CUL4B is a cullin scaffold that organizes DDB1-associated RING E3 ubiquitin ligases. It connects substrate-receptor assemblies to RBX1-containing catalytic machinery, supporting substrate ubiquitination and proteasomal turnover. CRL4B also supports nondegradative H2AK119 monoubiquitination and cooperates with PRC2 in repressive chromatin regulation. CUL4B-containing DDB2 complexes participate in damaged-DNA recognition and nucleotide-excision repair. CUL4B is enriched in the nucleus, with context-dependent cytoplasmic pools, and shares some functions with CUL4A while also assembling distinct regulatory complexes. Alternative products differ at the N terminus, including the nuclear-localization region.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000082 G1/S transition of mitotic cell cycle | NAS PMID:8681378 cul-1 is required for cell cycle exit in C. elegans and iden... | UNDECIDED | Summary: The cited cullin-family paper does not yet resolve this CUL4B-specific G1/S assertion. Reason: The accessible abstract studies C. elegans cul-1 and identifies a larger cullin family. It does not establish the human CUL4B-specific G1/S experiment. CUL4B has other cell-cycle evidence, but that does not verify this particular source attribution; the annotation is retained as uncertain rather than rejected as a paralog error. Supporting Evidence: PMID:8681378 The gene cul-1 (formerly lin-19) is a negative regulator of the cell cycle in C. elegans. |
| GO:0000209 protein polyubiquitination | IEA GO_REF:0000107 | ACCEPT | Summary: CUL4B supports protein polyubiquitination as a CRL4B scaffold. Reason: The literal mouse Cul4b source resolves to an experimental polyubiquitination annotation. Human CRL4B substrate-ubiquitination and proteasomal-turnover experiments independently support the conserved process. This is a scaffold contribution within an E3 complex, not an autonomous ubiquitin-transfer reaction. |
| GO:0003684 damaged DNA binding | IDA PMID:22334663 Monoubiquitinated histone H2A destabilizes photolesion-conta... | ACCEPT | Summary: CUL4B contributes to damaged-DNA binding within a DDB1βDDB2 ligase complex. Reason: Human reconstituted CRL4BβDDB2 complexes bind damaged DNA and nucleosomes. The original contributes_to qualifier correctly represents complex-level participation: DDB2 supplies damage recognition while CUL4B organizes the ligase. The evidence does not assign isolated sequence- or lesion-recognition activity to CUL4B. |
| GO:0005515 protein binding | IPI PMID:12609982 TIP120A associates with cullins and modulates ubiquitin liga... | MODIFY | Summary: The RBX1 interaction supports ubiquitin protein ligase binding. Reason: The curated interaction and the literal tagged-cullin affinity record identify RBX1, a RING E3 ligase component. This established interface is more informative than generic binding; the affinity experiment alone does not establish purified binary stoichiometry. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: file:human/CUL4B/CUL4B-uniprot.txt Part of a complex with RBX1 and TIP120A/CAND1 |
| GO:0005515 protein binding | IPI PMID:12609982 TIP120A associates with cullins and modulates ubiquitin liga... | KEEP AS NON CORE | Summary: CUL4B associates with the cullin regulator CAND1. Reason: Human HeLa purification and reciprocal association records support the CUL4BβCAND1 pair. CAND1 regulates cullin-complex assembly; this interaction does not make CUL4B an exchange factor. Retain the positive generic association as non-core under the project binding policy. Supporting Evidence: PMID:12609982 immunopurified CUL4B-containing complex from HeLa cells |
| GO:0005515 protein binding | IPI PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | KEEP AS NON CORE | Summary: The Q58WW2-containing cullin/DDB1 association remains a contextual interaction. Reason: The curated source represents association within the DDB1βcullin adaptor network. Selected original assays support that network, while the exact target-specific supplemental interaction was not independently recovered. Retain the established complex-association interpretation with curator deference, without treating all listed participants as a purified pair or as simultaneous CUL4A/CUL4B subunits. |
| GO:0005515 protein binding | IPI PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | KEEP AS NON CORE | Summary: The Q5H9S7-containing cullin/DDB1 association remains a contextual interaction. Reason: The curated source represents association within the DDB1βcullin adaptor network. Selected original assays support that network, while the exact target-specific supplemental interaction was not independently recovered. Retain the established complex-association interpretation with curator deference, without treating all listed participants as a purified pair or as simultaneous CUL4A/CUL4B subunits. |
| GO:0005515 protein binding | IPI PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | KEEP AS NON CORE | Summary: The Q5TAQ9-containing cullin/DDB1 association remains a contextual interaction. Reason: The curated source represents association within the DDB1βcullin adaptor network. Selected original assays support that network, while the exact target-specific supplemental interaction was not independently recovered. Retain the established complex-association interpretation with curator deference, without treating all listed participants as a purified pair or as simultaneous CUL4A/CUL4B subunits. |
| GO:0005515 protein binding | IPI PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | KEEP AS NON CORE | Summary: The Q8TEB1-containing cullin/DDB1 association remains a contextual interaction. Reason: The curated source represents association within the DDB1βcullin adaptor network. Selected original assays support that network, while the exact target-specific supplemental interaction was not independently recovered. Retain the established complex-association interpretation with curator deference, without treating all listed participants as a purified pair or as simultaneous CUL4A/CUL4B subunits. |
| GO:0005515 protein binding | IPI PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | KEEP AS NON CORE | Summary: The Q92466-containing cullin/DDB1 association remains a contextual interaction. Reason: The curated source represents association within the DDB1βcullin adaptor network. Selected original assays support that network, while the exact target-specific supplemental interaction was not independently recovered. Retain the established complex-association interpretation with curator deference, without treating all listed participants as a purified pair or as simultaneous CUL4A/CUL4B subunits. |
| GO:0005515 protein binding | IPI PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | KEEP AS NON CORE | Summary: The Q9BW61-containing cullin/DDB1 association remains a contextual interaction. Reason: The curated source represents association within the DDB1βcullin adaptor network. Selected original assays support that network, while the exact target-specific supplemental interaction was not independently recovered. Retain the established complex-association interpretation with curator deference, without treating all listed participants as a purified pair or as simultaneous CUL4A/CUL4B subunits. |
| GO:0005515 protein binding | IPI PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | KEEP AS NON CORE | Summary: The Q9Y4B6-containing cullin/DDB1 association remains a contextual interaction. Reason: The curated source represents association within the DDB1βcullin adaptor network. Selected original assays support that network, while the exact target-specific supplemental interaction was not independently recovered. Retain the established complex-association interpretation with curator deference, without treating all listed participants as a purified pair or as simultaneous CUL4A/CUL4B subunits. |
| GO:0005515 protein binding | IPI PMID:16964240 Molecular architecture and assembly of the DDB1-CUL4A ubiqui... | KEEP AS NON CORE | Summary: CUL4B associates with the substrate receptor WDTC1. Reason: The inspected 2006 purification passages establish CUL4AβWDTC1, leaving the exact CUL4B source experiment unresolved. Independent original CRL4βWDTC1 experiments explicitly identify CUL4B-containing complexes. This supports the gene-level association while preserving the original citation and its assay-access limit. |
