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Q13620

- CUL4B_HUMAN

UniProt

Q13620 - CUL4B_HUMAN

Protein

Cullin-4B

Gene

CUL4B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 4 (18 May 2010)
      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. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.6 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle Source: UniProtKB
    2. histone H2A monoubiquitination Source: UniProt
    3. positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
    4. positive regulation of protein catabolic process Source: Ensembl
    5. ubiquitin-dependent protein catabolic process Source: InterPro
    6. UV-damage excision repair Source: UniProt

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA repair, Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cullin-4B
    Short name:
    CUL-4B
    Gene namesi
    Name:CUL4B
    Synonyms:KIAA0695
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2555. CUL4B.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. Cul4B-RING E3 ubiquitin ligase complex Source: UniProtKB
    2. cytoplasm Source: HPA
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: HPA
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:300354]: A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti213 – 2131T → I in MRXS15; uncertain pathological significance. 2 Publications
    VAR_032273
    Natural varianti572 – 5721R → C in MRXS15. 2 Publications
    VAR_032274
    Natural varianti745 – 7451V → A in MRXS15. 2 Publications
    VAR_032275

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 584Missing: Distributed in cytoplasm. Fails to promote cell proliferation. No binding to KPNA2, KPNA4 and KPNA1. 1 Publication
    Mutagenesisi55 – 551K → A: No impairment in nuclear localization. 1 Publication
    Mutagenesisi56 – 561K → A: Disrupts nuclear localization and does not bind KPNA2, KPNA4, KPNA1; when associated with A-57. Disrupts nuclear localization. 1 Publication
    Mutagenesisi57 – 571R → A: Disrupts nuclear localization and does not bind KPNA2, KPNA4, KPNA1; when associated with A-56. Disrupts nuclear localization. 1 Publication
    Mutagenesisi58 – 581K → A: No impairment in nuclear localization. 1 Publication

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi300354. phenotype.
    Orphaneti85293. Cabezas syndrome.
    PharmGKBiPA27051.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 913913Cullin-4BPRO_0000393946Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491Phosphothreonine2 Publications
    Modified residuei53 – 531Phosphoserine1 Publication
    Modified residuei146 – 1461Phosphoserine2 Publications
    Modified residuei193 – 1931Phosphoserine1 Publication
    Cross-linki859 – 859Glycyl 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.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ13620.
    PaxDbiQ13620.
    PRIDEiQ13620.

    PTM databases

    PhosphoSiteiQ13620.

    Miscellaneous databases

    PMAP-CutDBQ13620.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13620.
    BgeeiQ13620.
    CleanExiHS_CUL4B.
    GenevestigatoriQ13620.

    Organism-specific databases

    HPAiCAB017786.
    HPA003046.
    HPA011880.

    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(DTL) complex with the putative substrate recognition component DTL. Component of the DCX(DDB2) complex with the putative substrate recognition component DDB2. Part of a complex with RBX1 and TIP120A/CAND1. Interacts with RBX1 GRWD1, MLST8, SMU1, TLE2, TLE3, VPRBP, DDA1, DCAF6, DCAF17, DDB2, DCAF8, TIP120A/CAND1 and TMEM113. Interacts with cyclin E and with importins alpha-1 (KPNA2), alpha-3 (KPNA4), alpha-5 (KPNA1) and beta-1 (KPNB1). May interact with WDR26, WDR51B, SNRNP40, WDR61, WDR76 and WDR5.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAND1Q86VP63EBI-456067,EBI-456077
    CDC37Q165432EBI-456067,EBI-295634
    DDB1Q1653115EBI-456067,EBI-350322
    RBX1P628774EBI-456067,EBI-398523

    Protein-protein interaction databases

    BioGridi114028. 315 interactions.
    DIPiDIP-31609N.
    IntActiQ13620. 35 interactions.
    MINTiMINT-4774381.
    STRINGi9606.ENSP00000384109.

