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Q14999

- CUL7_HUMAN

UniProt

Q14999 - CUL7_HUMAN

Protein

Cullin-7

Gene

CUL7

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 (23 Oct 2007)
      Previous versions | rss
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    Functioni

    Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695). Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5 (PubMed:24793696). Core component of a Cul7-RING ubiquitin-protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1 (PubMed:21572988, PubMed:24362026). Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) (PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradatation, thereby affecting cell proliferation and differentiation (PubMed:24362026). Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development (PubMed:20139075). Does not promote polyubiquitination and proteasomal degradation of p53/TP53 (PubMed:16547496, PubMed:17332328). While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions.8 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. endoplasmic reticulum unfolded protein response Source: Reactome
    4. epithelial to mesenchymal transition Source: UniProtKB
    5. Golgi organization Source: UniProtKB
    6. microtubule cytoskeleton organization Source: UniProtKB
    7. mitotic cytokinesis Source: UniProtKB
    8. placenta development Source: UniProtKB
    9. positive regulation of dendrite morphogenesis Source: UniProtKB
    10. protein ubiquitination Source: UniProtKB
    11. proteolysis Source: UniProtKB
    12. regulation of mitosis Source: UniProtKB
    13. ubiquitin-dependent protein catabolic process Source: InterPro
    14. vasculogenesis Source: UniProtKB
    15. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_18273. XBP1(S) activates chaperone genes.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cullin-7
    Short name:
    CUL-7
    Gene namesi
    Name:CUL7
    Synonyms:KIAA0076
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21024. CUL7.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmperinuclear region. Golgi apparatus
    Note: Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. During mitosis, localizes to the mitotic apparatus (PubMed:24793695). CCDC8 is required for centrosomal location (PubMed:24793695).1 Publication

    GO - Cellular componenti

    1. 3M complex Source: UniProtKB
    2. anaphase-promoting complex Source: UniProtKB
    3. centrosome Source: UniProtKB
    4. Cul7-RING ubiquitin ligase complex Source: UniProtKB
    5. cytoplasm Source: UniProtKB
    6. cytosol Source: Reactome
    7. Golgi apparatus Source: UniProtKB
    8. nucleus Source: HPA
    9. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Golgi apparatus

    Pathology & Biotechi

    Involvement in diseasei

    3M syndrome 1 (3M1) [MIM:273750]: An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1014 – 10141L → R in 3M1. 1 Publication
    VAR_026122
    Natural varianti1246 – 12461Q → G in 3M1; requires 2 nucleotide substitutions. 1 Publication
    VAR_026123
    Natural varianti1464 – 14641H → P in 3M1; impairs the ability to interact with RBX1, thus hampers the assembly of polyubiquitin chains. 1 Publication
    VAR_026124
    Natural varianti1588 – 15881L → P in 3M1. 1 Publication
    VAR_071120

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi273750. phenotype.
    Orphaneti2616. 3M syndrome.
    PharmGKBiPA134897835.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16981698Cullin-7PRO_0000119802Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei339 – 3391Phosphoserine1 Publication
    Cross-linki1576 – 1576Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)Sequence Analysis

    Post-translational modificationi

    According to a report, may not be neddylated despite the conserved consensus site for neddylation at Lys-1576.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14999.
    PaxDbiQ14999.
    PRIDEiQ14999.

    PTM databases

    PhosphoSiteiQ14999.

    Expressioni

    Tissue specificityi

    Highly expressed in fetal kidney and adult skeletal muscle. Also abundant in fetal brain, as well as in adult pancreas, kidney, placenta and heart. Detected in trophoblasts, lymphoblasts, osteoblasts, chondrocytes and skin fibroblasts.1 Publication

    Developmental stagei

    Highly expressed in invasive placental villi during first trimester.1 Publication

    Gene expression databases

    BgeeiQ14999.
    CleanExiHS_CUL7.
    GenevestigatoriQ14999.