| GO:0005515 protein binding | IPI PMID:17041588 CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repe... | KEEP AS NON CORE | Summary: DDB1 is a demonstrated CUL4B complex partner. Reason: The original human affinity-purification work and literal co-immunoprecipitation records identify DDB1 with CUL4B. DDB1 bridges substrate receptors to the cullin scaffold. Retain the positive association without inferring an additional autonomous molecular function. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17041588 CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repe... | KEEP AS NON CORE | Summary: CUL4B associates with the histone-binding protein GRWD1. Reason: The original CUL4B purification identifies GRWD1, and current literal records reproduce the tagged human-cell association. GRWD1 binding does not establish that CUL4B itself binds histones or performs ribosome assembly in this experiment. No narrower partner class is imposed from an incompletely established chaperone mechanism. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18775313 UBXD7 binds multiple ubiquitin ligases and implicates p97 in... | KEEP AS NON CORE | Summary: UBXN7 associates with CUL4B-containing complexes. Reason: The literal affinity record preserves the tagged-cell assay and spoke expansion. Independent human UBXN7βCUL4B coexpression/pull-down evidence supports the pair. This does not demonstrate that CUL4B itself has ubiquitin-receptor or segregase activity. |
| GO:0005515 protein binding | IPI PMID:19651607 Aryl hydrocarbon receptor suppresses intestinal carcinogenes... | KEEP AS NON CORE | Summary: The DDB1 association is retained with source-specific curator deference. Reason: The exact target pair was not recovered in the current interaction export and the cited paper is abstract-only in the selected cache. DDB1βCUL4B association is independently established by human purification and structural work, so the positive interaction is retained without claiming to have inspected this paperβs target experiment. |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | MODIFY | Summary: The HSP90AB1 association supports Hsp90 protein binding. Reason: The literal human tandem-affinity record identifies HSP90AB1 with tagged CUL4B. HSP90AB1 is an Hsp90 chaperone, making the class-specific binding term appropriate; co-purification does not establish a particular folding reaction or physiological dependence. Proposed replacements: Hsp90 protein binding |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | KEEP AS NON CORE | Summary: DDB1 association is reproduced in the quantitative cullin interaction screen. Reason: Literal affinity records identify DDB1 with CUL4B under the recorded untreated and neddylation-inhibitor conditions. These are cellular complex-association measurements, consistent with the established DDB1βCUL4B interface, and do not establish a new DDB1-dependent activity for CUL4B. |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | KEEP AS NON CORE | Summary: CAND1 association is retained in its recorded cullin-regulation conditions. Reason: Multiple literal affinity records recover CAND1 with CUL4B across the recorded treatment states. Retain this contextual regulatory association rather than infer constitutive occupancy, a fixed complex stoichiometry, or CUL4B-mediated nucleotide exchange. |
| GO:0005515 protein binding | IPI PMID:21778237 COMMD1 (copper metabolism MURR1 domain-containing protein 1)... | UNDECIDED | Summary: The source-specific UniProtKB:Q86X83 interaction panel remains unresolved. Reason: The original paperβs accessible text establishes a COMMDβcullin interaction survey and an explicit COMMD1βCUL4B association. The exact panel for this distinct COMMD partner was not inspected, and the current interaction export did not recover its literal pair. This is unresolved evidence, not evidence against binding or against the curator. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21778237 COMMD1 (copper metabolism MURR1 domain-containing protein 1)... | KEEP AS NON CORE | Summary: COMMD1 associates with CUL4B in the original cullin survey. Reason: The inspected original Results explicitly report COMMD1 association with each tested cullin, including CUL4B, in coexpression/pull-down experiments. The subsequent detailed CAND1-displacement mechanism centers on other cullins; it is not assigned wholesale to CUL4B. COMMD1 is not treated as an autonomous E3 enzyme. Supporting Evidence: PMID:21778237 COMMD1 interacts with multiple Cullins |
| GO:0005515 protein binding | IPI PMID:21778237 COMMD1 (copper metabolism MURR1 domain-containing protein 1)... | UNDECIDED | Summary: The source-specific UniProtKB:Q9GZQ3 interaction panel remains unresolved. Reason: The original paperβs accessible text establishes a COMMDβcullin interaction survey and an explicit COMMD1βCUL4B association. The exact panel for this distinct COMMD partner was not inspected, and the current interaction export did not recover its literal pair. This is unresolved evidence, not evidence against binding or against the curator. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21778237 COMMD1 (copper metabolism MURR1 domain-containing protein 1)... | UNDECIDED | Summary: The source-specific UniProtKB:Q9NX08 interaction panel remains unresolved. Reason: The original paperβs accessible text establishes a COMMDβcullin interaction survey and an explicit COMMD1βCUL4B association. The exact panel for this distinct COMMD partner was not inspected, and the current interaction export did not recover its literal pair. This is unresolved evidence, not evidence against binding or against the curator. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21778237 COMMD1 (copper metabolism MURR1 domain-containing protein 1)... | UNDECIDED | Summary: The source-specific UniProtKB:Q9UBI1 interaction panel remains unresolved. Reason: The original paperβs accessible text establishes a COMMDβcullin interaction survey and an explicit COMMD1βCUL4B association. The exact panel for this distinct COMMD partner was not inspected, and the current interaction export did not recover its literal pair. This is unresolved evidence, not evidence against binding or against the curator. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21778237 COMMD1 (copper metabolism MURR1 domain-containing protein 1)... | UNDECIDED | Summary: The source-specific UniProtKB:Q9Y6G5 interaction panel remains unresolved. Reason: The original paperβs accessible text establishes a COMMDβcullin interaction survey and an explicit COMMD1βCUL4B association. The exact panel for this distinct COMMD partner was not inspected, and the current interaction export did not recover its literal pair. This is unresolved evidence, not evidence against binding or against the curator. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22466964 NEDD8 links cullin-RING ubiquitin ligase function to the p97... | KEEP AS NON CORE | Summary: Human CUL4BβUBXN7 association is supported by cellular pull-down. Reason: The original reports coexpression of V5-tagged human CUL4B with UBXN7 and recovery of the complex. Purified cullin experiments elsewhere in the paper used CUL2 or CUL4A, so the CUL4B result remains a cellular association rather than a purified binary assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22939624 Quantitative analysis of HSP90-client interactions reveals p... | MODIFY | Summary: The HSP90AB1 interaction supports Hsp90 protein binding. Reason: The literal LUMIER record identifies the HSP90AB1βCUL4B pair in human 293T cells. The known partner class supports the specific term while preserving the tagged assay and avoiding a claim that a particular CUL4B product was shown to require Hsp90 for folding. Proposed replacements: Hsp90 protein binding |
| GO:0005515 protein binding | IPI PMID:22939624 Quantitative analysis of HSP90-client interactions reveals p... | KEEP AS NON CORE | Summary: CUL4B associates with the Hsp90 co-chaperone CDC37. Reason: The literal LUMIER association is positive. CDC37 recruits client proteins to Hsp90 and is a co-chaperone; its association alone does not establish that it independently folds CUL4B or justify assigning Hsp90 binding to this distinct partner. Keep the generic interaction as contextual. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23238014 CRL4B catalyzes H2AK119 monoubiquitination and coordinates w... | MODIFY | Summary: The RBX1 association supports E3 ligase binding. Reason: Literal co-immunoprecipitation and complex-fractionation records support RBX1 association with CUL4B, including mapped construct boundaries. RBX1 is the RING E3 component of CRL4B, so its partner class justifies the refinement without asserting autonomous ubiquitin catalysis by the cullin. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:23238014 CRL4B catalyzes H2AK119 monoubiquitination and coordinates w... | KEEP AS NON CORE | Summary: DDB1 association supports the CRL4B complex. Reason: The literal records retain co-immunoprecipitation, pull-down and construct information for DDB1 and CUL4B. Chromatin co-occupancy records are not treated as separate proof of binary binding. The established association is retained without manufacturing another molecular activity. