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Q86VP6

- CAND1_HUMAN

UniProt

Q86VP6 - CAND1_HUMAN

Protein

Cullin-associated NEDD8-dissociated protein 1

Gene

CAND1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    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.6 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: UniProtKB
    2. negative regulation of catalytic activity Source: UniProtKB
    3. positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: Ensembl
    4. protein ubiquitination Source: UniProtKB
    5. SCF complex assembly Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cullin-associated NEDD8-dissociated protein 1
    Alternative name(s):
    Cullin-associated and neddylation-dissociated protein 1
    TBP-interacting protein of 120 kDa A
    Short name:
    TBP-interacting protein 120A
    p120 CAND1
    Gene namesi
    Name:CAND1
    Synonyms:KIAA0829, TIP120, TIP120A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:30688. CAND1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Predominantly cytoplasmic.

    GO - Cellular componenti

    1. cullin-RING ubiquitin ligase complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. intracellular membrane-bounded organelle Source: HPA
    5. membrane Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142672207.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 12301229Cullin-associated NEDD8-dissociated protein 1PRO_0000089293Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei55 – 551N6-acetyllysine1 Publication
    Modified residuei335 – 3351Phosphoserine1 Publication
    Modified residuei971 – 9711N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ86VP6.
    PaxDbiQ86VP6.
    PRIDEiQ86VP6.

    PTM databases

    PhosphoSiteiQ86VP6.

    Expressioni

    Inductioni

    Repressed by miR-148a.1 Publication

    Gene expression databases

    ArrayExpressiQ86VP6.
    BgeeiQ86VP6.
    GenevestigatoriQ86VP6.

    Organism-specific databases

    HPAiHPA055748.

    Interactioni

    Subunit structurei

    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.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CUL1Q1361619EBI-456077,EBI-359390
    CUL2Q136173EBI-456077,EBI-456179
    CUL3Q136182EBI-456077,EBI-456129
    CUL4AQ136193EBI-456077,EBI-456106
    CUL4BQ136203EBI-456077,EBI-456067

    Protein-protein interaction databases

    BioGridi120937. 676 interactions.
    DIPiDIP-31608N.
    IntActiQ86VP6. 15 interactions.
    MINTiMINT-4999459.

    Structurei

    Secondary structure

    1
    1230
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 149
    Helixi20 – 3314
    Beta strandi35 – 373
    Helixi45 – 5612
    Helixi62 – 7615
    Helixi81 – 9414
    Beta strandi98 – 1003
    Helixi101 – 11616
    Helixi127 – 14216
    Helixi148 – 16417
    Turni170 – 1723
    Helixi173 – 1808
    Helixi181 – 1855
    Helixi189 – 20214
    Turni203 – 2053
    Helixi214 – 22411
    Helixi234 – 24411
    Helixi247 – 2493
    Helixi256 – 2649
    Turni269 – 2713
    Helixi272 – 28413
    Helixi291 – 30111
    Helixi348 – 36114
    Helixi368 – 3725
    Turni373 – 3753
    Helixi376 – 3805
    Beta strandi386 – 3883
    Helixi389 – 40517
    Helixi424 – 4318
    Helixi434 – 4429
    Helixi448 – 46417
    Turni466 – 4694
    Helixi470 – 4723
    Helixi473 – 48311
    Beta strandi487 – 4893
    Helixi491 – 50616
    Helixi510 – 5134
    Helixi514 – 5174
    Turni518 – 5203
    Helixi521 – 5288
    Helixi533 – 55018
    Beta strandi553 – 5553
    Helixi562 – 57615
    Beta strandi579 – 5813
    Helixi583 – 59917
    Helixi601 – 6033
    Helixi607 – 61812
    Beta strandi621 – 6233
    Helixi624 – 63512
    Helixi645 – 65814
    Helixi664 – 68017
    Helixi687 – 6948
    Helixi698 – 7003
    Helixi706 – 71914
    Helixi724 – 7296
    Turni730 – 7345
    Helixi735 – 7428
    Helixi749 – 76315
    Helixi772 – 7798
    Turni781 – 7855
    Helixi793 – 80917
    Helixi815 – 8184
    Turni819 – 8246
    Turni826 – 8294
    Helixi832 – 84817
    Helixi856 – 8638
    Helixi864 – 8663
    Helixi870 – 88617
    Helixi888 – 90013
    Helixi903 – 9053
    Helixi906 – 91813
    Turni923 – 9253
    Helixi926 – 93611
    Helixi947 – 96014
    Helixi963 – 9653
    Helixi967 – 9704
    Turni971 – 9733
    Beta strandi974 – 9774
    Helixi979 – 98810
    Helixi990 – 9923
    Helixi1001 – 10077
    Turni1009 – 10146
    Beta strandi1015 – 10195
    Helixi1021 – 103616
    Helixi1038 – 10403
    Helixi1042 – 10443
    Helixi1045 – 105410
    Helixi1060 – 10623
    Beta strandi1063 – 10686
    Beta strandi1071 – 10766
    Helixi1079 – 109416
    Beta strandi1098 – 11003
    Helixi1102 – 111110
    Helixi1117 – 113216
    Helixi1136 – 11394
    Turni1140 – 11456
    Helixi1146 – 11549
    Helixi1163 – 118220
    Beta strandi1190 – 11945
    Helixi1200 – 12089

