CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020146
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 COP9 signalosome complex subunit 4 
Protein Synonyms/Alias
 SGN4; Signalosome subunit 4; JAB1-containing signalosome subunit 4 
Gene Name
 COPS4 
Gene Synonyms/Alias
 CSN4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20MNSSGSHKDLAGKYRubiquitination[1, 2]
25SHKDLAGKYRQILEKacetylation[3]
137IPLETGQKQYNVDYKubiquitination[4]
150YKLETYLKIARLYLEubiquitination[4, 5]
200RVLDYRRKFIEAAQRubiquitination[5]
214RYNELSYKTIVHESEubiquitination[5]
227SERLEALKHALHCTIubiquitination[5]
251RMLATLFKDERCQQLubiquitination[5]
266AAYGILEKMYLDRIIubiquitination[5]
290AMLMPHQKATTADGSubiquitination[5]
334LLEIPAAKAEKIASQubiquitination[6]
337IPAAKAEKIASQMITubiquitination[5]
372EALPTWDKQIQSLCFubiquitination[5]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional 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. 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. 
Sequence Annotation
 DOMAIN 201 363 PCI.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 25 25 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Reference proteome; Signalosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 406 AA 
Protein Sequence
MAAAVRQDLA QLMNSSGSHK DLAGKYRQIL EKAIQLSGAE QLEALKAFVE AMVNENVSLV 60
ISRQLLTDFC THLPNLPDST AKEIYHFTLE KIQPRVISFE EQVASIRQHL ASIYEKEEDW 120
RNAAQVLVGI PLETGQKQYN VDYKLETYLK IARLYLEDDD PVQAEAYINR ASLLQNESTN 180
EQLQIHYKVC YARVLDYRRK FIEAAQRYNE LSYKTIVHES ERLEALKHAL HCTILASAGQ 240
QRSRMLATLF KDERCQQLAA YGILEKMYLD RIIRGNQLQE FAAMLMPHQK ATTADGSSIL 300
DRAVIEHNLL SASKLYNNIT FEELGALLEI PAAKAEKIAS QMITEGRMNG FIDQIDGIVH 360
FETREALPTW DKQIQSLCFQ VNNLLEKISQ TAPEWTAQAM EAQMAQ 406 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0008180; C:signalosome; IDA:UniProtKB.
 GO:0010388; P:cullin deneddylation; IDA:UniProtKB. 
Interpro
 IPR000717; PCI_dom.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF01399; PCI 
SMART
 SM00088; PINT 
PROSITE
  
PRINTS