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Q92905

- CSN5_HUMAN

UniProt

Q92905 - CSN5_HUMAN

Protein

COP9 signalosome complex subunit 5

Gene

COPS5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Probable protease subunit 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 the 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, 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. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. Promotes the proteasomal degradation of BRSK2.7 Publications

    Cofactori

    Divalent metal ions.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi138 – 1381Zinc; catalyticCurated
    Metal bindingi140 – 1401Zinc; catalyticBy similarity
    Metal bindingi151 – 1511Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metallopeptidase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. transcription coactivator activity Source: ProtInc
    5. translation initiation factor activity Source: ProtInc
    6. ubiquitin-specific protease activity Source: FlyBase

    GO - Biological processi

    1. cullin deneddylation Source: UniProtKB
    2. exosomal secretion Source: FlyBase
    3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    4. protein deneddylation Source: UniProtKB
    5. protein deubiquitination Source: FlyBase
    6. regulation of cell cycle Source: Ensembl
    7. regulation of JNK cascade Source: UniProtKB
    8. transcription from RNA polymerase II promoter Source: ProtInc
    9. translation Source: ProtInc
    10. translational initiation Source: GOC

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding

    Protein family/group databases

    MEROPSiM67.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    COP9 signalosome complex subunit 5 (EC:3.4.-.-)
    Short name:
    SGN5
    Short name:
    Signalosome subunit 5
    Alternative name(s):
    Jun activation domain-binding protein 1
    Gene namesi
    Name:COPS5
    Synonyms:CSN5, JAB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:2240. COPS5.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmperinuclear region. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle
    Note: Nuclear localization is diminished in the presence of IFIT3.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. COP9 signalosome Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. eukaryotic translation initiation factor 3 complex Source: ProtInc
    5. nucleus Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. synaptic vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoplasmic vesicle, Nucleus, Signalosome, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi138 – 1381H → Q: Abolishes ability to deneddylate cullins, without affecting the 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex. 1 Publication

    Organism-specific databases

    PharmGKBiPA26757.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 334333COP9 signalosome complex subunit 5PRO_0000194835Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ92905.
    PaxDbiQ92905.
    PRIDEiQ92905.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00009958.

    PTM databases

    PhosphoSiteiQ92905.

    Expressioni

    Gene expression databases

    ArrayExpressiQ92905.
    BgeeiQ92905.
    CleanExiHS_COPS5.
    GenevestigatoriQ92905.

    Organism-specific databases

    HPAiCAB004242.
    HPA004845.

    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, COPS2, COPS4, COPS6 and COPS7 (COPS7A or COPS7B). The CSN complex interacts with the BRISC complex. Also exists as monomeric form. Interacts with TP53, MIF, JUN, UCHL1, NCOA1, HIF1A, CDKN1B, BCL3, GFER, PGR, LHCGR, SMAD4, SMAD7, ID1, ID3, ITGB2 and TOP2A. Part of a complex consisting of RANBP9, Ran, DYRK1B and COPS5. Interacts with IFIT3. Interacts with BRSK2.16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCNDBP1O952735EBI-594661,EBI-748961
    CDKN1BP465273EBI-594661,EBI-519280
    F2RL1P550858EBI-594661,EBI-4303189
    FAM188AQ9H8M73EBI-594661,EBI-724928
    GPS1Q130983EBI-594661,EBI-725197
    OPRM1P353725EBI-594661,EBI-2624570
    RNF20Q5VTR22EBI-594661,EBI-2372238
    SMAD7O1510510EBI-594661,EBI-3861591
    TXNP105998EBI-594661,EBI-594644
    UCHL1P099363EBI-594661,EBI-714860

    Protein-protein interaction databases

    BioGridi116183. 778 interactions.
    DIPiDIP-34546N.
    IntActiQ92905. 126 interactions.
    MINTiMINT-1188008.
    STRINGi9606.ENSP00000350512.