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U6GX-ray3.10C1-1230[»]
    4A0CX-ray3.80A/B1-1230[»]
    ProteinModelPortaliQ86VP6.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86VP6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati2 – 3938HEAT 1Add
    BLAST
    Repeati44 – 8138HEAT 2Add
    BLAST
    Repeati83 – 11937HEAT 3Add
    BLAST
    Repeati131 – 16535HEAT 4Add
    BLAST
    Repeati171 – 20838HEAT 5Add
    BLAST
    Repeati210 – 24738HEAT 6Add
    BLAST
    Repeati248 – 28235HEAT 7Add
    BLAST
    Repeati289 – 36678HEAT 8Add
    BLAST
    Repeati370 – 40738HEAT 9Add
    BLAST
    Repeati424 – 46744HEAT 10Add
    BLAST
    Repeati471 – 51040HEAT 11Add
    BLAST
    Repeati515 – 55238HEAT 12Add
    BLAST
    Repeati563 – 60240HEAT 13Add
    BLAST
    Repeati606 – 64338HEAT 14Add
    BLAST
    Repeati646 – 68338HEAT 15Add
    BLAST
    Repeati688 – 72538HEAT 16Add
    BLAST
    Repeati729 – 76840HEAT 17Add
    BLAST
    Repeati770 – 80839HEAT 18Add
    BLAST
    Repeati809 – 84537HEAT 19Add
    BLAST
    Repeati852 – 88938HEAT 20Add
    BLAST
    Repeati890 – 92738HEAT 21Add
    BLAST
    Repeati928 – 96033HEAT 22Add
    BLAST
    Repeati961 – 99838HEAT 23Add
    BLAST
    Repeati1002 – 103938HEAT 24Add
    BLAST
    Repeati1043 – 109755HEAT 25Add
    BLAST
    Repeati1099 – 113335HEAT 26Add
    BLAST
    Repeati1140 – 118950HEAT 27Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi314 – 34431Asp-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CAND family.Curated
    Contains 27 HEAT repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG278162.
    HOVERGENiHBG053467.
    InParanoidiQ86VP6.
    KOiK17263.
    OMAiTRPAQSW.
    OrthoDBiEOG77HDCZ.
    PhylomeDBiQ86VP6.
    TreeFamiTF300355.

    Family and domain databases

    Gene3Di1.25.10.10. 2 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR013932. TATA-bd_TIP120.
    [Graphical view]
    PfamiPF08623. TIP120. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86VP6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV     50
    KMILKLLEDK NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE 100
    QLRDISSIGL KTVIGELPPA SSGSALAANV CKKITGRLTS AIAKQEDVSV 150
    QLEALDIMAD MLSRQGGLLV NFHPSILTCL LPQLTSPRLA VRKRTIIALG 200
    HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA ISRQAGHRIG 250
    EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI 300
    CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR 350
    RAAAKCLDAV VSTRHEMLPE FYKTVSPALI SRFKEREENV KADVFHAYLS 400
    LLKQTRPVQS WLCDPDAMEQ GETPLTMLQS QVPNIVKALH KQMKEKSVKT 450
    RQCCFNMLTE LVNVLPGALT QHIPVLVPGI IFSLNDKSSS SNLKIDALSC 500
    LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL LVTQQLVKVI 550
    RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL 600
    GDNLGSDLPN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE 650
    GVPILASFLR KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL 700
    ISESDMHVSQ MAISFLTTLA KVYPSSLSKI SGSILNELIG LVRSPLLQGG 750
    ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT GPVYSQSTAL THKQSYYSIA 800
    KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL SLGEVGHHID 850
    LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT 900
    SQPKRQYLLL HSLKEIISSA SVVGLKPYVE NIWALLLKHC ECAEEGTRNV 950
    VAECLGKLTL IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI 1000
    DPLLKNCIGD FLKTLEDPDL NVRRVALVTF NSAAHNKPSL IRDLLDTVLP 1050
    HLYNETKVRK ELIREVEMGP FKHTVDDGLD IRKAAFECMY TLLDSCLDRL 1100
    DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ RLDRLVEPLR 1150
    ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS 1200
    QISSNPELAA IFESIQKDSS STNLESMDTS 1230
    Length:1,230
    Mass (Da):136,376
    Last modified:June 7, 2005 - v2
    Checksum:iFE344558F72D79D8
    GO
    Isoform 2 (identifier: Q86VP6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         458-625: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,062
    Mass (Da):117,889
    Checksum:i2045EBFCEE84468B
    GO
    Isoform 3 (identifier: Q86VP6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-157: Missing.
         549-560: VIRPLDQPSSFD → AHHMPEAQWLRL
         561-1230: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:403
    Mass (Da):45,539
    Checksum:i4EC2B75A93D82663
    GO

