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P61202

- CSN2_MOUSE

UniProt

P61202 - CSN2_MOUSE

Protein

COP9 signalosome complex subunit 2

Gene

Cops2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (10 May 2004)
      Previous versions | rss
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    Functioni

    Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Involved in early stage of neuronal differentiation via its interaction with NIF3L1.3 Publications

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. transcription corepressor activity Source: MGI

    GO - Biological processi

    1. cell proliferation Source: MGI
    2. cullin deneddylation Source: Ensembl
    3. negative regulation of transcription, DNA-templated Source: MGI
    4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. neuron differentiation Source: Ensembl
    6. skeletal muscle cell differentiation Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    COP9 signalosome complex subunit 2
    Short name:
    SGN2
    Short name:
    Signalosome subunit 2
    Alternative name(s):
    Alien homolog
    JAB1-containing signalosome subunit 2
    Thyroid receptor-interacting protein 15
    Short name:
    TR-interacting protein 15
    Short name:
    TRIP-15
    Gene namesi
    Name:Cops2
    Synonyms:Csn2, Trip15
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1330276. Cops2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. COP9 signalosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Signalosome

    Pathology & Biotechi

    Disruption phenotypei

    Its absence causes arrest of embryo development at the peri-implantation stage. Blastocysts without Cops2 fail to outgrow in culture and exhibit a cell proliferation defect in inner cell mass, accompanied by a slight decrease in Oct4. In addition, lack of Cops2 disrupts the CSN complex and results in a drastic increase in cyclin E. It also induces elevated levels of p53 and p21, which may contribute to premature cell cycle arrest of the mutant.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443COP9 signalosome complex subunit 2PRO_0000120969Add
    BLAST

    Post-translational modificationi

    Phosphorylated by CK2 and PKD kinases.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP61202.
    PaxDbiP61202.
    PRIDEiP61202.

    PTM databases

    PhosphoSiteiP61202.

    Expressioni

    Tissue specificityi

    Widely expressed in embryonic, fetal and adult tissues, except cartilage and smooth muscle.1 Publication

    Gene expression databases

    ArrayExpressiP61202.
    BgeeiP61202.
    CleanExiMM_CSN2.
    GenevestigatoriP61202.

    Interactioni

    Subunit structurei

    Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and COPS8. In the complex, it probably interacts directly with COPS1, COPS4, COPS5 COPS6 and COPS7 (COPS7A or COPS7B). Specifically interacts with the ligand binding domain of the thyroid receptor (TR). Does not require the presence of thyroid hormone for its interaction. Interacts with IRF8/ICSBP1 and with nuclear receptors NR2F1 and NR0B1 By similarity. Interacts with NIF3L1. Interacts with CUL1 and CUL2.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi198836. 20 interactions.
    MINTiMINT-1869849.

    Structurei

    3D structure databases

    ProteinModelPortaliP61202.
    SMRiP61202. Positions 71-98, 133-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini248 – 413166PCIAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CSN2 family.Curated
    Contains 1 PCI domain.Curated

    Phylogenomic databases

    eggNOGiCOG5159.
    GeneTreeiENSGT00530000063301.
    HOVERGENiHBG003924.
    KOiK12176.
    OMAiYGLEYSE.
    OrthoDBiEOG7H7926.
    TreeFamiTF105738.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.25.40.10. 1 hit.
    InterProiIPR013143. PAM.
    IPR000717. PCI_dom.
    IPR011990. TPR-like_helical.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF01399. PCI. 1 hit.
    [Graphical view]
    SMARTiSM00753. PAM. 1 hit.
    SM00088. PINT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P61202-1) [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

    MSDMEDDFMC DDEEDYDLEY SEDSNSEPNV DLENQYYNSK ALKEDDPKAA    50
    LSSFQKVLEL EGEKGEWGFK ALKQMIKINF KLTNFPEMMN RYKQLLTYIR 100
    SAVTRNYSEK SINSILDYIS TSKQMDLLQE FYETTLEALK DAKNDRLWFK 150
    TNTKLGKLYL EREEYGKLQK ILRQLHQSCQ TDDGEDDLKK GTQLLEIYAL 200
    EIQMYTAQKN NKKLKALYEQ SLHIKSAIPH PLIMGVIREC GGKMHLREGE 250
    FEKAHTDFFE AFKNYDESGS PRRTTCLKYL VLANMLMKSG INPFDSQEAK 300
    PYKNDPEILA MTNLVSAYQN NDITEFEKIL KTNHSNIMDD PFIREHIEEL 350
    LRNIRTQVLI KLIKPYTRIH IPFISKELNI DVADVESLLV QCILDNTIHG 400
    RIDQVNQLLE LDHQKRGGAR YTALDKWTNQ LNSLNQAVVS KLA 443
    Length:443
    Mass (Da):51,597
    Last modified:May 10, 2004 - v1
    Checksum:i1DB6FA774C13BC59
    GO
    Isoform 2 (identifier: P61202-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         124-124: Q → QNSDFLCQ

    Show »
    Length:450
    Mass (Da):52,405
    Checksum:i581DE764677E90C0
    GO

    Sequence cautioni

    The sequence AAH23096.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401K → Y in BAB26900. (PubMed:16141072)Curated
    Sequence conflicti52 – 521S → T in BAB26900. (PubMed:16141072)Curated
    Sequence conflicti344 – 3441R → K in AAH23096. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei124 – 1241Q → QNSDFLCQ in isoform 2. 1 PublicationVSP_011885

