DDB1 (DNA damage-binding protein 1; p127, UV-DDB1, XAP-1) is a large (1140 aa) WD40 beta-propeller protein built from three seven-bladed beta-propeller domains (BPA, BPB and BPC) that serves as the central adaptor of CUL4-RING E3 ubiquitin ligases (CRL4). Its BPB propeller docks onto the N-terminus of the cullin scaffold CUL4A or CUL4B (assembled with the RING protein RBX1/ROC1), while a cleft between the BPA and BPC propellers, together with a helix-loop-helix (H-box) surface, captures a large family of interchangeable substrate-receptor subunits known as DCAFs (DDB1- and CUL4-associated factors), most of which engage DDB1 through a conserved WDxR motif on their own WD40 propeller. DDB1 itself is not catalytic and is not the direct nucleic-acid-binding subunit; by interchanging DCAF receptors it confers substrate specificity on numerous distinct DCX (DDB1-CUL4-X-box) ligase complexes that ubiquitinate and target their substrates for proteasomal degradation, and cullin-RING ligases as a class account for roughly a fifth of regulated proteasomal protein turnover. Systematic interactome studies (BioID/AP-MS/pulse-SILAC) indicate that only a minority of candidate WD40 proteins are bona fide DDB1/CUL4 receptors under any given condition, so DDB1's functional output is strongly context- and stimulus-dependent and is largely encoded by which DCAF is conditionally recruited. Structurally, DDB1's BPB propeller binds the CUL4 N-terminus while the BPA-BPC double-propeller cleft (with an H-box helical surface) captures receptors and viral hijackers; receptors that are intrinsically disordered (e.g. AMBRA1) become stabilized upon DDB1 engagement. With its dedicated receptor DDB2, DDB1 forms the UV-DDB complex that recognizes UV-induced photolesions (cyclobutane pyrimidine dimers and 6-4 photoproducts), apurinic sites and mismatches in chromatin and initiates global-genome nucleotide excision repair, in part by ubiquitinating histones (H2A, H3, H4) and XPC at damage sites; in a noncanonical capacity UV-DDB also stimulates base-excision-repair enzymes (e.g. OGG1, MUTYH, APE1 and the glycosylase SMUG1), promoting turnover of oxidative DNA lesions. With the DCAF ERCC8/CSA, DDB1-CUL4 contributes to transcription-coupled repair by ubiquitinating stalled RNA polymerase II and CSB/ERCC6. Other DDB1-CUL4 complexes regulate DNA replication licensing (CDT1, p21 via DTL/CDT2), cell-cycle progression through the DCAF AMBRA1 (which directs ubiquitination of cyclin D/cyclin D1), the circadian clock (CRY1), histone methylation, and many additional substrates. DDB1 is predominantly cytoplasmic at steady state and translocates to the nucleus after UV irradiation, accumulating at sites of DNA damage; the two cullin scaffolds it uses show partitioning tendencies (CUL4B largely nuclear, CUL4A more cytoplasmic) so that DDB1-containing CRL4 assemblies can act in distinct compartments depending on scaffold usage. It is a frequent target of viral hijacking (e.g. paramyxovirus V, HBV HBx, HIV Vpr/Vpx, HCMV proteins), which redirect CRL4 toward host antiviral or restriction factors; during influenza A virus infection the CRL4 interactome is rewired and DDB1 (with DCAF11/DCAF12L1) participates in non-degradative polyubiquitination of the viral polymerase subunit PB2. DDB1 is also the platform exploited by thalidomide/lenalidomide molecular-glue degraders acting through the DCAF cereblon (CRBN) and, more broadly, is an actionable induced-proximity node for targeted protein degradation, with surface residues such as Arg928 (a validated molecular-glue hotspot, e.g. in CDK12-cyclin K degrader ternary complexes) and Cys173 (engaged by covalent DDB1 recruiters) used to direct CRL4-dependent degradation of clinically relevant proteins including BRD4 and the androgen receptor. Monoallelic de novo DDB1 missense variants cause a recessive-DNA-repair-related neurodevelopmental syndrome (WHIKERS).
Definition: Any process, here mediated by the UV-DDB (DDB1-DDB2) complex, that increases the catalytic activity or turnover of base-excision-repair DNA glycosylases/AP endonucleases (e.g. OGG1, MUTYH, APE1, SMUG1) on oxidative or other base lesions. Current GO has terms for base-excision repair and for damaged-DNA binding, but no specific term capturing a complex acting in trans to stimulate BER enzyme activity, which is the reported noncanonical UV-DDB role.