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | KEEP AS NON CORE | Summary: The CDC37 interaction is a contextual co-chaperone association. Reason: The literal human-cell LUMIER record reproduces the pair. CDC37 is a client-recruiting Hsp90 co-chaperone, and this association neither establishes autonomous folding catalysis nor a kinase activity for CUL4B. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25435324 Structural mechanism of nuclear transport mediated by import... | KEEP AS NON CORE | Summary: The established CUL4BβCAND1 association is retained. Reason: The cited transport study is abstract-only in the selected cache and its exact target pair was not recovered in the current export. Independent human CUL4BβCAND1 purification supports the biological association; retain it with curator deference without importing this paperβs transport mechanism into CUL4B. |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | KEEP AS NON CORE | Summary: The tested ZMAT4 isoform-2 construct associates with CUL4B in yeast two-hybrid assays. Reason: The literal records identify Q9H898-2 and distinguish wild-type from CUL4B variant constructs. The partner backbone matches the official isoform. A zinc-finger annotation alone does not establish a sequence-specific transcription-factor class, and the yeast assay is not proof of a native human transcription complex. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | MODIFY | Summary: The RBX1 affinity association supports ubiquitin protein ligase binding. Reason: The human tagged-bait affinity record identifies RBX1 with CUL4B. Its established RING E3 role supports the binding refinement; spoke expansion and cellular extraction do not imply a purified two-protein interface. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | KEEP AS NON CORE | Summary: DDB1 is recovered with CUL4B in the interaction network. Reason: The literal human affinity record supports the established DDB1βCUL4B complex association. Keep this positive screen assertion without inferring a new function from network proximity or counting it as a separate stoichiometric measurement. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | KEEP AS NON CORE | Summary: CAND1 is recovered with CUL4B in the interaction network. Reason: The literal human affinity record supports CAND1 association with the cullin. This contextual regulatory interaction remains non-core; it does not establish CUL4B transport activity or an enzymatic role for CAND1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | KEEP AS NON CORE | Summary: DCNL3 associates with CUL4B in the human DCNL survey. Reason: The inspected original affinity-purification and immunoblot experiments support the DCNL3βCUL4B association. The current exportβs lack of the pair is not a negative result. DCNL proteins participate in cullin neddylation; that role does not make CUL4B a NEDD8 ligase or establish a ubiquitin-E3 partner classification for this binding row. Supporting Evidence: PMID:26906416 all DCNLs interact with most cullin subtypes |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | KEEP AS NON CORE | Summary: DCNL2 associates with CUL4B in the human DCNL survey. Reason: The inspected original affinity-purification and immunoblot experiments support the DCNL2βCUL4B association. The current exportβs lack of the pair is not a negative result. DCNL proteins participate in cullin neddylation; that role does not make CUL4B a NEDD8 ligase or establish a ubiquitin-E3 partner classification for this binding row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | KEEP AS NON CORE | Summary: DCNL1 associates with CUL4B in the human DCNL survey. Reason: The inspected original affinity-purification and immunoblot experiments support the DCNL1βCUL4B association. The current exportβs lack of the pair is not a negative result. DCNL proteins participate in cullin neddylation; that role does not make CUL4B a NEDD8 ligase or establish a ubiquitin-E3 partner classification for this binding row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | KEEP AS NON CORE | Summary: DCNL5 associates with CUL4B in the human DCNL survey. Reason: The inspected original affinity-purification and immunoblot experiments support the DCNL5βCUL4B association. The current exportβs lack of the pair is not a negative result. DCNL proteins participate in cullin neddylation; that role does not make CUL4B a NEDD8 ligase or establish a ubiquitin-E3 partner classification for this binding row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | MODIFY | Summary: RBX1 binding is consistent with the demonstrated CRL4B complex. Reason: The cited abstract explicitly identifies CUL4BβDDB1βDCAF4 complexes and substrate ubiquitination, while the exact RBX1 panel remains uninspected. The established CUL4BβRBX1 interface independently supports the E3-partner class; retain the source assay limit rather than claim a new purified interaction. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | KEEP AS NON CORE | Summary: CUL4BβDDB1 association is supported in the DCAF4 study. Reason: The cited abstract explicitly reports assembly of both CUL4A- and CUL4B-containing DDB1βDCAF4 ligases. Retain the positive CUL4BβDDB1 association while distinguishing these alternative complexes and acknowledging that the target full-text panel was not inspected. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: The RBX1 proteomic association supports E3 ligase binding. Reason: The literal BioPlex record identifies the CUL4BβRBX1 pair in the human 293T affinity-purification network. RBX1βs E3 class supports refinement; screen context and co-complex detection do not invalidate binding or establish autonomous cullin catalysis. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: DDB1 association is reproduced in the HCT116 interaction network. Reason: The literal BioPlex record identifies the human HCT116 CUL4BβDDB1 association. This supports the existing core complex relationship, with cell-line and tagged-bait scope retained rather than assuming universal abundance or stoichiometry. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The DDB1 interaction remains positive with an unresolved screen-specific target entry. Reason: The exact OpenCell target entry was not independently recovered. DDB1βCUL4B association is established by separate human purification and structural work, so the gene-level interaction is retained with explicit curator deference; no claim is made to have inspected the missing entry. |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | KEEP AS NON CORE | Summary: The SPOP association is retained in its mutation-sensitive proximity-assay context. Reason: The literal BRET/proximity records include SPOP variant-dependent gains and other mutation-feature states. They support a contextual CUL4B association, not a universal wild-type complex. SPOP is a substrate receptor rather than the catalytic RING E3, so its binding does not justify an E3-enzyme binding refinement here. Supporting Evidence: PMID:35512704 gain of interactions encompassing both oncogenic and tumor suppressor mutations |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: The established CAND1 association is retained without claiming an inspected target screen entry. Reason: The studyβs human U2OS affinity-proteomics framework was read, but the specific target-pair table was not recovered. Independent human CUL4BβCAND1 purification supports the biological association, which is retained with curator deference and without assigning a new localization or structural interface from the multimodal map. |
| GO:0005634 nucleus | EXP PMID:18593899 The cullin 4B-based UV-damaged DNA-binding protein ligase bi... | ACCEPT | Summary: CUL4B is a nuclear cullin scaffold. Reason: The inspected original nuclear-complex context supports the location, consistent with independent CUL4B localization and HPA observations. This gene-level assertion does not assign identical nuclear localization to each alternative product. |
| GO:0005634 nucleus | EXP PMID:19801544 Characterization of nuclear localization signal in the N ter... | ACCEPT | Summary: An N-terminal localization signal supports nuclear enrichment of the long CUL4B product. Reason: Original localization experiments identify a functional N-terminal NLS. The paperβs positions 37β40 map to the 895-residue product, corresponding to positions 55β58 of the displayed 913-residue product. The short 717-residue splice form is not equated with these tested constructs. Supporting Evidence: PMID:19801544 NLS in CUL4B is located in its N terminus |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: Nuclear localization is a supported phylogenetic inheritance. Reason: The actual PTHR11932 tree and exact target MSA place CUL4B below the asserted PTN002631076 node. Literal IBD and experimental donor records agree with the source set, including valid target evidence. Human localization independently supports this inherited location; the targetβs inclusion is not circular. |