    Structurei

    Secondary structure

    1
    913
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi210 – 2123
    Helixi215 – 22814
    Helixi237 – 25014
    Helixi253 – 27018
    Helixi271 – 2766
    Helixi282 – 30625
    Helixi308 – 3125
    Turni315 – 3173
    Helixi324 – 33512
    Turni336 – 3383
    Helixi340 – 35819
    Helixi365 – 37713
    Helixi381 – 3844
    Helixi386 – 40722
    Helixi410 – 43021
    Helixi434 – 4363
    Helixi437 – 44812
    Helixi450 – 4523
    Helixi453 – 46614
    Helixi470 – 48011
    Helixi486 – 50722
    Beta strandi511 – 5133
    Helixi515 – 53319
    Helixi538 – 54912
    Helixi841 – 86020
    Beta strandi861 – 8655
    Helixi866 – 87611
    Helixi883 – 89513
    Beta strandi898 – 9014
    Beta strandi908 – 9114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DO7NMR-A826-913[»]
    4A0CX-ray3.80C/E192-913[»]
    4A0LX-ray7.40E/H192-913[»]
    4A64X-ray2.57A/B/C/D206-557[»]
    ProteinModelPortaliQ13620.
    SMRiQ13620. Positions 206-913.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13620.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi55 – 584Nuclear localization signal1 Publication

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi3 – 193191Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the cullin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5647.
    HOVERGENiHBG003619.
    KOiK10609.
    OMAiLQKGLNH.
    OrthoDBiEOG75TMB5.
    PhylomeDBiQ13620.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13620-2) [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

    MMSQSSGSGD GNDDEATTSK DGGFSSPSPS AAAAAQEVRS ATDGNTSTTP    50
    PTSAKKRKLN SSSSSSSNSS NEREDFDSTS SSSSTPPLQP RDSASPSTSS 100
    FCLGVSVAAS SHVPIQKKLR FEDTLEFVGF DAKMAEESSS SSSSSSPTAA 150
    TSQQQQLKNK SILISSVASV HHANGLAKSS TTVSSFANSK PGSAKKLVIK 200
    NFKDKPKLPE NYTDETWQKL KEAVEAIQNS TSIKYNLEEL YQAVENLCSY 250
    KISANLYKQL RQICEDHIKA QIHQFREDSL DSVLFLKKID RCWQNHCRQM 300
    IMIRSIFLFL DRTYVLQNSM LPSIWDMGLE LFRAHIISDQ KVQNKTIDGI 350
    LLLIERERNG EAIDRSLLRS LLSMLSDLQI YQDSFEQRFL EETNRLYAAE 400
    GQKLMQEREV PEYLHHVNKR LEEEADRLIT YLDQTTQKSL IATVEKQLLG 450
    EHLTAILQKG LNNLLDENRI QDLSLLYQLF SRVRGGVQVL LQQWIEYIKA 500
    FGSTIVINPE KDKTMVQELL DFKDKVDHII DICFLKNEKF INAMKEAFET 550
    FINKRPNKPA ELIAKYVDSK LRAGNKEATD EELEKMLDKI MIIFRFIYGK 600
    DVFEAFYKKD LAKRLLVGKS ASVDAEKSML SKLKHECGAA FTSKLEGMFK 650
    DMELSKDIMI QFKQYMQNQN VPGNIELTVN ILTMGYWPTY VPMEVHLPPE 700
    MVKLQEIFKT FYLGKHSGRK LQWQSTLGHC VLKAEFKEGK KELQVSLFQT 750
    LVLLMFNEGE EFSLEEIKQA TGIEDGELRR TLQSLACGKA RVLAKNPKGK 800
    DIEDGDKFIC NDDFKHKLFR IKINQIQMKE TVEEQASTTE RVFQDRQYQI 850
    DAAIVRIMKM RKTLSHNLLV SEVYNQLKFP VKPADLKKRI ESLIDRDYME 900
    RDKENPNQYN YIA 913
    Length:913
    Mass (Da):103,982
    Last modified:May 18, 2010 - v4
    Checksum:i3E58C5868FDF0700
    GO
    Isoform 2 (identifier: Q13620-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: MMSQSSGSGDGNDDEATTSKDG → MFPT

    Note: Contains a N-acetylmethionine at position 1. Contains a phosphoserine at position 8. Contains a phosphoserine at position 10.

