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Q13617

- CUL2_HUMAN

UniProt

Q13617 - CUL2_HUMAN

Protein

Cullin-2

Gene

CUL2

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 2 (14 Aug 2001)
      Previous versions | rss
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    Functioni

    Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. May serve as a rigid scaffold in the complex and 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 By similarity. The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF).By similarity

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: ProtInc
    2. cellular response to hypoxia Source: Reactome
    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. protein ubiquitination Source: UniProtKB-UniPathway
    7. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    8. ubiquitin-dependent protein catabolic process Source: InterPro
    9. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cullin-2
    Short name:
    CUL-2
    Gene namesi
    Name:CUL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:2552. CUL2.

    Subcellular locationi

    GO - Cellular componenti

    1. Cul2-RING ubiquitin ligase complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA
    5. VCB complex Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi621 – 6211K → R: No effect on conjugation with NEDD8. 1 Publication
    Mutagenesisi689 – 6891K → R: Loss of conjugation with NEDD8. 1 Publication
    Mutagenesisi719 – 7191K → R: No effect on conjugation with NEDD8. 1 Publication

    Organism-specific databases

    PharmGKBiPA27048.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 745745Cullin-2PRO_0000119790Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei393 – 3931N6-acetyllysine1 Publication
    Modified residuei661 – 6611Phosphothreonine1 Publication
    Cross-linki689 – 689Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)

    Post-translational modificationi

    CBC(VHL) complex formation seems to promote neddylation. Deneddylated via its interaction with the COP9 signalosome (CSN) complex By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ13617.
    PaxDbiQ13617.
    PRIDEiQ13617.

    PTM databases

    PhosphoSiteiQ13617.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13617.
    BgeeiQ13617.
    CleanExiHS_CUL2.
    GenevestigatoriQ13617.

    Organism-specific databases

    HPAiCAB002677.
    HPA024578.

    Interactioni

    Subunit structurei

    Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes formed of CUL2, Elongin BC (TCEB1 and TCEB2), RBX1 and a variable substrate-specific adapter. Component of the ECS(VHL) or CBC(VHL) complex containing VHL. Component of the ECS(MED8) complex with the probable substrate recognition component MED8. Component of the ECS(LRR1) complex with the probable substrate recognition component LRR1. Component of a probable ECS E3 ubiquitin-protein ligase complex containing CUL2, RBX1, TCEB1, TCEB2 and FEM1B. Part of an E3 ubiquitin-protein ligase complex including ZYG11B, CUL2 and Elongin BC. Part of an E3 ubiquitin-protein ligase complex including ZYG11BL, CUL2 and Elongin BC. Interacts with RBX1, RNF7, FEM1B and TIP120A/CAND1. Interacts with COPS2, and MED8. Interacts with human respiratory syncytial virus (HRSV) protein NS1. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 and CUL2. Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex substrate recognition component.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAND1Q86VP63EBI-456179,EBI-456077
    COMMD1Q8N6683EBI-456179,EBI-1550112
    RBX1P628775EBI-456179,EBI-398523
    TCEB1Q153695EBI-456179,EBI-301231
    VHLP403379EBI-456179,EBI-301246
    vifP125045EBI-456179,EBI-779991From a different organism.

    Protein-protein interaction databases

    BioGridi114031. 454 interactions.
    DIPiDIP-31612N.
    IntActiQ13617. 40 interactions.
    MINTiMINT-1523339.
    STRINGi9606.ENSP00000363880.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13617.
    SMRiQ13617. Positions 8-745.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cullin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5647.
    HOVERGENiHBG106177.
    InParanoidiQ13617.
    KOiK03870.
    OMAiVMLDYVE.
    OrthoDBiEOG7X3QQG.
    PhylomeDBiQ13617.
    TreeFamiTF101152.

    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: Q13617-1) [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

    MSLKPRVVDF DETWNKLLTT IKAVVMLEYV ERATWNDRFS DIYALCVAYP    50
    EPLGERLYTE TKIFLENHVR HLHKRVLESE EQVLVMYHRY WEEYSKGADY 100
    MDCLYRYLNT QFIKKNKLTE ADLQYGYGGV DMNEPLMEIG ELALDMWRKL 150
    MVEPLQAILI RMLLREIKND RGGEDPNQKV IHGVINSFVH VEQYKKKFPL 200
    KFYQEIFESP FLTETGEYYK QEASNLLQES NCSQYMEKVL GRLKDEEIRC 250
    RKYLHPSSYT KVIHECQQRM VADHLQFLHA ECHNIIRQEK KNDMANMYVL 300
    LRAVSTGLPH MIQELQNHIH DEGLRATSNL TQENMPTLFV ESVLEVHGKF 350
    VQLINTVLNG DQHFMSALDK ALTSVVNYRE PKSVCKAPEL LAKYCDNLLK 400
    KSAKGMTENE VEDRLTSFIT VFKYIDDKDV FQKFYARMLA KRLIHGLSMS 450
    MDSEEAMINK LKQACGYEFT SKLHRMYTDM SVSADLNNKF NNFIKNQDTV 500
    IDLGISFQIY VLQAGAWPLT QAPSSTFAIP QELEKSVQMF ELFYSQHFSG 550
    RKLTWLHYLC TGEVKMNYLG KPYVAMVTTY QMAVLLAFNN SETVSYKELQ 600
    DSTQMNEKEL TKTIKSLLDV KMINHDSEKE DIDAESSFSL NMNFSSKRTK 650
    FKITTSMQKD TPQEMEQTRS AVDEDRKMYL QAAIVRIMKA RKVLRHNALI 700
    QEVISQSRAR FNPSISMIKK CIEVLIDKQY IERSQASADE YSYVA 745
    Length:745
    Mass (Da):86,983
    Last modified:August 14, 2001 - v2
    Checksum:i30647248F671AB0E
    GO
    Isoform 2 (identifier: Q13617-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MYRVTWSTFWLRFQHYTCTM

