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Clusterin (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-2) [Cleaved into: Clusterin beta chain (ApoJalpha) (Complement cytolysis inhibitor a chain); Clusterin alpha chain (ApoJbeta) (Complement cytolysis inhibitor b chain)]

 CLUS_HUMAN              Reviewed;         449 AA.
P10909; B2R9Q1; B3KSE6; P11380; P11381; Q2TU75; Q5HYC1; Q7Z5B9;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
22-NOV-2017, entry version 205.
RecName: Full=Clusterin;
AltName: Full=Aging-associated gene 4 protein;
AltName: Full=Apolipoprotein J;
Short=Apo-J;
AltName: Full=Complement cytolysis inhibitor;
Short=CLI;
AltName: Full=Complement-associated protein SP-40,40;
AltName: Full=Ku70-binding protein 1;
AltName: Full=NA1/NA2;
AltName: Full=Testosterone-repressed prostate message 2;
Short=TRPM-2;
Contains:
RecName: Full=Clusterin beta chain;
AltName: Full=ApoJalpha;
AltName: Full=Complement cytolysis inhibitor a chain;
Contains:
RecName: Full=Clusterin alpha chain;
AltName: Full=ApoJbeta;
AltName: Full=Complement cytolysis inhibitor b chain;
Flags: Precursor;
Name=CLU; Synonyms=APOJ, CLI, KUB1; ORFNames=AAG4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF
N-TERMINUS, SUBUNIT, DISULFIDE BONDS, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Liver;
PubMed=2780565; DOI=10.1073/pnas.86.18.7123;
Jenne D.E., Tschopp J.;
"Molecular structure and functional characterization of a human
complement cytolysis inhibitor found in blood and seminal plasma:
identity to sulfated glycoprotein 2, a constituent of rat testis
fluid.";
Proc. Natl. Acad. Sci. U.S.A. 86:7123-7127(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL NUCLEOTIDE SEQUENCE [MRNA]
(ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=8181474; DOI=10.1111/j.1432-1033.1994.tb18807.x;
Wong P., Taillefer D., Lakins J., Pineault J., Chader G.,
Tenniswood M.;
"Molecular characterization of human TRPM-2/clusterin, a gene
associated with sperm maturation, apoptosis and neurodegeneration.";
Eur. J. Biochem. 221:917-925(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND PARTIAL
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Stomach, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Small intestine;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-317; ASN-328 AND
LEU-396.
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND PARTIAL
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain, and Spinal ganglion;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 23-33; 229-242; 303-317 AND 397-403, SUBUNIT, AND
INTERACTION WITH APOA1.
PubMed=1903064;
James R.W., Hochstrasser A.-C., Borghini I., Martin B.M., Pometta D.,
Hochstrasser D.F.;
"Characterization of a human high density lipoprotein-associated
protein, NA1/NA2. Identity with SP-40,40, an inhibitor of complement-
mediated cytolysis.";
Arterioscler. Thromb. 11:645-652(1991).
[10]
PROTEIN SEQUENCE OF 23-52 AND 228-257, SUBUNIT, DISULFIDE BOND,
PROTEOLYTIC PROCESSING, GLYCOSYLATION, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=2387851;
de Silva H., Stuart W.D., Park Y.B., Mao S.J.T., Gil C.M.,
Wetterau J.R., Busch S.J., Harmony J.A.K.;
"Purification and characterization of apolipoprotein J.";
J. Biol. Chem. 265:14292-14297(1990).
[11]
PROTEIN SEQUENCE OF 23-41 AND 228-246, INTERACTION WITH APP,
SUBCELLULAR LOCATION, DISULFIDE BOND, AND TISSUE SPECIFICITY.
PubMed=8328966; DOI=10.1042/bj2930027;
Ghiso J., Matsubara E., Koudinov A., Choi-Miura N.-H., Tomita M.,
Wisniewski T., Frangione B.;
"The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is
complexed to SP-40,40 (apolipoprotein J), an inhibitor of the
complement membrane-attack complex.";
Biochem. J. 293:27-30(1993).
[12]
PROTEIN SEQUENCE OF 23-37 AND 228-242.
PubMed=2601725; DOI=10.1016/0161-5890(89)90139-9;
Choi N.H., Mazda T., Tomita M.;
"A serum protein SP40,40 modulates the formation of membrane attack
complex of complement on erythrocytes.";
Mol. Immunol. 26:835-840(1989).
[13]
PROTEIN SEQUENCE OF 23-33 AND 228-240, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=3154963;
Hochstrasser A.-C., James R.W., Martin B.M., Harrington M.,
Hochstrasser D.F., Pometta D., Merril C.R.;
"HDL particle associated proteins in plasma and cerebrospinal fluid:
identification and partial sequencing.";
Appl. Theor. Electrophor. 1:73-76(1988).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 34-449 (ISOFORMS 1/2/4), PARTIAL PROTEIN
SEQUENCE, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=1974459; DOI=10.1021/bi00474a025;
de Silva H.V., Harmony J.A.K., Stuart W.D., Gil C.M., Robbins J.;
"Apolipoprotein J: structure and tissue distribution.";
Biochemistry 29:5380-5389(1990).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 61-449.
