CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011467
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Clusterin 
Protein Synonyms/Alias
 Apolipoprotein J; Apo-J; Clustrin; Sulfated glycoprotein 2; SGP-2; Clusterin beta chain; Clusterin alpha chain 
Gene Name
 Clu 
Gene Synonyms/Alias
 Apoj; Msgp-2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
341ERLTEQYKELLQSFQubiquitination[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
 Functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Promotes apoptosis when in the nucleus. Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation (By similarity). 
Sequence Annotation
 MOTIF 77 80 Nuclear localization signal.
 MOTIF 442 446 Nuclear localization signal.
 CARBOHYD 102 102 N-linked (GlcNAc...) (Probable).
 CARBOHYD 144 144 N-linked (GlcNAc...) (Probable).
 CARBOHYD 290 290 N-linked (GlcNAc...).
 CARBOHYD 327 327 N-linked (GlcNAc...).
 CARBOHYD 353 353 N-linked (GlcNAc...) (Probable).
 CARBOHYD 373 373 N-linked (GlcNAc...) (Probable).
 DISULFID 101 312 Interchain (between beta and alpha
 DISULFID 112 304 Interchain (between beta and alpha
 DISULFID 115 301 Interchain (between beta and alpha
 DISULFID 120 294 Interchain (between beta and alpha
 DISULFID 128 284 Interchain (between beta and alpha  
Keyword
 Chaperone; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane; Microsome; Mitochondrion; Nucleus; Reference proteome; Secreted; Signal; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 448 AA 
Protein Sequence
MKILLLCVAL LLIWDNGMVL GEQEVSDNEL QELSTQGSRY INKEIQNAVQ GVKHIKTLIE 60
KTNAERKSLL NSLEEAKKKK EDALEDTRDS EMKLKAFPEV CNETMMALWE ECKPCLKHTC 120
MKFYARVCRS GSGLVGQQLE EFLNQSSPFY FWMNGDRIDS LLESDRQQSQ VLDAMQDSFA 180
RASGIIDTLF QDRFFARELH DPHYFSPIGF PHKRPHFLYP KSRLVRSLMS PSHYGPPSFH 240
NMFQPFFEMI HQAQQAMDVQ LHSPAFQFPD VDFLREGEDD RTVCKEIRRN STGCLKMKGQ 300
CEKCQEILSV DCSTNNPAQA NLRQELNDSL QVAERLTEQY KELLQSFQSK MLNTSSLLEQ 360
LNDQFNWVSQ LANLTQGEDK YYLRVSTVTT HSSDSEVPSR VTEVVVKLFD SDPITVVLPE 420
EVSKDNPKFM DTVAEKALQE YRRKSRAE 448 
Gene Ontology
 GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0031012; C:extracellular matrix; IEA:Compara.
 GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
 GO:0034366; C:spherical high-density lipoprotein particle; ISS:UniProtKB.
 GO:0051787; F:misfolded protein binding; ISS:UniProtKB.
 GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
 GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
 GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
 GO:0032463; P:negative regulation of protein homooligomerization; ISS:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
 GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
 GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
 GO:0050821; P:protein stabilization; ISS:UniProtKB.
 GO:0051788; P:response to misfolded protein; ISS:UniProtKB.
 GO:0009615; P:response to virus; IEA:Compara. 
Interpro
 IPR016016; Clusterin.
 IPR000753; Clusterin-like.
 IPR016015; Clusterin_C.
 IPR016014; Clusterin_N. 
Pfam
 PF01093; Clusterin 
SMART
 SM00035; CLa
 SM00030; CLb 
PROSITE
 PS00492; CLUSTERIN_1
 PS00493; CLUSTERIN_2 
PRINTS