    Organism-specific databases

    HPAiCAB015449.
    HPA030095.
    HPA030096.

    Interactioni

    Subunit structurei

    Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1. Part of a Cul7-RING complex consisting of CUL7, RBX1, SKP1 and FBXW8. Interacts with a complex of SKP1 and FBXW8, but not with SKP1 alone. Interacts with CUL9; leading to inhibit CUL9 activity. Interacts with FBXW8; interaction is mutually exclusive of binding to CUL9 or p53/TP53. Interacts with p53/TP53; the interaction preferentially involves tetrameric and dimeric p53/TP53. The CUL7-CUL9 heterodimer seems to interact specifically with p53/TP53. Interacts with CUL1; the interactions seems to be mediated by FBXW8. Interacts with SV40 Large T antigen; this interaction seems to inhibit CUL7. Interacts with OBSL1.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TP53P046374EBI-308606,EBI-366083

    Protein-protein interaction databases

    BioGridi115159. 28 interactions.
    DIPiDIP-31618N.
    DIP-60187N.
    IntActiQ14999. 10 interactions.
    STRINGi9606.ENSP00000265348.

    Structurei

    Secondary structure

    1
    1698
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi360 – 3623
    Beta strandi363 – 3664
    Helixi367 – 37610
    Beta strandi382 – 3854
    Beta strandi397 – 4037
    Beta strandi407 – 4148
    Turni415 – 4184
    Beta strandi419 – 4246
    Helixi425 – 4273
    Beta strandi428 – 4303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JNGNMR-A360-460[»]
    ProteinModelPortaliQ14999.
    SMRiQ14999. Positions 360-435, 1388-1576.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14999.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini814 – 993180DOCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni360 – 460101Interaction with TP53Add
    BLAST

    Sequence similaritiesi

    Belongs to the cullin family.PROSITE-ProRule annotation
    Contains 1 DOC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG48148.
    HOGENOMiHOG000024831.
    HOVERGENiHBG103792.
    InParanoidiQ14999.
    KOiK10613.
    OMAiTFEHYYQ.
    OrthoDBiEOG70S74H.
    PhylomeDBiQ14999.
    TreeFamiTF101154.

    Family and domain databases

    Gene3Di2.30.30.30. 1 hit.
    2.60.120.260. 1 hit.
    InterProiIPR004939. APC_su10/DOC_dom.
    IPR016024. ARM-type_fold.
    IPR021097. CPH_domain.
    IPR016158. Cullin_homology.
    IPR001373. Cullin_N.
    IPR008979. Galactose-bd-like.
    IPR014722. Rib_L2_dom2.
    [Graphical view]
    PfamiPF03256. APC10. 1 hit.
    PF11515. Cul7. 1 hit.
    PF00888. Cullin. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 3 hits.
    SSF49785. SSF49785. 1 hit.
    SSF75632. SSF75632. 2 hits.
    PROSITEiPS50069. CULLIN_2. 1 hit.
    PS51284. DOC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14999-1) [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