    Show »
    Length:895
    Mass (Da):102,299
    Checksum:i25B25D253C1C2B71
    GO
    Isoform 3 (identifier: Q13620-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-196: Missing.
         197-203: LVIKNFK → MIDPDFA

    Show »
    Length:717
    Mass (Da):84,017
    Checksum:iD50E2D33B73E6CB9
    GO

    Sequence cautioni

    The sequence AAK16812.1 differs from that shown. Reason: Frameshift at position 115.
    The sequence AAB67315.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691S → R in BAG53936. (PubMed:14702039)Curated
    Sequence conflicti126 – 1261E → G in CAD97843. (PubMed:17974005)Curated
    Sequence conflicti142 – 1421S → P in BAG53936. (PubMed:14702039)Curated
    Sequence conflicti196 – 1961K → N in AAK16812. 1 PublicationCurated
    Sequence conflicti265 – 2651E → G in BAG53936. (PubMed:14702039)Curated
    Sequence conflicti268 – 2681I → M in AAK16812. 1 PublicationCurated
    Sequence conflicti485 – 4851G → D in CAD97843. (PubMed:17974005)Curated
    Sequence conflicti664 – 6641Q → QVK in AAK16812. 1 PublicationCurated
    Sequence conflicti727 – 7271L → I in AAR13073. (PubMed:14578910)Curated
    Sequence conflicti727 – 7271L → I in AAH36216. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031L → P.1 Publication
    Corresponds to variant rs61759504 [ dbSNP | Ensembl ].
    VAR_032272
    Natural varianti213 – 2131T → I in MRXS15; uncertain pathological significance. 2 Publications
    VAR_032273
    Natural varianti572 – 5721R → C in MRXS15. 2 Publications
    VAR_032274
    Natural varianti745 – 7451V → A in MRXS15. 2 Publications
    VAR_032275

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 196196Missing in isoform 3. 1 PublicationVSP_039084Add
    BLAST
    Alternative sequencei1 – 2222MMSQS…TSKDG → MFPT in isoform 2. 4 PublicationsVSP_039085Add
    BLAST
    Alternative sequencei197 – 2037LVIKNFK → MIDPDFA in isoform 3. 1 PublicationVSP_039086

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY365125 mRNA. Translation: AAR13073.1.
    AF212995 mRNA. Translation: AAK16812.1. Frameshift.
    AK123688 mRNA. Translation: BAG53936.1.
    AK299081 mRNA. Translation: BAH12944.1.
    AK315037 mRNA. Translation: BAG37520.1.
    BX537787 mRNA. Translation: CAD97843.1.
    AC002476 Genomic DNA. Translation: AAB67315.1. Sequence problems.
    AL451005, AC002476 Genomic DNA. Translation: CAI41370.1.
    CH471107 Genomic DNA. Translation: EAX11877.1.
    BC036216 mRNA. Translation: AAH36216.1.
    AB014595 mRNA. Translation: BAA31670.2.
    U58091 mRNA. Translation: AAC50548.1.
    CCDSiCCDS35379.1. [Q13620-2]
    CCDS43987.1. [Q13620-1]
    RefSeqiNP_001073341.1. NM_001079872.1. [Q13620-1]
    NP_003579.3. NM_003588.3. [Q13620-2]
    UniGeneiHs.102914.

    Genome annotation databases

    EnsembliENST00000371322; ENSP00000360373; ENSG00000158290. [Q13620-1]
    ENST00000404115; ENSP00000384109; ENSG00000158290. [Q13620-2]
    GeneIDi8450.
    KEGGihsa:8450.
    UCSCiuc004esv.3. human. [Q13620-1]
    uc004esw.3. human. [Q13620-2]

