CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018873
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 COP9 signalosome complex subunit 5 
Protein Synonyms/Alias
 SGN5; Signalosome subunit 5; Jun activation domain-binding protein 1 
Gene Name
 COPS5 
Gene Synonyms/Alias
 CSN5; JAB1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11SGSGMAQKTWELANNubiquitination[1, 2]
30QSIDEIYKYDKKQQQubiquitination[1, 2, 3, 4, 5]
33DEIYKYDKKQQQEILubiquitination[2, 3, 5, 6]
34EIYKYDKKQQQEILAubiquitination[3, 4, 5]
43QQEILAAKPWTKDHHubiquitination[3]
47LAAKPWTKDHHYFKYacetylation[7]
47LAAKPWTKDHHYFKYubiquitination[1, 2, 4, 5]
56HHYFKYCKISALALLubiquitination[1, 2, 4, 8]
125AAYIENAKQVGRLENubiquitination[3, 4, 5]
180TRTISAGKVNLGAFRubiquitination[4]
191GAFRTYPKGYKPPDEubiquitination[1, 2, 4]
194RTYPKGYKPPDEGPSubiquitination[1, 2, 3, 4]
210YQTIPLNKIEDFGVHubiquitination[4]
236FKSSLDRKLLELLWNubiquitination[1, 2, 4]
309KATRDSCKTTIEAIHubiquitination[4]
326MSQVIKDKLFNQINIubiquitination[4]
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] 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]
 [4] 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]
 [5] 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]
 [6] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [7] 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]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional 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. 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. Promotes the proteasomal degradation of BRSK2. 
Sequence Annotation
 DOMAIN 53 164 MPN.
 MOTIF 138 151 JAMM motif.
 METAL 138 138 Zinc; catalytic (Probable).
 METAL 140 140 Zinc; catalytic (By similarity).
 METAL 151 151 Zinc; catalytic (By similarity).
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Protease; Reference proteome; Signalosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 334 AA 
Protein Sequence
MAASGSGMAQ KTWELANNMQ EAQSIDEIYK YDKKQQQEIL AAKPWTKDHH YFKYCKISAL 60
ALLKMVMHAR SGGNLEVMGL MLGKVDGETM IIMDSFALPV EGTETRVNAQ AAAYEYMAAY 120
IENAKQVGRL ENAIGWYHSH PGYGCWLSGI DVSTQMLNQQ FQEPFVAVVI DPTRTISAGK 180
VNLGAFRTYP KGYKPPDEGP SEYQTIPLNK IEDFGVHCKQ YYALEVSYFK SSLDRKLLEL 240
LWNKYWVNTL SSSSLLTNAD YTTGQVFDLS EKLEQSEAQL GRGSFMLGLE THDRKSEDKL 300
AKATRDSCKT TIEAIHGLMS QVIKDKLFNQ INIS 334 
Gene Ontology
 GO:0005852; C:eukaryotic translation initiation factor 3 complex; TAS:ProtInc.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0008180; C:signalosome; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008237; F:metallopeptidase activity; IMP:UniProtKB.
 GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
 GO:0003743; F:translation initiation factor activity; TAS:ProtInc.
 GO:0010388; P:cullin deneddylation; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0051726; P:regulation of cell cycle; IEA:Compara.
 GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR000555; JAB1_Mov34_MPN_PAD1. 
Pfam
 PF01398; JAB 
SMART
 SM00232; JAB_MPN 
PROSITE
  
PRINTS