    MVGELRYREF RVPLGPGLHA YPDELIRQRV GHDGHPEYQI RWLILRRGDE     50
    GDGGSGQVDC KAEHILLWMS KDEIYANCHK MLGEDGQVIG PSQESAGEVG 100
    ALDKSVLEEM ETDVKSLIQR ALRQLEECVG TIPPAPLLHT VHVLSAYASI 150
    EPLTGVFKDP RVLDLLMHML SSPDYQIRWS AGRMIQALSS HDAGTRTQIL 200
    LSLSQQEAIE KHLDFDSRCA LLALFAQATL SEHPMSFEGI QLPQVPGRVL 250
    FSLVKRYLHV TSLLDQLNDS AAEPGAQNTS APEELSGERG QLELEFSMAM 300
    GTLISELVQA MRWDQASDRP RSSARSPGSI FQPQLADVSP GLPAAQAQPS 350
    FRRSRRFRPR SEFASGNTYA LYVRDTLQPG MRVRMLDDYE EISAGDEGEF 400
    RQSNNGVPPV QVFWESTGRT YWVHWHMLEI LGFEEDIEDM VEADEYQGAV 450
    ASRVLGRALP AWRWRPMTEL YAVPYVLPED EDTEECEHLT LAEWWELLFF 500
    IKKLDGPDHQ EVLQILQENL DGEILDDEIL AELAVPIELA QDLLLTLPQR 550
    LNDSALRDLI NCHVYKKYGP EALAGNQAYP SLLEAQEDVL LLDAQAQAKD 600
    SEDAAKVEAK EPPSQSPNTP LQRLVEGYGP AGKILLDLEQ ALSSEGTQEN 650
    KVKPLLLQLQ RQPQPFLALM QSLDTPETNR TLHLTVLRIL KQLVDFPEAL 700
    LLPWHEAVDA CMACLRSPNT DREVLQELIF FLHRLTSVSR DYAVVLNQLG 750
    ARDAISKALE KHLGKLELAQ ELRDMVFKCE KHAHLYRKLI TNILGGCIQM 800
    VLGQIEDHRR THQPINIPFF DVFLRYLCQG SSVEVKEDKC WEKVEVSSNP 850
    HRASKLTDHN PKTYWESNGS AGSHYITLHM RRGILIRQLT LLVASEDSSY 900
    MPARVVVCGG DSTSSLHTEL NSVNVMPSAS RVILLENLTR FWPIIQIRIK 950
    RCQQGGIDTR IRGLEILGPK PTFWPVFREQ LCRHTRLFYM VRAQAWSQDM 1000
    AEDRRSLLHL SSRLNGALRQ EQNFADRFLP DDEAAQALGK TCWEALVSPV 1050
    VQNITSPDED GISPLGWLLD QYLECQEAVF NPQSRGPAFF SRVRRLTHLL 1100
    VHVEPCEAPP PVVATPRPKG RNRSHDWSSL ATRGLPSSIM RNLTRCWRAV 1150
    VEKQVNNFLT SSWRDDDFVP RYCEHFNILQ NSSSELFGPR AAFLLALQNG 1200
    CAGALLKLPF LKAAHVSEQF ARHIDQQIQG SRIGGAQEME RLAQLQQCLQ 1250
    AVLIFSGLEI ATTFEHYYQH YMADRLLGVV SSWLEGAVLE QIGPCFPNRL 1300
    PQQMLQSLST SKELQRQFHV YQLQQLDQEL LKLEDTEKKI QVGLGASGKE 1350
    HKSEKEEEAG AAAVVDVAEG EEEEEENEDL YYEGAMPEVS VLVLSRHSWP 1400
    VASICHTLNP RTCLPSYLRG TLNRYSNFYN KSQSHPALER GSQRRLQWTW 1450
    LGWAELQFGN QTLHVSTVQM WLLLYLNDLK AVSVESLLAF SGLSADMLNQ 1500
    AIGPLTSSRG PLDLHEQKDI PGGVLKIRDG SKEPRSRWDI VRLIPPQTYL 1550
    QAEGEDGQNL EKRRNLLNCL IVRILKAHGD EGLHIDQLVC LVLEAWQKGP 1600
    CPPRGLVSSL GKGSACSSTD VLSCILHLLG KGTLRRHDDR PQVLSYAVPV 1650
    TVMEPHTESL NPGSSGPNPP LTFHTLQIRS RGVPYASCTA TQSFSTFR 1698
    Length:1,698
    Mass (Da):191,161
    Last modified:October 23, 2007 - v2
    Checksum:iEC9EED17E98FC9A1
    GO
    Isoform 2 (identifier: Q14999-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSRGFWLAEPLAGTGPHPAPVAADSRGCSSVPRRHAPSRLSVSTPSRGPGARM
         194-194: G → GEGQCGEEGKAGEGLGRLRDSQDTVAGASDLIR

    Note: No experimental confirmation available.

