Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1.
Network organization of the human autophagy system.
A proteome-scale map of the human interactome network.
Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15.
Structural insights into DDA1 function as a core component of the CRL4-DDB1 ubiquitin ligase.
Systematic identification of cancer cell vulnerabilities to natural killer cell-mediated immune surveillance.
Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15.
Aryl Sulfonamides Degrade RBM39 and RBM23 by Recruitment to CRL4-DCAF15.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Falcon deep research report for human DDA1
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DDA1 binds DDB1 with high affinity through a conserved extreme N-terminal segment (~first 28 residues) that docks into a groove on the BPA beta-propeller of DDB1, defining its anchoring mechanism within CRL4 ligases.
"Shabek et al. mapped DDB1 binding to a conserved **N-terminal 28-aa segment** (DDA1-NT), solved the **DDB1–DDA1-NT crystal structure at ~3.1 Å**, and localized binding to a groove on the **BPA propeller** of DDB1"
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DDA1 is best supported as a small structural/regulatory subunit of DDB1-CUL4 ligases rather than an enzyme, modulating ligase architecture and ubiquitination output in a context-dependent manner.
"DDA1 is not an enzyme** (no independent catalytic reaction is described). Instead, it is best supported as a **small structural/regulatory subunit** of certain DDB1–CUL4 E3 ligase assemblies that can modulate ligase architecture and ubiquitination output in a **context-dependent** manner"
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DDA1 is an integral component of CRL4(CSA) that coordinates ubiquitination dynamics during transcription-coupled nucleotide excision repair (TC-NER) and is required for efficient repair turnover/progression.
"DDA1 was identified as a **CSA interactor** by single-step complex isolation/MS and shown by cryo-EM to be an **integral CRL4CSA component**; functionally, DDA1 was concluded to **coordinate ubiquitination dynamics during TC-NER** and be **required for efficient turnover/progression** of the repair process"
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DDA1 provides a modest but reproducible thermal stabilization of the CSA-DDB1 module, with stabilization driven mainly by DDA1-DDB1 contacts.
"DDA1 provided a modest, reproducible **~1 °C** thermal stabilization of CSA–DDB1 measured by nanoDSF, and truncation removing a CSA-interacting helix had a similar stabilization, implying stabilization is driven mainly by **DDA1–DDB1** contacts"
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