CSN5B_ARATH - dbPTM
CSN5B_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSN5B_ARATH
UniProt AC Q9FVU9
Protein Name COP9 signalosome complex subunit 5b
Gene Name CSN5B {ECO:0000303|PubMed:23424245}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 358
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. 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. 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 (By similarity). The CSN complex is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of PSIAA6 by regulating the activity of the Ubl ligase SCF-TIR complex. Not involved in CSN's deneddylation/derubylation activity. [PubMed: 15486099]
Protein Sequence MEGSSSTIARKTWELENSILTVDSPDSTSDNIFYYDDTSQTRFQQEKPWENDPHYFKRVKISALALLKMVVHARSGGTIEIMGLMQGKTDGDTIIVMDAFALPVEGTETRVNAQDDAYEYMVEYSQTNKLAGRLENVVGWYHSHPGYGCWLSGIDVSTQRLNQQHQEPFLAVVIDPTRTVSAGKVEIGAFRTYSKGYKPPDEPVSEYQTIPLNKIEDFGVHCKQYYSLDVTYFKSSLDSHLLDLLWNKYWVNTLSSSPLLGNGDYVAGQISDLAEKLEQAESHLVQSRFGGVVPSSLHKKKEDESQLTKITRDSAKITVEQVHGLMSQVIKDELFNSMRQSNNKSPTDSSDPDPMITY
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
1Acetylation-------MEGSSSTI
-------CCCCCCHH
13.69-
75PhosphorylationKMVVHARSGGTIEIM
HHHHHHHCCCEEEEE
42.2119880383
282PhosphorylationEKLEQAESHLVQSRF
HHHHHHHHHHHHHHH
33.2525368622
287PhosphorylationAESHLVQSRFGGVVP
HHHHHHHHHHCCCCC
22.6725368622

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 CSN5B_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSN5B_ARATH !!

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 CSN5B_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSN3_ARATHCOP13physical
11684663
CSN1_ARATHFUS6physical
11684663
CSN1_ARATHFUS6physical
15486099
CSN2_ARATHFUS12physical
15486099
CSN3_ARATHCOP13physical
15486099
CSN4_ARATHCOP8physical
15486099
CSN7_ARATHFUS5physical
15486099
CSN8_ARATHCOP9physical
15486099
CSN6A_ARATHCSN6Aphysical
15486099
RAC10_ARATHRAC10physical
21798944
VATF_ARATHAT4G02620physical
21798944
GAT24_ARATHZML1physical
21798944
CSN8_ARATHCOP9physical
21798944
TTL3_ARATHTTL3physical
21798944
TIM8_ARATHTIM8physical
21798944
RTL2_ARATHRTL2physical
21798944
MOS1_ARATHMOS1physical
21798944
SAR1A_ARATHSAR2physical
21798944
LOR15_ARATHAT5G01750physical
21798944
COL14_ARATHAT2G33500physical
21798944
ULT1_ARATHULT1physical
21798944
GMPP1_ARATHCYT1physical
23424245
CSN6A_ARATHCSN6Aphysical
11742986
CSN6B_ARATHCSN6Bphysical
11742986
CSN8_ARATHCOP9physical
11742986
CSN7_ARATHFUS5physical
11742986

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSN5B_ARATH

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Related Literatures of Post-Translational Modification

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