Definition: Assembly by a DDB1-CUL4 (CRL4) E3 ligase complex of a polyubiquitin signal on a substrate that does not target it for proteasomal degradation but instead modulates its activity, localization or interactions (e.g. the reported non-degradative polyubiquitination of the influenza A virus polymerase subunit PB2). Distinguishes the regulatory, non-degradative ubiquitin output of CRL4 from the canonical proteasome-targeting branch.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006281 DNA repair | IBA GO_REF:0000033 | ACCEPT | Summary: DDB1 functions in DNA repair via the UV-DDB complex (parent of nucleotide excision repair). Reason: Correct core process; UV-DDB initiates NER. Redundant with the more specific NER terms. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively |
| GO:0035861 site of double-strand break | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: IBA 'site of double-strand break' localization; DDB1's documented genome-stability role is via UV-photolesion (NER) recognition, not DSB sites. Reason: Phylogenetically inferred; DDB1's direct DNA-damage activity is global-genome NER through UV-DDB, so DSB-site localization over-reaches. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: DDB1, as the CRL4 adaptor, drives proteasome-mediated ubiquitin-dependent degradation of DCAF-recruited substrates. Reason: Core biological process; numerous DCX(DDB1-CUL4-X) complexes ubiquitinate substrates for proteasomal degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0003676 nucleic acid binding | IEA GO_REF:0000002 | REMOVE | Summary: Generic nucleic acid binding (InterPro IEA); DDB1 itself is not a sequence/nucleic-acid-binding protein, DNA recognition is via the DDB2 subunit of UV-DDB. Reason: DDB1 is the adaptor/scaffold subunit of UV-DDB and the DCX(DDB1-CUL4) ligases; it does not itself bind nucleic acid. Direct lesion/DNA contact in UV-DDB is made by the DDB2 subunit. This InterPro2GO electronic mapping (GO_REF:0000002) is a false-positive attribution of a DNA-binding function to the wrong subunit and should be removed. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: Nuclear localization, consistent with DDB1's UV-DDB/CRL4 functions on chromatin; DDB1 accumulates in nuclei after UV. Reason: Well-supported localization; DDB1 translocates to and acts in the nucleus at DNA-damage sites. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Cytoplasmic localization; DDB1 is primarily cytoplasmic at steady state and translocates to the nucleus after UV. Reason: Directly supported; DDB1 is primarily cytoplasmic and relocates to nuclei following UV irradiation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Primarily cytoplasmic (PubMed:10777491, PubMed:11673459) |
| GO:0034644 cellular response to UV | IEA GO_REF:0000117 | ACCEPT | Summary: DDB1/UV-DDB mediates the cellular response to UV-induced DNA damage. Reason: Core UV-response process; UV-DDB recognizes UV photolesions and recruits NER machinery. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0005515 protein binding | IPI PMID:10777491 Nuclear transport of human DDB protein induced by ultraviole... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:16227264 Simian virus 5 V protein acts as an adaptor, linking DDB1 to... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:16473935 The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderm... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:17041588 CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repe... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:17314515 HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:17360488 HIV-1 Vpr function is mediated by interaction with the damag... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:19109893 Structural basis of UV DNA-damage recognition by the DDB1-DD... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:19264781 The human immunodeficiency virus type 2 Vpx protein usurps t... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:19651607 Aryl hydrocarbon receptor suppresses intestinal carcinogenes... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:19966799 A promiscuous alpha-helical motif anchors viral hijackers an... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:20855601 INO80 chromatin remodeling complex promotes the removal of U... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:21113133 RNAi-based screening identifies the Mms22L-Nfkbil2 complex a... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:22039351 Regulation of nucleotide excision repair by UV-DDB: prioriti... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:22157821 VprBP binds full-length RAG1 and is required for B-cell deve... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:22810585 Viral immune modulators perturb the human molecular network ... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:22822215 Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB) ... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:23238014 CRL4B catalyzes H2AK119 monoubiquitination and coordinates w... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:23314863 SCFFbxw5 mediates transient degradation of actin remodeller ... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:24292623 The myeloma drug lenalidomide promotes the cereblon-dependen... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:24412650 Premature activation of the SLX4 complex by Vpr promotes G2/... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:24500646 Ubiquitin ligase defect by DCAF8 mutation causes HMSN2 with ... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:26131937 Lenalidomide induces ubiquitination and degradation of CK1Ξ± ... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:26909574 Structural basis of lenalidomide-induced CK1Ξ± degradation by... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:29691401 Methylated DNMT1 and E2F1 are targeted for proteolysis by L3... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:30564455 Structural insights into DDA1 function as a core component o... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:31391242 DCAF8, a novel MuRF1 interaction partner, promotes muscle at... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:9418871 DDB, a putative DNA repair protein, can function as a transc... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0006511 ubiquitin-dependent protein catabolic process | IEA GO_REF:0000120 | ACCEPT | Summary: DDB1 enables ubiquitin-dependent protein catabolism as the CRL4 adaptor. Reason: Core process (parent of proteasome-mediated catabolism); CRL4/DCX complexes target substrates for degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000120 | ACCEPT | Summary: DDB1 is required for protein ubiquitination by CRL4/DCX E3 ligase complexes. Reason: Core process; DDB1 adaptor function is essential for CRL4-mediated substrate ubiquitination. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0042752 regulation of circadian rhythm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of circadian rhythm) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 |