    Structurei

    Secondary structure

    1
    334
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1611
    Helixi33 – 4210
    Turni45 – 473
    Beta strandi54 – 585
    Helixi59 – 7113
    Turni72 – 743
    Beta strandi78 – 869
    Beta strandi89 – 979
    Helixi104 – 1074
    Helixi112 – 12413
    Beta strandi125 – 1273
    Beta strandi133 – 1397
    Turni141 – 1433
    Helixi149 – 16113
    Beta strandi167 – 1704
    Beta strandi183 – 1886
    Beta strandi221 – 2233
    Beta strandi225 – 2317
    Helixi235 – 25016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4F7OX-ray2.60A/B1-257[»]
    ProteinModelPortaliQ92905.
    SMRiQ92905. Positions 2-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 164112MPNAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi138 – 15114JAMM motifAdd
    BLAST

    Domaini

    The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex By similarity.By similarity

    Sequence similaritiesi

    Belongs to the peptidase M67A family. CSN5 subfamily.Curated
    Contains 1 MPN (JAB/Mov34) domain.Curated

    Phylogenomic databases

    eggNOGiCOG1310.
    HOGENOMiHOG000116528.
    HOVERGENiHBG051137.
    InParanoidiQ92905.
    KOiK09613.
    OMAiMQEVQSI.
    OrthoDBiEOG72NRQC.
    PhylomeDBiQ92905.
    TreeFamiTF105601.

    Family and domain databases

    InterProiIPR000555. JAMM/MPN+_dom.
    [Graphical view]
    PfamiPF01398. JAB. 1 hit.
    [Graphical view]
    SMARTiSM00232. JAB_MPN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q92905-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASGSGMAQ KTWELANNMQ EAQSIDEIYK YDKKQQQEIL AAKPWTKDHH    50
    YFKYCKISAL ALLKMVMHAR SGGNLEVMGL MLGKVDGETM IIMDSFALPV 100
    EGTETRVNAQ AAAYEYMAAY IENAKQVGRL ENAIGWYHSH PGYGCWLSGI 150
    DVSTQMLNQQ FQEPFVAVVI DPTRTISAGK VNLGAFRTYP KGYKPPDEGP 200
    SEYQTIPLNK IEDFGVHCKQ YYALEVSYFK SSLDRKLLEL LWNKYWVNTL 250
    SSSSLLTNAD YTTGQVFDLS EKLEQSEAQL GRGSFMLGLE THDRKSEDKL 300
    AKATRDSCKT TIEAIHGLMS QVIKDKLFNQ INIS 334
    Length:334
    Mass (Da):37,579
    Last modified:January 23, 2007 - v4
    Checksum:iB5742F4AAD03A1CF
    GO

    Sequence cautioni

    The sequence AAL82571.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 453KPW → NLG in AAD03468. (PubMed:9341143)Curated
    Sequence conflicti129 – 1291R → H in AAB16847. (PubMed:8837781)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65928 mRNA. Translation: AAB16847.1.
    U70734 mRNA. Translation: AAD03468.1.
    CR541678 mRNA. Translation: CAG46479.1.
    BC001187 mRNA. Translation: AAH01187.1.
    BC001859 mRNA. Translation: AAH01859.1.
    BC007272 mRNA. Translation: AAH07272.1.
    BX648542 mRNA. Translation: CAH10375.1.
    AY078082 mRNA. Translation: AAL82571.1. Different initiation.
    CCDSiCCDS6198.1.
    PIRiS71820.
    RefSeqiNP_006828.2. NM_006837.2.
    UniGeneiHs.491912.

    Genome annotation databases

    EnsembliENST00000357849; ENSP00000350512; ENSG00000121022.
    GeneIDi10987.
    KEGGihsa:10987.
    UCSCiuc003xxd.3. human.