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087688 mRNA. Translation: AAC36309.1.
    AF114247
    , AF114236, AF114237, AF114238, AF114239, AF114240, AF114241, AF114242, AF114244, AF114245, AF114246 Genomic DNA. Translation: AAD26162.1.
    AK010383 mRNA. Translation: BAB26900.1.
    AK084421 mRNA. Translation: BAC39179.1.
    AK132207 mRNA. Translation: BAE21033.1.
    BC023096 mRNA. Translation: AAH23096.1. Different initiation.
    AF071312 mRNA. Translation: AAC33899.1.
    CCDSiCCDS16679.1. [P61202-1]
    CCDS71133.1. [P61202-2]
    RefSeqiNP_001272441.1. NM_001285512.1.
    NP_034069.2. NM_009939.3. [P61202-1]
    UniGeneiMm.3596.

    Genome annotation databases

    EnsembliENSMUST00000028635; ENSMUSP00000028635; ENSMUSG00000027206. [P61202-1]
    ENSMUST00000110463; ENSMUSP00000106090; ENSMUSG00000027206. [P61202-2]
    GeneIDi12848.
    KEGGimmu:12848.
    UCSCiuc008mdb.1. mouse. [P61202-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087688 mRNA. Translation: AAC36309.1 .
    AF114247
    , AF114236 , AF114237 , AF114238 , AF114239 , AF114240 , AF114241 , AF114242 , AF114244 , AF114245 , AF114246 Genomic DNA. Translation: AAD26162.1 .
    AK010383 mRNA. Translation: BAB26900.1 .
    AK084421 mRNA. Translation: BAC39179.1 .
    AK132207 mRNA. Translation: BAE21033.1 .
    BC023096 mRNA. Translation: AAH23096.1 . Different initiation.
    AF071312 mRNA. Translation: AAC33899.1 .
    CCDSi CCDS16679.1. [P61202-1 ]
    CCDS71133.1. [P61202-2 ]
    RefSeqi NP_001272441.1. NM_001285512.1.
    NP_034069.2. NM_009939.3. [P61202-1 ]
    UniGenei Mm.3596.

    3D structure databases

    ProteinModelPortali P61202.
    SMRi P61202. Positions 71-98, 133-441.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198836. 20 interactions.
    MINTi MINT-1869849.

    PTM databases

    PhosphoSitei P61202.

    Proteomic databases

    MaxQBi P61202.
    PaxDbi P61202.
    PRIDEi P61202.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028635 ; ENSMUSP00000028635 ; ENSMUSG00000027206 . [P61202-1 ]
    ENSMUST00000110463 ; ENSMUSP00000106090 ; ENSMUSG00000027206 . [P61202-2 ]
    GeneIDi 12848.
    KEGGi mmu:12848.
    UCSCi uc008mdb.1. mouse. [P61202-1 ]

    Organism-specific databases

    CTDi 9318.
    MGIi MGI:1330276. Cops2.

    Phylogenomic databases

    eggNOGi COG5159.
    GeneTreei ENSGT00530000063301.
    HOVERGENi HBG003924.
    KOi K12176.
    OMAi YGLEYSE.
    OrthoDBi EOG7H7926.
    TreeFami TF105738.

    Miscellaneous databases

    ChiTaRSi COPS2. mouse.
    NextBioi 282396.
    PROi P61202.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61202.
    Bgeei P61202.
    CleanExi MM_CSN2.
    Genevestigatori P61202.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.25.40.10. 1 hit.
    InterProi IPR013143. PAM.
    IPR000717. PCI_dom.
    IPR011990. TPR-like_helical.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF01399. PCI. 1 hit.
    [Graphical view ]
    SMARTi SM00753. PAM. 1 hit.
    SM00088. PINT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Coding sequence, genomic organization, chromosomal localization, and expression pattern of the signalosome component Cops2: the mouse homologue of Drosophila alien."
      Schaefer L., Beermann M.L., Miller J.B.
      Genomics 56:310-316(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "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: Eye.
    3. "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] OF 2-443 (ISOFORM 1).
      Strain: Czech II.
      Tissue: Mammary tumor.
    4. "The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex."
      Wei N., Tsuge T., Serino G., Dohmae N., Takio K., Matsui M., Deng X.-W.
      Curr. Biol. 8:919-922(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-443 (ISOFORM 1), IDENTIFICATION IN THE CSN COMPLEX.
      Strain: C57BL/6.
    5. "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: FUNCTION, INTERACTION WITH CUL1 AND CUL2.
    6. "The role of transcriptional corepressor Nif3l1 in early stage of neural differentiation via cooperation with Trip15/CSN2."
      Akiyama H., Fujisawa N., Tashiro Y., Takanabe N., Sugiyama A., Tashiro F.
      J. Biol. Chem. 278:10752-10762(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NIF3L1.
    7. "Disruption of the COP9 signalosome Csn2 subunit in mice causes deficient cell proliferation, accumulation of p53 and cyclin E, and early embryonic death."
      Lykke-Andersen K., Schaefer L., Menon S., Deng X.-W., Miller J.B., Wei N.
      Mol. Cell. Biol. 23:6790-6797(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiCSN2_MOUSE
    AccessioniPrimary (citable) accession number: P61202
    Secondary accession number(s): O88950
    , Q15647, Q3V1W6, Q8R5B0, Q9CWU1, Q9R249, Q9UNQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3