    Sequence cautioni

    The sequence BAA74852.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAB55090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti272 – 2721R → K in BAB55365. (PubMed:14702039)Curated
    Sequence conflicti457 – 4571M → I in BAB55090. (PubMed:14702039)Curated
    Sequence conflicti606 – 6061S → P in AAF67492. (PubMed:10931946)Curated
    Sequence conflicti609 – 6091P → S in AAF67492. (PubMed:10931946)Curated
    Sequence conflicti1047 – 10471T → S in AAF67492. (PubMed:10931946)Curated
    Sequence conflicti1177 – 11771M → T in BAB55090. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti803 – 8031V → A.
    Corresponds to variant rs12580996 [ dbSNP | Ensembl ].
    VAR_054041
    Natural varianti952 – 9521A → V.1 Publication
    Corresponds to variant rs17854618 [ dbSNP | Ensembl ].
    VAR_025327

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 157157Missing in isoform 3. 1 PublicationVSP_013947Add
    BLAST
    Alternative sequencei458 – 625168Missing in isoform 2. 1 PublicationVSP_013948Add
    BLAST
    Alternative sequencei549 – 56012VIRPL…PSSFD → AHHMPEAQWLRL in isoform 3. 1 PublicationVSP_013949Add
    BLAST
    Alternative sequencei561 – 1230670Missing in isoform 3. 1 PublicationVSP_013950Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020636 mRNA. Translation: BAA74852.2. Different initiation.
    AF157326 mRNA. Translation: AAF67492.1.
    AL133560 mRNA. Translation: CAB63714.1.
    AL136810 mRNA. Translation: CAB66744.1.
    AL833880 mRNA. Translation: CAD38737.1.
    CH471054 Genomic DNA. Translation: EAW97172.1.
    BC004232 mRNA. Translation: AAH04232.1.
    BC026220 mRNA. Translation: AAH26220.1.
    BC050341 mRNA. Translation: AAH50341.1.
    AK027404 mRNA. Translation: BAB55090.1. Different initiation.
    AK027783 mRNA. Translation: BAB55365.1.
    AK314358 mRNA. Translation: BAG36990.1.
    CCDSiCCDS8977.1. [Q86VP6-1]
    PIRiT43441.
    RefSeqiNP_060918.2. NM_018448.3. [Q86VP6-1]
    UniGeneiHs.546407.

    Genome annotation databases

    EnsembliENST00000544619; ENSP00000444089; ENSG00000111530.
    ENST00000545606; ENSP00000442318; ENSG00000111530. [Q86VP6-1]
    GeneIDi55832.
    KEGGihsa:55832.
    UCSCiuc001stn.2. human. [Q86VP6-1]
    uc001sto.2. human. [Q86VP6-2]

    Polymorphism databases

    DMDMi67460541.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020636 mRNA. Translation: BAA74852.2 . Different initiation.
    AF157326 mRNA. Translation: AAF67492.1 .
    AL133560 mRNA. Translation: CAB63714.1 .
    AL136810 mRNA. Translation: CAB66744.1 .
    AL833880 mRNA. Translation: CAD38737.1 .
    CH471054 Genomic DNA. Translation: EAW97172.1 .
    BC004232 mRNA. Translation: AAH04232.1 .
    BC026220 mRNA. Translation: AAH26220.1 .
    BC050341 mRNA. Translation: AAH50341.1 .
    AK027404 mRNA. Translation: BAB55090.1 . Different initiation.
    AK027783 mRNA. Translation: BAB55365.1 .
    AK314358 mRNA. Translation: BAG36990.1 .
    CCDSi CCDS8977.1. [Q86VP6-1 ]
    PIRi T43441.
    RefSeqi NP_060918.2. NM_018448.3. [Q86VP6-1 ]
    UniGenei Hs.546407.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U6G X-ray 3.10 C 1-1230 [» ]
    4A0C X-ray 3.80 A/B 1-1230 [» ]
    ProteinModelPortali Q86VP6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120937. 676 interactions.
    DIPi DIP-31608N.
    IntActi Q86VP6. 15 interactions.
    MINTi MINT-4999459.

