CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009322
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 COP9 signalosome complex subunit 2 
Protein Synonyms/Alias
 SGN2; Signalosome subunit 2; Alien homolog; JAB1-containing signalosome subunit 2; Thyroid receptor-interacting protein 15; TR-interacting protein 15; TRIP-15 
Gene Name
 Cops2 
Gene Synonyms/Alias
 Csn2; Trip15 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
338TEFEKILKTNHSNIMubiquitination[1]
371QVLIKLIKPYTRIHIubiquitination[1]
422LLELDHQKRGGARYTubiquitination[1]
433ARYTALDKWTNQLNSubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Essential 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. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, 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. Involved in early stage of neuronal differentiation via its interaction with NIF3L1. 
Sequence Annotation
 DOMAIN 248 413 PCI.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Signalosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 443 AA 
Protein Sequence
MSDMEDDFMC DDEEDYDLEY SEDSNSEPNV DLENQYYNSK ALKEDDPKAA LSSFQKVLEL 60
EGEKGEWGFK ALKQMIKINF KLTNFPEMMN RYKQLLTYIR SAVTRNYSEK SINSILDYIS 120
TSKQNSDFLC QMDLLQEFYE TTLEALKDAK NDRLWFKTNT KLGKLYLERE EYGKLQKILR 180
QLHQSCQTDD GEDDLKKGTQ LLEIYALEIQ MYTAQKNNKK LKALYEQSLH IKSAIPHPLI 240
MGVIRECGGK MHLREGEFEK AHTDFFEAFK NYDESGSPRR TTCLKYLVLA NMLMKSGINP 300
FDSQEAKPYK NDPEILAMTN LVSAYQNNDI TEFEKILKTN HSNIMDDPFI REHIEELLRN 360
IRTQVLIKLI KPYTRIHIPF ISKELNIDVA DVESLLVQCI LDNTIHGRID QVNQLLELDH 420
QKRGGARYTA LDKWTNQLNS LNQAVVSKLA 450 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0008180; C:signalosome; ISS:UniProtKB.
 GO:0003714; F:transcription corepressor activity; IDA:MGI.
 GO:0008283; P:cell proliferation; IMP:MGI.
 GO:0010388; P:cullin deneddylation; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
 GO:0030182; P:neuron differentiation; IEA:Compara.
 GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI. 
Interpro
 IPR013143; PAM.
 IPR000717; PCI_dom.
 IPR011990; TPR-like_helical.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF01399; PCI 
SMART
 SM00753; PAM
 SM00088; PINT 
PROSITE
  
PRINTS