    Note: No experimental confirmation available.

    Show »
    Length:764
    Mass (Da):89,492
    Checksum:i11890883B1EA53A4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201T → I in BAH13294. (PubMed:14702039)Curated
    Sequence conflicti95 – 984SKGA → IRHE in AAC50545. (PubMed:8681378)Curated
    Sequence conflicti681 – 6811Q → H in AAC50545. (PubMed:8681378)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti109 – 1091N → S.2 Publications
    Corresponds to variant rs1131503 [ dbSNP | Ensembl ].
    VAR_011374

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MYRVTWSTFWLRFQHYTCTM in isoform 2. 1 PublicationVSP_044498

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U83410 mRNA. Translation: AAC51190.1.
    AF126404 mRNA. Translation: AAD23581.1.
    AK095217 mRNA. Translation: BAG53007.1.
    AK300491 mRNA. Translation: BAH13294.1.
    AL392046 Genomic DNA. Translation: CAI13163.1.
    CH471072 Genomic DNA. Translation: EAW85924.1.
    CH471072 Genomic DNA. Translation: EAW85925.1.
    CH471072 Genomic DNA. Translation: EAW85926.1.
    CH471072 Genomic DNA. Translation: EAW85927.1.
    CH471072 Genomic DNA. Translation: EAW85928.1.
    BC009591 mRNA. Translation: AAH09591.1.
    BC110901 mRNA. Translation: AAI10902.1.
    U58088 mRNA. Translation: AAC50545.1.
    CCDSiCCDS55709.1. [Q13617-2]
    CCDS7179.1. [Q13617-1]
    RefSeqiNP_001185706.1. NM_001198777.1. [Q13617-1]
    NP_001185707.1. NM_001198778.1. [Q13617-2]
    NP_001185708.1. NM_001198779.1.
    NP_003582.2. NM_003591.3. [Q13617-1]
    UniGeneiHs.82919.

    Genome annotation databases

    EnsembliENST00000374748; ENSP00000363880; ENSG00000108094. [Q13617-1]
    ENST00000374749; ENSP00000363881; ENSG00000108094. [Q13617-1]
    ENST00000374751; ENSP00000363883; ENSG00000108094. [Q13617-1]
    ENST00000537177; ENSP00000444856; ENSG00000108094. [Q13617-2]
    GeneIDi8453.
    KEGGihsa:8453.
    UCSCiuc001ixv.3. human. [Q13617-1]
    uc010qer.2. human. [Q13617-2]

    Polymorphism databases

    DMDMi19863260.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U83410 mRNA. Translation: AAC51190.1 .
    AF126404 mRNA. Translation: AAD23581.1 .
    AK095217 mRNA. Translation: BAG53007.1 .
    AK300491 mRNA. Translation: BAH13294.1 .
    AL392046 Genomic DNA. Translation: CAI13163.1 .
    CH471072 Genomic DNA. Translation: EAW85924.1 .
    CH471072 Genomic DNA. Translation: EAW85925.1 .
    CH471072 Genomic DNA. Translation: EAW85926.1 .
    CH471072 Genomic DNA. Translation: EAW85927.1 .
    CH471072 Genomic DNA. Translation: EAW85928.1 .
    BC009591 mRNA. Translation: AAH09591.1 .
    BC110901 mRNA. Translation: AAI10902.1 .
    U58088 mRNA. Translation: AAC50545.1 .
    CCDSi CCDS55709.1. [Q13617-2 ]
    CCDS7179.1. [Q13617-1 ]
    RefSeqi NP_001185706.1. NM_001198777.1. [Q13617-1 ]
    NP_001185707.1. NM_001198778.1. [Q13617-2 ]
    NP_001185708.1. NM_001198779.1.
    NP_003582.2. NM_003591.3. [Q13617-1 ]
    UniGenei Hs.82919.

    3D structure databases

    ProteinModelPortali Q13617.
    SMRi Q13617. Positions 8-745.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114031. 454 interactions.
    DIPi DIP-31612N.
    IntActi Q13617. 40 interactions.
    MINTi MINT-1523339.
    STRINGi 9606.ENSP00000363880.

    PTM databases

    PhosphoSitei Q13617.