| GO:0045722 positive regulation of gluconeogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Context-specific downstream process (positive regulation of gluconeogenesis) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1- mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1- mediated gluconeogenesis in the liver |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IEA GO_REF:0000120 | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0000109 nucleotide-excision repair complex | IPI PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: DDB1 is part of the UV-DDB (DDB1-DDB2) nucleotide excision repair recognition complex. Reason: Core component of the UV-DDB complex that recognizes UV-induced DNA damage and recruits NER factors. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0005634 nucleus | IDA PMID:14751237 Human DDB2 splicing variants are dominant negative inhibitor... | ACCEPT | Summary: Nuclear localization, consistent with DDB1's UV-DDB/CRL4 functions on chromatin; DDB1 accumulates in nuclei after UV. Reason: Well-supported localization; DDB1 translocates to and acts in the nucleus at DNA-damage sites. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005634 nucleus | NAS PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: Nuclear localization, consistent with DDB1's UV-DDB/CRL4 functions on chromatin; DDB1 accumulates in nuclei after UV. Reason: Well-supported localization; DDB1 translocates to and acts in the nucleus at DNA-damage sites. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0006289 nucleotide-excision repair | NAS PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: DDB1, as part of UV-DDB, functions in nucleotide excision repair of UV lesions. Reason: Core biological process; UV-DDB recognizes UV photolesions and initiates global-genome NER. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0006974 DNA damage response | ISS GO_REF:0000114 | ACCEPT | Summary: DDB1 acts in the DNA damage response through UV-DDB lesion recognition and CRL4-mediated damage signaling. Reason: Core process; UV-DDB recognizes damage and CRL4(DDB2/DTL) couples damage to ubiquitination. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0006974 DNA damage response | EXP PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: DDB1 acts in the DNA damage response through UV-DDB lesion recognition and CRL4-mediated damage signaling. Reason: Core process; UV-DDB recognizes damage and CRL4(DDB2/DTL) couples damage to ubiquitination. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0007283 spermatogenesis | NAS PMID:29907856 Deletion of DDB1- and CUL4- associated factor-17 (Dcaf17) ge... | KEEP AS NON CORE | Summary: Context-specific downstream process (spermatogenesis) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0008283 cell population proliferation | NAS PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | KEEP AS NON CORE | Summary: Context-specific downstream process (cell population proliferation) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0010506 regulation of autophagy | NAS PMID:31267705 Regulation of MAGE-A3/6 by the CRL4-DCAF12 ubiquitin ligase ... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of autophagy) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0030174 regulation of DNA-templated DNA replication initiation | NAS PMID:16861906 L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of DNA replication initiation) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0031297 replication fork processing | NAS PMID:30018425 The replication initiation determinant protein (RepID) modul... | KEEP AS NON CORE | Summary: Context-specific downstream process (replication fork processing) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0031297 replication fork processing | NAS PMID:33503431 DCAF14 promotes stalled fork stability to maintain genome in... | KEEP AS NON CORE | Summary: Context-specific downstream process (replication fork processing) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:16861906 L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IPI PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | EXP PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:25108355 Structure of the human Cereblon-DDB1-lenalidomide complex re... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:27113764 The antiobesity factor WDTC1 suppresses adipogenesis via the... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:28212551 NRIP/DCAF6 stabilizes the androgen receptor protein by displ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:29691401 Methylated DNMT1 and E2F1 are targeted for proteolysis by L3... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IPI PMID:31693891 Aryl Sulfonamides Degrade RBM39 and RBM23 by Recruitment to ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IPI PMID:34595758 The CRL4(DCAF1) cullin-RING ubiquitin ligase is activated fo... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:16861906 L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:25108355 Structure of the human Cereblon-DDB1-lenalidomide complex re... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IPI PMID:27113764 The antiobesity factor WDTC1 suppresses adipogenesis via the... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:29691401 Methylated DNMT1 and E2F1 are targeted for proteolysis by L3... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:31452512 Systematic identification of cancer cell vulnerabilities to ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:33898171 OTUD1 Activates Caspase-Independent and Caspase-Dependent Ap... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:34595758 The CRL4(DCAF1) cullin-RING ubiquitin ligase is activated fo... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0032814 regulation of natural killer cell activation | NAS PMID:31452512 Systematic identification of cancer cell vulnerabilities to ... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of natural killer cell activation) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0034644 cellular response to UV | ISS GO_REF:0000114 | ACCEPT | Summary: DDB1/UV-DDB mediates the cellular response to UV-induced DNA damage. Reason: Core UV-response process; UV-DDB recognizes UV photolesions and recruits NER machinery. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0034644 cellular response to UV | EXP PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: DDB1/UV-DDB mediates the cellular response to UV-induced DNA damage. Reason: Core UV-response process; UV-DDB recognizes UV photolesions and recruits NER machinery. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0040029 epigenetic regulation of gene expression | NAS PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | KEEP AS NON CORE | Summary: Context-specific downstream process (epigenetic regulation of gene expression) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0040029 epigenetic regulation of gene expression | NAS PMID:34429321 Systematic Profiling of DNMT3A Variants Reveals Protein Inst... | KEEP AS NON CORE | Summary: Context-specific downstream process (epigenetic regulation of gene expression) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0040029 epigenetic regulation of gene expression | NAS PMID:34720086 Cul4A-DDB1-mediated monoubiquitination of phosphoglycerate d... | KEEP AS NON CORE | Summary: Context-specific downstream process (epigenetic regulation of gene expression) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0042127 regulation of cell population proliferation | NAS PMID:33869224 Hippo-Independent Regulation of Yki/Yap/Taz: A Non-canonical... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of cell population proliferation) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0042981 regulation of apoptotic process | NAS PMID:33898171 OTUD1 Activates Caspase-Independent and Caspase-Dependent Ap... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of apoptotic process) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0045995 regulation of embryonic development | NAS PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of embryonic development) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0060964 regulation of miRNA-mediated gene silencing | NAS PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase dur... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of miRNA-mediated gene silencing) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0070914 UV-damage excision repair | IDA PMID:14751237 Human DDB2 splicing variants are dominant negative inhibitor... | ACCEPT | Summary: DDB1/UV-DDB participates in UV-damage excision repair (global-genome NER of UV photoproducts). Reason: Core process directly supported; UV-DDB recognizes CPD/6-4PP lesions to initiate repair. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches |
| GO:0080135 regulation of cellular response to stress | NAS PMID:31586112 TFEB activates Nrf2 by repressing its E3 ubiquitin ligase DC... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of cellular response to stress) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:1901987 regulation of cell cycle phase transition | NAS PMID:16861906 L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of cell cycle phase transition) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:1901987 regulation of cell cycle phase transition | NAS PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates ... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of cell cycle phase transition) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:1902412 regulation of mitotic cytokinesis | NAS PMID:34758320 Phosphorylation at Ser68 facilitates DCAF11-mediated ubiquit... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of mitotic cytokinesis) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:1904178 negative regulation of adipose tissue development | NAS PMID:27113764 The antiobesity factor WDTC1 suppresses adipogenesis via the... | KEEP AS NON CORE | Summary: Context-specific downstream process (negative regulation of adipose tissue development) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:2000036 regulation of stem cell population maintenance | NAS PMID:29691401 Methylated DNMT1 and E2F1 are targeted for proteolysis by L3... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of stem cell population maintenance) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:2000036 regulation of stem cell population maintenance | NAS PMID:30442713 Proteolysis of methylated SOX2 protein is regulated by L3MBT... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of stem cell population maintenance) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005634 nucleus | EXP PMID:10777491 Nuclear transport of human DDB protein induced by ultraviole... | ACCEPT | Summary: Nuclear localization, consistent with DDB1's UV-DDB/CRL4 functions on chromatin; DDB1 accumulates in nuclei after UV. Reason: Well-supported localization; DDB1 translocates to and acts in the nucleus at DNA-damage sites. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005634 nucleus | EXP PMID:11673459 UV-damaged DNA-binding proteins are targets of CUL-4A-mediat... | ACCEPT | Summary: Nuclear localization, consistent with DDB1's UV-DDB/CRL4 functions on chromatin; DDB1 accumulates in nuclei after UV. Reason: Well-supported localization; DDB1 translocates to and acts in the nucleus at DNA-damage sites. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005737 cytoplasm | EXP PMID:10777491 Nuclear transport of human DDB protein induced by ultraviole... | ACCEPT | Summary: Cytoplasmic localization; DDB1 is primarily cytoplasmic at steady state and translocates to the nucleus after UV. Reason: Directly supported; DDB1 is primarily cytoplasmic and relocates to nuclei following UV irradiation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Primarily cytoplasmic (PubMed:10777491, PubMed:11673459) |
| GO:0005737 cytoplasm | EXP PMID:11673459 UV-damaged DNA-binding proteins are targets of CUL-4A-mediat... | ACCEPT | Summary: Cytoplasmic localization; DDB1 is primarily cytoplasmic at steady state and translocates to the nucleus after UV. Reason: Directly supported; DDB1 is primarily cytoplasmic and relocates to nuclei following UV irradiation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Primarily cytoplasmic (PubMed:10777491, PubMed:11673459) |
| GO:0005634 nucleus | IDA PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | ACCEPT | Summary: DDB1 is active in the nucleus, where CRL4/UV-DDB complexes act on chromatin substrates and DNA damage. Reason: Nuclear activity is well documented; DDB1 accumulates at DNA-damage sites and acts on nuclear substrates. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0032991 protein-containing complex | IDA PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | KEEP AS NON CORE | Summary: Generic protein-containing complex membership; subsumed by the specific CRL4/UV-DDB complex annotations. Reason: Correct but uninformative; the specific CUL4-RING/UV-DDB complex terms better capture DDB1's complex roles. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | ACCEPT | Summary: DDB1, as the CRL4 adaptor, drives proteasome-mediated ubiquitin-dependent degradation of DCAF-recruited substrates. Reason: Core biological process; numerous DCX(DDB1-CUL4-X) complexes ubiquitinate substrates for proteasomal degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | ACCEPT | Summary: DDB1 provides the scaffold/adaptor activity that links CUL4 to DCAF substrate receptors in CRL4 complexes. Reason: Captures DDB1's central molecular role as the CRL4 adaptor scaffold; consistent with structural studies and with deep-research synthesis that DDB1 is a non-catalytic adaptor whose receptor (DCAF) identity sets substrate specificity. