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Q13619

- CUL4A_HUMAN

UniProt

Q13619 - CUL4A_HUMAN

Protein

Cullin-4A

Gene

CUL4A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (30 May 2006)
      Previous versions | rss
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    Functioni

    Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein 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 is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. DCX(DET1-COP1) directs ubiquitination of JUN. DCX(DDB2) directs ubiquitination of XPC. DCX(DDB2) ubiquitinates histones H3-H4 and is required for efficient histone deposition during replication-coupled (H3.1) and replication-independent (H3.3) nucleosome assembly, probably by facilitating the transfer of H3 from ASF1A/ASF1B to other chaperones involved in histone deposition. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. DCX(DTL) directs autoubiquitination of DTL.8 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: ProtInc
    2. DNA repair Source: UniProtKB-KW
    3. G1/S transition of mitotic cell cycle Source: ProtInc
    4. intrinsic apoptotic signaling pathway Source: ProtInc
    5. negative regulation of cell proliferation Source: ProtInc
    6. positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
    7. protein ubiquitination Source: UniProtKB-UniPathway
    8. regulation of protein metabolic process Source: Ensembl
    9. ubiquitin-dependent protein catabolic process Source: InterPro
    10. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    DNA damage, DNA repair, Host-virus interaction, Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cullin-4A
    Short name:
    CUL-4A
    Gene namesi
    Name:CUL4A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:2554. CUL4A.

    Subcellular locationi

    GO - Cellular componenti

    1. Cul4A-RING E3 ubiquitin ligase complex Source: UniProtKB
    2. Cul4-RING E3 ubiquitin ligase complex Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 905LYQAV → AAAAA: Largely reduces interaction with DDB1; abolishes interaction with DDB2.
    Mutagenesisi139 – 1424WQDH → AADA: Largely reduces interaction with DDB1; abolishes interaction with DDB2.

    Organism-specific databases

    PharmGKBiPA27050.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 759759Cullin-4APRO_0000119795Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Phosphoserine2 Publications
    Cross-linki33 – 33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Cross-linki705 – 705Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)By similarity

    Post-translational modificationi

    Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex By similarity. Deneddylated by Epstein-Barr virus BPLF1 leading to a S-phase-like environment that is required for efficient replication of the viral genome.By similarity2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ13619.
    PaxDbiQ13619.
    PRIDEiQ13619.

    PTM databases

    PhosphoSiteiQ13619.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13619.
    BgeeiQ13619.
    CleanExiHS_CUL4A.
    GenevestigatoriQ13619.

    Interactioni

    Subunit structurei

    Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes that seem to consist of DDB1, CUL4A or CUL4B, RBX1 and a variable substrate recognition component which seems to belong to a protein family described as DCAF (Ddb1- and Cul4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Component of the CSA complex (DCX(ERCC8) complex) containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II. Component of the DCX(DET1-COP1) complex with the substrate recognition component DET1 and COP1. Component of the DCX(DDB2) complex with the substrate recognition component DDB2. Component of the DCX(DTL) complex with the putative substrate recognition component DTL. Interacts with DDB1, RBX1, RNF7, CTD1, TIP120A/CAND1, SKP2, CDKN1B, MDM2, TP53 and HOXA9. Interacts with DDB2; the interactions with DDB2 and CAND1 are mutually exclusive. Interacts with VPRBP, DTL, DDA1, DCAF6, DCAF4, DCAF16, DCAF17, DET1, WDTC1, DCAF5, DCAF11, WDR24A, RFWD2, PAFAH1B1, ERCC8, GRWD1, FBXW5, RBBP7, GNB2, WSB1, WSB2, NUP43, PWP1, FBXW8, ATG16L1, KATNB1, RBBP4, RBBP5, LRWD1 and DCAF8. May interact with WDR26, WDR51B, SNRNP40, WDR61, WDR76, WDR5. Can self-associate. Interacts with Epstein-Barr virus BPLF1.18 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAND1Q86VP63EBI-456106,EBI-456077
    DDB1Q165314EBI-456106,EBI-350322
    DDB2Q924662EBI-456106,EBI-1176171
    RBBP5Q152913EBI-456106,EBI-592823

    Protein-protein interaction databases

    BioGridi114029. 279 interactions.
    DIPiDIP-31610N.
    IntActiQ13619. 35 interactions.
    MINTiMINT-4532640.
    STRINGi9606.ENSP00000364589.