    Polymorphism databases

    DMDMi296439468.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY365125 mRNA. Translation: AAR13073.1 .
    AF212995 mRNA. Translation: AAK16812.1 . Frameshift.
    AK123688 mRNA. Translation: BAG53936.1 .
    AK299081 mRNA. Translation: BAH12944.1 .
    AK315037 mRNA. Translation: BAG37520.1 .
    BX537787 mRNA. Translation: CAD97843.1 .
    AC002476 Genomic DNA. Translation: AAB67315.1 . Sequence problems.
    AL451005 , AC002476 Genomic DNA. Translation: CAI41370.1 .
    CH471107 Genomic DNA. Translation: EAX11877.1 .
    BC036216 mRNA. Translation: AAH36216.1 .
    AB014595 mRNA. Translation: BAA31670.2 .
    U58091 mRNA. Translation: AAC50548.1 .
    CCDSi CCDS35379.1. [Q13620-2 ]
    CCDS43987.1. [Q13620-1 ]
    RefSeqi NP_001073341.1. NM_001079872.1. [Q13620-1 ]
    NP_003579.3. NM_003588.3. [Q13620-2 ]
    UniGenei Hs.102914.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DO7 NMR - A 826-913 [» ]
    4A0C X-ray 3.80 C/E 192-913 [» ]
    4A0L X-ray 7.40 E/H 192-913 [» ]
    4A64 X-ray 2.57 A/B/C/D 206-557 [» ]
    ProteinModelPortali Q13620.
    SMRi Q13620. Positions 206-913.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114028. 315 interactions.
    DIPi DIP-31609N.
    IntActi Q13620. 35 interactions.
    MINTi MINT-4774381.
    STRINGi 9606.ENSP00000384109.

    PTM databases

    PhosphoSitei Q13620.

    Polymorphism databases

    DMDMi 296439468.

    Proteomic databases

    MaxQBi Q13620.
    PaxDbi Q13620.
    PRIDEi Q13620.

    Protocols and materials databases

    DNASUi 8450.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371322 ; ENSP00000360373 ; ENSG00000158290 . [Q13620-1 ]
    ENST00000404115 ; ENSP00000384109 ; ENSG00000158290 . [Q13620-2 ]
    GeneIDi 8450.
    KEGGi hsa:8450.
    UCSCi uc004esv.3. human. [Q13620-1 ]
    uc004esw.3. human. [Q13620-2 ]

    Organism-specific databases

    CTDi 8450.
    GeneCardsi GC0XM119658.
    H-InvDB HIX0017025.
    HGNCi HGNC:2555. CUL4B.
    HPAi CAB017786.
    HPA003046.
    HPA011880.
    MIMi 300304. gene.
    300354. phenotype.
    neXtProti NX_Q13620.
    Orphaneti 85293. Cabezas syndrome.
    PharmGKBi PA27051.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5647.
    HOVERGENi HBG003619.
    KOi K10609.
    OMAi LQKGLNH.
    OrthoDBi EOG75TMB5.
    PhylomeDBi Q13620.
    TreeFami TF101153.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    EvolutionaryTracei Q13620.
    GeneWikii CUL4B.
    GenomeRNAii 8450.
    NextBioi 31618.
    PMAP-CutDB Q13620.
    PROi Q13620.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13620.
    Bgeei Q13620.
    CleanExi HS_CUL4B.
    Genevestigatori Q13620.

