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Q92905

- CSN5_HUMAN

UniProt

Q92905 - CSN5_HUMAN

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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

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

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. transcription coactivator activity Source: ProtInc
  4. translation initiation factor activity Source: ProtInc
  5. 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
Complete GO annotation...

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. synaptic vesicle Source: UniProtKB
Complete GO annotation...

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

BgeeiQ92905.
CleanExiHS_COPS5.
ExpressionAtlasiQ92905. baseline and differential.
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. 788 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 – 1611Combined sources
Helixi33 – 4210Combined sources
Turni45 – 473Combined sources
Beta strandi54 – 585Combined sources
Helixi59 – 7113Combined sources
Turni72 – 743Combined sources
Beta strandi78 – 869Combined sources
Beta strandi89 – 979Combined sources
Helixi104 – 1074Combined sources
Helixi112 – 12413Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi133 – 1397Combined sources
Turni141 – 1433Combined sources
Helixi149 – 16113Combined sources
Beta strandi167 – 1704Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi225 – 2317Combined sources
Helixi235 – 25016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D10X-ray3.80E/M1-334[»]
4D18X-ray4.08E/M12-334[»]
4F7OX-ray2.60A/B1-257[»]
ProteinModelPortaliQ92905.
SMRiQ92905. Positions 24-333.
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.
GeneTreeiENSGT00550000074850.
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

        10         20         30         40         50
MAASGSGMAQ KTWELANNMQ EAQSIDEIYK YDKKQQQEIL AAKPWTKDHH
60 70 80 90 100
YFKYCKISAL ALLKMVMHAR SGGNLEVMGL MLGKVDGETM IIMDSFALPV
110 120 130 140 150
EGTETRVNAQ AAAYEYMAAY IENAKQVGRL ENAIGWYHSH PGYGCWLSGI
160 170 180 190 200
DVSTQMLNQQ FQEPFVAVVI DPTRTISAGK VNLGAFRTYP KGYKPPDEGP
210 220 230 240 250
SEYQTIPLNK IEDFGVHCKQ YYALEVSYFK SSLDRKLLEL LWNKYWVNTL
260 270 280 290 300
SSSSLLTNAD YTTGQVFDLS EKLEQSEAQL GRGSFMLGLE THDRKSEDKL
310 320 330
AKATRDSCKT TIEAIHGLMS QVIKDKLFNQ INIS
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4D10 X-ray 3.80 E/M 1-334 [» ]
4D18 X-ray 4.08 E/M 12-334 [» ]
4F7O X-ray 2.60 A/B 1-257 [» ]
ProteinModelPortali Q92905.
SMRi Q92905. Positions 24-333.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116183. 788 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 GC08M067955.
HGNCi HGNC:2240. COPS5.
HPAi CAB004242.
HPA004845.
MIMi 604850. gene.
neXtProti NX_Q92905.
PharmGKBi PA26757.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1310.
GeneTreei ENSGT00550000074850.
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

Bgeei Q92905.
CleanExi HS_COPS5.
ExpressionAtlasi Q92905. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 135 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