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Q13616

- CUL1_HUMAN

UniProt

Q13616 - CUL1_HUMAN

Protein

Cullin-1

Gene

CUL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (14 Aug 2001)
      Previous versions | rss
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    Functioni

    Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and exchange of the substrate recognition component is mediated by TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO1) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) direct ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2.8 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. cell cycle arrest Source: ProtInc
    3. cell proliferation Source: Ensembl
    4. G1/S transition of mitotic cell cycle Source: Reactome
    5. G2/M transition of mitotic cell cycle Source: Reactome
    6. intrinsic apoptotic signaling pathway Source: ProtInc
    7. mitotic cell cycle Source: Reactome
    8. negative regulation of cell proliferation Source: ProtInc
    9. Notch signaling pathway Source: Reactome
    10. organ morphogenesis Source: Ensembl
    11. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    12. protein monoubiquitination Source: Ensembl
    13. protein ubiquitination Source: UniProtKB
    14. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    15. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    16. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_115697. Prolactin receptor signaling.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_160305. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_22442. Interleukin-1 signaling.
    REACT_24941. Circadian Clock.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_821. Cyclin D associated events in G1.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    SignaLinkiQ13616.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cullin-1
    Short name:
    CUL-1
    Gene namesi
    Name:CUL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:2551. CUL1.

    Subcellular locationi

    GO - Cellular componenti

    1. cullin-RING ubiquitin ligase complex Source: MGI
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. SCF ubiquitin ligase complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27047.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 776776Cullin-1PRO_0000119787Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki708 – 708Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki720 – 720Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)

    Post-translational modificationi

    Neddylated; which enhances the ubiquitination activity of SCF and prevents binding of the inhibitor CAND1. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. Deneddylated by Epstein-Barr virus BPLF1 leading to a S-phase-like environment that is required for efficient replication of the viral genome.5 Publications

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ13616.
    PaxDbiQ13616.
    PeptideAtlasiQ13616.
    PRIDEiQ13616.

    PTM databases

    PhosphoSiteiQ13616.

    Expressioni

    Tissue specificityi

    Expressed in lung fibroblasts.1 Publication

    Gene expression databases

    ArrayExpressiQ13616.
    BgeeiQ13616.
    CleanExiHS_CUL1.
    GenevestigatoriQ13616.

    Organism-specific databases

    HPAiCAB002676.
    HPA050796.

    Interactioni

    Subunit structurei

    Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein as substrate-specific subunit. Component of the SCF(FBXW11) complex containing FBXW11. Component of the SCF(SKP2) complex containing SKP2, in which it interacts directly with SKP1, SKP2 and RBX1. Component of the SCF(FBXW2) complex containing FBXw2. Component of the SCF(FBXO32) complex containing FBXO32. Component of the probable SCF(FBXO7) complex containing FBXO7. Component of the SCF(FBXO10) complex containing FBXO10. Component of the SCF(FBXO11) complex containing FBXO11. Component of the SCF(FBXO25) complex containing FBXO25. Component of the SCF(FBXO33) complex containing FBXO33. Component of the probable SCF(FBXO4) complex containing FBXO4. Component of the SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC. This complex binds phosphorylated NFKBIA. Part of a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Component of the SCF(FBXO17) complex, composed of SKP1, CUL1 and FBXO17. Component of the SCF(FBXO27) complex, composed of SKP1, CUL1 and FBXO27. Component of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF. Component of the SCF(FBXL3) complex composed of CUL1, SKP1, RBX1 and FBXL3. Component of the SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21. Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and FBXW7. Interacts with CHEK2; mediates CHEK2 ubiquitination and regulates its function. Part of a complex with TIP120A/CAND1 and RBX1. The unneddylated form interacts with TIP120A/CAND1 and the interaction mediates the exchange of the F-box substrate-specific subunit. Can self-associate. Interacts with FBXW8. Interacts with RNF7. Interacts with CUL7; the interaction seems to be mediated by FBXW8. Interacts with TRIM21. Interacts with COPS2. Interacts with Epstein-Barr virus BPLF1. Interacts with human adenovirus early E1A protein; this interaction inhibits RBX1-CUL1-dependent elongation reaction of ubiquitin chains by the SCF(FBXW7) complex.22 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BTRCQ9Y2975EBI-359390,EBI-307461
    CAND1Q86VP619EBI-359390,EBI-456077
    CCNYQ8ND763EBI-359390,EBI-1049189
    CDC34P494273EBI-359390,EBI-975634
    Fbxl21Q8BFZ43EBI-359390,EBI-6898235From a different organism.
    Fbxl3Q8C4V43EBI-359390,EBI-1266589From a different organism.
    FBXO4Q9UKT52EBI-359390,EBI-960409
    FBXW11Q9UKB12EBI-359390,EBI-355189
    m005RQ837305EBI-359390,EBI-6859930From a different organism.
    MDM2Q009873EBI-359390,EBI-389668
    NEDD8Q158435EBI-359390,EBI-716247
    RBX1P6287712EBI-359390,EBI-398523
    SKP1P632089EBI-359390,EBI-307486
    SKP2Q133099EBI-359390,EBI-456291
    UBE2MP610812EBI-359390,EBI-1041660