    Show »
    Length:1,782
    Mass (Da):199,750
    Checksum:i3CFC980A4E8C4EB2
    GO

    Sequence cautioni

    The sequence BAA07551.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti616 – 6161S → G.
    Corresponds to variant rs7774330 [ dbSNP | Ensembl ].
    VAR_048841
    Natural varianti813 – 8131Q → R.3 Publications
    Corresponds to variant rs9381231 [ dbSNP | Ensembl ].
    VAR_026121
    Natural varianti852 – 8521R → Q.
    Corresponds to variant rs34574340 [ dbSNP | Ensembl ].
    VAR_048842
    Natural varianti1014 – 10141L → R in 3M1. 1 Publication
    VAR_026122
    Natural varianti1246 – 12461Q → G in 3M1; requires 2 nucleotide substitutions. 1 Publication
    VAR_026123
    Natural varianti1246 – 12461Q → H.
    Corresponds to variant rs36071170 [ dbSNP | Ensembl ].
    VAR_048843
    Natural varianti1464 – 14641H → P in 3M1; impairs the ability to interact with RBX1, thus hampers the assembly of polyubiquitin chains. 1 Publication
    VAR_026124
    Natural varianti1588 – 15881L → P in 3M1. 1 Publication
    VAR_071120

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MSRGFWLAEPLAGTGPHPAP VAADSRGCSSVPRRHAPSRL SVSTPSRGPGARM in isoform 2. 1 PublicationVSP_046105
    Alternative sequencei194 – 1941G → GEGQCGEEGKAGEGLGRLRD SQDTVAGASDLIR in isoform 2. 1 PublicationVSP_046106

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38548 mRNA. Translation: BAA07551.2. Different initiation.
    AK302668 mRNA. Translation: BAG63902.1.
    AL355385, AL136304 Genomic DNA. Translation: CAI13779.1.
    AL136304, AL355385 Genomic DNA. Translation: CAI19793.1.
    BC033647 mRNA. Translation: AAH33647.1.
    CCDSiCCDS4881.1. [Q14999-1]
    CCDS55003.1. [Q14999-2]
    RefSeqiNP_001161842.1. NM_001168370.1. [Q14999-2]
    NP_055595.2. NM_014780.4. [Q14999-1]
    UniGeneiHs.520136.

    Genome annotation databases

    EnsembliENST00000265348; ENSP00000265348; ENSG00000044090. [Q14999-1]
    ENST00000535468; ENSP00000438788; ENSG00000044090. [Q14999-2]
    GeneIDi9820.
    KEGGihsa:9820.
    UCSCiuc003otq.3. human. [Q14999-1]

    Polymorphism databases

    DMDMi160370003.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38548 mRNA. Translation: BAA07551.2 . Different initiation.
    AK302668 mRNA. Translation: BAG63902.1 .
    AL355385 , AL136304 Genomic DNA. Translation: CAI13779.1 .
    AL136304 , AL355385 Genomic DNA. Translation: CAI19793.1 .
    BC033647 mRNA. Translation: AAH33647.1 .
    CCDSi CCDS4881.1. [Q14999-1 ]
    CCDS55003.1. [Q14999-2 ]
    RefSeqi NP_001161842.1. NM_001168370.1. [Q14999-2 ]
    NP_055595.2. NM_014780.4. [Q14999-1 ]
    UniGenei Hs.520136.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JNG NMR - A 360-460 [» ]
    ProteinModelPortali Q14999.
    SMRi Q14999. Positions 360-435, 1388-1576.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115159. 28 interactions.
    DIPi DIP-31618N.
    DIP-60187N.
    IntActi Q14999. 10 interactions.
    STRINGi 9606.ENSP00000265348.

    PTM databases

    PhosphoSitei Q14999.

