Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

COP9 signalosome complex subunit 5

Gene

COPS5

Organism
Homo sapiens (Human)
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. 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)DescriptionActionsGraphical viewLength
Metal bindingi138Zinc; catalyticCurated1
Metal bindingi140Zinc; catalyticBy similarity1
Metal bindingi151Zinc; catalyticBy similarity1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • metallopeptidase activity Source: UniProtKB
  • thiol-dependent ubiquitin-specific protease activity Source: FlyBase
  • transcription coactivator activity Source: ProtInc
  • translation initiation factor activity Source: ProtInc

GO - Biological processi

  • cullin deneddylation Source: UniProtKB
  • exosomal secretion Source: FlyBase
  • nucleotide-excision repair, DNA damage recognition Source: Reactome
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein deneddylation Source: UniProtKB
  • protein deubiquitination Source: FlyBase
  • regulation of cell cycle Source: Ensembl
  • regulation of IRE1-mediated unfolded protein response Source: ParkinsonsUK-UCL
  • regulation of JNK cascade Source: UniProtKB
  • transcription-coupled nucleotide-excision repair Source: Reactome
  • transcription from RNA polymerase II promoter Source: ProtInc
  • translation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
SIGNORiQ92905.

Protein family/group databases

MEROPSiM67.A02.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:2240. COPS5.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • COP9 signalosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • eukaryotic translation initiation factor 3 complex Source: ProtInc
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • synaptic vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi138H → Q: Abolishes ability to deneddylate cullins, without affecting the 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex. 1 Publication1

Organism-specific databases

DisGeNETi10987.
OpenTargetsiENSG00000121022.
PharmGKBiPA26757.

Polymorphism and mutation databases

BioMutaiCOPS5.
DMDMi55976562.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001948352 – 334COP9 signalosome complex subunit 5Add BLAST333

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine2 Publications1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ92905.
MaxQBiQ92905.
PaxDbiQ92905.
PeptideAtlasiQ92905.
PRIDEiQ92905.

2D gel databases

REPRODUCTION-2DPAGEIPI00009958.

PTM databases

iPTMnetiQ92905.
PhosphoSitePlusiQ92905.
SwissPalmiQ92905.

Expressioni

Gene expression databases

BgeeiENSG00000121022.
CleanExiHS_COPS5.
ExpressionAtlasiQ92905. baseline and differential.
GenevisibleiQ92905. HS.

Organism-specific databases

HPAiCAB004242.
HPA004845.
HPA051531.

Interactioni

Subunit structurei

Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 isoform 1 (PubMed:26456823). In the complex, it probably interacts directly with COPS1, COPS2, COPS4, COPS6 and COPS7 (COPS7A or COPS7B) and COPS9 isoform 1 (PubMed:26456823). Interacts with COPS9 isoform 2 (PubMed:23776465). 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. Interacts with ZDHHC16 (PubMed:17123647).19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNDBP1O952735EBI-594661,EBI-748961
CDKN1BP465273EBI-594661,EBI-519280
COPS3Q9UNS29EBI-594661,EBI-350590
F2RL1P550858EBI-594661,EBI-4303189
FAM188AQ9H8M73EBI-594661,EBI-724928
GPS1Q130984EBI-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. 807 interactors.
DIPiDIP-34546N.
IntActiQ92905. 134 interactors.
MINTiMINT-1188008.
STRINGi9606.ENSP00000350512.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 16Combined sources11
Helixi33 – 42Combined sources10
Turni45 – 47Combined sources3
Beta strandi54 – 58Combined sources5
Helixi59 – 71Combined sources13
Turni72 – 74Combined sources3
Beta strandi78 – 86Combined sources9
Beta strandi89 – 97Combined sources9
Helixi104 – 107Combined sources4
Helixi112 – 124Combined sources13
Beta strandi125 – 127Combined sources3
Beta strandi133 – 139Combined sources7
Turni141 – 143Combined sources3
Helixi149 – 161Combined sources13
Beta strandi167 – 170Combined sources4
Beta strandi183 – 188Combined sources6
Beta strandi221 – 223Combined sources3
Beta strandi225 – 231Combined sources7
Helixi235 – 250Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4D10X-ray3.80E/M1-334[»]
4D18X-ray4.08E/M12-334[»]
4F7OX-ray2.60A/B1-257[»]
4WSNX-ray5.50E/M/U/c/k/s14-334[»]
ProteinModelPortaliQ92905.
SMRiQ92905.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 164MPNAdd BLAST112

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi138 – 151JAMM motifAdd BLAST14

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

eggNOGiKOG1554. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00550000074850.
HOGENOMiHOG000116528.
HOVERGENiHBG051137.
InParanoidiQ92905.
KOiK09613.
OMAiMQEVQSI.
OrthoDBiEOG091G0AAO.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti43 – 45KPW → NLG in AAD03468 (PubMed:9341143).Curated3
Sequence conflicti129R → H in AAB16847 (PubMed:8837781).Curated1

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.
UCSCiuc003xxe.4. human.

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.
CCDSiCCDS6198.1.
PIRiS71820.
RefSeqiNP_006828.2. NM_006837.2.
UniGeneiHs.491912.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4D10X-ray3.80E/M1-334[»]
4D18X-ray4.08E/M12-334[»]
4F7OX-ray2.60A/B1-257[»]
4WSNX-ray5.50E/M/U/c/k/s14-334[»]
ProteinModelPortaliQ92905.
SMRiQ92905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116183. 807 interactors.
DIPiDIP-34546N.
IntActiQ92905. 134 interactors.
MINTiMINT-1188008.
STRINGi9606.ENSP00000350512.

Protein family/group databases

MEROPSiM67.A02.

PTM databases

iPTMnetiQ92905.
PhosphoSitePlusiQ92905.
SwissPalmiQ92905.

Polymorphism and mutation databases

BioMutaiCOPS5.
DMDMi55976562.

2D gel databases

REPRODUCTION-2DPAGEIPI00009958.

Proteomic databases

EPDiQ92905.
MaxQBiQ92905.
PaxDbiQ92905.
PeptideAtlasiQ92905.
PRIDEiQ92905.

Protocols and materials databases

DNASUi10987.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357849; ENSP00000350512; ENSG00000121022.
GeneIDi10987.
KEGGihsa:10987.
UCSCiuc003xxe.4. human.

Organism-specific databases

CTDi10987.
DisGeNETi10987.
GeneCardsiCOPS5.
HGNCiHGNC:2240. COPS5.
HPAiCAB004242.
HPA004845.
HPA051531.
MIMi604850. gene.
neXtProtiNX_Q92905.
OpenTargetsiENSG00000121022.
PharmGKBiPA26757.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1554. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00550000074850.
HOGENOMiHOG000116528.
HOVERGENiHBG051137.
InParanoidiQ92905.
KOiK09613.
OMAiMQEVQSI.
OrthoDBiEOG091G0AAO.
PhylomeDBiQ92905.
TreeFamiTF105601.

Enzyme and pathway databases

ReactomeiR-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
SIGNORiQ92905.

Miscellaneous databases

ChiTaRSiCOPS5. human.
GenomeRNAii10987.
PROiQ92905.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000121022.
CleanExiHS_COPS5.
ExpressionAtlasiQ92905. baseline and differential.
GenevisibleiQ92905. HS.

Family and domain databases

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

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 30, 2016
This is version 157 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

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.