    Protein-protein interaction databases

    BioGridi114032. 670 interactions.
    DIPiDIP-17013N.
    IntActiQ13616. 62 interactions.
    MINTiMINT-120495.
    STRINGi9606.ENSP00000326804.

    Structurei

    Secondary structure

    1
    776
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 3114
    Turni32 – 343
    Helixi39 – 5214
    Helixi87 – 10519
    Turni106 – 1094
    Turni111 – 1144
    Helixi115 – 13622
    Helixi138 – 1436
    Beta strandi144 – 1463
    Helixi159 – 1657
    Helixi168 – 1714
    Turni172 – 1776
    Helixi178 – 18710
    Turni188 – 1903
    Helixi199 – 21012
    Turni211 – 2133
    Beta strandi215 – 2195
    Helixi226 – 2316
    Helixi233 – 25422
    Helixi261 – 27313
    Turni274 – 2796
    Beta strandi281 – 2844
    Helixi285 – 29511
    Beta strandi296 – 3005
    Helixi301 – 31212
    Helixi318 – 32811
    Helixi333 – 35523
    Helixi359 – 3613
    Helixi363 – 38220
    Turni383 – 3875
    Helixi389 – 40416
    Helixi407 – 4126
    Helixi417 – 43014
    Helixi439 – 45315
    Helixi459 – 47517
    Helixi482 – 52544
    Turni526 – 5283
    Beta strandi532 – 54110
    Turni542 – 5443
    Helixi557 – 5593
    Helixi560 – 56910
    Turni570 – 5734
    Beta strandi579 – 5813
    Helixi583 – 5853
    Beta strandi589 – 5979
    Beta strandi600 – 6023
    Helixi605 – 6128
    Helixi613 – 6153
    Beta strandi616 – 6216
    Helixi622 – 6287
    Helixi633 – 64513
    Turni646 – 6483
    Beta strandi652 – 6543
    Turni658 – 6603
    Beta strandi668 – 6714
    Beta strandi678 – 6825
    Helixi691 – 70010
    Helixi703 – 72220
    Beta strandi723 – 7264
    Helixi727 – 73812
    Turni739 – 7413
    Helixi746 – 75813
    Beta strandi761 – 7655
    Beta strandi768 – 7747

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LDJX-ray3.00A17-776[»]
    1LDKX-ray3.10A15-410[»]
    B411-776[»]
    1U6GX-ray3.10A1-776[»]
    3RTRX-ray3.21A/C/E/G411-776[»]
    3TDUX-ray1.50C/D702-776[»]
    3TDZX-ray2.00C/D702-776[»]
    4F52X-ray3.00A/C411-690[»]
    ProteinModelPortaliQ13616.
    SMRiQ13616. Positions 17-776.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13616.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cullin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5647.
    HOGENOMiHOG000176713.
    HOVERGENiHBG106177.
    InParanoidiQ13616.
    KOiK03347.
    OMAiNEAFNGE.
    OrthoDBiEOG7X3QQG.
    PhylomeDBiQ13616.
    TreeFamiTF101151.