    Polymorphism databases

    DMDMi 160370003.

    Proteomic databases

    MaxQBi Q14999.
    PaxDbi Q14999.
    PRIDEi Q14999.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265348 ; ENSP00000265348 ; ENSG00000044090 . [Q14999-1 ]
    ENST00000535468 ; ENSP00000438788 ; ENSG00000044090 . [Q14999-2 ]
    GeneIDi 9820.
    KEGGi hsa:9820.
    UCSCi uc003otq.3. human. [Q14999-1 ]

    Organism-specific databases

    CTDi 9820.
    GeneCardsi GC06M043006.
    GeneReviewsi CUL7.
    HGNCi HGNC:21024. CUL7.
    HPAi CAB015449.
    HPA030095.
    HPA030096.
    MIMi 273750. phenotype.
    609577. gene.
    neXtProti NX_Q14999.
    Orphaneti 2616. 3M syndrome.
    PharmGKBi PA134897835.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG48148.
    HOGENOMi HOG000024831.
    HOVERGENi HBG103792.
    InParanoidi Q14999.
    KOi K10613.
    OMAi TFEHYYQ.
    OrthoDBi EOG70S74H.
    PhylomeDBi Q14999.
    TreeFami TF101154.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_18273. XBP1(S) activates chaperone genes.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    EvolutionaryTracei Q14999.
    GeneWikii CUL7.
    GenomeRNAii 9820.
    NextBioi 36986.
    PROi Q14999.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q14999.
    CleanExi HS_CUL7.
    Genevestigatori Q14999.