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 file:human/DDB1/DDB1-deep-research-falcon.md DDB1βs primary biochemical role is not catalytic; rather, it is an E3-ligase adaptor/scaffold that couples the CUL4A/B cullin scaffold to substrate receptors (commonly termed DCAFs, for βDDB1- and CUL4-associated factorsβ), enabling substrate selection for ubiquitination by CRL4 complexes |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IDA PMID:32355176 The cooperative action of CSB, CSA, and UVSSA target TFIIH t... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IDA PMID:34526721 Structural basis of human transcription-DNA repair coupling. | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0005515 protein binding | IPI PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005634 nucleus | IDA PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | ACCEPT | Summary: DDB1 is active in the nucleus, where CRL4/UV-DDB complexes act on chromatin substrates and DNA damage. Reason: Nuclear activity is well documented; DDB1 accumulates at DNA-damage sites and acts on nuclear substrates. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005730 nucleolus | IDA PMID:11673459 UV-damaged DNA-binding proteins are targets of CUL-4A-mediat... | KEEP AS NON CORE | Summary: Nucleolar localization reported (IDA); a secondary compartment relative to DDB1's main nuclear/cytoplasmic pools. Reason: Plausible secondary localization (e.g. SIRT7/nucleolar regulation context); not the core site of DDB1 action. |
| GO:0007056 spindle assembly involved in female meiosis | IDA PMID:31492966 The CRL4-DCAF13 ubiquitin E3 ligase supports oocyte meiotic ... | KEEP AS NON CORE | Summary: Context-specific downstream process (spindle assembly involved in female meiosis) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | ACCEPT | Summary: DDB1, as the CRL4 adaptor, drives proteasome-mediated ubiquitin-dependent degradation of DCAF-recruited substrates. Reason: Core biological process; numerous DCX(DDB1-CUL4-X) complexes ubiquitinate substrates for proteasomal degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:31492966 The CRL4-DCAF13 ubiquitin E3 ligase supports oocyte meiotic ... | ACCEPT | Summary: DDB1, as the CRL4 adaptor, drives proteasome-mediated ubiquitin-dependent degradation of DCAF-recruited substrates. Reason: Core biological process; numerous DCX(DDB1-CUL4-X) complexes ubiquitinate substrates for proteasomal degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0044725 epigenetic programming in the zygotic pronuclei | IDA PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | KEEP AS NON CORE | Summary: Context-specific downstream process (epigenetic programming in zygotic pronuclei) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IDA PMID:31492966 The CRL4-DCAF13 ubiquitin E3 ligase supports oocyte meiotic ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | ACCEPT | Summary: DDB1 provides the scaffold/adaptor activity that links CUL4 to DCAF substrate receptors in CRL4 complexes. Reason: Captures DDB1's central molecular role as the CRL4 adaptor scaffold; consistent with structural studies. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:31492966 The CRL4-DCAF13 ubiquitin E3 ligase supports oocyte meiotic ... | ACCEPT | Summary: DDB1 provides the scaffold/adaptor activity that links CUL4 to DCAF substrate receptors in CRL4 complexes. Reason: Captures DDB1's central molecular role as the CRL4 adaptor scaffold; consistent with structural studies. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 |
| GO:0045732 positive regulation of protein catabolic process | IDA PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A u... | ACCEPT | Summary: DDB1 positively regulates catabolism of CRL4 substrates by assembling functional ligase complexes. Reason: Core regulatory aspect of DDB1's adaptor role in promoting substrate degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0097602 cullin family protein binding | IDA PMID:10585395 Cullin 4A associates with the UV-damaged DNA-binding protein... | ACCEPT | Summary: DDB1 directly binds the cullin scaffold (CUL4A/CUL4B), the basis of its adaptor function. Reason: Cullin binding is a specific, informative molecular interaction underlying CRL4 assembly. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0005634 nucleus | IDA PMID:10585395 Cullin 4A associates with the UV-damaged DNA-binding protein... | ACCEPT | Summary: DDB1 is active in the nucleus, where CRL4/UV-DDB complexes act on chromatin substrates and DNA damage. Reason: Nuclear activity is well documented; DDB1 accumulates at DNA-damage sites and acts on nuclear substrates. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0003684 damaged DNA binding | IDA PMID:22334663 Monoubiquitinated histone H2A destabilizes photolesion-conta... | KEEP AS NON CORE | Summary: Damaged-DNA binding is contributed by the UV-DDB complex (DDB2 is the direct DNA-contacting subunit); DDB1 contributes within the complex. Reason: DDB1 contributes to UV-damaged DNA recognition as part of UV-DDB, but DDB2 is the primary lesion-binding subunit; retained as a contributory, non-core function. The contributes_to qualifier is appropriate here, since deep-research synthesis confirms DDB2 directly binds the lesion while DDB1 is the partner scaffold. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches file:human/DDB1/DDB1-deep-research-falcon.md within this heterodimer, DDB2 is the principal DNA-damage-binding subunit, whereas DDB1 acts as the partner subunit that supports downstream steps, including coupling to ubiquitination machinery |
| GO:0005515 protein binding | IPI PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A u... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IDA PMID:31686031 Structural complementarity facilitates E7820-mediated degrad... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0016567 protein ubiquitination | IDA PMID:28886238 SIRT7 deacetylates DDB1 and suppresses the activity of the C... | ACCEPT | Summary: DDB1 is required for protein ubiquitination by CRL4/DCX E3 ligase complexes. Reason: Core process; DDB1 adaptor function is essential for CRL4-mediated substrate ubiquitination. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IDA PMID:28886238 SIRT7 deacetylates DDB1 and suppresses the activity of the C... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0006511 ubiquitin-dependent protein catabolic process | IMP PMID:26431207 CUL4-DDB1-CDT2 E3 Ligase Regulates the Molecular Clock Activ... | ACCEPT | Summary: DDB1 enables ubiquitin-dependent protein catabolism as the CRL4 adaptor. Reason: Core process (parent of proteasome-mediated catabolism); CRL4/DCX complexes target substrates for degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0016567 protein ubiquitination | IDA PMID:26431207 CUL4-DDB1-CDT2 E3 Ligase Regulates the Molecular Clock Activ... | ACCEPT | Summary: DDB1 is required for protein ubiquitination by CRL4/DCX E3 ligase complexes. Reason: Core process; DDB1 adaptor function is essential for CRL4-mediated substrate ubiquitination. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0045722 positive regulation of gluconeogenesis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Context-specific downstream process (positive regulation of gluconeogenesis) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1- mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1- mediated gluconeogenesis in the liver |