| GO:0005634 nucleus | IDA PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | ACCEPT | Summary: Nuclear localization is established for CUL4B; the particular RGS2-source assay remains unresolved. Reason: Accept the established nuclear location with curator deference. Independent PMID:19801544 localization and NLS experiments support nuclear CUL4B. The inspected PMID:25970626 RGS2 study establishes complex assembly and turnover, but its particular nuclear-localization or nuclear-activity assay was not verified. The curated GO-CAM placement is not treated as a second experimental observation; the literal is_active_in relationship remains unchanged. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: The nuclear location is independently supported despite a nonmatching current rule branch. Reason: The original annotation combines ARBA00026330 with UniProt location SL-0191. The recovered current ARBA conditions do not match the selected target record, while the nuclear UniProt location and direct human evidence remain valid. Preserve both literal inputs and accept the location without claiming the rule was reproduced. Supporting Evidence: file:human/CUL4B/CUL4B-uniprot.txt file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005634 nucleus | NAS PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: Nuclear CRL4BβDDB2 function supports the location. Reason: The original structural and reconstitution work places CRL4B in damaged-chromatin recognition and repair. Independent target-localization experiments support the nuclear assignment; the truncated crystallographic construct does not establish localization of all alternative products. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: HPA supports CUL4B nucleoplasmic localization. Reason: The official HPA record reports enhanced nucleoplasmic localization across several human cell lines and antibodies, with additional cytosolic or vesicular staining in some conditions. The evidence is not exclusive to nucleoplasm and does not resolve individual splice products. Supporting Evidence: GO_REF:0000052 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5652005 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5652005 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5652009 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5652009 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5689317 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5689317 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5689861 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5689861 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690213 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5690213 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690988 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5690988 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690990 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5690990 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690991 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5690991 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690996 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5690996 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5691000 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5691000 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5691006 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5691006 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5696655 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5696655 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5696664 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5696664 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5696670 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-5696670 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6781833 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6781833 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6781867 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6781867 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782004 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782004 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782069 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782069 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782131 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782131 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782138 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782138 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782141 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782141 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782204 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782204 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782208 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782208 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782211 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782211 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782224 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782224 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782227 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782227 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782234 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782234 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782943 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6782943 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6790454 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6790454 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6790487 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-6790487 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8952638 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-8952638 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8952639 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-8952639 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8955245 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-8955245 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8955285 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-8955285 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8956045 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-8956045 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9684118 | ACCEPT | Summary: The Reactome event places a CUL4B-containing complex in the nucleoplasm. Reason: The complete saved Reactome object traversal links this source event through its physical entities to human Q13620 in a nucleoplasmic complex. The modeled event supports the location; alternative cullins in a defined set are not assumed to coexist in one complex, and pathway membership alone is not treated as a new molecular activity. Supporting Evidence: Reactome:R-HSA-9684118 file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: A cytoplasmic CUL4B pool is supported alongside predominant nuclear localization. Reason: The literal UniProt cytoplasm mapping is compatible with cell-state-dependent ortholog observations and nonnuclear staining in human HPA assays. Keep the broad cytoplasmic location as contextual rather than narrow it to cytosol across all cells or products. Supporting Evidence: file:human/CUL4B/CUL4B-uniprot.txt file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The ortholog-supported cytoplasmic location is context dependent. Reason: The mouse Cul4b source has a genuine experimental cytoplasm record, distinct from its electronic location mapping. Official annotation describes changing nuclear/cytoplasmic distribution during oocyte maturation, and human HPA supports a nonnuclear pool. Preserve the transfer without claiming all products or all cell states share it. Supporting Evidence: file:human/CUL4B/CUL4B-uniprot.txt file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0006289 nucleotide-excision repair | NAS PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: CRL4B contributes to nucleotide-excision repair through damaged-chromatin recognition. Reason: Separate CRL4A and CRL4B assemblies were structurally and biochemically examined in the original study. CUL4B organizes the DDB1βDDB2 ligase arm rather than making the nuclease incision itself. This performed scaffold role supports involvement in nucleotide-excision repair. |
| GO:0006511 ubiquitin-dependent protein catabolic process | IEA GO_REF:0000120 | MODIFY | Summary: Ubiquitin-dependent substrate turnover is more precisely proteasome mediated. Reason: The combined cullin-domain and ortholog inputs agree with direct human CUL4B-dependent substrate ubiquitination and proteasome-sensitive degradation. Refine the broad catabolic process to the demonstrated ubiquitin-dependent proteasomal route without rewriting any source field. Proposed replacements: proteasome-mediated ubiquitin-dependent protein catabolic process |