    Polymorphism databases

    DMDMi 19863260.

    Proteomic databases

    MaxQBi Q13617.
    PaxDbi Q13617.
    PRIDEi Q13617.

    Protocols and materials databases

    DNASUi 8453.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374748 ; ENSP00000363880 ; ENSG00000108094 . [Q13617-1 ]
    ENST00000374749 ; ENSP00000363881 ; ENSG00000108094 . [Q13617-1 ]
    ENST00000374751 ; ENSP00000363883 ; ENSG00000108094 . [Q13617-1 ]
    ENST00000537177 ; ENSP00000444856 ; ENSG00000108094 . [Q13617-2 ]
    GeneIDi 8453.
    KEGGi hsa:8453.
    UCSCi uc001ixv.3. human. [Q13617-1 ]
    uc010qer.2. human. [Q13617-2 ]

    Organism-specific databases

    CTDi 8453.
    GeneCardsi GC10M035338.
    HGNCi HGNC:2552. CUL2.
    HPAi CAB002677.
    HPA024578.
    MIMi 603135. gene.
    neXtProti NX_Q13617.
    PharmGKBi PA27048.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5647.
    HOVERGENi HBG106177.
    InParanoidi Q13617.
    KOi K03870.
    OMAi VMLDYVE.
    OrthoDBi EOG7X3QQG.
    PhylomeDBi Q13617.
    TreeFami TF101152.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi CUL2. human.
    GeneWikii CUL2.
    GenomeRNAii 8453.
    NextBioi 31634.
    PROi Q13617.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13617.
    Bgeei Q13617.
    CleanExi HS_CUL2.
    Genevestigatori Q13617.

    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 von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins."
      Pause A., Lee S., Worrel R., Chen D.Y.T., Burgess W.H., Linehan W.M., Klausner R.D.
      Proc. Natl. Acad. Sci. U.S.A. 94:2156-2161(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-109, IDENTIFICATION IN COMPLEX WITH VHL AND ELONGIN BC.
      Tissue: Kidney.
    2. "Identification of NEDD8-conjugation site in human cullin-2."
      Wada H., Yeh E.T.H., Kamitani T.
      Biochem. Biophys. Res. Commun. 257:100-105(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-109, MUTAGENESIS OF LYS-621; LYS-689 AND LYS-719, NEDDYLATION AT LYS-689.
      Tissue: Brain.
    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 AND 2).
      Tissue: Prostate.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain and Skin.
    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 95-745.
    8. "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity."
      Ohta T., Michel J.J., Schottelius A.J., Xiong Y.
      Mol. Cell 3:535-541(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBX1 AND RNF7.
    9. "Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex."
      Kamura T., Sato S., Iwai K., Czyzyk-Krzeska M., Conaway R.C., Conaway J.W.
      Proc. Natl. Acad. Sci. U.S.A. 97:10430-10435(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN CBC(VHL) COMPLEX.
    10. "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase."
      Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E., Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.
      J. Biol. Chem. 276:29748-29753(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH VHL; ELONGIN BC AND RBX1.
    11. "Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase."
      Brower C.S., Sato S., Tomomori-Sato C., Kamura T., Pause A., Stearman R., Klausner R.D., Malik S., Lane W.S., Sorokina I., Roeder R.G., Conaway J.W., Conaway R.C.
      Proc. Natl. Acad. Sci. U.S.A. 99:10353-10358(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH MED8.
    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. "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.
    14. "VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases."
      Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C., Conaway J.W., Nakayama K.I.
      Genes Dev. 18:3055-3065(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRR1 AND FEM1B.
    15. "The Caenorhabditis elegans cell-cycle regulator ZYG-11 defines a conserved family of CUL-2 complex components."
      Vasudevan S., Starostina N.G., Kipreos E.T.
      EMBO Rep. 8:279-286(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH TCEB1 AND ZYG11B, IDENTIFICATION IN COMPLEX WITH TCEB1; TCEB2 AND CUL2.
    16. "Respiratory syncytial virus NS1 protein degrades STAT2 by using the Elongin-Cullin E3 ligase."
      Elliott J., Lynch O.T., Suessmuth Y., Qian P., Boyd C.R., Burrows J.F., Buick R., Stevenson N.J., Touzelet O., Gadina M., Power U.F., Johnston J.A.
      J. Virol. 81:3428-3436(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRSV VIRUS PROTEIN NS1.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1 activation by suppressing PP5."
      Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T., Kuranaga E., Miura M., Takeda K., Ichijo H.
      Mol. Cell 48:692-704(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTS WITH KLHDC10.
    21. Cited for: IDENTIFICATION IN A COMPLEX WITH LIMD1; EGLN1/PHD2; VHL AND TCEB2.

    Entry informationi

    Entry nameiCUL2_HUMAN
    AccessioniPrimary (citable) accession number: Q13617
    Secondary accession number(s): B3KT95
    , B7Z6K8, D3DRY6, G3V1S2, O00200, Q5T2B6, Q9UNF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: August 14, 2001
    Last modified: October 1, 2014
    This is version 136 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3