Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  COP9 signalosome complex subunit 5  

UniProtKB / Swiss-Prot ID :  CSN5_HUMAN

Gene Name (Synonyms) : 
COPS5, CSN5, JAB1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein Function :  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. 

Protein Sequence MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHAR...
Predicted Secondary Structure CCCCCCCCHHHHHCCCCCCCCCCCHHHHHHCCHHHHHHHHHHCCCCCCCCCCCEEEECHHHHHHHHHHCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAASGS
---CCCCCC
15.44UniProtKB
Link
11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GMAQKTWEL
CCHHHHHCC
46.17Phosphositeplus
Link
30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DEIYKYDKK
HHHHHCCHH
53.27Phosphositeplus
Link
33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YKYDKKQQQ
HHCCHHHHH
49.76Phosphositeplus
Link
34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KYDKKQQQE
HCCHHHHHH
50.90Phosphositeplus
Link
43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ILAAKPWTK
HHHHCCCCC
35.17Phosphositeplus
Link
47Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KPWTKDHHY
CCCCCCCCC
51.72Phosphositeplus
Link
47N6-acetyllysineKPWTKDHHY
CCCCCCCCC
51.72HPRD
Link
47N6-acetyllysineKPWTKDHHY
CCCCCCCCC
51.72Phosphositeplus
Link
47N6-acetyllysine.KPWTKDHHY
CCCCCCCCC
51.72UniProtKB
Link
56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FKYCKISAL
CCEEEECHH
36.28Phosphositeplus
Link
120PhosphotyrosineYMAAYIENA
HHHHHHHHH
10.14HPRD
Link
125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IENAKQVGR
HHHHHHCCC
58.03Phosphositeplus
Link
194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PKGYKPPDE
CCCCCCCCC
59.76Phosphositeplus
Link
236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SLDRKLLEL
HHHHHHHHH
58.03Phosphositeplus
Link
261PhosphotyrosineTNADYTTGQ
CCCCHHHHH
12.09HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
GFI1B_HUMANphysical interactionMINT-2868992MINT16713569
MIF_HUMANphysical interactionMINT-58210MINT15757663
MIF_HUMANphysical interactionMINT-58209MINT15757663
MIF_HUMANphysical interactionMINT-58211MINT15757663
SMAD2_HUMANphysical interactionMINT-61595MINT15231748
Q9H290_HUMANphysical interactionMINT-50626MINT15304329
Q9H290_HUMANphysical interactionMINT-50625MINT15304329
Q9H290_HUMANphysical interactionMINT-50636MINT15304329
Q9H290_HUMANphysical interactionMINT-50637MINT15304329
UCHL1_HUMANcolocalization
physical interaction
physical interaction
EBI-1181993
EBI-1181968
EBI-1
intact12082530
12082530
12082530
Q9NS19_HUMANcolocalization
colocalization
physical interaction
physical interaction
physical interaction
EBI-1385524
EBI-1385510
EBI-1
intact15887118
15887118
15887118
15887118
15887118
BCL3_HUMANin vivoHPRD:06888HPRD10362352
JUN_HUMANin vitroHPRD:06888HPRD8837781
JUND_HUMANin vitroHPRD:06888HPRD8837781
MIF_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:06888HPRD11089976
P53_HUMANin vitroHPRD:06888HPRD11285227
UCHL1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:06888HPRD12082530
ALR_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:06888HPRD11709497
SMAD4_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:06888HPRD11818334
S10A7_HUMANin vivo
yeast 2-hybrid
HPRD:06888HPRD12702588
CUL5_HUMANin vitroHPRD:06888HPRD11337588
HAND2_HUMANyeast 2-hybridHPRD:06888HPRD11812799
RN139_HUMANin vitroHPRD:06888HPRD12032852
HIF1A_HUMANin vitro
in vivo
HPRD:06888HPRD11707426
CSN2_HUMANin vitroHPRD:06888HPRD11285227
11337588
NCOA1_HUMANin vitro
yeast 2-hybrid
HPRD:06888HPRD10722692
PAR2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:06888HPRD16410250
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Characterization of the human COP9 signalosome complex using affinitypurification and mass spectrometry.";
Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.;
J. Proteome Res. 7:4914-4925(2008).
Cited for: IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,AND ACETYLATION AT ALA-2.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures