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Overview

Uniprot IDQ86VP6
Protein NameCullin-associated NEDD8-dissociated protein 1
Gene NameCAND1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1163 KVKANSVKQEFEKQD
574 DLFTCTIKRLKAADI
577 TCTIKRLKAADIDQE
60 ILKLLEDKNGEVQNL
971 ETLLPRLKGYLISGS

Function

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

Protein Sequence

10 MASASYHISN 20 LLEKMTSSDK 30 DFRFMATNDL 40 MTELQKDSIK 50 LDDDSERKVV 60 KMILKLLEDK 70 NGEVQNLAVK 80 CLGPLVSKVK 90 EYQVETIVDT 100 LCTNMLSDKE 110 QLRDISSIGL 120 KTVIGELPPA 130 SSGSALAANV 140 CKKITGRLTS 150 AIAKQEDVSV 160 QLEALDIMAD 170 MLSRQGGLLV 180 NFHPSILTCL 190 LPQLTSPRLA 200 VRKRTIIALG 210 HLVMSCGNIV 220 FVDLIEHLLS 230 ELSKNDSMST 240 TRTYIQCIAA 250 ISRQAGHRIG 260 EYLEKIIPLV 270 VKFCNVDDDE 280 LREYCIQAFE 290 SFVRRCPKEV 300 YPHVSTIINI 310 CLKYLTYDPN 320 YNYDDEDEDE 330 NAMDADGGDD 340 DDQGSDDEYS 350 DDDDMSWKVR 360 RAAAKCLDAV 370 VSTRHEMLPE 380 FYKTVSPALI 390 SRFKEREENV 400 KADVFHAYLS 410 LLKQTRPVQS 420 WLCDPDAMEQ 430 GETPLTMLQS 440 QVPNIVKALH 450 KQMKEKSVKT 460 RQCCFNMLTE 470 LVNVLPGALT 480 QHIPVLVPGI 490 IFSLNDKSSS 500 SNLKIDALSC 510 LYVILCNHSP 520 QVFHPHVQAL 530 VPPVVACVGD 540 PFYKITSEAL 550 LVTQQLVKVI 560 RPLDQPSSFD 570 ATPYIKDLFT 580 CTIKRLKAAD 590 IDQEVKERAI 600 SCMGQIICNL 610 GDNLGSDLPN 620 TLQIFLERLK 630 NEITRLTTVK 640 ALTLIAGSPL 650 KIDLRPVLGE 660 GVPILASFLR 670 KNQRALKLGT 680 LSALDILIKN 690 YSDSLTAAMI 700 DAVLDELPPL 710 ISESDMHVSQ 720 MAISFLTTLA 730 KVYPSSLSKI 740 SGSILNELIG 750 LVRSPLLQGG 760 ALSAMLDFFQ 770 ALVVTGTNNL 780 GYMDLLRMLT 790 GPVYSQSTAL 800 THKQSYYSIA 810 KCVAALTRAC 820 PKEGPAVVGQ 830 FIQDVKNSRS 840 TDSIRLLALL 850 SLGEVGHHID 860 LSGQLELKSV 870 ILEAFSSPSE 880 EVKSAASYAL 890 GSISVGNLPE 900 YLPFVLQEIT 910 SQPKRQYLLL 920 HSLKEIISSA 930 SVVGLKPYVE 940 NIWALLLKHC 950 ECAEEGTRNV 960 VAECLGKLTL 970 IDPETLLPRL 980 KGYLISGSSY 990 ARSSVVTAVK 1000 FTISDHPQPI 1010 DPLLKNCIGD 1020 FLKTLEDPDL 1030 NVRRVALVTF 1040 NSAAHNKPSL 1050 IRDLLDTVLP 1060 HLYNETKVRK 1070 ELIREVEMGP 1080 FKHTVDDGLD 1090 IRKAAFECMY 1100 TLLDSCLDRL 1110 DIFEFLNHVE 1120 DGLKDHYDIK 1130 MLTFLMLVRL 1140 STLCPSAVLQ 1150 RLDRLVEPLR 1160 ATCTTKVKAN 1170 SVKQEFEKQD 1180 ELKRSAMRAV 1190 AALLTIPEAE 1200 KSPLMSEFQS 1210 QISSNPELAA 1220 IFESIQKDSS 1230 STNLESMDTS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0031461 cullin-RING ubiquitin ligase complex
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0034774 secretory granule lumen
Cellular Component GO:0000151 ubiquitin ligase complex
Molecular Function GO:0017025 TBP-class protein binding
Biological Process GO:0030154 cell differentiation
Biological Process GO:0043086 negative regulation of catalytic activity
Biological Process GO:0045899 positive regulation of RNA polymerase II transcription preinitiation complex assembly
Biological Process GO:0016567 protein ubiquitination
Biological Process GO:0010265 SCF complex assembly

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.