    Structurei

    Secondary structure

    1
    759
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni58 – 614
    Helixi62 – 7110
    Helixi83 – 9311
    Turni96 – 983
    Helixi99 – 12123
    Helixi130 – 15223
    Helixi154 – 1574
    Turni158 – 1625
    Beta strandi165 – 1673
    Helixi170 – 18011
    Turni181 – 1833
    Beta strandi184 – 1863
    Helixi189 – 1913
    Helixi193 – 2019
    Turni202 – 2065
    Helixi211 – 22313
    Turni227 – 2315
    Helixi232 – 25322
    Helixi256 – 26914
    Helixi271 – 2744
    Turni275 – 2773
    Turni280 – 2823
    Helixi283 – 29412
    Turni295 – 2973
    Helixi300 – 3045
    Helixi307 – 3115
    Turni312 – 3143
    Helixi316 – 32813
    Helixi332 – 35221
    Helixi355 – 3573
    Turni358 – 3603
    Helixi361 – 37717
    Turni378 – 3825
    Helixi384 – 39815
    Helixi404 – 41714
    Helixi421 – 4233
    Helixi429 – 44012
    Helixi446 – 46217
    Helixi469 – 48012
    Turni481 – 4833
    Turni485 – 4884
    Helixi489 – 51325
    Beta strandi522 – 5298
    Turni530 – 5323
    Helixi545 – 55915
    Beta strandi564 – 5663
    Helixi571 – 5733
    Beta strandi575 – 5795
    Beta strandi588 – 5925
    Helixi593 – 6019
    Helixi610 – 6167
    Helixi621 – 6299
    Turni630 – 6367
    Beta strandi638 – 6414
    Beta strandi645 – 6473
    Beta strandi653 – 6564
    Beta strandi665 – 6684
    Helixi670 – 6745
    Helixi678 – 70629
    Beta strandi707 – 7115
    Helixi713 – 72210
    Beta strandi723 – 7253
    Helixi729 – 74113
    Beta strandi754 – 7563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HYEX-ray3.10C1-759[»]
    4A0KX-ray5.93A38-759[»]
    ProteinModelPortaliQ13619.
    SMRiQ13619. Positions 41-759.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13619.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cullin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5647.
    HOVERGENiHBG003619.
    InParanoidiQ13619.
    KOiK10609.
    OMAiHVVEVCF.
    OrthoDBiEOG75TMB5.
    PhylomeDBiQ13619.
    TreeFamiTF101153.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13619-1) [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

    MADEAPRKGS FSALVGRTNG LTKPAALAAA PAKPGGAGGS KKLVIKNFRD    50
    RPRLPDNYTQ DTWRKLHEAV RAVQSSTSIR YNLEELYQAV ENLCSHKVSP 100
    MLYKQLRQAC EDHVQAQILP FREDSLDSVL FLKKINTCWQ DHCRQMIMIR 150
    SIFLFLDRTY VLQNSTLPSI WDMGLELFRT HIISDKMVQS KTIDGILLLI 200
    ERERSGEAVD RSLLRSLLGM LSDLQVYKDS FELKFLEETN CLYAAEGQRL 250
    MQEREVPEYL NHVSKRLEEE GDRVITYLDH STQKPLIACV EKQLLGEHLT 300
    AILQKGLDHL LDENRVPDLA QMYQLFSRVR GGQQALLQHW SEYIKTFGTA 350
    IVINPEKDKD MVQDLLDFKD KVDHVIEVCF QKNERFVNLM KESFETFINK 400
    RPNKPAELIA KHVDSKLRAG NKEATDEELE RTLDKIMILF RFIHGKDVFE 450
    AFYKKDLAKR LLVGKSASVD AEKSMLSKLK HECGAAFTSK LEGMFKDMEL 500
    SKDIMVHFKQ HMQNQSDSGP IDLTVNILTM GYWPTYTPME VHLTPEMIKL 550
    QEVFKAFYLG KHSGRKLQWQ TTLGHAVLKA EFKEGKKEFQ VSLFQTLVLL 600
    MFNEGDGFSF EEIKMATGIE DSELRRTLQS LACGKARVLI KSPKGKEVED 650
    GDKFIFNGEF KHKLFRIKIN QIQMKETVEE QVSTTERVFQ DRQYQIDAAI 700
    VRIMKMRKTL GHNLLVSELY NQLKFPVKPG DLKKRIESLI DRDYMERDKD 750
    NPNQYHYVA 759
    Length:759
    Mass (Da):87,680
    Last modified:May 30, 2006 - v3
    Checksum:i3C4C6A1BBD94D51B
    GO
    Isoform 2 (identifier: Q13619-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: Missing.