| GO:0006974 DNA damage response | IBA GO_REF:0000033 | ACCEPT | Summary: DNA-damage response is supported by the on-path cullin IBD and human CRL4B experiments. Reason: The reconstructed target lineage includes PTN000232236 with the literal IBD and experimental source joins. Human damaged-DNA/nucleosome and repair-complex evidence independently supports the inherited process. No loss or divergent target function was established. |
| GO:0006974 DNA damage response | ISS GO_REF:0000114 | ACCEPT | Summary: The homologous-complex transfer is biologically supported for CUL4B. Reason: ComplexPortal CPX-477 explicitly describes the CUL4A variant, so it is not a literal CUL4B-membership record. The original ISS assertion is a homology transfer, independently supported by human CUL4B-specific damaged-DNA complex reconstitution. Preserve that distinction rather than treating family homology as direct membership. |
| GO:0007283 spermatogenesis | NAS PMID:29907856 Deletion of DDB1- and CUL4- associated factor-17 (Dcaf17) ge... | KEEP AS NON CORE | Summary: Spermatogenesis is a contextual developmental role of cullin-4 scaffolds. Reason: The cited studyβs selected text discusses established mouse Cul4b reproductive phenotypes while its own principal perturbation is Dcaf17. Retain the contextual annotation with that source distinction; it is not a demonstrated human sperm assay or a separate molecular activity. Supporting Evidence: |
| GO:0008283 cell population proliferation | NAS PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | KEEP AS NON CORE | Summary: CUL4B contributes to proliferation in the studied colon-cancer context. Reason: The cited abstract explicitly reports CUL4B knockdown, ST7 accumulation and reduced proliferation, colony formation and tumour growth. Retain this context-specific outcome of the ligase pathway without treating proliferation as a distinct intrinsic activity or claiming full-text assay inspection. Supporting Evidence: PMID:30945288 knockdown of c-Myc, CUL4A or CUL4B |
| GO:0010467 gene expression | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: CUL4B-dependent gene-expression regulation is supported in the mouse neural context. Reason: The literal mouse donor is an experimental Cul4b annotation. Its indexed abstract describes CUL4B/PRC2 repression of Ptgds and downstream GFAP expression. This supports a conserved contextual regulatory contribution; it does not assign direct DNA recognition or autonomous transcription-factor activity to CUL4B. Supporting Evidence: file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0010498 proteasomal protein catabolic process | IDA PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | MODIFY | Summary: The RGS2 turnover assay supports ubiquitin-dependent proteasomal catabolism. Reason: CUL4B depletion and complex/turnover experiments distinguish its role from CUL4A and connect RGS2 ubiquitination to proteasomal degradation. The more informative process term represents that route. The original source relationship is preserved and the cullin is not described as a protease. Proposed replacements: proteasome-mediated ubiquitin-dependent protein catabolic process Supporting Evidence: PMID:25970626 RGS2 is ubiquitinated |
| GO:0010498 proteasomal protein catabolic process | IMP PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | MODIFY | Summary: The RGS2 turnover assay supports ubiquitin-dependent proteasomal catabolism. Reason: CUL4B depletion and complex/turnover experiments distinguish its role from CUL4A and connect RGS2 ubiquitination to proteasomal degradation. The more informative process term represents that route. The original source relationship is preserved and the cullin is not described as a protease. Proposed replacements: proteasome-mediated ubiquitin-dependent protein catabolic process Supporting Evidence: PMID:25970626 rapid degradation by the proteasome |
| GO:0010506 regulation of autophagy | NAS PMID:31267705 Regulation of MAGE-A3/6 by the CRL4-DCAF12 ubiquitin ligase ... | UNDECIDED | Summary: The CUL4B-specific contribution to autophagy is unresolved for this source. Reason: The accessible abstract identifies CRL4βDCAF12-dependent MAGE-A3/6 turnover during starvation, but the target-specific CUL4B construct and perturbation were not established after unsuccessful full-original retrieval. Preserve the source assertion as uncertain rather than infer that a CRL4 family result either proves or excludes the B paralog. Supporting Evidence: |
| GO:0016567 protein ubiquitination | IBA GO_REF:0000033 | ACCEPT | Summary: Protein ubiquitination is a conserved activity of CUL4B-containing ligase complexes. Reason: The actual tree places CUL4B below PTN002631076; the matching IBD and experimental donor records are genuine. Human reconstitution independently supports a scaffold contribution to substrate ubiquitination. This does not equate cullin scaffolding with autonomous ubiquitin-transfer catalysis. |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000120 | ACCEPT | Summary: The recovered rule and pathway inputs support protein ubiquitination. Reason: ARBA00027966 has a matching current condition branch, and the UniPathway ubiquitination input agrees with human CRL4B experiments. Preserve the separate sources and interpret CUL4B as the organizing component of the ligase. |
| GO:0016567 protein ubiquitination | IMP PMID:28437394 Selective degradation of splicing factor CAPERΞ± by anticance... | ACCEPT | Summary: CUL4B participation in ubiquitination is retained with source-specific curator deference. Reason: The selected abstract reports CRL4βDCAF15-mediated ubiquitination in human cells, while the exact CUL4B experiment is not independently visible. Human CUL4B ubiquitination is established by other direct work, so retain the existing experimental annotation without asserting that the inaccessible target assay was inspected. |
| 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: CUL4B contributes to shared CRL4 control of replication licensing. Reason: The exact CUL4B assay in PMID:16861906 remains uninspected. Independently, PMID:30018425 demonstrates CUL4B chromatin recruitment and endogenous RepID association in human cells. Joint CUL4A/B depletion increases re-replication, especially after RepID loss, whereas either individual depletion leaves cell-cycle distribution unchanged with compensatory recruitment of the other cullin. Together with the demonstrated RepID/CDT1 licensing mechanism, this supports retaining a contextual, partly redundant CRL4B contribution to initiation control. The replication-origin ChIP assayed CUL4A, not CUL4B; neither a B-specific origin assay nor initiation catalysis by CUL4B is claimed. |
| GO:0031297 replication fork processing | NAS PMID:30018425 The replication initiation determinant protein (RepID) modul... | UNDECIDED | Summary: The replication-initiation experiments do not settle a stalled-fork-processing annotation. Reason: The inspected source establishes RepID-dependent recruitment of CUL4B to chromatin and combined CUL4A/B replication effects. GO:0031297 specifically concerns processing needed to restart a stalled fork; the relevant restart assay was not established in the inspected passages. Preserve the positive replication context while leaving this more specific assertion uncertain. Supporting Evidence: |
| GO:0031461 cullin-RING ubiquitin ligase complex | IEA GO_REF:0000002 | MODIFY | Summary: The cullin complex can be specified as the CUL4B-containing ligase. Reason: The InterPro cullin-domain mapping is sound but broad. Human structural and reconstitution evidence identifies a CUL4BβDDB1βRBX1 complex, allowing refinement to its B-specific complex without implying a mixed CUL4A/CUL4B assembly. Proposed replacements: Cul4B-RING E3 ubiquitin ligase complex |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | EXP PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | MODIFY | Summary: The directly studied CUL4B complex is the B-specific CRL4 variant. Reason: The source studies separate CRL4A and CRL4B structures and reconstituted assemblies. It does not show both cullins in one A-specific complex. Refine the complex identity to the experimentally established CUL4B variant. Proposed replacements: Cul4B-RING E3 ubiquitin ligase complex Supporting Evidence: PMID:22118460 structures of the fully assembled DDB1-DDB2-CUL4A/B-RBX1 |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IEA GO_REF:0000117 | MODIFY | Summary: The complex assignment should identify the CUL4B variant. Reason: ARBA00085920 was unavailable from the current rule endpoint, so its conditions were not reconstructed. Independent human structural evidence establishes the B-specific