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Q3TCH7

- CUL4A_MOUSE

UniProt

Q3TCH7 - CUL4A_MOUSE

Protein

Cullin-4A

Gene

Cul4a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation 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. In association with RBX1, DDB1 and DDB2 is required for histone H3 and histone H4 ubiquitination in response to ultraviolet and may be important for subsequent DNA repair. 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 By similarity.By similarity

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. hemopoiesis Source: MGI
    3. negative regulation of granulocyte differentiation Source: MGI
    4. positive regulation of cell proliferation Source: MGI
    5. positive regulation of G1/S transition of mitotic cell cycle Source: MGI
    6. positive regulation of protein catabolic process Source: MGI
    7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
    8. protein ubiquitination Source: UniProtKB-UniPathway
    9. regulation of DNA damage checkpoint Source: MGI
    10. regulation of nucleotide-excision repair Source: MGI
    11. regulation of protein metabolic process Source: MGI
    12. somatic stem cell maintenance Source: MGI
    13. ubiquitin-dependent protein catabolic process Source: MGI
    14. 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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1914487. Cul4a.

    Subcellular locationi

    GO - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 759759Cullin-4APRO_0000236184Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex By similarity. Deneddylated by murine cytomegalovirus M48 leading to a S-phase-like environment that is required for efficient replication of the viral genome.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ3TCH7.
    PaxDbiQ3TCH7.
    PRIDEiQ3TCH7.

    PTM databases

    PhosphoSiteiQ3TCH7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ3TCH7.
    BgeeiQ3TCH7.
    CleanExiMM_CUL4A.
    GenevestigatoriQ3TCH7.

    Interactioni

    Subunit structurei

    Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes that seem to be formed 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 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 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(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 murine cytomegalovirus M48.1 Publication

    Protein-protein interaction databases

    BioGridi221235. 13 interactions.
    IntActiQ3TCH7. 5 interactions.
    MINTiMINT-4122171.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3TCH7.
    SMRiQ3TCH7. Positions 41-759.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cullin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5647.
    GeneTreeiENSGT00730000110449.
    HOGENOMiHOG000176712.
    HOVERGENiHBG003619.
    InParanoidiQ3TCH7.
    KOiK10609.
    OMAiHVVEVCF.
    OrthoDBiEOG75TMB5.
    PhylomeDBiQ3TCH7.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q3TCH7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADEGPRKGS VSALMGRTNG LTKPAALAGG PAKPGGTGGS RKLVIKNFRD    50
    RPRLPDNYTQ DTWRKLHEAV KAIQSSTSIR YNLEELYQAV ENLCSHKVSP 100
    TLYKQLRQVC EDHVQAQILP FREDSLDSVL FLKKINTCWQ DHCRQMIMIR 150
    SIFLFLDRTY VLQNSMLPSI WDMGLELFRN HIISDRMVQS KTIDGILLLI 200
    GRERSGEAVD RSLLRSLLSM LSDLQVYKDS FELKFLEETN CLYAAEGQRL 250
    MQDREVPEYL NHVSKRLEEE ADRVITYLDH STQKPLIACV EKQLLGEHLT 300
    AILQKGLEHL LDENRVPDLT QMYQLFSRVK GGQHALLQHW SEYIKTFGTT 350
    IVINPEKDKD MVQDLLDFKD KVDHVVEVCF QRNERFINLM KESFETFINK 400
    RPNKPAELIA KHVDSKLRAG NKEATDEELE RILDKIMILF RFIHGKDVFE 450
    AFYKKDLAKR LLVGKSASVD AEKSMLSKLK HECGAAFTSK LEGMFKDMEL 500
    SKDIMVHFKQ HMQNQSAPGP IDLTVNILTM GYWPTYTPME VHLPPEMVRL 550
    QEVFKTFYLG KHSGRKLQWQ TTLGHAVLKA DFKEGKKEFQ VSLFQTLVLL 600
    MFNEGDGFSF EEIKMATGIE DSELRRTLQS LACGKARVLI KSPKGKEVED 650
    GDKFIFNADF KHKLFRIKIN QIQMKETVEE QVSTTERVFQ DRQYQIDAAI 700
    VRIMKMRKTL GHNLLVSELY NQLKFPVKPG DLKKRIESLI DRDYMERDKD 750
    SPNQYHYVA 759
    Length:759
    Mass (Da):87,753
    Last modified:October 11, 2005 - v1
    Checksum:i464271E22FB65F2D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti756 – 7561H → R in BAE40173. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK168215 mRNA. Translation: BAE40173.1.
    AK170722 mRNA. Translation: BAE41979.1.
    BC010211 mRNA. Translation: AAH10211.2.
    CCDSiCCDS52485.1.
    RefSeqiNP_666319.2. NM_146207.2.
    UniGeneiMm.212861.

    Genome annotation databases

    EnsembliENSMUST00000016680; ENSMUSP00000016680; ENSMUSG00000031446.
    GeneIDi99375.
    KEGGimmu:99375.
    UCSCiuc009kww.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK168215 mRNA. Translation: BAE40173.1 .
    AK170722 mRNA. Translation: BAE41979.1 .
    BC010211 mRNA. Translation: AAH10211.2 .
    CCDSi CCDS52485.1.
    RefSeqi NP_666319.2. NM_146207.2.
    UniGenei Mm.212861.

    3D structure databases

    ProteinModelPortali Q3TCH7.
    SMRi Q3TCH7. Positions 41-759.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 221235. 13 interactions.
    IntActi Q3TCH7. 5 interactions.
    MINTi MINT-4122171.

    PTM databases

    PhosphoSitei Q3TCH7.

    Proteomic databases

    MaxQBi Q3TCH7.
    PaxDbi Q3TCH7.
    PRIDEi Q3TCH7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000016680 ; ENSMUSP00000016680 ; ENSMUSG00000031446 .
    GeneIDi 99375.
    KEGGi mmu:99375.
    UCSCi uc009kww.2. mouse.

    Organism-specific databases

    CTDi 8451.
    MGIi MGI:1914487. Cul4a.

    Phylogenomic databases

    eggNOGi COG5647.
    GeneTreei ENSGT00730000110449.
    HOGENOMi HOG000176712.
    HOVERGENi HBG003619.
    InParanoidi Q3TCH7.
    KOi K10609.
    OMAi HVVEVCF.
    OrthoDBi EOG75TMB5.
    PhylomeDBi Q3TCH7.
    TreeFami TF101153.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi CUL4A. mouse.
    NextBioi 353901.
    PROi Q3TCH7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q3TCH7.
    Bgeei Q3TCH7.
    CleanExi MM_CUL4A.
    Genevestigatori Q3TCH7.

    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 transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c and NOD.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "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 MURINE CYTOMEGALOVIRUS M48, DENEDDYLATION BY MURINE CYTOMEGALOVIRUS M48.

    Entry informationi

    Entry nameiCUL4A_MOUSE
    AccessioniPrimary (citable) accession number: Q3TCH7
    Secondary accession number(s): Q3THM3, Q91Z44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3