    Show »
    Length:659
    Mass (Da):76,821
    Checksum:i56D4D196BB1074CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti281 – 2811S → T in BAD93235. (PubMed:15811626)Curated
    Sequence conflicti339 – 3468HWSEYIKT → NSARARAA in AAC50547. (PubMed:8681378)Curated
    Sequence conflicti496 – 4961K → R in BAD93235. (PubMed:15811626)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti644 – 6441K → R.
    Corresponds to variant rs2302757 [ dbSNP | Ensembl ].
    VAR_020341

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_018577Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077188 mRNA. Translation: AAD45191.1.
    AY365124 mRNA. Translation: AAR13072.1.
    AB178950 mRNA. Translation: BAD93235.1.
    AL136221 Genomic DNA. Translation: CAM18410.1.
    AL136221 Genomic DNA. Translation: CAI13795.1.
    BC008308 mRNA. Translation: AAH08308.2.
    AB012193 mRNA. Translation: BAA33146.1.
    U58090 mRNA. Translation: AAC50547.1.
    CCDSiCCDS41908.1. [Q13619-1]
    CCDS9533.1. [Q13619-2]
    RefSeqiNP_001008895.1. NM_001008895.2. [Q13619-1]
    NP_001265442.1. NM_001278513.1. [Q13619-2]
    NP_003580.1. NM_003589.2. [Q13619-2]
    UniGeneiHs.339735.

    Genome annotation databases

    EnsembliENST00000326335; ENSP00000322132; ENSG00000139842. [Q13619-2]
    ENST00000375440; ENSP00000364589; ENSG00000139842. [Q13619-1]
    ENST00000375441; ENSP00000364590; ENSG00000139842. [Q13619-2]
    ENST00000451881; ENSP00000389118; ENSG00000139842. [Q13619-2]
    GeneIDi8451.
    KEGGihsa:8451.
    UCSCiuc010agu.3. human. [Q13619-1]

    Polymorphism databases

    DMDMi108936013.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077188 mRNA. Translation: AAD45191.1 .
    AY365124 mRNA. Translation: AAR13072.1 .
    AB178950 mRNA. Translation: BAD93235.1 .
    AL136221 Genomic DNA. Translation: CAM18410.1 .
    AL136221 Genomic DNA. Translation: CAI13795.1 .
    BC008308 mRNA. Translation: AAH08308.2 .
    AB012193 mRNA. Translation: BAA33146.1 .
    U58090 mRNA. Translation: AAC50547.1 .
    CCDSi CCDS41908.1. [Q13619-1 ]
    CCDS9533.1. [Q13619-2 ]
    RefSeqi NP_001008895.1. NM_001008895.2. [Q13619-1 ]
    NP_001265442.1. NM_001278513.1. [Q13619-2 ]
    NP_003580.1. NM_003589.2. [Q13619-2 ]
    UniGenei Hs.339735.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HYE X-ray 3.10 C 1-759 [» ]
    4A0K X-ray 5.93 A 38-759 [» ]
    ProteinModelPortali Q13619.
    SMRi Q13619. Positions 41-759.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114029. 279 interactions.
    DIPi DIP-31610N.
    IntActi Q13619. 35 interactions.
    MINTi MINT-4532640.
    STRINGi 9606.ENSP00000364589.

    PTM databases

    PhosphoSitei Q13619.

    Polymorphism databases

    DMDMi 108936013.

    Proteomic databases

    MaxQBi Q13619.
    PaxDbi Q13619.
    PRIDEi Q13619.

    Protocols and materials databases

    DNASUi 8451.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326335 ; ENSP00000322132 ; ENSG00000139842 . [Q13619-2 ]
    ENST00000375440 ; ENSP00000364589 ; ENSG00000139842 . [Q13619-1 ]
    ENST00000375441 ; ENSP00000364590 ; ENSG00000139842 . [Q13619-2 ]
    ENST00000451881 ; ENSP00000389118 ; ENSG00000139842 . [Q13619-2 ]
    GeneIDi 8451.
    KEGGi hsa:8451.
    UCSCi uc010agu.3. human. [Q13619-1 ]

    Organism-specific databases

    CTDi 8451.
    GeneCardsi GC13P113863.
    HGNCi HGNC:2554. CUL4A.
    MIMi 603137. gene.
    neXtProti NX_Q13619.
    PharmGKBi PA27050.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5647.
    HOVERGENi HBG003619.
    InParanoidi Q13619.
    KOi K10609.
    OMAi HVVEVCF.
    OrthoDBi EOG75TMB5.
    PhylomeDBi Q13619.
    TreeFami TF101153.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    EvolutionaryTracei Q13619.
    GeneWikii CUL4A.
    GenomeRNAii 8451.
    NextBioi 31624.
    PROi Q13619.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13619.
    Bgeei Q13619.
    CleanExi HS_CUL4A.
    Genevestigatori Q13619.