    Polymorphism databases

    DMDMi55976562.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65928 mRNA. Translation: AAB16847.1 .
    U70734 mRNA. Translation: AAD03468.1 .
    CR541678 mRNA. Translation: CAG46479.1 .
    BC001187 mRNA. Translation: AAH01187.1 .
    BC001859 mRNA. Translation: AAH01859.1 .
    BC007272 mRNA. Translation: AAH07272.1 .
    BX648542 mRNA. Translation: CAH10375.1 .
    AY078082 mRNA. Translation: AAL82571.1 . Different initiation.
    CCDSi CCDS6198.1.
    PIRi S71820.
    RefSeqi NP_006828.2. NM_006837.2.
    UniGenei Hs.491912.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4F7O X-ray 2.60 A/B 1-257 [» ]
    ProteinModelPortali Q92905.
    SMRi Q92905. Positions 2-327.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116183. 778 interactions.
    DIPi DIP-34546N.
    IntActi Q92905. 126 interactions.
    MINTi MINT-1188008.
    STRINGi 9606.ENSP00000350512.

    Protein family/group databases

    MEROPSi M67.002.

    PTM databases

    PhosphoSitei Q92905.

    Polymorphism databases

    DMDMi 55976562.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00009958.

    Proteomic databases

    MaxQBi Q92905.
    PaxDbi Q92905.
    PRIDEi Q92905.

    Protocols and materials databases

    DNASUi 10987.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357849 ; ENSP00000350512 ; ENSG00000121022 .
    GeneIDi 10987.
    KEGGi hsa:10987.
    UCSCi uc003xxd.3. human.

    Organism-specific databases

    CTDi 10987.
    GeneCardsi GC08M068005.
    HGNCi HGNC:2240. COPS5.
    HPAi CAB004242.
    HPA004845.
    MIMi 604850. gene.
    neXtProti NX_Q92905.
    PharmGKBi PA26757.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1310.
    HOGENOMi HOG000116528.
    HOVERGENi HBG051137.
    InParanoidi Q92905.
    KOi K09613.
    OMAi MQEVQSI.
    OrthoDBi EOG72NRQC.
    PhylomeDBi Q92905.
    TreeFami TF105601.

    Miscellaneous databases

    ChiTaRSi COPS5. human.
    GenomeRNAii 10987.
    NextBioi 41743.
    PROi Q92905.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92905.
    Bgeei Q92905.
    CleanExi HS_COPS5.
    Genevestigatori Q92905.