| GO:0005515 protein binding | IPI PMID:28437394 Selective degradation of splicing factor CAPERΞ± by anticance... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0006974 DNA damage response | IMP PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | ACCEPT | Summary: DDB1 acts in the DNA damage response through UV-DDB lesion recognition and CRL4-mediated damage signaling. Reason: Core process; UV-DDB recognizes damage and CRL4(DDB2/DTL) couples damage to ubiquitination. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0016567 protein ubiquitination | IMP PMID:28437394 Selective degradation of splicing factor CAPERΞ± by anticance... | ACCEPT | Summary: DDB1 is required for protein ubiquitination by CRL4/DCX E3 ligase complexes. Reason: Core process; DDB1 adaptor function is essential for CRL4-mediated substrate ubiquitination. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0032991 protein-containing complex | IMP PMID:28437394 Selective degradation of splicing factor CAPERΞ± by anticance... | KEEP AS NON CORE | Summary: Generic protein-containing complex membership; subsumed by the specific CRL4/UV-DDB complex annotations. Reason: Correct but uninformative; the specific CUL4-RING/UV-DDB complex terms better capture DDB1's complex roles. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0045732 positive regulation of protein catabolic process | IMP PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | ACCEPT | Summary: DDB1 positively regulates catabolism of CRL4 substrates by assembling functional ligase complexes. Reason: Core regulatory aspect of DDB1's adaptor role in promoting substrate degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0005515 protein binding | IPI PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0071987 WD40-repeat domain binding | IPI PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | ACCEPT | Summary: DDB1 binds the WD40-repeat domains of DCAF substrate receptors via its beta-propeller surface. Reason: WD40-repeat binding is the specific mechanism by which DDB1 recruits DCAF receptors; informative MF. Supporting Evidence: PMID:16949367 the interaction of WD40-containing DCAFs with Ddb1 requires a conserved "WDXR" motif. |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IMP PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0030674 protein-macromolecule adaptor activity | IPI PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A u... | ACCEPT | Summary: DDB1 acts as the molecular adaptor bridging CUL4 and substrate-receptor (DCAF) modules. Reason: Adaptor activity is the defining DDB1 molecular function; better than bare protein binding. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A u... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IMP PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A u... | ACCEPT | Summary: DDB1, as the CRL4 adaptor, drives proteasome-mediated ubiquitin-dependent degradation of DCAF-recruited substrates. Reason: Core biological process; numerous DCX(DDB1-CUL4-X) complexes ubiquitinate substrates for proteasomal degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0097602 cullin family protein binding | IPI PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A u... | ACCEPT | Summary: DDB1 directly binds the cullin scaffold (CUL4A/CUL4B), the basis of its adaptor function. Reason: Cullin binding is a specific, informative molecular interaction underlying CRL4 assembly. Supporting Evidence: PMID:14739464 human DET1 (hDET1) promotes ubiquitination and degradation of the proto-oncogenic transcription factor c-Jun by assembling a multisubunit ubiquitin ligase containing DNA Damage Binding Protein-1 (DDB1), cullin 4A (CUL4A), Regulator of Cullins-1 (ROC1), and constitutively photomorphogenic-1. |
| GO:0010498 proteasomal protein catabolic process | IMP PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | ACCEPT | Summary: DDB1/CUL4B complex activity drives proteasomal catabolism of substrates (e.g. RGS2). Reason: Core process supported by IMP; DDB1-containing CRL4 complexes promote substrate degradation. Supporting Evidence: PMID:25970626 we identified a novel E3 ligase complex containing cullin 4B (CUL4B), DNA damage binding protein 1 (DDB1) and F-box protein 44 (FBXO44) that mediates RGS2 protein degradation. |
| GO:0044877 protein-containing complex binding | IPI PMID:11564863 Human STAGA complex is a chromatin-acetylating transcription... | KEEP AS NON CORE | Summary: Binds the STAGA/protein complex; more informative than bare protein binding but ancillary. Reason: Records association with a multiprotein complex; subsidiary to the core adaptor/complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0000781 chromosome, telomeric region | HDA PMID:19135898 Purification of proteins associated with specific genomic Lo... | KEEP AS NON CORE | Summary: Telomeric chromatin localization from high-throughput locus-proteomics (HDA); peripheral to core function. Reason: High-throughput chromatin-association data; a context-specific localization, not a core DDB1 compartment. |
| GO:0005737 cytoplasm | IDA PMID:23137809 DDB1 is a cellular substrate of NS3/4A protease and required... | ACCEPT | Summary: Cytoplasmic localization; DDB1 is primarily cytoplasmic at steady state and translocates to the nucleus after UV. Reason: Directly supported; DDB1 is primarily cytoplasmic and relocates to nuclei following UV irradiation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Primarily cytoplasmic (PubMed:10777491, PubMed:11673459) |
| GO:0019076 viral release from host cell | IMP PMID:23137809 DDB1 is a cellular substrate of NS3/4A protease and required... | KEEP AS NON CORE | Summary: Viral-hijacking phenotype: pathogens redirect the DDB1-CUL4 ligase; ancillary to DDB1's endogenous function. Reason: Reflects viral usurpation of the CRL4 adaptor (e.g. HCV NS3/4A context); a host-pathogen interaction outcome, not a core endogenous role. |
| GO:0045070 positive regulation of viral genome replication | IMP PMID:23137809 DDB1 is a cellular substrate of NS3/4A protease and required... | KEEP AS NON CORE | Summary: Viral-hijacking phenotype: pathogens redirect the DDB1-CUL4 ligase; ancillary to DDB1's endogenous function. Reason: Reflects viral usurpation of the CRL4 adaptor (e.g. HCV NS3/4A context); a host-pathogen interaction outcome, not a core endogenous role. |
