the 3M complex) with HDAC4 and HDAC5; it is negatively regulated by ANKRA2 (PubMed:25752541)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16140746"}],"value":"(Microbial infection) Interacts with SV40 Large T antigen; this interaction seems to inhibit CUL7"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q14999","intActId":"EBI-308606"},"interactantTwo":{"uniProtKBAccession":"O75147-2","geneName":"OBSL1","intActId":"EBI-15927144"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14999","intActId":"EBI-308606"},"interactantTwo":{"uniProtKBAccession":"P04637","geneName":"TP53","intActId":"EBI-366083"},"numberOfExperiments":19,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24793695"}],"value":"Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. During mitosis, localizes to the mitotic apparatus (PubMed:24793695). CCDC8 is required for centrosomal location (PubMed:24793695)"}]},"subcellularLocations":[{"location":{"value":"Cytoplasm","id":"SL-0086"}},{"location":{"value":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome","id":"SL-0048"}},{"location":{"value":"Cytoplasm, perinuclear region","id":"SL-0198"}},{"location":{"value":"Golgi apparatus","id":"SL-0132"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q14999-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q14999-2"],"sequenceIds":["VSP_046105","VSP_046106"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16142236"}],"value":"Highly expressed in fetal kidney and adult skeletal muscle. Also abundant in fetal brain, as well as in adult pancreas, kidney, placenta and heart. Detected in trophoblasts, lymphoblasts, osteoblasts, chondrocytes and skin fibroblasts"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20139075"}],"value":"Highly expressed in invasive placental villi during first trimester"}],"commentType":"DEVELOPMENTAL STAGE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16547496"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17298945"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17332328"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35982156"}],"value":"The CPH domain is essential for interaction with p53/TP53"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17332328"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35982156"}],"value":"According to a report, may not be neddylated despite the conserved consensus site for neddylation at Lys-1576 (PubMed:17332328). Structural study of the Cul7-RING(FBXW8) reveals that both CUL7 and RBX1 are in orientations that are incompatible with neddylation (PubMed:35982156)"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"3M syndrome 1","diseaseAccession":"DI-00011","acronym":"3M1","description":"An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies.","diseaseCrossReference":{"database":"MIM","id":"273750"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16142236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17675530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23018678"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00330"}],"value":"Belongs to the cullin family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAA07551.2","note":"Extended 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