    Family and domain databases

    Gene3Di1.10.10.10. 2 hits.
    InterProiIPR016157. Cullin_CS.
    IPR016158. Cullin_homology.
    IPR001373. Cullin_N.
    IPR019559. Cullin_neddylation_domain.
    IPR016159. Cullin_repeat-like_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00888. Cullin. 1 hit.
    PF10557. Cullin_Nedd8. 1 hit.
    [Graphical view]
    SMARTiSM00182. CULLIN. 1 hit.
    SM00884. Cullin_Nedd8. 1 hit.
    [Graphical view]
    SUPFAMiSSF74788. SSF74788. 1 hit.
    SSF75632. SSF75632. 1 hit.
    PROSITEiPS01256. CULLIN_1. 1 hit.
    PS50069. CULLIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q13616-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSTRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY    50
    NYCTSVHQSN QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL 100
    TNLLKDGEDL MDESVLKFYT QQWEDYRFSS KVLNGICAYL NRHWVRRECD 150
    EGRKGIYEIY SLALVTWRDC LFRPLNKQVT NAVLKLIEKE RNGETINTRL 200
    ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT ERFYTRESTE 250
    FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL 300
    EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA 350
    AIEKCGEAAL NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG 400
    RFINNNAVTK MAQSSSKSPE LLARYCDSLL KKSSKNPEEA ELEDTLNQVM 450
    VVFKYIEDKD VFQKFYAKML AKRLVHQNSA SDDAEASMIS KLKQACGFEY 500
    TSKLQRMFQD IGVSKDLNEQ FKKHLTNSEP LDLDFSIQVL SSGSWPFQQS 550
    CTFALPSELE RSYQRFTAFY ASRHSGRKLT WLYQLSKGEL VTNCFKNRYT 600
    LQASTFQMAI LLQYNTEDAY TVQQLTDSTQ IKMDILAQVL QILLKSKLLV 650
    LEDENANVDE VELKPDTLIK LYLGYKNKKL RVNINVPMKT EQKQEQETTH 700
    KNIEEDRKLL IQAAIVRIMK MRKVLKHQQL LGEVLTQLSS RFKPRVPVIK 750
    KCIDILIEKE YLERVDGEKD TYSYLA 776
    Length:776
    Mass (Da):89,679
    Last modified:August 14, 2001 - v2
    Checksum:i6625A1FFA7799BBA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 8224Missing in AAC50544. (PubMed:8681378)CuratedAdd
    BLAST
    Sequence conflicti726 – 7261K → R in CAD97651. (PubMed:17974005)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58087 mRNA. Translation: AAC50544.1.
    AF062536 mRNA. Translation: AAC36681.1.
    BX537409 mRNA. Translation: CAD97651.1.
    AC005229 Genomic DNA. Translation: AAM49153.1.
    CH471146 Genomic DNA. Translation: EAW80074.1.
    BC125119 mRNA. Translation: AAI25120.1.
    BC125120 mRNA. Translation: AAI25121.1.
    CCDSiCCDS34772.1.
    RefSeqiNP_003583.2. NM_003592.2.
    XP_005250117.1. XM_005250060.2.
    UniGeneiHs.146806.

    Genome annotation databases

    EnsembliENST00000325222; ENSP00000326804; ENSG00000055130.
    ENST00000409469; ENSP00000387160; ENSG00000055130.
    ENST00000602748; ENSP00000473318; ENSG00000055130.
    GeneIDi8454.
    KEGGihsa:8454.
    UCSCiuc003wey.3. human.

    Polymorphism databases

    DMDMi19863257.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58087 mRNA. Translation: AAC50544.1 .
    AF062536 mRNA. Translation: AAC36681.1 .
    BX537409 mRNA. Translation: CAD97651.1 .
    AC005229 Genomic DNA. Translation: AAM49153.1 .
    CH471146 Genomic DNA. Translation: EAW80074.1 .
    BC125119 mRNA. Translation: AAI25120.1 .
    BC125120 mRNA. Translation: AAI25121.1 .
    CCDSi CCDS34772.1.
    RefSeqi NP_003583.2. NM_003592.2.
    XP_005250117.1. XM_005250060.2.
    UniGenei Hs.146806.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LDJ X-ray 3.00 A 17-776 [» ]
    1LDK X-ray 3.10 A 15-410 [» ]
    B 411-776 [» ]
    1U6G X-ray 3.10 A 1-776 [» ]
    3RTR X-ray 3.21 A/C/E/G 411-776 [» ]
    3TDU X-ray 1.50 C/D 702-776 [» ]
    3TDZ X-ray 2.00 C/D 702-776 [» ]
    4F52 X-ray 3.00 A/C 411-690 [» ]
    ProteinModelPortali Q13616.
    SMRi Q13616. Positions 17-776.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114032. 670 interactions.
    DIPi DIP-17013N.
    IntActi Q13616. 62 interactions.
    MINTi MINT-120495.
    STRINGi 9606.ENSP00000326804.

    PTM databases

    PhosphoSitei Q13616.

    Polymorphism databases

    DMDMi 19863257.

