Cullin-associated NEDD8-dissociated protein 1

CAND1 (Cullin-associated NEDD8-dissociated protein 1) is a key assembly factor in SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes (UniProt: Q86VP6). It functions as an F-box protein exchange factor, promoting substrate-recognition subunit turnover within SCF and likely other cullin-RING complexes through coupling with neddylation cycles. In its deneddylated state, CAND1 binds cullin-RBX1 to increase SCF complex dissociation and facilitate F-box protein exchange, thereby modulating the cellular repertoire of E3 ligase specificities.

No tissue-specific or pathway associations are annotated in UniProt for CAND1, and no primary disease associations are listed in the UniProt record (UniProt: Q86VP6).

CAND1 is associated with Alzheimer's Disease in this curated dataset. According to Chaparral AD proteomics analysis of post-mortem AD brain versus age-matched controls, CAND1 is upregulated with a mean log2 fold-change of +0.18 across one subcellular fraction from TMT-labeled, data-dependent acquisition proteomics. This modest elevation may reflect altered ubiquitin ligase dynamics in AD neuropathology, though the functional significance remains to be elucidated.