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Details on Person UniProt:Q86VP6 CAND1

Class:IdReferenceGeneProduct:221237
_chainChangeLoginitiator methionine:1 added on Fri February 6 2015;chain:2-1230 added on Fri February 6 2015;initiator methionine:1 for 221237 removed on Fri Nov 03 2023;initiator methionine: for 221237 added on Fri Nov 03 2023;initiator methionine: for 221237 removed on Fri Aug 15 2025;initiator methionine:1 for 221237 added on Fri Aug 15 2025
_displayNameUniProt:Q86VP6 CAND1
_timestamp2025-08-15 21:51:35
chaininitiator methionine:1
chain:2-1230
checksumFE344558F72D79D8
commentFUNCTION Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes.SUBUNIT Interacts with TBP (By similarity). Part of a complex that contains CUL1 and RBX1. Interacts with unneddylated cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5. Does not bind neddylated CUL1. Interaction with cullins is abolished in presence of COMMD1, which antagonizes with CAND1 for interacting with cullins. Interacts with ERCC6 (PubMed:26030138). Interacts with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5; these interactions are bridged by cullins and strongly inhibits the neddylation of cullins (PubMed:24192928, PubMed:25349211, PubMed:26906416).INTERACTION Predominantly cytoplasmic.ALTERNATIVE PRODUCTS Repressed by miR-148a.MISCELLANEOUS A model has been proposed to explain the mechanisms of cullin-RING E3 ubiquitin ligase complexes assembly. According to this hypothesis, cullin-RING E3 ubiquitin ligase complexes exist in a 'stable' active state when saturated with substrate, occluding access to deneddylation by the COP9 signalosome (CSN) complex. The neddylation-conjugated cullin-RING E3 ubiquitin ligase complexes mediate ubiquitination of substrates and can recruit downstream factors involved in substrate degradation. Depletion of the substrate promotes the ability of CSN to bind the cullin-RING E3 ubiquitin ligase complex and mediate deneddylation. In this 'intermediate' deneddylated state, the complex can bind CAND1 and enter the 'exchange' state, resulting in high increase in dissociation rate of the substrate-recognition subunit. The resulting CAND1-cullin-RING complex rapidly assembles with another available substrate-recognition subunit to form an unstable ternary intermediate and yield a new cullin-RING E3 ubiquitin ligase complex. Subsequent neddylation of the cullin, which is stabilized by substrate, completes the cycle (PubMed:23453757).SIMILARITY Belongs to the CAND family.SEQUENCE CAUTION Extended N-terminus.SEQUENCE CAUTION Truncated N-terminus.
created[InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53
descriptionrecommendedName: Cullin-associated NEDD8-dissociated protein 1 alternativeName: Cullin-associated and neddylation-dissociated protein 1 alternativeName: TBP-interacting protein of 120 kDa A shortName: TBP-interacting protein 120A alternativeName: p120 CAND1
geneNameCAND1
KIAA0829
TIP120
TIP120A
identifierQ86VP6
isSequenceChangedFALSE
keyword3D-structure
Acetylation
Alternative splicing
Cytoplasm
Direct protein sequencing
Nucleus
Phosphoprotein
Proteomics identification
Reference proteome
Repeat
Ubl conjugation pathway
modified[InstanceEdit:9836292] Weiser, Joel, 2023-05-25
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
[InstanceEdit:9917590] Weiser, Joel, 2024-08-09
[InstanceEdit:9926675] Weiser, Joel, 2024-11-03
[InstanceEdit:9963647] Weiser, Joel, 2025-08-15
nameCAND1
referenceDatabase[ReferenceDatabase:2] UniProt
referenceGene[ReferenceDNASequence:8958083] ENSEMBL:ENSG00000111530 CAND1 [Homo sapiens]
secondaryIdentifierCAND1_HUMAN
B2RAU3
O94918
Q6PIY4
Q8NDJ4
Q96JZ9
Q96T19
Q9BTC4
Q9H0G2
Q9P0H7
Q9UF85
sequenceLength1230
species[Species:48887] Homo sapiens
(isoformParent)[ReferenceIsoform:221238] UniProt:Q86VP6-2 CAND1 [Homo sapiens]
[ReferenceIsoform:221239] UniProt:Q86VP6-3 CAND1 [Homo sapiens]
[ReferenceIsoform:409881] UniProt:Q86VP6-1 CAND1 [Homo sapiens]
(referenceEntity)[EntityWithAccessionedSequence:5691146] CAND1 [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:6801390] CAND1 [secretory granule lumen] [Homo sapiens]
[EntityWithAccessionedSequence:6801399] CAND1 [ficolin-1-rich granule lumen] [Homo sapiens]
[EntityWithAccessionedSequence:6801558] CAND1 [extracellular exosome] [Homo sapiens]
[EntityWithAccessionedSequence:6806498] CAND1 [extracellular region] [Homo sapiens]
[EntityWithAccessionedSequence:8955089] CAND1 [nucleoplasm] [Homo sapiens]
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