CSN4_MOUSE - dbPTM
CSN4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSN4_MOUSE
UniProt AC O88544
Protein Name COP9 signalosome complex subunit 4
Gene Name Cops4
Organism Mus musculus (Mouse).
Sequence Length 406
Subcellular Localization Cytoplasm. Nucleus. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle.
Protein Description Component 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 SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Also involved in the deneddylation of non-cullin subunits such as STON2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, 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 (By similarity)..
Protein Sequence MAAAVRQDLAQLMNSSGSHKDLAGKYRQILEKAIQLSGTEQLEALKAFVEAMVNENVSLVISRQLLTDFCTHLPNLPDSTAKEVYHFTLEKIQPRVISFEEQVASIRQHLASIYEKEEDWRNAAQVLVGIPLETGQKQYNVDYKLETYLKIARLYLEDDDPVQAEAYINRASLLQNESTNEQLQIHYKVCYARVLDYRRKFIEAAQRYNELSYKTIVHESERLEALKHALHCTILASAGQQRSRMLATLFKDERCQQLAAYGILEKMYLDRIIRGNQLQEFAAMLMPHQKATTADGSSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ
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------MAAAVRQDL
------CCHHHHHHH
12.25-
15PhosphorylationDLAQLMNSSGSHKDL
HHHHHHCCCCCCHHH
23.3121659604
18PhosphorylationQLMNSSGSHKDLAGK
HHHCCCCCCHHHHHH
29.3428059163
25AcetylationSHKDLAGKYRQILEK
CCHHHHHHHHHHHHH
31.49-
25MalonylationSHKDLAGKYRQILEK
CCHHHHHHHHHHHHH
31.4926320211
70S-nitrosocysteineRQLLTDFCTHLPNLP
HHHHHHHHHCCCCCC
2.33-
70S-nitrosylationRQLLTDFCTHLPNLP
HHHHHHHHHCCCCCC
2.3320925432
143PhosphorylationQKQYNVDYKLETYLK
CCEECCCHHHHHHHH
17.12-
148PhosphorylationVDYKLETYLKIARLY
CCHHHHHHHHHHHHH
9.16-
237PhosphorylationLHCTILASAGQQRSR
HHHHHHHCCHHHHHH
29.5028464351
251AcetylationRMLATLFKDERCQQL
HHHHHHHCCHHHHHH
62.8922826441
297PhosphorylationKATTADGSSILDRAV
CCCCCCCCCHHHHHH
18.11-
298PhosphorylationATTADGSSILDRAVI
CCCCCCCCHHHHHHH
32.47-
337UbiquitinationIPAAKAEKIASQMIT
CHHHHHHHHHHHHHH
48.72-

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 CSN4_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSN4_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 CSN4_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSN6_MOUSECops6physical
22956996

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSN4_MOUSE

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Related Literatures of Post-Translational Modification

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