Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on curation of immunofluorescence data
A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1.
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DCAF11 is one of 18 DDB1- and CUL4-associated factors (DCAFs) that serve as substrate receptors, docking on DDB1 via a conserved WDXR motif.
"we identify 18 Ddb1- and Cul4-associated factors (DCAFs), including 14 containing WD40 repeats. DCAFs interact with multiple surfaces on Ddb1, and the interaction of WD40-containing DCAFs with Ddb1 requires a conserved WDXR motif."
Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery.
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WD40-repeat DCAFs dock on the DDB1 double-beta-propeller of the DDB1-CUL4A-ROC1 ligase to present substrates for ubiquitination.
"DDB1 uses one beta-propeller domain for cullin scaffold binding and a variably attached separate double-beta-propeller fold for substrate presentation."
Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex.
Global landscape of HIV-human protein complexes.
Quantitative Mass Spectrometry Identifies Novel Host Binding Partners for Pathogenic Escherichia coli Type III Secretion System Effectors.
Architecture of the human interactome defines protein communities and disease networks.
TFEB activates Nrf2 by repressing its E3 ubiquitin ligase DCAF11 and promoting phosphorylation of p62.
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DCAF11 is a functional E3 ubiquitin ligase substrate receptor for NRF2, binding the DIDLID sequence of the Neh2 domain to mediate its degradation; TFEB transcriptionally represses DCAF11 to stabilize NRF2.
"DCAF11 and DDB1-Cul4/Roc1 bind to the DIDLID sequence of the Neh2 domain of Nrf2 to mediate its degradation."
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Phosphorylation at Ser68 facilitates DCAF11-mediated ubiquitination and degradation of CENP-A during the cell cycle.
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DCAF11 is the E3 ligase that specifically mediates phospho-Ser68-primed polyubiquitination and degradation of CENP-A; its deletion impairs CENP-A degradation and causes mislocalization.
"DCAF11 (DDB1 and CUL4 associated factor 11/WDR23) is the E3 ligase that specifically mediates the observed polyubiquitination. Deletion of DCAF11 hampers CENP-A degradation and causes its mislocalization."
OpenCell: Endogenous tagging for the cartography of human cellular organization.
AcM-UBE2M transfers NEDD8 to CRL4 E3 ubiquitin ligase complex
NEDD8:AcM-UBE2M binds CRL4 E3 ubiquitin ligase complex
CAND1 binds CRL4 E3 ubiquitin ligase in the nucleus
COMMDs displace CAND1 from CRL4 E3 ubiquitin ligase complex
COP9 signalosome deneddylates nuclear CRL4 E3 ubiquitin ligase complex
Falcon deep research report for DCAF11
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DCAF11/WDR23 is a CRL4 substrate receptor with multiple DCAF11-specific substrates reported in the primary literature, including NRF2 (DIDLID degron in the Neh2 domain), p21Cip1/CDKN1A (CRL4B-DCAF11, S-phase progression), and SLBP (phospho-dependent end-of-S-phase degradation); it has additionally been developed as a recruited E3 ligase for targeted protein degradation.
"DCAF11 (WDR23) is a multifunctional substrate receptor within the CRL4 E3 ubiquitin ligase complex that regulates diverse cellular processes including oxidative stress response, cell cycle progression, DNA damage repair, metabolic homeostasis, and host-pathogen interactions."