Details for: CAND1

Gene ID: 55832

Symbol: CAND1

Ensembl ID: ENSG00000111530

Description: cullin associated and neddylation dissociated 1

Associated with

Other Information

Genular Protein ID: 1991515818

Symbol: CAND1_HUMAN

Name: Cullin-associated NEDD8-dissociated protein 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 10048485

Title: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.

PubMed ID: 10048485

DOI: 10.1093/dnares/5.6.355

PubMed ID: 10931946

Title: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.

PubMed ID: 10931946

DOI: 10.1073/pnas.160270997

PubMed ID: 11230166

Title: Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.

PubMed ID: 11230166

DOI: 10.1101/gr.gr1547r

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 12504026

Title: CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex.

PubMed ID: 12504026

DOI: 10.1016/s1097-2765(02)00784-0

PubMed ID: 12504025

Title: NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases.

PubMed ID: 12504025

DOI: 10.1016/s1097-2765(02)00783-9

PubMed ID: 12609982

Title: TIP120A associates with cullins and modulates ubiquitin ligase activity.

PubMed ID: 12609982

DOI: 10.1074/jbc.m213070200

PubMed ID: 16449638

Title: CAND1-mediated substrate adaptor recycling is required for efficient repression of Nrf2 by Keap1.

PubMed ID: 16449638

DOI: 10.1128/mcb.26.4.1235-1244.2006

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20820187

Title: miR-148a is an androgen-responsive microRNA that promotes LNCaP prostate cell growth by repressing its target CAND1 expression.

PubMed ID: 20820187

DOI: 10.1038/pcan.2010.32

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21778237

Title: COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding.

PubMed ID: 21778237

DOI: 10.1074/jbc.m111.278408

PubMed ID: 21249194

Title: Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo.

PubMed ID: 21249194

DOI: 10.1371/journal.pone.0016071

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23453757

Title: Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.

PubMed ID: 23453757

DOI: 10.1016/j.cell.2013.02.024

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24192928

Title: Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity and nuclear localization.

PubMed ID: 24192928

DOI: 10.1158/1078-0432.ccr-13-1252

PubMed ID: 25349211

Title: SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1).

PubMed ID: 25349211

DOI: 10.1074/jbc.m114.585505

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26030138

Title: Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin Dynamics.

PubMed ID: 26030138

DOI: 10.1371/journal.pone.0128558

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 26906416

Title: Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.

PubMed ID: 26906416

DOI: 10.1242/jcs.181784

PubMed ID: 15537541

Title: Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases.

PubMed ID: 15537541

DOI: 10.1016/j.cell.2004.10.019

PubMed ID: 22118460

Title: The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation.

PubMed ID: 22118460

DOI: 10.1016/j.cell.2011.10.035

Sequence Information:

  • Length: 1230
  • Mass: 136376
  • Checksum: FE344558F72D79D8
  • Sequence:
  • MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILKLLEDK 
    NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE QLRDISSIGL KTVIGELPPA 
    SSGSALAANV CKKITGRLTS AIAKQEDVSV QLEALDIMAD MLSRQGGLLV NFHPSILTCL 
    LPQLTSPRLA VRKRTIIALG HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA 
    ISRQAGHRIG EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI 
    CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR RAAAKCLDAV 
    VSTRHEMLPE FYKTVSPALI SRFKEREENV KADVFHAYLS LLKQTRPVQS WLCDPDAMEQ 
    GETPLTMLQS QVPNIVKALH KQMKEKSVKT RQCCFNMLTE LVNVLPGALT QHIPVLVPGI 
    IFSLNDKSSS SNLKIDALSC LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL 
    LVTQQLVKVI RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL 
    GDNLGSDLPN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE GVPILASFLR 
    KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL ISESDMHVSQ MAISFLTTLA 
    KVYPSSLSKI SGSILNELIG LVRSPLLQGG ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT 
    GPVYSQSTAL THKQSYYSIA KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL 
    SLGEVGHHID LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT 
    SQPKRQYLLL HSLKEIISSA SVVGLKPYVE NIWALLLKHC ECAEEGTRNV VAECLGKLTL 
    IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI DPLLKNCIGD FLKTLEDPDL 
    NVRRVALVTF NSAAHNKPSL IRDLLDTVLP HLYNETKVRK ELIREVEMGP FKHTVDDGLD 
    IRKAAFECMY TLLDSCLDRL DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ 
    RLDRLVEPLR ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS 
    QISSNPELAA IFESIQKDSS STNLESMDTS

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.