    PTM databases

    PhosphoSitei Q86VP6.

    Polymorphism databases

    DMDMi 67460541.

    Proteomic databases

    MaxQBi Q86VP6.
    PaxDbi Q86VP6.
    PRIDEi Q86VP6.

    Protocols and materials databases

    DNASUi 55832.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000544619 ; ENSP00000444089 ; ENSG00000111530 .
    ENST00000545606 ; ENSP00000442318 ; ENSG00000111530 . [Q86VP6-1 ]
    GeneIDi 55832.
    KEGGi hsa:55832.
    UCSCi uc001stn.2. human. [Q86VP6-1 ]
    uc001sto.2. human. [Q86VP6-2 ]

    Organism-specific databases

    CTDi 55832.
    GeneCardsi GC12P067663.
    HGNCi HGNC:30688. CAND1.
    HPAi HPA055748.
    MIMi 607727. gene.
    neXtProti NX_Q86VP6.
    PharmGKBi PA142672207.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278162.
    HOVERGENi HBG053467.
    InParanoidi Q86VP6.
    KOi K17263.
    OMAi TRPAQSW.
    OrthoDBi EOG77HDCZ.
    PhylomeDBi Q86VP6.
    TreeFami TF300355.

    Miscellaneous databases

    ChiTaRSi CAND1. human.
    EvolutionaryTracei Q86VP6.
    GeneWikii CAND1.
    GenomeRNAii 55832.
    NextBioi 61049.
    PROi Q86VP6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86VP6.
    Bgeei Q86VP6.
    Genevestigatori Q86VP6.

    Family and domain databases

    Gene3Di 1.25.10.10. 2 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR013932. TATA-bd_TIP120.
    [Graphical view ]
    Pfami PF08623. TIP120. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adrenal gland.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-952.
      Tissue: Cervix, Testis and Uterus.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Placenta.
    8. Bienvenut W.V., Ramsay A., Leung H.Y.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14 AND 374-382, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    9. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14; 535-548; 668-679; 730-743; 859-873; 958-969 AND 983-990, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    10. "CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex."
      Zheng J., Yang X., Harrell J.M., Ryzhikov S., Shim E.-H., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H.
      Mol. Cell 10:1519-1526(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1 AND RBX1.
    11. "NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases."
      Liu J., Furukawa M., Matsumoto T., Xiong Y.
      Mol. Cell 10:1511-1518(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1 AND RBX1, INTERACTION WITH UNNEDDYLATED CUL1; CUL4A AND CUL5.
    12. "TIP120A associates with cullins and modulates ubiquitin ligase activity."
      Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.
      J. Biol. Chem. 278:15905-15910(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B AND RBX1, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "CAND1-mediated substrate adaptor recycling is required for efficient repression of Nrf2 by Keap1."
      Lo S.C., Hannink M.
      Mol. Cell. Biol. 26:1235-1244(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CUL3.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-971, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "miR-148a is an androgen-responsive microRNA that promotes LNCaP prostate cell growth by repressing its target CAND1 expression."
      Murata T., Takayama K., Katayama S., Urano T., Horie-Inoue K., Ikeda K., Takahashi S., Kawazu C., Hasegawa A., Ouchi Y., Homma Y., Hayashizaki Y., Inoue S.
      Prostate Cancer Prostatic Dis. 13:356-361(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding."
      Mao X., Gluck N., Chen B., Starokadomskyy P., Li H., Maine G.N., Burstein E.
      J. Biol. Chem. 286:32355-32365(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CUL2.
    21. "Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo."
      Chua Y.S., Boh B.K., Ponyeam W., Hagen T.
      PLoS ONE 6:E16071-E16071(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CUL2; CUL3; CUL4A AND CUL5, SUBCELLULAR LOCATION.
    22. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins."
      Pierce N.W., Lee J.E., Liu X., Sweredoski M.J., Graham R.L., Larimore E.A., Rome M., Zheng N., Clurman B.E., Hess S., Shan S.O., Deshaies R.J.
      Cell 153:206-215(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, REACTION MECHANISM.
    25. "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases."
      Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J., Xiong Y., Zheng N.
      Cell 119:517-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CUL1 AND RBX1.
    26. "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation."
      Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M., Faty M., Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S., Gut H., Sugasawa K., Thoma N.H.
      Cell 147:1024-1039(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEX WITH CUL4B AND RBX1.

    Entry informationi

    Entry nameiCAND1_HUMAN
    AccessioniPrimary (citable) accession number: Q86VP6
    Secondary accession number(s): B2RAU3
    , O94918, Q6PIY4, Q8NDJ4, Q96JZ9, Q96T19, Q9BTC4, Q9H0G2, Q9P0H7, Q9UF85
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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