complex, supporting a biological refinement while preserving the literal historical rule and explicitly leaving its current provenance unresolved. Proposed replacements: Cul4B-RING E3 ubiquitin ligase complex |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | MODIFY | Summary: CUL4B belongs to its own DDB1-containing CRL4 complex. Reason: Selected original network evidence and independent structural reconstitution distinguish the CUL4B complex from the CUL4A complex. Refine the paralog-specific complex term without denying the shared DDB1/adaptor network or altering the original source record. Proposed replacements: Cul4B-RING E3 ubiquitin ligase complex |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:28212551 NRIP/DCAF6 stabilizes the androgen receptor protein by displ... | MODIFY | Summary: The biologically established CUL4B assembly is the B-specific complex. Reason: The inspected NRIP/DCAF6 study directly describes CUL4A experiments, leaving its CUL4B attribution unverified. Independent CUL4B-specific structural and biochemical work supports the B-complex refinement. This corrects the complex description without claiming that the cited paper directly assayed CUL4B. Proposed replacements: Cul4B-RING E3 ubiquitin ligase complex |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IBA GO_REF:0000033 | ACCEPT | Summary: Cul4B complex membership is supported by an on-path B-clade IBD. Reason: The actual target lineage includes PTN002631089, and the literal IBD/donor joins match the source annotation. Independent human structural evidence confirms B-specific complex membership. Target self-evidence is a valid experimental contribution to the phylogenetic assertion. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IDA PMID:18794347 PCNA-dependent regulation of p21 ubiquitylation and degradat... | ACCEPT | Summary: CUL4B complex membership is retained with explicit curator deference. Reason: The selected cache supplies the abstract, not the original target experiment. Membership of CUL4B in its DDB1/RBX1 ligase complex is independently established by human structural and biochemical work, so retain the positive experimental annotation while leaving this particular assay unverified. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IDA PMID:21628527 Selective ubiquitylation of p21 and Cdt1 by UBCH8 and UBE2G ... | ACCEPT | Summary: CUL4B complex membership is retained with explicit curator deference. Reason: The selected cache supplies the abstract, not the original target experiment. Membership of CUL4B in its DDB1/RBX1 ligase complex is independently established by human structural and biochemical work, so retain the positive experimental annotation while leaving this particular assay unverified. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IDA PMID:22334663 Monoubiquitinated histone H2A destabilizes photolesion-conta... | ACCEPT | Summary: Human reconstitution directly supports CUL4B ligase-complex membership. Reason: The original assembles and assays CRL4BβDDB2 with human components and distinguishes its properties from the CUL4A complex. This is direct complex evidence; the structural truncation is not taken as proof that all splice products have identical activity. Supporting Evidence: PMID:22334663 DDB1-CUL4B(DDB2) E3 ligase specifically binds to |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IEA GO_REF:0000120 | ACCEPT | Summary: The matching rule and ortholog evidence support the CUL4B complex. Reason: ARBA00085917 has a matching current branch, and the mouse source resolves to Cul4b records. Independent human structural evidence confirms the B-specific complex. These are distinct sources of support, not evidence for simultaneous A/B occupancy. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IPI PMID:27113764 The antiobesity factor WDTC1 suppresses adipogenesis via the... | ACCEPT | Summary: The WDTC1 study identifies a CUL4B-containing CRL4 complex. Reason: Inspected original Results and interaction captions identify WDTC1 in DDB1βCUL4A/BβROC1 complexes, including a CUL4B association. This supports membership without equating alternative A- and B-containing complexes or resolving their different effects on adipogenesis. Supporting Evidence: |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:16861906 L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and... | ACCEPT | Summary: The established CUL4B ligase complex is retained with its source scope explicit. Reason: The accessible abstract identifies human CUL4βDDB1βCDT2 assemblies. The source-specific B experiment remains uninspected; independent CUL4B structures establish the target complex, so retain membership with curator deference. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | ACCEPT | Summary: The established CUL4B ligase complex is retained with its source scope explicit. Reason: The original DDB1βcullin adaptor-network work supports CRL4 organization, corroborated by separate CUL4B structural assemblies. Complex membership does not mean every co-purified adaptor occupies one simultaneous assembly. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: The established CUL4B ligase complex is retained with its source scope explicit. Reason: The source directly studies a separate CUL4BβDDB1βDDB2 structure and reconstituted ligase. The CUL4B construct is residues 192β913 and must not be equated with the 717-residue splice product. Supporting Evidence: |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:25108355 Structure of the human Cereblon-DDB1-lenalidomide complex re... | ACCEPT | Summary: The established CUL4B ligase complex is retained with its source scope explicit. Reason: The selected abstract describes cereblon-associated CRL4 assembly without independently resolving its B-specific construct. Target complex membership is independently established by human CUL4B structural work; retain it without claiming the inaccessible target assay was read. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates ... | ACCEPT | Summary: The established CUL4B ligase complex is retained with its source scope explicit. Reason: The selected abstract reports Cullin-4βAMBRA1 regulation of autophagy without resolving the CUL4B-specific experiment. The target complex is independently established, so membership is retained while source-specific process claims remain separate. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:29691401 Methylated DNMT1 and E2F1 are targeted for proteolysis by L3... | ACCEPT | Summary: The established CUL4B ligase complex is retained with its source scope explicit. Reason: The inspected human-cell experiments include endogenous CUL4B co-immunoprecipitation and combined CUL4A/B perturbation in DNMT1 turnover. These support the B-containing complex without equating the separate L3MBTL3 developmental experiments with CUL4B-specific stem-cell assays. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | ACCEPT | Summary: The established CUL4B ligase complex is retained with its source scope explicit. Reason: The source abstract explicitly reports separate CUL4A- and CUL4B-containing DDB1βDCAF4 ligases and substrate turnover. This positive complex statement agrees with independently established CUL4B organization; full target figures were not inspected. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:31452512 Systematic identification of cancer cell vulnerabilities to ... | ACCEPT | Summary: The established CUL4B ligase complex is retained with its source scope explicit. Reason: The inspected sourceβs mechanistic cullin evidence is CUL4A-centered. Nevertheless, independent CUL4B-specific structures and reconstitution establish this target complex. Retain membership while recording the citation limit; the paperβs natural-killer-cell experiments are not silently reassigned to CUL4B. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:33898171 OTUD1 Activates Caspase-Independent and Caspase-Dependent Ap... | ACCEPT | Summary: The established CUL4B ligase complex is retained with its source scope explicit. Reason: The inspected paper uses CUL4AβDDB1/DCAF10 constructs and perturbations. Independent CUL4B-specific structural/reconstitution work establishes the target complex. Retain the biologically correct membership without claiming CUL4B-specific apoptosis evidence from this source. |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:34595758 The CRL4(DCAF1) cullin-RING ubiquitin ligase is activated fo... | ACCEPT | Summary: The established CUL4B ligase complex is retained with its source scope explicit. Reason: The inspected CRL4βDCAF1 assembly experiments use CUL4A, including purified oligomeric forms. Independent CUL4B-specific structural evidence establishes B-complex membership, but the A-complex oligomerization and activity results are not automatically transferred to B. |
| GO:0031625 ubiquitin protein ligase binding | IBA GO_REF:0000033 | ACCEPT | Summary: E3 ligase binding is supported by the inherited cullin interface. Reason: The actual tree and IBD place the conserved binding assertion at PTN002631076 on the CUL4B lineage. Experimental donor joins and the human RBX1 interface support the term. Donor number is not used as a confidence score, and the source does not assert autonomous ubiquitin catalysis by CUL4B. |
| GO:0031625 ubiquitin protein ligase binding | IEA GO_REF:0000002 | ACCEPT | Summary: The cullin-domain mapping agrees with direct E3-component association. Reason: The two InterPro cullin-domain inputs are compatible with the demonstrated CUL4BβRBX1 interface. The annotation describes binding the ligase component; it does not imply that the cullin is itself the catalytic RING enzyme. |
| GO:0032814 regulation of natural killer cell activation | NAS PMID:31452512 Systematic identification of cancer cell vulnerabilities to ... | UNDECIDED | Summary: CUL4B-specific regulation of natural killer cell activation remains unresolved. Reason: The original includes both target-cell susceptibility assays and CD107a degranulation measurements in primary natural killer cells. Its mechanistic cullin evidence is CUL4A-centered, however, and a CUL4B-specific intervention was not established. Neither absence of an inspected B assay nor the DCAF15 result justifies a negative conclusion about CUL4B. Supporting Evidence: |
| GO:0032991 protein-containing complex | IDA PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | MODIFY | Summary: The demonstrated assembly is a CUL4B-containing ligase complex. Reason: CUL4B, RBX1 and adaptor/substrate components are associated in the RGS2-turnover study. The B-specific complex term is more informative than generic protein-containing complex; the paper explicitly leaves direct FBXO44βRGS2 molecular contact unresolved. Proposed replacements: Cul4B-RING E3 ubiquitin ligase complex Supporting Evidence: |
| GO:0034644 cellular response to UV | IEA GO_REF:0000117 | ACCEPT | Summary: The current rule and human repair evidence support cellular UV response. Reason: ARBA00026679 has a matching current branch. Human CRL4B damaged-DNA binding and histone ubiquitination provide independent mechanistic support for participation in the UV response, without assigning the incision reaction to the scaffold. |
| GO:0034644 cellular response to UV | ISS GO_REF:0000114 | ACCEPT | Summary: The homologous-complex UV-response transfer is independently supported in CUL4B. Reason: CPX-477 is the CUL4A complex, not a direct CUL4B membership record. Human CUL4B-specific damaged-DNA and nucleosome experiments independently support the transferred response, while the original ISS source is preserved. |
| GO:0040029 epigenetic regulation of gene expression | NAS PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | UNDECIDED | Summary: The CUL4B-specific epigenetic contribution is unresolved in this DCAF13 study. Reason: The accessible abstract reports CRL4βDCAF13-dependent SUV39H1 turnover and mouse preimplantation phenotypes. The target-specific CUL4B construct and experiment were not recovered. Preserve the positive family-level mechanism without assuming it identifies the B paralog or treating lack of access as a contradiction. Independent PMID:23238014 establishes a CRL4B chromatin-repression role, but does not resolve the DCAF13-specific attribution. |
| GO:0040029 epigenetic regulation of gene expression | NAS PMID:34429321 Systematic Profiling of DNMT3A Variants Reveals Protein Inst... | KEEP AS NON CORE | Summary: CUL4B is implicated in context-specific control of the epigenetic regulator DNMT3A. Reason: The inspected source identifies CUL4B with RBX1 and DCAF8 in a DNMT3A stability screen; subsequent mechanistic work centers on DCAF8. Retain a contextual regulatory contribution through protein turnover, without assigning CUL4B methyltransferase activity or claiming that the screen directly measured each downstream methylation event. Independent PMID:23238014 supports the separate nondegradative H2AK119/PRC2 repression role represented in the scaffold core. |
| GO:0040029 epigenetic regulation of gene expression | NAS PMID:34720086 Cul4A-DDB1-mediated monoubiquitination of phosphoglycerate d... | UNDECIDED | Summary: The CUL4B-specific epigenetic assertion remains unresolved for this PHGDH source. Reason: Selected complete original Results, Methods and Discussion describe CUL4A-dependent PHGDH monoubiquitination and downstream SAM/SETD1A regulation. Those inspected assays do not establish the corresponding CUL4B result. Other CRL4B chromatin functions remain positive, but they do not silently substitute for this source-specific evidence. PMID:23238014 supports that separate CRL4B chromatin role, not the PHGDH-specific CUL4B assertion. |
| 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: CUL4B contributes to context-dependent regulation of cell proliferation. Reason: Independent PMID:19801544 reports reduced proliferation after CUL4B silencing, together with cyclin E accumulation and prolonged S phase. Retain this broad process as a contextual role. The original PMID:33869224 passage concerns CRL4-DCAF12/Yki-Yap-Taz, and its CUL4B-specific attribution remains unverified; the independent evidence does not authenticate that particular mechanism. |
| GO:0042254 ribosome biogenesis | IBA GO_REF:0000033 | ACCEPT | Summary: Ribosome biogenesis is supported by the on-path IBD and targeted human follow-up assays. Reason: The target lies below PTN001377530 with the literal IBD and experimental donor joins intact. The human study separately tested CUL4A/B co-depletion and found nucleolar pre-ribosome maturation defects; CUL4B need not have been a single-gene primary-screen hit. This supports inheritance without claiming an autonomous ribosome-assembly activity. |
| GO:0042254 ribosome biogenesis | IEA GO_REF:0000120 | ACCEPT | Summary: The recovered rule and ortholog chain support the ribosome-biogenesis annotation. Reason: ARBA00026817 has a matching current branch, and the mouse donor carries both propagated and experimental records. The broader chain reaches the actual human CUL4A/B depletion assays and the on-path IBD; it is not evaluated only as a reciprocal electronic transfer. |
| GO:0042254 ribosome biogenesis | IMP PMID:26711351 Genome-wide RNAi Screening Identifies Protein Modules Requir... | ACCEPT | Summary: Human CUL4A/B perturbation supports a contribution to ribosome biogenesis. Reason: Inspected original Results report mild effects after individual CUL4A or CUL4B depletion, but nucleolar retention of RPS2/ENP1 and altered rRNA maturation after combined depletion. These targeted assays support redundant CRL4 participation, not direct ribosomal structural membership or equal activity of all CUL4B products. Supporting Evidence: PMID:26711351 uncover a requirement for the CRL4 E3 ubiquitin ligase in nucleolar ribosome biogenesis |
| GO:0042981 regulation of apoptotic process | NAS PMID:33898171 OTUD1 Activates Caspase-Independent and Caspase-Dependent Ap... | UNDECIDED | Summary: CUL4B-specific apoptosis regulation is unresolved in this source. Reason: The inspected DCAF10 study explicitly uses CUL4AβDDB1 constructs, antibodies and knockdown experiments. A corresponding CUL4B contribution to the reported apoptotic phenotype was not established. The B-complex membership annotation remains supported independently, but does not settle this process-specific assertion. Supporting Evidence: |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: Proteasome-dependent substrate turnover is supported by phylogeny and direct target evidence. Reason: The actual CUL4B lineage descends from PTN002631076 and the literal IBD/donor records are intact. Human CUL4B-dependent RGS2 ubiquitination and proteasomal turnover independently establish the process. Target experimental evidence in the donor set is valid grounding rather than circularity. |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | ACCEPT | Summary: CUL4B participates in ubiquitin-dependent proteasomal turnover of RGS2. Reason: The original distinguishes CUL4B from CUL4A through depletion, complex association and substrate half-life experiments. The ligase scaffold promotes substrate ubiquitination upstream of proteasomal destruction; it is not the protease that performs degradation. Supporting Evidence: PMID:25970626 RGS2 protein degradation is mediated by a novel CUL4B-DDB1-FBXO44 E3 ligase. |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IEA GO_REF:0000117 | ACCEPT | Summary: The current ARBA rule supports the established proteasomal pathway. Reason: ARBA00026940 matches the selected CUL4B record at two alternative branches. Direct human substrate-turnover experiments corroborate the rule conclusion. Branch indices are not treated as separate biological observations. |