| GO:0046726 positive regulation by virus of viral protein levels in host cell | IMP PMID:23137809 DDB1 is a cellular substrate of NS3/4A protease and required... | KEEP AS NON CORE | Summary: Viral-hijacking phenotype: pathogens redirect the DDB1-CUL4 ligase; ancillary to DDB1's endogenous function. Reason: Reflects viral usurpation of the CRL4 adaptor (e.g. HCV NS3/4A context); a host-pathogen interaction outcome, not a core endogenous role. |
| GO:0051702 biological process involved in interaction with symbiont | IDA PMID:23137809 DDB1 is a cellular substrate of NS3/4A protease and required... | KEEP AS NON CORE | Summary: Viral-hijacking phenotype: pathogens redirect the DDB1-CUL4 ligase; ancillary to DDB1's endogenous function. Reason: Reflects viral usurpation of the CRL4 adaptor (e.g. HCV NS3/4A context); a host-pathogen interaction outcome, not a core endogenous role. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IDA PMID:21628527 Selective ubiquitylation of p21 and Cdt1 by UBCH8 and UBE2G ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IDA PMID:22334663 Monoubiquitinated histone H2A destabilizes photolesion-conta... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0070914 UV-damage excision repair | IDA PMID:22334663 Monoubiquitinated histone H2A destabilizes photolesion-conta... | ACCEPT | Summary: DDB1/UV-DDB participates in UV-damage excision repair (global-genome NER of UV photoproducts). Reason: Core process directly supported; UV-DDB recognizes CPD/6-4PP lesions to initiate repair. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches |
| GO:0005576 extracellular region | HDA PMID:22664934 Comparison of tear protein levels in breast cancer patients ... | MARK AS OVER ANNOTATED | Summary: Extracellular/exosome localization from large-scale proteomics; DDB1 is a nuclear/cytoplasmic CRL4 adaptor. Reason: High-throughput body-fluid/exosome proteomics detections do not reflect DDB1's functional nuclear/cytoplasmic localization. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Primarily cytoplasmic (PubMed:10777491, PubMed:11673459) |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | MARK AS OVER ANNOTATED | Summary: Extracellular/exosome localization from large-scale proteomics; DDB1 is a nuclear/cytoplasmic CRL4 adaptor. Reason: High-throughput body-fluid/exosome proteomics detections do not reflect DDB1's functional nuclear/cytoplasmic localization. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Primarily cytoplasmic (PubMed:10777491, PubMed:11673459) |
| GO:1901990 regulation of mitotic cell cycle phase transition | IMP PMID:17088560 DNA nucleotide excision repair-dependent signaling to checkp... | KEEP AS NON CORE | Summary: Context-specific downstream process (regulation of mitotic cell cycle phase transition) mediated by a particular DCAF-defined CRL4 complex; ancillary to DDB1's core adaptor/NER roles. Reason: DDB1 contributes via substrate-specific CRL4 complexes, but this is a pleiotropic downstream outcome rather than DDB1's core molecular function. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5652005 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5652009 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5689317 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5689861 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690213 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690988 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690990 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690991 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690996 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5691000 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5691006 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5696655 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5696664 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5696670 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6781833 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6781867 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782004 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782069 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782131 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782138 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782141 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782204 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782208 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782211 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782224 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782227 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782234 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782943 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6790454 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6790487 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8952638 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8952639 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8955245 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8955285 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8956045 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9684118 | KEEP AS NON CORE | Summary: Nucleoplasm localization (Reactome/IDA), a sub-compartment consistent with nuclear CRL4/NER activity. Reason: Correct nuclear sub-localization; subsumed by the nucleus annotations and Reactome NER/CRL4 pathway context. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IDA PMID:18381890 WD40 protein FBW5 promotes ubiquitination of tumor suppresso... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0005515 protein binding | IPI PMID:17932509 Proteomic and functional analysis of Argonaute-containing mR... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:12732143 The ubiquitin ligase activity in the DDB2 and CSA complexes ... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IMP PMID:20223979 Identification of a primary target of thalidomide teratogeni... | ACCEPT | Summary: DDB1, as the CRL4 adaptor, drives proteasome-mediated ubiquitin-dependent degradation of DCAF-recruited substrates. Reason: Core biological process; numerous DCX(DDB1-CUL4-X) complexes ubiquitinate substrates for proteasomal degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:18794347 PCNA-dependent regulation of p21 ubiquitylation and degradat... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:20129063 CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to pro... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:20223979 Identification of a primary target of thalidomide teratogeni... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IDA PMID:18794347 PCNA-dependent regulation of p21 ubiquitylation and degradat... | ACCEPT | Summary: DDB1 is a core (adaptor) subunit of CUL4A/CUL4B-RING E3 ubiquitin ligase (CRL4/DCX) complexes; correct core localization/complex membership. Reason: DDB1 forms the adaptor of CRL4 complexes (DDB1-CUL4A/B-RBX1) that dock DCAF substrate receptors; well supported structurally and biochemically. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1 |
