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Protein

COP9 signalosome complex subunit 5

Gene

Cops5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Promotes the proteasomal degradation of BRSK2. 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.

Cofactori

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.

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
Kip1 C-terminus-interacting protein 2
Gene namesi
Name:Cops5
Synonyms:Csn5, Jab1, Kic2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1349415. Cops5.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • COP9 signalosome Source: MGI
  • cytoplasm Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • synaptic vesicle Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi151 – 1511D → N: Abolishes ability to deneddylate cullins, but keeps ability to stabilize HIF1A protein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 334333COP9 signalosome complex subunit 5PRO_0000194836Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO35864.
MaxQBiO35864.
PaxDbiO35864.
PeptideAtlasiO35864.
PRIDEiO35864.

2D gel databases

REPRODUCTION-2DPAGEO35864.

PTM databases

iPTMnetiO35864.
PhosphoSiteiO35864.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiO35864.
ExpressionAtlasiO35864. baseline and differential.
GenevisibleiO35864. MM.

Interactioni

Subunit structurei

Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, 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, BCL3, GFER, PGR, LHCGR, SMAD4, SMAD7, ITGB2 and TOP2A. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5. Interacts with CDKN1B, HIF1A, ID1 and ID3. Interacts with IFIT3. Interacts with BRSK2 (By similarity). Interacts with ZDHHC16 (By similarity).By similarity

Protein-protein interaction databases

BioGridi205030. 18 interactions.
IntActiO35864. 2 interactions.
MINTiMINT-2620150.
STRINGi10090.ENSMUSP00000027050.

Structurei

3D structure databases

ProteinModelPortaliO35864.
SMRiO35864. 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.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1554. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00550000074850.
HOGENOMiHOG000116528.
HOVERGENiHBG051137.
InParanoidiO35864.
KOiK09613.
OMAiFVVMDAF.
OrthoDBiEOG72NRQC.
PhylomeDBiO35864.
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.

O35864-1 [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 INVA
Length:334
Mass (Da):37,549
Last modified:January 23, 2007 - v3
Checksum:iAD06BF4AAD03A1CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70736 mRNA. Translation: AAD03470.1.
AF068223 mRNA. Translation: AAF61318.1.
AF065386 mRNA. Translation: AAC17179.1.
AK012499 mRNA. Translation: BAB28282.1.
AK146271 mRNA. Translation: BAE27030.1.
AK151492 mRNA. Translation: BAE30445.1.
BC046753 mRNA. Translation: AAH46753.1.
CCDSiCCDS14818.1.
RefSeqiNP_001264030.1. NM_001277101.1.
NP_038743.1. NM_013715.2.
UniGeneiMm.402384.

Genome annotation databases

EnsembliENSMUST00000027050; ENSMUSP00000027050; ENSMUSG00000025917.
GeneIDi26754.
KEGGimmu:26754.
UCSCiuc007ahe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70736 mRNA. Translation: AAD03470.1.
AF068223 mRNA. Translation: AAF61318.1.
AF065386 mRNA. Translation: AAC17179.1.
AK012499 mRNA. Translation: BAB28282.1.
AK146271 mRNA. Translation: BAE27030.1.
AK151492 mRNA. Translation: BAE30445.1.
BC046753 mRNA. Translation: AAH46753.1.
CCDSiCCDS14818.1.
RefSeqiNP_001264030.1. NM_001277101.1.
NP_038743.1. NM_013715.2.
UniGeneiMm.402384.

3D structure databases

ProteinModelPortaliO35864.
SMRiO35864. Positions 24-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205030. 18 interactions.
IntActiO35864. 2 interactions.
MINTiMINT-2620150.
STRINGi10090.ENSMUSP00000027050.

Protein family/group databases

MEROPSiM67.002.

PTM databases

iPTMnetiO35864.
PhosphoSiteiO35864.

2D gel databases

REPRODUCTION-2DPAGEO35864.

Proteomic databases

EPDiO35864.
MaxQBiO35864.
PaxDbiO35864.
PeptideAtlasiO35864.
PRIDEiO35864.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027050; ENSMUSP00000027050; ENSMUSG00000025917.
GeneIDi26754.
KEGGimmu:26754.
UCSCiuc007ahe.2. mouse.

Organism-specific databases

CTDi10987.
MGIiMGI:1349415. Cops5.

Phylogenomic databases

eggNOGiKOG1554. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00550000074850.
HOGENOMiHOG000116528.
HOVERGENiHBG051137.
InParanoidiO35864.
KOiK09613.
OMAiFVVMDAF.
OrthoDBiEOG72NRQC.
PhylomeDBiO35864.
TreeFamiTF105601.

Enzyme and pathway databases

ReactomeiR-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.

Miscellaneous databases

PROiO35864.
SOURCEiSearch...

Gene expression databases

BgeeiO35864.
ExpressionAtlasiO35864. baseline and differential.
GenevisibleiO35864. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1."
    Tomoda K., Kubota Y., Kato J.-Y.
    Nature 398:160-165(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CDKN1B.
    Strain: NIH Swiss.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
  4. "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].
    Strain: BALB/cJ and C57BL/6J.
    Tissue: Bone marrow and Embryo.
  5. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  6. Lubec G., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 192-210 AND 220-230, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Hippocampus.
  7. "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: IDENTIFICATION IN THE CSN COMPLEX.
    Strain: C57BL/6J.
  8. "Jab1 interacts directly with HIF-1alpha and regulates its stability."
    Bae M.-K., Ahn M.-Y., Jeong J.-W., Bae M.-H., Lee Y.M., Bae S.-K., Park J.-W., Kim K.-R., Kim K.-W.
    J. Biol. Chem. 277:9-12(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIF1A.
  9. "Distinct aerobic and hypoxic mechanisms of HIF-alpha regulation by CSN5."
    Bemis L., Chan D.A., Finkielstein C.V., Qi L., Sutphin P.D., Chen X., Stenmark K., Giaccia A.J., Zundel W.
    Genes Dev. 18:739-744(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-151.
  10. "Ubiquitin-dependent degradation of Id1 and Id3 is mediated by the COP9 signalosome."
    Berse M., Bounpheng M., Huang X., Christy B., Pollmann C., Dubiel W.
    J. Mol. Biol. 343:361-370(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ID1 AND ID3.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCSN5_MOUSE
AccessioniPrimary (citable) accession number: O35864
Secondary accession number(s): Q3UA70, Q8C1S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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 (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.