| GO:0045995 regulation of embryonic development | NAS PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | UNDECIDED | Summary: The source-specific CUL4B contribution to embryonic development remains uncertain. Reason: The accessible abstract establishes Dcaf13 loss-of-function and CRL4-dependent chromatin regulation during mouse preimplantation development. Full target-paralog evidence was not recovered, so the DCAF13/family result is not automatically assigned to CUL4B or rejected as a misattribution. Supporting Evidence: |
| GO:0048708 astrocyte differentiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The ortholog-supported astrocyte phenotype is a contextual developmental function. Reason: The actual mouse Cul4b IMP donor and its abstract report altered astrocyte-marker-positive cell generation after neural-progenitor Cul4b loss, with PTGDS-dependent gene repression. Retain the inherited broad developmental annotation as non-core; do not narrow its sign or claim a human differentiation assay from the mouse source. Supporting Evidence: file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0060964 regulation of miRNA-mediated gene silencing | NAS PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase dur... | UNDECIDED | Summary: The CUL4B-specific contribution to miRNA-mediated silencing is unresolved. Reason: The inspected original purifies a DCAF12βCUL4A complex and follows its silencing mechanism. A corresponding CUL4B experiment was not established in the selected original passages. This leaves target attribution uncertain rather than disproving a role for another CRL4 assembly. Supporting Evidence: |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: CUL4B was detected in the human urinary-exosome proteomic preparation. Reason: The linked NHLBI urinary-exosome database identifies CUL4B/NP_003579 with one peptide and assigns the entry to PMID:19056867. The study used pooled normal human urine and evaluated single-peptide identifications manually. Retain the source-positive detection as contextual localization, without inferring active secretion, a vesicle-specific function or a particular alternative product. Nuclear enrichment is not evidence against detection in this preparation. |
| GO:0070914 UV-damage excision repair | IDA PMID:22334663 Monoubiquitinated histone H2A destabilizes photolesion-conta... | MODIFY | Summary: The demonstrated repair pathway is nucleotide-excision repair. Reason: The official GO:0070914 definition specifies "an endonuclease that introduces a single-strand incision immediately 5' of a UV-induced damage site"; exact synonyms identify UVDE-dependent excision repair/UVER. Its is_a parents are DNA repair (GO:0006281) and cellular response to UV (GO:0034644). The source instead assays human CRL4B-DDB2 damaged-chromatin binding and histone ubiquitination in mammalian nucleotide-excision repair. Retain the refinement to GO:0006289, with the original IDA tuple unchanged. The source guide links the definition and flags the same-source DDB1/DDB2 assertions for separate review. Proposed replacements: nucleotide-excision repair Supporting Evidence: PMID:22334663 subsequently initiates NER file:human/CUL4B/CUL4B-source-evidence.yaml |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IDA PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | MODIFY | Summary: The demonstrated cullin-4 complex can be specified as the B variant. Reason: DDB1/adaptor association and independent structural reconstitution establish a CUL4B-containing ligase. The B-specific complex term preserves this evidence more precisely than the parent Cul4 complex term and does not imply that both paralogs occupy the same assembly. Proposed replacements: Cul4B-RING E3 ubiquitin ligase complex |
| GO:0080135 regulation of cellular response to stress | NAS PMID:31586112 TFEB activates Nrf2 by repressing its E3 ubiquitin ligase DC... | UNDECIDED | Summary: CUL4B-specific stress-response regulation remains unresolved in the cited TFEB study. Reason: The inspected source follows TFEB/DCAF11βNRF2 regulation, and the cited mechanistic precursor uses CUL4A. The CUL4B-specific role was not established in that chain. Retain the stress biology without assigning its target-paralog mechanism from family nomenclature alone. Supporting Evidence: |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:25970626 FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends... | ACCEPT | Summary: CUL4B supplies ubiquitin-ligase complex scaffold activity. Reason: Human CRL4B association and substrate-turnover experiments support the organizing function of the cullin between the DDB1/adaptor arm and RBX1-containing catalytic arm. Preserve the original contributes_to qualifier and distinguish scaffolding from autonomous E3 chemistry. |
| 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: CUL4B participates in shared CRL4 regulation of cell-cycle progression. Reason: The precise CUL4B experiment in the cited PMID:16861906 remains uninspected. Independent human-cell experiments in PMID:30018425 show CUL4B chromatin recruitment and compensatory recruitment after CUL4A depletion. Joint A/B depletion alters G2/M distribution and DNA synthesis, particularly in RepID-depleted cells, while individual CUL4B depletion alone does not alter the measured phase distribution. This supports a contextual, redundant ligase contribution to phase regulation rather than a CUL4B-only transition mechanism. |
| GO:1901987 regulation of cell cycle phase transition | NAS PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates ... | KEEP AS NON CORE | Summary: CUL4B contributes to cell-cycle phase regulation in a defined experimental context. Reason: Independent PMID:19801544 reports CUL4B silencing, cyclin E accumulation and prolonged S phase, supporting a contextual contribution to phase progression. The selected PMID:25499913 abstract concerns Cullin-4/AMBRA1 and autophagy dynamics; its CUL4B-specific phase-transition experiment remains unverified. Retention rests on the separate positive CUL4B evidence, not an assumed equivalence between autophagy and cell-cycle regulation. |
| GO:1902412 regulation of mitotic cytokinesis | NAS PMID:34758320 Phosphorylation at Ser68 facilitates DCAF11-mediated ubiquit... | UNDECIDED | Summary: CENP-A turnover does not yet resolve the asserted CUL4B cytokinesis role. Reason: The selected abstract establishes DCAF11-dependent CENP-A degradation during the cell cycle. The target-specific CUL4B perturbation and a cytokinesis endpoint were not independently recovered. Preserve the curated assertion as uncertain rather than equating centromere-protein turnover with demonstrated cytokinesis regulation. Supporting Evidence: |
| GO:1904178 negative regulation of adipose tissue development | NAS PMID:27113764 The antiobesity factor WDTC1 suppresses adipogenesis via the... | UNDECIDED | Summary: CUL4B-specific suppression of adipose development is not resolved by this source alone. Reason: The original establishes WDTC1βCRL4-dependent adipogenic suppression, but Cul4b depletion in mouse 3T3-L1 cells reduced proliferation and inhibited adipogenesis, and the authors explicitly caution that the cullin RNAi phenotypes cannot be clearly assessed. Complex association remains positive; the specific negative-regulation assignment is left uncertain rather than treated as either disproved or directly demonstrated. Supporting Evidence: |
| GO:2000036 regulation of stem cell population maintenance | NAS PMID:29691401 Methylated DNMT1 and E2F1 are targeted for proteolysis by L3... | UNDECIDED | Summary: The source-specific CUL4B stem-cell-maintenance role remains unresolved. Reason: The human DNMT1-turnover experiments include CUL4B, but the inspected developmental and hematopoietic discussion centers on L3MBTL3 perturbation. The exact CUL4B stem-cell-maintenance intervention was not established, so the protein-turnover mechanism is not silently promoted into this distinct process assertion. Supporting Evidence: |
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Download this section (compressed HTML)Q: Which N-terminally distinct CUL4B products assemble active ligases and enter the nucleus under physiological conditions?
Q: Which source-specific developmental, stress, epigenetic and miRNA phenotypes have direct CUL4B evidence rather than an unresolved CRL4-family or CUL4A attribution?
Q: What CUL4B-specific mechanism reconciles the WDTC1 complex association with the opposing, proliferation-confounded adipogenesis phenotypes in the original cullin knockdown experiment?
Q: Can the unavailable ARBA00085920 rule and the nonmatching ARBA00026330 branch be reconciled with the original annotation release while preserving the independently supported CUL4B complex and nuclear location?
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