    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. "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 2), FUNCTION, INTERACTION WITH CDT1.
    2. "Molecular cloning of a full-length cullin, CUL4B and identification of its interacting proteins."
      Du M., Zu Z., Sansores-Garcia L., Wu K.K.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "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; 2 AND 3).
      Tissue: Chondrocyte, Teratocarcinoma and Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Fetal liver.
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Testis.
    8. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-913 (ISOFORMS 1/2).
      Tissue: Brain.
    9. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    10. "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 626-913.
    11. "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.
    12. "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.
    13. "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, IDENTIFICATION IN A COMPLEX WITH RBX1 AND TIP120A.
    14. "Involvement of CUL4 ubiquitin E3 ligases in regulating CDK inhibitors Dacapo/p27Kip1 and cyclin E degradation."
      Higa L.A., Yang X., Zheng J., Banks D., Wu M., Ghosh P., Sun H., Zhang H.
      Cell Cycle 5:71-77(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CYCLIN E.
    15. "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.
    16. "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; DDA1; DCAF6; DCAF17; DDB2 AND DCAF8.
    17. "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 DTL; DDB2; TMEM113; WDR5B; WDR82; WDR26; GRWD1; WDR51B; SNRNP40; DCAF8; WDR61; WDR76; WDR5; SMU1; TLE2 AND TLE3.
    18. "Mutation in CUL4B, which encodes a member of cullin-RING ubiquitin ligase complex, causes X-linked mental retardation."
      Zou Y., Liu Q., Chen B., Zhang X., Guo C., Zhou H., Li J., Gao G., Guo Y., Yan C., Wei J., Shao C., Gong Y.
      Am. J. Hum. Genet. 80:561-566(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MRXS15.
    19. "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A."
      Guerrero-Santoro J., Kapetanaki M.G., Hsieh C.L., Gorbachinsky I., Levine A.S., Rapic-Otrin V.
      Cancer Res. 68:5014-5022(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    20. "mTORC1 signaling requires proteasomal function and the involvement of CUL4-DDB1 ubiquitin E3 ligase."
      Ghosh P., Wu M., Zhang H., Sun H.
      Cell Cycle 7:373-381(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MLST8.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-53; SER-146 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Characterization of nuclear localization signal in the N terminus of CUL4B and its essential role in cyclin E degradation and cell cycle progression."
      Zou Y., Mi J., Cui J., Lu D., Zhang X., Guo C., Gao G., Liu Q., Chen B., Shao C., Gong Y.
      J. Biol. Chem. 284:33320-33332(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KPNA2; KPNA4; KPNA1 AND KPNB1, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF LYS-55; LYS-56; ARG-57; LYS-58 AND 55-LYS--LYS-58.
    24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49 AND SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. "A novel nonsense mutation in CUL4B gene in three brothers with X-linked mental retardation syndrome."
      Badura-Stronka M., Jamsheer A., Materna-Kiryluk A., Sowinska A., Kiryluk K., Budny B., Latos-Bielenska A.
      Clin. Genet. 77:141-144(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE, INVOLVEMENT IN MRXS15.
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-10 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Solution structure of the winged helix-turn-helix motif of human cul-4b."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 826-913.
    31. "Mutations in CUL4B, which encodes a ubiquitin E3 ligase subunit, cause an X-linked mental retardation syndrome associated with aggressive outbursts, seizures, relative macrocephaly, central obesity, hypogonadism, pes cavus, and tremor."
      Tarpey P.S., Raymond F.L., O'Meara S., Edkins S., Teague J., Butler A., Dicks E., Stevens C., Tofts C., Avis T., Barthorpe S., Buck G., Cole J., Gray K., Halliday K., Harrison R., Hills K., Jenkinson A.
      , Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Varian J., West S., Widaa S., Mallya U., Moon J., Luo Y., Holder S., Smithson S.F., Hurst J.A., Clayton-Smith J., Kerr B., Boyle J., Shaw M., Vandeleur L., Rodriguez J., Slaugh R., Easton D.F., Wooster R., Bobrow M., Srivastava A.K., Stevenson R.E., Schwartz C.E., Turner G., Gecz J., Futreal P.A., Stratton M.R., Partington M.
      Am. J. Hum. Genet. 80:345-352(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MRXS15 ILE-213; CYS-572 AND ALA-745, VARIANT PRO-103.
    32. "A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation."
      Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C., O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M., Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J.
      , Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M., Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., Wray P., Teague J., Butler A., Jenkinson A., Jia M., Richardson D., Shepherd R., Wooster R., Tejada M.I., Martinez F., Carvill G., Goliath R., de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., Raynaud M., Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., Mallya U., Moon J., Parnau J., Mohammed S., Tolmie J.L., Shoubridge C., Corbett M., Gardner A., Haan E., Rujirabanjerd S., Shaw M., Vandeleur L., Fullston T., Easton D.F., Boyle J., Partington M., Hackett A., Field M., Skinner C., Stevenson R.E., Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L., Futreal P.A., Stratton M.R.
      Nat. Genet. 41:535-543(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MRXS15 ILE-213; CYS-572 AND ALA-745.

    Entry informationi

    Entry nameiCUL4B_HUMAN
    AccessioniPrimary (citable) accession number: Q13620
    Secondary accession number(s): B1APK5
    , B3KVX4, B7Z5K8, Q6PIE4, Q6UP07, Q7Z673, Q9BY37, Q9UEB7, Q9UED7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 141 of the entry and version 4 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 X
      Human chromosome X: 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