| GO:0005515 protein binding | IPI PMID:16964240 Molecular architecture and assembly of the DDB1-CUL4A ubiqui... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005515 protein binding | IPI PMID:20223979 Identification of a primary target of thalidomide teratogeni... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0005634 nucleus | IDA PMID:20223979 Identification of a primary target of thalidomide teratogeni... | ACCEPT | Summary: Nuclear localization, consistent with DDB1's UV-DDB/CRL4 functions on chromatin; DDB1 accumulates in nuclei after UV. Reason: Well-supported localization; DDB1 translocates to and acts in the nucleus at DNA-damage sites. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005737 cytoplasm | IDA PMID:20223979 Identification of a primary target of thalidomide teratogeni... | ACCEPT | Summary: Cytoplasmic localization; DDB1 is primarily cytoplasmic at steady state and translocates to the nucleus after UV. Reason: Directly supported; DDB1 is primarily cytoplasmic and relocates to nuclei following UV irradiation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Primarily cytoplasmic (PubMed:10777491, PubMed:11673459) |
| GO:0006511 ubiquitin-dependent protein catabolic process | IDA PMID:11673459 UV-damaged DNA-binding proteins are targets of CUL-4A-mediat... | ACCEPT | Summary: DDB1 enables ubiquitin-dependent protein catabolism as the CRL4 adaptor. Reason: Core process (parent of proteasome-mediated catabolism); CRL4/DCX complexes target substrates for degradation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0005634 nucleus | IDA PMID:18593899 The cullin 4B-based UV-damaged DNA-binding protein ligase bi... | ACCEPT | Summary: Nuclear localization, consistent with DDB1's UV-DDB/CRL4 functions on chromatin; DDB1 accumulates in nuclei after UV. Reason: Well-supported localization; DDB1 translocates to and acts in the nucleus at DNA-damage sites. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459) |
| GO:0005737 cytoplasm | IDA PMID:18593899 The cullin 4B-based UV-damaged DNA-binding protein ligase bi... | ACCEPT | Summary: Cytoplasmic localization; DDB1 is primarily cytoplasmic at steady state and translocates to the nucleus after UV. Reason: Directly supported; DDB1 is primarily cytoplasmic and relocates to nuclei following UV irradiation. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Primarily cytoplasmic (PubMed:10777491, PubMed:11673459) |
| GO:0005515 protein binding | IPI PMID:12732143 The ubiquitin ligase activity in the DDB2 and CSA complexes ... | KEEP AS NON CORE | Summary: Bare protein binding from interaction studies (DCAFs, cullins, viral hijackers, substrates); real but uninformative. Reason: Per curation guidelines bare protein binding is uninformative; DDB1's specific interactions are captured by the adaptor/scaffold, cullin-binding and complex annotations. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt DDB1 may recruit specific substrate targeting subunits to the DCX complex |
| GO:0006289 nucleotide-excision repair | TAS PMID:8407967 Characterization of a human DNA damage binding protein impli... | ACCEPT | Summary: DDB1, as part of UV-DDB, functions in nucleotide excision repair of UV lesions. Reason: Core biological process; UV-DDB recognizes UV photolesions and initiates global-genome NER. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair |
| GO:0003677 DNA binding | TAS PMID:8798680 Mutations specific to the xeroderma pigmentosum group E Ddb-... | KEEP AS NON CORE | Summary: DNA binding attributed historically to the UV-damaged DNA-binding factor (DDB); the direct lesion-binding subunit is DDB2. Reason: Reflects the historical UV-DDB damaged-DNA-binding activity; DDB1's contribution is as the complex scaffold rather than the direct DNA-contacting subunit. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches |
| GO:0003684 damaged DNA binding | TAS PMID:8407967 Characterization of a human DNA damage binding protein impli... | KEEP AS NON CORE | Summary: Damaged-DNA binding is contributed by the UV-DDB complex (DDB2 is the direct DNA-contacting subunit); DDB1 contributes within the complex. Reason: DDB1 contributes to UV-damaged DNA recognition as part of UV-DDB, but DDB2 is the primary lesion-binding subunit; retained as a contributory, non-core function. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches |
| GO:0006281 DNA repair | TAS PMID:8798680 Mutations specific to the xeroderma pigmentosum group E Ddb-... | ACCEPT | Summary: DDB1 functions in DNA repair via the UV-DDB complex (parent of nucleotide excision repair). Reason: Correct core process; UV-DDB initiates NER. Redundant with the more specific NER terms. Supporting Evidence: file:human/DDB1/DDB1-uniprot.txt Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively |
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Download this section (compressed HTML)Q: Which DCAF-defined CRL4 complexes represent the physiologically dominant DDB1 functions across tissues, and how is DCAF exchange on the DDB1 propeller cluster regulated (e.g. by CAND1, neddylation, or DDB1 acetylation)?
Q: How separable are DDB1's UV-DDB/NER role and its broader CRL4 adaptor role, given that NER-defective DDB1 phenotypes (e.g. the WHIKERS neurodevelopmental syndrome) may also reflect loss of DCAF-dependent substrate turnover?
Q: Is the noncanonical stimulation of base-excision-repair enzymes (OGG1, MUTYH, APE1, SMUG1) by UV-DDB attributable to DDB1 itself or solely to the DDB2 subunit, and does it require an assembled CRL4 ligase or only the UV-DDB heterodimer?
Q: Under which infections or stresses does DDB1-CUL4 switch from degradative to non-degradative (regulatory) ubiquitination of substrates such as influenza PB2, and which DCAFs (e.g. DCAF11, DCAF12L1) determine that switch?
Experiment: Degron/auxin-inducible depletion of DDB1 followed by quantitative ubiquitinome and proteome profiling, with and without UV, to define the endogenous substrate repertoire attributable to each major DCAF and to separate NER from non-NER CRL4 functions.
Experiment: Structure-guided point mutations in the DDB1 BPB propeller cleft that selectively block DCAF (WDxR-motif) docking while preserving CUL4 binding, to test which phenotypes depend on substrate-receptor recruitment versus UV-DDB lesion recognition.
Experiment: Reconstitute purified UV-DDB (DDB1-DDB2) with and without DDB1, plus recombinant BER enzymes (OGG1, MUTYH, APE1, SMUG1), and use single-molecule and ensemble kinetics to determine whether DDB1 is required for the reported stimulation of BER enzyme activity and lesion handoff.
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