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Protein Page:
COPS5 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
COPS5 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. 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, p27Kip1, BCL3, GFER, PGR, LHCGR, SMAD4, SMAD7, ID1, ID3, ITGB2 and TOP2A. Part of a complex consisting of RANBP9, Ran, DYRK1B and COPS5. Belongs to the peptidase M67A family. CSN5 subfamily. Note: This description may include information from UniProtKB.
Protein type: Transcription, coactivator/corepressor; Adaptor/scaffold; Nuclear receptor co-regulator; EC 3.4.-.-; Translation; Protease
Cellular Component: signalosome; eukaryotic translation initiation factor 3 complex; synaptic vesicle; perinuclear region of cytoplasm; cytoplasm; nucleolus; nucleus; cell junction
Molecular Function: protein binding; metallopeptidase activity; translation initiation factor activity; metal ion binding; transcription coactivator activity; ubiquitin-specific protease activity
Biological Process: transcription from RNA polymerase II promoter; protein deneddylation; cullin deneddylation; protein deubiquitination; translation; regulation of cell cycle; translational initiation; positive regulation of transcription from RNA polymerase II promoter; proteolysis; regulation of JNK cascade
Reference #:  Q92905 (UniProtKB)
Alt. Names/Synonyms: 38 kDa Mov34 homolog; COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis); COP9 signalosome complex subunit 5; COPS5; CSN5; JAB1; Jun activation domain-binding protein 1; MGC3149; MOV-34; SGN5; Signalosome subunit 5
Gene Symbols: COPS5
Molecular weight: 37,579 Da
Basal Isoelectric point: 6.1  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

COPS5

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K11-ub SGSGMAQkTWELANN
0 2 K30-ub QSIDEIYkYDkkQQQ
0 1 K33-ub DEIYkYDkkQQQEIL
0 1 K34-ub EIYkYDkkQQQEILA
0 1 K43-ub QQEILAAkPWTkDHH
0 1 K47-ac LAAkPWTkDHHYFKy
0 1 K47-ub LAAkPWTkDHHYFKy
0 1 Y54-p kDHHYFKyCkISALA
0 2 K56-ub HHYFKyCkISALALL
0 1 S58 YFKyCkISALALLKM
0 1 S71-p KMVMHARsGGNLEVM
0 1 K125-ub AAYIENAkQVGRLEN
0 1 K194-ub RTYPKGYkPPDEGPS
0 9 Y203-p PDEGPSEyQTIPLNK
0 1 K236-ub FKSSLDRkLLELLWN
0 4 S284-p EAQLGRGsFMLGLET
1 0 S320-p EAIHGLMsQVIKDkL
0 1 K326-ac MsQVIKDkLFNQINI
  mouse

 
K11 SGSGMAQKTWELANN
K30 QSIDEIYKYDKKQQQ
K33 DEIYKYDKKQQQEIL
K34 EIYKYDKKQQQEILA
K43 QQEILAAKPWTKDHH
K47 LAAKPWTKDHHYFKY
K47 LAAKPWTKDHHYFKY
Y54 KDHHYFKYCkIsALA
K56-ub HHYFKYCkIsALALL
S58-p YFKYCkIsALALLKM
S71 KMVMHARSGGNLEVM
K125 AAYIENAKQVGRLEN
K194 RTYPKGYKPPDEGPS
Y203 PDEGPSEYQTIPLNK
K236 FKSSLDRKLLELLWN
S284-p EAQLGRGsFMLGLET
S320 EAIHGLMSQVIKDKL
K326 MSQVIKDKLFNQINV
  rat

 
K11 SGSGMAQKTWELANN
K30 QSIDEIYKYDKKQQQ
K33 DEIYKYDKKQQQEIL
K34 EIYKYDKKQQQEILA
K43 QQEILAAKPWTKDHH
K47 LAAKPWTKDHHYFKY
K47 LAAKPWTKDHHYFKY
Y54 KDHHYFKYCKISALA
K56 HHYFKYCKISALALL
S58 YFKYCKISALALLKM
S71 KMVMHARSGGNLEVM
K125 AAYIENAKQVGRLEN
K194 RTYPKGYKPPDEGPS
Y203 PDEGPSEYQTIPLNK
K236 FKSSLDRKLLELLWN
S284 EAQLGRGSFMLGLET
S320 EAIHGLMSQVIKDKL
K326 MSQVIKDKLFNQINV
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