    Proteomic databases

    MaxQBi Q13616.
    PaxDbi Q13616.
    PeptideAtlasi Q13616.
    PRIDEi Q13616.

    Protocols and materials databases

    DNASUi 8454.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325222 ; ENSP00000326804 ; ENSG00000055130 .
    ENST00000409469 ; ENSP00000387160 ; ENSG00000055130 .
    ENST00000602748 ; ENSP00000473318 ; ENSG00000055130 .
    GeneIDi 8454.
    KEGGi hsa:8454.
    UCSCi uc003wey.3. human.

    Organism-specific databases

    CTDi 8454.
    GeneCardsi GC07P148395.
    HGNCi HGNC:2551. CUL1.
    HPAi CAB002676.
    HPA050796.
    MIMi 603134. gene.
    neXtProti NX_Q13616.
    PharmGKBi PA27047.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5647.
    HOGENOMi HOG000176713.
    HOVERGENi HBG106177.
    InParanoidi Q13616.
    KOi K03347.
    OMAi NEAFNGE.
    OrthoDBi EOG7X3QQG.
    PhylomeDBi Q13616.
    TreeFami TF101151.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_115697. Prolactin receptor signaling.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_160305. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_22442. Interleukin-1 signaling.
    REACT_24941. Circadian Clock.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_821. Cyclin D associated events in G1.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    SignaLinki Q13616.

    Miscellaneous databases

    ChiTaRSi CUL1. human.
    EvolutionaryTracei Q13616.
    GeneWikii CUL1.
    GenomeRNAii 8454.
    NextBioi 31638.
    PROi Q13616.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13616.
    Bgeei Q13616.
    CleanExi HS_CUL1.
    Genevestigatori Q13616.