    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. "The human homologue for the Caenorhabditis elegans cul-4 gene is amplified and overexpressed in primary breast cancers."
      Chen L.-C., Manjeshwar S., Lu Y., Moore D., Ljung B.M., Kuo W.L., Dairkee S.H., Wernick M., Collins C., Smith H.S.
      Cancer Res. 58:3677-3683(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint."
      Higa L.A., Mihaylov I.S., Banks D.P., Zheng J., Zhang H.
      Nat. Cell Biol. 5:1008-1015(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDT1.
    3. "DDB2, the xeroderma pigmentosum group E gene product, is directly ubiquitylated by Cullin 4A-based ubiquitin ligase complex."
      Matsuda N., Azuma K., Saijo M., Iemura S., Hioki Y., Natsume T., Chiba T., Tanaka K., Tanaka K.
      DNA Repair 4:537-545(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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).
      Tissue: Lung.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 236-759 (ISOFORMS 1/2), NEDDYLATION.
    7. "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] OF 339-759 (ISOFORMS 1/2).
    8. "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.
    9. "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.
    10. "The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage."
      Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.
      Cell 113:357-367(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CSA COMPLEX WITH RBX1; DDB1 AND ERCC8, INTERACTION OF THE CSA COMPLEX WITH RNA POLYMERASE II AND THE COP9 SIGNALOSOME.
    11. "CUL-4A stimulates ubiquitylation and degradation of the HOXA9 homeodomain protein."
      Zhang Y., Morrone G., Zhang J., Chen X., Lu X., Ma L., Moore M., Zhou P.
      EMBO J. 22:6057-6067(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HOXA9, FUNCTION IN UBIQUITINATION OF HOXA9.
    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: INTERACTION WITH TIP120A.
    13. "Cul4A physically associates with MDM2 and participates in the proteolysis of p53."
      Nag A., Bagchi S., Raychaudhuri P.
      Cancer Res. 64:8152-8155(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MDM2 AND TP53, FUNCTION IN UBIQUITINATION OF TP53.
    14. "Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage."
      Hu J., McCall C.M., Ohta T., Xiong Y.
      Nat. Cell Biol. 6:1003-1009(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDB1, FUNCTION IN CTD1 UBIQUITINATION.
    15. "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase."
      Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D., Deshaies R.J., Dixit V.M.
      Science 303:1371-1374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE DCX(DET1-COP1) COMPLEX WITH DDB1; RBX1; COP1 AND DET1.
    16. Cited for: INTERACTION WITH DDB1; DDB2 AND CAND1, MUTAGENESIS OF 86-LEU--VAL-90 AND 139-TRP--HIS-142.
    17. "DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases."
      He Y.J., McCall C.M., Hu J., Zeng Y., Xiong Y.
      Genes Dev. 20:2949-2954(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VPRBP; DDB2; ERCC8; DCAF11; GRWD1; RFWD2; FBXW5; RBBP7; GNB2; WSB1; WSB2; NUP43; PWP1; FBXW8; ATG16L1; KATNB1 AND RBBP4, MUTAGENESIS OF 86-LEU--VAL-90 AND 139-TRP--HIS-142.
    18. "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage."
      Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., Zhang Y.
      Mol. Cell 22:383-394(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH DDB1; DDB2 AND RBX1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
    19. "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1."
      Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.
      Mol. Cell 23:709-721(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VPRBP; DTL; DDA1; DCAF6; DCAF4; DCAF16; DCAF17; DDB2; DET1; WDTC1; DCAF5; DCAF11; WDR24A; RFWD2; PAFAH1B1 AND DCAF8.
    20. "Cul4A and DDB1 associate with Skp2 to target p27Kip1 for proteolysis involving the COP9 signalosome."
      Bondar T., Kalinina A., Khair L., Kopanja D., Nag A., Bagchi S., Raychaudhuri P.
      Mol. Cell. Biol. 26:2531-2539(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKP2 AND CDKN1B, FUNCTION IN UBIQUITINATION OF CDKN1B.
    21. "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation."
      Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.
      Nat. Cell Biol. 8:1277-1283(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDB2; WDR26; RBBP5; RFWD2; WDR51B; SNRNP40; WDR61; WDR76 AND WDR5.
    22. "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.
    23. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "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.
    26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Orc2 protects ORCA from ubiquitin-mediated degradation."
      Shen Z., Prasanth S.G.
      Cell Cycle 11:3578-3589(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRWD1.
    29. "A Cul4 E3 ubiquitin ligase regulates histone hand-off during nucleosome assembly."
      Han J., Zhang H., Zhang H., Wang Z., Zhou H., Zhang Z.
      Cell 155:817-829(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF H3.
    30. "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration."
      Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.
      Mol. Cell 49:1147-1158(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF DTL.
    31. "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery."
      Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.
      Nature 443:590-593(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH DDB1; RBX1 AND SV5-V.
    32. "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 (5.93 ANGSTROMS) OF 38-759 IN COMPLEX WITH DDB1; RBX1 AND DDB2.

    Entry informationi

    Entry nameiCUL4A_HUMAN
    AccessioniPrimary (citable) accession number: Q13619
    Secondary accession number(s): A2A2W2
    , O75834, Q589T6, Q5TC62, Q6UP08, Q9UP17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 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 13
      Human chromosome 13: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3