NP_001822.3
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
52,495 Da
NCBI Official Full Name
clusterin preproprotein
NCBI Official Synonym Full Names
clusterin
NCBI Official Synonym Symbols
CLI; AAG4; APOJ; CLU1; CLU2; KUB1; SGP2; APO-J; SGP-2; SP-40; TRPM2; TRPM-2; NA1/NA2 [Similar Products]
NCBI Protein Information
clusterin; apolipoprotein J; ku70-binding protein 1; sulfated glycoprotein 2; aging-associated protein 4; complement lysis inhibitor; complement cytolysis inhibitor; complement-associated protein SP-40,40; testosterone-repressed prostate message 2
UniProt Protein Name
Clusterin
UniProt Synonym Protein Names
Aging-associated gene 4 protein; Apolipoprotein J; Apo-J; Complement cytolysis inhibitor; CLI; Complement-associated protein SP-40,40; Ku70-binding protein 1; NA1/NA2; Testosterone-repressed prostate message 2; TRPM-2Cleaved into the following 2 chains:Clusterin beta chain; Alternative name(s):; ApoJalpha; Complement cytolysis inhibitor a chainClusterin alpha chain; Alternative name(s):; ApoJbeta; Complement cytolysis inhibitor b chain
UniProt Synonym Gene Names
UniProt Entry Name
CLUS_HUMAN
NCBI Summary for CLU
The protein encoded by this gene is a secreted chaperone that can under some stress conditions also be found in the cell cytosol. It has been suggested to be involved in several basic biological events such as cell death, tumor progression, and neurodegenerative disorders. Alternate splicing results in both coding and non-coding variants.[provided by RefSeq, May 2011]
UniProt Comments for CLU
CLU: Isoform 1 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. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms 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. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. Belongs to the clusterin family. 5 isoforms of the human protein are produced by alternative splicing.
Protein type: Apoptosis; Secreted, signal peptide; Secreted; Mitochondrial
Chromosomal Location of Human Ortholog: 8p21-p12
Cellular Component: Golgi apparatus; extracellular matrix; extracellular space; mitochondrion; perinuclear region of cytoplasm; endoplasmic reticulum; mitochondrial membrane; cytoplasm; extracellular region; nucleus; cytosol
Molecular Function: protein binding; ubiquitin protein ligase binding; chaperone binding; ATPase activity; misfolded protein binding
Biological Process: platelet activation; response to misfolded protein; release of cytochrome c from mitochondria; positive regulation of nitric oxide biosynthetic process; protein stabilization; positive regulation of apoptosis; response to virus; cell morphogenesis; microglial cell activation; positive regulation of tumor necrosis factor production; negative regulation of protein homooligomerization; activation of NF-kappaB transcription factor; complement activation; reverse cholesterol transport; platelet degranulation; myelin maintenance in the central nervous system; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; protein import; innate immune response; lipid metabolic process; chaperone-mediated protein complex assembly; blood coagulation; complement activation, classical pathway
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Pathways associated with CLU elisa kit
Diseases associated with CLU elisa kit
Organs/Tissues associated with CLU elisa kit
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