    Family and domain databases

    Gene3Di 1.10.10.10. 2 hits.
    InterProi IPR016157. Cullin_CS.
    IPR016158. Cullin_homology.
    IPR001373. Cullin_N.
    IPR019559. Cullin_neddylation_domain.
    IPR016159. Cullin_repeat-like_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00888. Cullin. 1 hit.
    PF10557. Cullin_Nedd8. 1 hit.
    [Graphical view ]
    SMARTi SM00182. CULLIN. 1 hit.
    SM00884. Cullin_Nedd8. 1 hit.
    [Graphical view ]
    SUPFAMi SSF74788. SSF74788. 1 hit.
    SSF75632. SSF75632. 1 hit.
    PROSITEi PS01256. CULLIN_1. 1 hit.
    PS50069. CULLIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family."
      Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.
      Cell 85:829-839(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Human CUL-1, but not other cullin family members, selectively interacts with SKP1 to form a complex with SKP2 and cyclin A."
      Michel J.J., Xiong Y.
      Cell Growth Differ. 9:435-449(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Endometrium.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
    7. "Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha."
      Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q.
      Mol. Cell 3:527-533(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBX1, IDENTIFICATION IN SCF COMPLEX WITH RBX1; SKP1 AND SKP2.
    8. "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity."
      Ohta T., Michel J.J., Schottelius A.J., Xiong Y.
      Mol. Cell 3:535-541(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBX1 AND RNF7.
    9. "Covalent modification of all members of human cullin family proteins by NEDD8."
      Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N., Kato S., Tanaka K.
      Oncogene 18:6829-6834(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NEDDYLATION AT LYS-720.
    10. "Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha."
      Read M.A., Brownell J.E., Gladysheva T.B., Hottelet M., Parent L.A., Coggins M.B., Pierce J.W., Podust V.N., Luo R.-S., Chau V., Palombella V.J.
      Mol. Cell. Biol. 20:2326-2333(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NEDDYLATION.
    11. "Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth, but not for germination: chip profiling implicates its role in cell cycle regulation."
      Swaroop M., Wang Y., Miller P., Duan H., Jatkoe T., Madore S.J., Sun Y.
      Oncogene 19:2855-2866(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF7.
    12. Cited for: INTERACTION WITH COPS2.
    13. "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: INTERACTION WITH TIP120A.
    14. "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: INTERACTION WITH TIP120A.
    15. "Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region."
      Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.
      J. Biol. Chem. 279:32592-32602(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SCF(FBXO7) COMPLEX.
    16. Cited for: RECONSTITUTION OF THE SCF(FBXO32) COMPLEX, FUNCTION IN UBIQUITINATION OF MYOD1.
    17. "FBW2 targets GCMa to the ubiquitin-proteasome degradation system."
      Yang C.S., Yu C., Chuang H.C., Chang C.W., Chang G.D., Yao T.P., Chen H.
      J. Biol. Chem. 280:10083-10090(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GCM1, FUNCTION IN UBIQUITINATION OF GCM1.
    18. "FBXO25, an F-box protein homologue of atrogin-1, is not induced in atrophying muscle."
      Maragno A.L., Baqui M.M., Gomes M.D.
      Biochim. Biophys. Acta 1760:966-972(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECONSTITUTION OF THE SCF(FBXO25) COMPLEX.
    19. "Proteasomal degradation of the multifunctional regulator YB-1 is mediated by an F-Box protein induced during programmed cell death."
      Lutz M., Wempe F., Bahr I., Zopf D., von Melchner H.
      FEBS Lett. 580:3921-3930(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SCF(FBXO33) COMPLEX WITH SKP1; RBX1 AND FBXO33.
    20. "Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein."
      Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M., Krek W.
      Mol. Cell. Biol. 26:5994-6004(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, INTERACTION WITH TRIM21.
    21. "Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells -- evidence for cullin dimerization."
      Chew E.H., Poobalasingam T., Hawkey C.J., Hagen T.
      Cell. Signal. 19:1071-1080(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION.
    22. "FBXO11 promotes the neddylation of p53 and inhibits its transcriptional activity."
      Abida W.M., Nikolaev A., Zhao W., Zhang W., Gu W.
      J. Biol. Chem. 282:1797-1804(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SCF(FBXO11) COMPLEX WITH SKP1; RBX1 AND FBXO11.
    23. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-708 AND LYS-720.
      Tissue: Mammary cancer.
    24. "Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation."
      Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., Schulman B.A.
      Cell 134:995-1006(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NEDDYLATION AT LYS-720.
    25. "Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases."
      Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.
      J. Biol. Chem. 283:12717-12729(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FBXO44; FBXO17 AND FBXO27, IDENTIFICATION IN SCF-COMPLEX.
    26. "Regulation of Chk2 ubiquitination and signaling through autophosphorylation of serine 379."
      Lovly C.M., Yan L., Ryan C.E., Takada S., Piwnica-Worms H.
      Mol. Cell. Biol. 28:5874-5885(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CHEK2 UBIQUITINATION, INTERACTION WITH CHEK2.
    27. Cited for: FUNCTION, INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
    28. "A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication by regulating the activity of cullin-RING ligases."
      Gastaldello S., Hildebrand S., Faridani O., Callegari S., Palmkvist M., Di Guglielmo C., Masucci M.G.
      Nat. Cell Biol. 12:351-361(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS BPLF1, DENEDDYLATION BY EPSTEIN-BARR VIRUS BPLF1.
    29. "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation."
      D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L., Washburn M.P., Dynlacht B., Pagano M.
      Nature 466:138-142(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SCF(CCNF) COMPLEX.
    30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas."
      Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C., di Celle P.F., Chapuy B., Shipp M., Chiarle R., Pagano M.
      Nature 481:90-93(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF BCL6, IDENTIFICATION IN THE SCF(FBXO11) COMPLEX.
    32. "SCF(Fbxo9) and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma."
      Fernandez-Saiz V., Targosz B.S., Lemeer S., Eichner R., Langer C., Bullinger L., Reiter C., Slotta-Huspenina J., Schroeder S., Knorn A.M., Kurutz J., Peschel C., Pagano M., Kuster B., Bassermann F.
      Nat. Cell Biol. 15:72-81(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SCF(FBXO9) COMPLEX, FUNCTION.
    33. Cited for: FUNCTION IN UBIQUITINATION OF BCL2, IDENTIFICATION IN THE SCF(FBXO10) COMPLEX.
    34. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 17-776 IN COMPLEX WITH 19-108 OF RBX1, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH RBX1; SKP1 AND SKP2.
    35. "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 CAND1 AND ROC1, NEDDYLATION AT LYS-720, SUBUNIT.
    36. "N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex."
      Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.
      Science 334:674-678(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 702-776 IN COMPLEX WITH DCUN1D1 AND UBE2M.

    Entry informationi

    Entry nameiCUL1_HUMAN
    AccessioniPrimary (citable) accession number: Q13616
    Secondary accession number(s): D3DWG3
    , O60719, Q08AL6, Q8IYW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: August 14, 2001
    Last modified: October 1, 2014
    This is version 142 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3