    Family and domain databases

    Gene3Di 2.30.30.30. 1 hit.
    2.60.120.260. 1 hit.
    InterProi IPR004939. APC_su10/DOC_dom.
    IPR016024. ARM-type_fold.
    IPR021097. CPH_domain.
    IPR016158. Cullin_homology.
    IPR001373. Cullin_N.
    IPR008979. Galactose-bd-like.
    IPR014722. Rib_L2_dom2.
    [Graphical view ]
    Pfami PF03256. APC10. 1 hit.
    PF11515. Cul7. 1 hit.
    PF00888. Cullin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 3 hits.
    SSF49785. SSF49785. 1 hit.
    SSF75632. SSF75632. 2 hits.
    PROSITEi PS50069. CULLIN_2. 1 hit.
    PS51284. DOC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-813.
      Tissue: Bone marrow.
    2. "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] (ISOFORM 2), VARIANT ARG-813.
      Tissue: Testis.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-813.
      Tissue: Eye.
    5. "CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex."
      Dias D.C., Dolios G., Wang R., Pan Z.Q.
      Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH SKP1; FBXW8 AND RBX1.
    6. "Targeted disruption of p185/Cul7 gene results in abnormal vascular morphogenesis."
      Arai T., Kasper J.S., Skaar J.R., Ali S.H., Takahashi C., DeCaprio J.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:9855-9860(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBX1, IDENTIFICATION IN A COMPLEX WITH SKP1; FBXW8; RBX1 AND GLMN.
    7. "Simian virus 40 large T antigen's association with the CUL7 SCF complex contributes to cellular transformation."
      Kasper J.S., Kuwabara H., Arai T., Ali S.H., DeCaprio J.A.
      J. Virol. 79:11685-11692(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SV40 LARGE ANTIGEN, IDENTIFICATION IN A SFC(CUL7)-LIKE COMPLEX.
    8. "Dimerization of CUL7 and PARC is not required for all CUL7 functions and mouse development."
      Skaar J.R., Arai T., DeCaprio J.A.
      Mol. Cell. Biol. 25:5579-5589(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CUL9.
    9. "Cytoplasmic localized ubiquitin ligase cullin 7 binds to p53 and promotes cell growth by antagonizing p53 function."
      Andrews P., He Y.J., Xiong Y.
      Oncogene 25:4534-4548(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RBX1 AND TP53, SUBCELLULAR LOCATION.
    10. Cited for: FUNCTION, INTERACTION WITH CUL9; SKP1; FBXW8; RBX1 AND TP53, LACK OF NEDDYLATION.
    11. "Clinical, molecular and histopathological features of short stature syndrome with novel CUL7 mutation in Yakuts: new population isolate in Asia."
      Maksimova N., Hara K., Miyashia A., Nikolaeva I., Shiga A., Nogovicina A., Sukhomyasova A., Argunov V., Shvedova A., Ikeuchi T., Nishizawa M., Kuwano R., Onodera O.
      J. Med. Genet. 44:772-778(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN 3M1.
    12. "The CUL7 E3 ubiquitin ligase targets insulin receptor substrate 1 for ubiquitin-dependent degradation."
      Xu X., Sarikas A., Dias-Santagata D.C., Dolios G., Lafontant P.J., Tsai S.C., Zhu W., Nakajima H., Nakajima H.O., Field L.J., Wang R., Pan Z.Q.
      Mol. Cell 30:403-414(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Exome sequencing identifies CCDC8 mutations in 3-M syndrome, Suggesting that CCDC8 Contributes in a Pathway with CUL7 and OBSL1 to Control Human Growth."
      Hanson D., Murray P.G., O'Sullivan J., Urquhart J., Daly S., Bhaskar S.S., Biesecker L.G., Skae M., Smith C., Cole T., Kirk J., Chandler K., Kingston H., Donnai D., Clayton P.E., Black G.C.
      Am. J. Hum. Genet. 89:148-153(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH OBSL1.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi morphology and dendrite patterning."
      Litterman N., Ikeuchi Y., Gallardo G., O'Connell B.C., Sowa M.E., Gygi S.P., Harper J.W., Bonni A.
      PLoS Biol. 9:E1001060-E1001060(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FBXW8 AND OBSL1, SUBCELLULAR LOCATION.
    18. "Ubiquitin ligase cullin 7 induces epithelial-mesenchymal transition in human choriocarcinoma cells."
      Fu J., Lv X., Lin H., Wu L., Wang R., Zhou Z., Zhang B., Wang Y.L., Tsang B.K., Zhu C., Wang H.
      J. Biol. Chem. 285:10870-10879(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    19. "The CUL7/F-box and WD repeat domain containing 8 (CUL7/Fbxw8) ubiquitin ligase promotes degradation of hematopoietic progenitor kinase 1."
      Wang H., Chen Y., Lin P., Li L., Zhou G., Liu G., Logsdon C., Jin J., Abbruzzese J.L., Tan T.H., Wang H.
      J. Biol. Chem. 289:4009-4017(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FBXW8.
    20. Cited for: FUNCTION, IDENTIFICATION IN THE 3M COMPLEX, SUBCELLULAR LOCATION.
    21. "CUL9 mediates the functions of the 3M complex and ubiquitylates survivin to maintain genome integrity."
      Li Z., Pei X.H., Yan J., Yan F., Cappell K.M., Whitehurst A.W., Xiong Y.
      Mol. Cell 54:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CUL9.
    22. "The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53."
      Kaustov L., Lukin J., Lemak A., Duan S., Ho M., Doherty R., Penn L.Z., Arrowsmith C.H.
      J. Biol. Chem. 282:11300-11307(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 360-460, INTERACTION WITH TP53.
    23. Cited for: VARIANTS 3M1 ARG-1014; GLY-1246 AND PRO-1464, TISSUE SPECIFICITY.
    24. Cited for: VARIANT 3M1 PRO-1588.

    Entry informationi

    Entry nameiCUL7_HUMAN
    AccessioniPrimary (citable) accession number: Q14999
    Secondary accession number(s): B4DYZ0, F5H0L1, Q5T654
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 23, 2007
    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 6
      Human chromosome 6: 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

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