Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9D4H8

- CUL2_MOUSE

UniProt

Q9D4H8 - CUL2_MOUSE

Protein

Cullin-2

Gene

Cul2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (07 Nov 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.By similarity

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

    1. protein catabolic process Source: MGI
    2. protein ubiquitination Source: UniProtKB-UniPathway
    3. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_199108. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cullin-2
    Short name:
    CUL-2
    Gene namesi
    Name:Cul2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1918995. Cul2.

    Subcellular locationi

    GO - Cellular componenti

    1. Cul2-RING ubiquitin ligase complex Source: Ensembl
    2. VCB complex Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 745745Cullin-2PRO_0000119791Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9D4H8.
    PaxDbiQ9D4H8.
    PRIDEiQ9D4H8.

    PTM databases

    PhosphoSiteiQ9D4H8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9D4H8.
    BgeeiQ9D4H8.
    CleanExiMM_CUL2.
    GenevestigatoriQ9D4H8.

    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.2 Publications

    Protein-protein interaction databases

    BioGridi214895. 6 interactions.
    IntActiQ9D4H8. 7 interactions.
    MINTiMINT-4092642.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D4H8.
    SMRiQ9D4H8. Positions 4-745.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cullin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5647.
    GeneTreeiENSGT00730000110820.
    HOGENOMiHOG000176713.
    HOVERGENiHBG106177.
    InParanoidiQ9D4H8.
    KOiK03870.
    OMAiVMLDYVE.
    OrthoDBiEOG7X3QQG.
    PhylomeDBiQ9D4H8.
    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: Q9D4H8-1) [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
    EPLGERLYAE TKIFLESHVR HLYKRVLESE EQVLVMYHRY WEEYSKGADY 100
    MDCLYRYLNT QYIKKNKLTE ADIQYGYGGV DMNEPLMEIG ELALDMWRKL 150
    MVEPLQNILI RMLLREIKND RGGEDPNQKV IHGVINSFVH VEQYKKKFPL 200
    KFYQGIFVSP FLTETGEYYK QEASNLLQES NCSQYMEKVL GRLKDEEIRC 250
    RKYLHPSSYT KVIHECQQRM VADHLQFLHS ECHSIIQQER KNDMANMYVL 300
    LRAVSSGLPH MIEELQKHIH DEGLRATSNL TQEHMPTLFV ESVLEVHGKF 350
    VQLINTVLNG DQHFMSALDK ALTSVVNYRE PKSVCKAPEL LAKYCDNLLK 400
    KSAKGMTENE VEDKLTSFIT VFKYIDDKDV FQKFYARMLA KRLIHGLSMS 450
    MDSEEAMINK LKQACGYEFT SKLHRMYTDM SVSADLNNKF NNFIRNQDTV 500
    IDLGISFQIY VLQAGAWPLT QAPSSTFAIP QELEKSVQMF ELFYSQHFSG 550
    RKLTWLHYLC TGEVKMNYLG KPYVAMVTTY QMAVLLAFNN SETVSYKELQ 600
    DSTQMNEKEL TKTIKSLLDV KMINHDSEKE DIDAESSFSL NMSFSSKRTK 650
    FKITTSMQKD TPQELEQTRS AVDEDRKMYL QAAIVRIMKA RKVLRHNALI 700
    QEVISQSRAR FNPSISMIKK CIEVLIDKQY IERSQASADE YSYVA 745
    Length:745
    Mass (Da):86,877
    Last modified:November 7, 2003 - v2
    Checksum:i311C05CC262692E0
    GO
    Isoform 2 (identifier: Q9D4H8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         664-702: Missing.

    Show »
    Length:706
    Mass (Da):82,271
    Checksum:iDDF5F2945896FA3D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti612 – 6121K → R in BAB30283. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei664 – 70239Missing in isoform 2. 2 PublicationsVSP_008823Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK016520 mRNA. Translation: BAB30283.1.
    AK160597 mRNA. Translation: BAE35903.1.
    BC026779 mRNA. Translation: AAH26779.1.
    BC027428 mRNA. Translation: AAH27428.1.
    BC025902 mRNA. Translation: AAH25902.1.
    CCDSiCCDS29032.2. [Q9D4H8-1]
    RefSeqiNP_083678.2. NM_029402.3. [Q9D4H8-1]
    XP_006526337.1. XM_006526274.1. [Q9D4H8-1]
    XP_006526338.1. XM_006526275.1. [Q9D4H8-1]
    UniGeneiMm.291707.
    Mm.443148.

