CSN5_MOUSE - dbPTM
CSN5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSN5_MOUSE
UniProt AC O35864
Protein Name COP9 signalosome complex subunit 5
Gene Name Cops5
Organism Mus musculus (Mouse).
Sequence Length 334
Subcellular Localization Cytoplasm, cytosol . Nucleus . Cytoplasm, perinuclear region . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle . Nuclear localization is diminished in the presence of IFIT3.
Protein Description 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..
Protein Sequence MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINVA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAASGSGMA
------CCCCCCCHH
15.44-
24PhosphorylationNNMQEAQSIDEIYKY
HHHHHHHHHHHHHCC
38.7729899451
34UbiquitinationEIYKYDKKQQQEILA
HHHCCCHHHHHHHHH
50.9027667366
56UbiquitinationHHYFKYCKISALALL
CHHHHHHHHHHHHHH
36.2822790023
58PhosphorylationYFKYCKISALALLKM
HHHHHHHHHHHHHHH
11.6118779572
203PhosphorylationPDEGPSEYQTIPLNK
CCCCCCCCCCEEHHH
18.4629514104
218GlutathionylationIEDFGVHCKQYYALE
CCCCCCCCEEEEEEH
2.4624333276
284PhosphorylationEAQLGRGSFMLGLET
HHHHCCCCHHHCCCC
13.2125521595

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CSN5_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSN5_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CSN5_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_MOUSEVcpphysical
19826004
CDN1B_MOUSECdkn1bphysical
10086358
XPO1_MOUSEXpo1physical
11704659
CDN1B_MOUSECdkn1bphysical
11704659
JUN_MOUSEJunphysical
11704659
CSN4_MOUSECops4physical
11704659
CSN6_MOUSECops6physical
11704659
CSN7B_MOUSECops7bphysical
11704659
CSN8_MOUSECops8physical
11704659
RANB9_MOUSERanbp9physical
23926111
CDC53_YEASTCDC53physical
22956996
CUL1_HUMANCUL1physical
24973710

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSN5_MOUSE

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Related Literatures of Post-Translational Modification

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