    Family and domain databases

    InterProi IPR000555. JAMM/MPN+_dom.
    [Graphical view ]
    Pfami PF01398. JAB. 1 hit.
    [Graphical view ]
    SMARTi SM00232. JAB_MPN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new group of conserved coactivators that increase the specificity of AP-1 transcription factors."
      Claret F.-X., Hibi M., Dhut S., Toda T., Karin M.
      Nature 383:453-457(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH JUN.
    2. "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly."
      Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C., Hinnebusch A.G., Hershey J.W.B.
      J. Biol. Chem. 272:27042-27052(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
      Tissue: Brain, Eye and Muscle.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-47.
      Tissue: Liver.
    6. Bienvenut W.V., Quadroni M.
      Submitted (OCT-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11; 57-64; 181-187; 237-244 AND 273-282, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    7. "The fusion gene of human Jun activation domain binding protein and membrane cofactor protein which cloned from multiple myeloma cell line ARH-77."
      Hu W., Tian J.
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 146-334.
    8. "A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits."
      Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R., Schade R., Gordon C., Naumann M., Dubiel W.
      FASEB J. 12:469-478(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
    9. "The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators."
      Dechend R., Hirano F., Lehmann K., Heissmeyer V., Ansieau S., Wulczyn F.G., Scheidereit C., Leutz A.
      Oncogene 18:3316-3323(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCL3.
    10. Cited for: INTERACTION WITH NCOA1 AND PGR.
    11. Cited for: INTERACTION WITH MIF.
    12. "Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity."
      Bianchi E., Denti S., Granata A., Bossi G., Geginat J., Villa A., Rogge L., Pardi R.
      Nature 404:617-621(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB2.
    13. "COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system."
      Bech-Otschir D., Kraft R., Huang X., Henklein P., Kapelari B., Pollmann C., Dubiel W.
      EMBO J. 20:1630-1639(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53.
    14. Cited for: FUNCTION, COMPOSITION OF THE CSN COMPLEX.
    15. "Jab1 antagonizes TGF-beta signaling by inducing Smad4 degradation."
      Wan M., Cao X., Wu Y., Bai S., Wu L., Shi X., Wang N., Cao X.
      EMBO Rep. 3:171-176(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMAD4.
    16. "Intracrine hepatopoietin potentiates AP-1 activity through JAB1 independent of MAPK pathway."
      Lu C., Li Y., Zhao Y., Xing G., Tang F., Wang Q., Sun Y., Wei H., Yang X., Wu C., Chen J., Guan K.-L., Zhang C., Chen H., He F.
      FASEB J. 16:90-92(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GFER.
    17. Cited for: INTERACTION WITH UCHL1.
    18. "The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage."
      Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.
      Cell 113:357-367(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome."
      Uhle S., Medalia O., Waldron R., Dumdey R., Henklein P., Bech-Otschir D., Huang X., Berse M., Sperling J., Schade R., Dubiel W.
      EMBO J. 22:1302-1312(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M."
      Zou Y., Lim S., Lee K., Deng X., Friedman E.
      J. Biol. Chem. 278:49573-49581(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH RAN; RANBP9 AND DYRK1B.
    21. "Interaction between glucose-regulated destruction domain of DNA topoisomerase IIalpha and MPN domain of Jab1/CSN5."
      Yun J., Tomida A., Andoh T., Tsuruo T.
      J. Biol. Chem. 279:31296-31303(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOP2A.
    22. "Jab1/CSN5, a component of the COP9 signalosome, regulates transforming growth factor beta signaling by binding to Smad7 and promoting its degradation."
      Kim B.-C., Lee H.-J., Park S.H., Lee S.R., Karpova T.S., McNally J.G., Felici A., Lee D.K., Kim S.-J.
      Mol. Cell. Biol. 24:2251-2262(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMAD7.
    23. "RIG-G as a key mediator of the antiproliferative activity of interferon-related pathways through enhancing p21 and p27 proteins."
      Xiao S., Li D., Zhu H.Q., Song M.G., Pan X.R., Jia P.M., Peng L.L., Dou A.X., Chen G.Q., Chen S.J., Chen Z., Tong J.H.
      Proc. Natl. Acad. Sci. U.S.A. 103:16448-16453(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH IFIT3.
    24. "Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry."
      Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.
      J. Proteome Res. 7:4914-4925(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1."
      Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., Cohen R.E.
      EMBO J. 28:621-631(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE SIGNALOSOME COMPLEX, INTERACTION WITH THE BRISC COMPLEX, MUTAGENESIS OF HIS-138.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process."
      Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.
      EMBO J. 30:181-193(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    29. "Jab1 interacts with brain-specific kinase 2 (BRSK2) and promotes its degradation in the ubiquitin-proteasome pathway."
      Zhou J., Wan B., Li R., Gu X., Zhong Z., Wang Y., Yu L.
      Biochem. Biophys. Res. Commun. 422:647-652(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRSK2, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiCSN5_HUMAN
    AccessioniPrimary (citable) accession number: Q92905
    Secondary accession number(s): O15386
    , Q6AW95, Q86WQ4, Q9BQ17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 133 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    The CSN complex is associated with some 'Lys-63'-specific deubiquitination. Such activity is however not mediated by the core CSN complex but by the BRCC3/BRCC36 component of the BRISC complex.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3