    Genome annotation databases

    EnsembliENSMUST00000025073; ENSMUSP00000025073; ENSMUSG00000024231. [Q9D4H8-2]
    ENSMUST00000162301; ENSMUSP00000125403; ENSMUSG00000024231. [Q9D4H8-1]
    GeneIDi71745.
    KEGGimmu:71745.
    UCSCiuc008dxz.2. mouse. [Q9D4H8-2]
    uc008dya.2. mouse. [Q9D4H8-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK016520 mRNA. Translation: BAB30283.1 .
    AK160597 mRNA. Translation: BAE35903.1 .
    BC026779 mRNA. Translation: AAH26779.1 .
    BC027428 mRNA. Translation: AAH27428.1 .
    BC025902 mRNA. Translation: AAH25902.1 .
    CCDSi CCDS29032.2. [Q9D4H8-1 ]
    RefSeqi NP_083678.2. NM_029402.3. [Q9D4H8-1 ]
    XP_006526337.1. XM_006526274.1. [Q9D4H8-1 ]
    XP_006526338.1. XM_006526275.1. [Q9D4H8-1 ]
    UniGenei Mm.291707.
    Mm.443148.

    3D structure databases

    ProteinModelPortali Q9D4H8.
    SMRi Q9D4H8. Positions 4-745.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 214895. 6 interactions.
    IntActi Q9D4H8. 7 interactions.
    MINTi MINT-4092642.

    PTM databases

    PhosphoSitei Q9D4H8.

    Proteomic databases

    MaxQBi Q9D4H8.
    PaxDbi Q9D4H8.
    PRIDEi Q9D4H8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025073 ; ENSMUSP00000025073 ; ENSMUSG00000024231 . [Q9D4H8-2 ]
    ENSMUST00000162301 ; ENSMUSP00000125403 ; ENSMUSG00000024231 . [Q9D4H8-1 ]
    GeneIDi 71745.
    KEGGi mmu:71745.
    UCSCi uc008dxz.2. mouse. [Q9D4H8-2 ]
    uc008dya.2. mouse. [Q9D4H8-1 ]

    Organism-specific databases

    CTDi 8453.
    MGIi MGI:1918995. Cul2.

    Phylogenomic databases

    eggNOGi COG5647.
    GeneTreei ENSGT00730000110820.
    HOGENOMi HOG000176713.
    HOVERGENi HBG106177.
    InParanoidi Q9D4H8.
    KOi K03870.
    OMAi VMLDYVE.
    OrthoDBi EOG7X3QQG.
    PhylomeDBi Q9D4H8.
    TreeFami TF101152.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_199108. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    NextBioi 334387.
    PROi Q9D4H8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D4H8.
    Bgeei Q9D4H8.
    CleanExi MM_CUL2.
    Genevestigatori Q9D4H8.

    Family and domain databases

    Gene3Di 1.10.10.10. 2 hits.
    InterProi IPR016157. Cullin_CS.
    IPR016158. Cullin_homology.
    IPR001373. Cullin_N.
    IPR019559. Cullin_neddylation_domain.
    IPR016159. Cullin_repeat-like_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00888. Cullin. 1 hit.
    PF10557. Cullin_Nedd8. 1 hit.
    [Graphical view ]
    SMARTi SM00182. CULLIN. 1 hit.
    SM00884. Cullin_Nedd8. 1 hit.
    [Graphical view ]
    SUPFAMi SSF74788. SSF74788. 1 hit.
    SSF75632. SSF75632. 1 hit.
    PROSITEi PS01256. CULLIN_1. 1 hit.
    PS50069. CULLIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Testis.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and Czech II.
      Tissue: Mammary tumor.
    3. "The COP9 signalosome inhibits p27(kip1) degradation and impedes G1-S phase progression via deneddylation of SCF Cul1."
      Yang X., Menon S., Lykke-Andersen K., Tsuge T., Xiao D., Wang X., Rodriguez-Suarez R.J., Zhang H., Wei N.
      Curr. Biol. 12:667-672(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COPS2.
    4. "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: INTERACTION WITH MED8.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiCUL2_MOUSE
    AccessioniPrimary (citable) accession number: Q9D4H8
    Secondary accession number(s): Q3TUR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: November 7, 2003
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3