TISSUE=Astrocytoma;
PubMed=1924317; DOI=10.1073/pnas.88.19.8577;
Danik M., Chabot J.G., Mercier C., Benabid A.L., Chauvin C.,
Quirion R., Suh M.;
"Human gliomas and epileptic foci express high levels of a mRNA
related to rat testicular sulfated glycoprotein 2, a purported marker
of cell death.";
Proc. Natl. Acad. Sci. U.S.A. 88:8577-8581(1991).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 140-449.
TISSUE=Fetal liver;
Glew M.D., Kirszbaum L., Bozas S.E., Walker I.D.;
Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
[17]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Liver;
PubMed=2721499;
Kirszbaum L., Sharpe J.A., Murphy B., D'Apice J.F.A., Classon B.,
Hudson P., Walker I.D.;
"Molecular cloning and characterization of the novel, human
complement-associated protein, SP-40,40: a link between the complement
and reproductive systems.";
EMBO J. 8:711-718(1989).
[18]
PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION AT
ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374.
PubMed=1551440; DOI=10.1016/0014-5793(92)80330-J;
Kirszbaum L., Bozas S.E., Walker I.D.;
"SP-40,40, a protein involved in the control of the complement
pathway, possesses a unique array of disulphide bridges.";
FEBS Lett. 297:70-76(1992).
[19]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kim J.W.;
"Identification of human aging-associated gene.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[20]
INTERACTION WITH APOA1.
PubMed=1742316; DOI=10.1016/0005-2760(91)90167-G;
Ehnholm C., Bozas S.E., Tenkanen H., Kirszbaum L., Metso J.,
Murphy B., Walker I.D.;
"The apolipoprotein A-I binding protein of placenta and the SP-40,40
protein of human blood are different proteins which both bind to
apolipoprotein A-I.";
Biochim. Biophys. Acta 1086:255-260(1991).
[21]
DISULFIDE BONDS.
PubMed=1491011;
Choi-Miura N.H., Takahashi Y., Nakano Y., Tobe T., Tomita M.;
"Identification of the disulfide bonds in human plasma protein SP-
40,40 (apolipoprotein-J).";
J. Biochem. 112:557-561(1992).
[22]
INTERACTION WITH PON1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8292612; DOI=10.1021/bi00169a026;
Kelso G.J., Stuart W.D., Richter R.J., Furlong C.E.,
Jordan-Starck T.C., Harmony J.A.K.;
"Apolipoprotein J is associated with paraoxonase in human plasma.";
Biochemistry 33:832-839(1994).
[23]
GLYCOSYLATION AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND
ASN-374.
TISSUE=Serum;
PubMed=9336835; DOI=10.1002/pro.5560061007;
Kapron J.T., Hilliard G.M., Lakins J.N., Tenniswood M.P., West K.A.,
Carr S.A., Crabb J.W.;
"Identification and characterization of glycosylation sites in human
serum clusterin.";
Protein Sci. 6:2120-2133(1997).
[24]
FUNCTION, SUBCELLULAR LOCATION, ABSENCE OF ATPASE ACTIVITY, AND TISSUE
SPECIFICITY.
PubMed=11123922; DOI=10.1021/bi002189x;
Poon S., Easterbrook-Smith S.B., Rybchyn M.S., Carver J.A.,
Wilson M.R.;
"Clusterin is an ATP-independent chaperone with very broad substrate
specificity that stabilizes stressed proteins in a folding-competent
state.";
Biochemistry 39:15953-15960(2000).
[25]
FUNCTION, AND SUBUNIT.
PubMed=12047389; DOI=10.1046/j.1432-1033.2002.02957.x;
Hatters D.M., Wilson M.R., Easterbrook-Smith S.B., Howlett G.J.;
"Suppression of apolipoprotein C-II amyloid formation by the
extracellular chaperone, clusterin.";
Eur. J. Biochem. 269:2789-2794(2002).
[26]
FUNCTION, SUBUNIT, AND CIRCULAR DICHROISM.
PubMed=12176985; DOI=10.1074/jbc.M204855200;
Poon S., Rybchyn M.S., Easterbrook-Smith S.B., Carver J.A.,
Pankhurst G.J., Wilson M.R.;
"Mildly acidic pH activates the extracellular molecular chaperone
clusterin.";
J. Biol. Chem. 277:39532-39540(2002).
[27]
ALTERNATIVE SPLICING, IDENTIFICATION OF ISOFORM 4, FUNCTION,
INTERACTION WITH XRCC6, AND SUBCELLULAR LOCATION.
PubMed=12551933; DOI=10.1074/jbc.M209233200;
Leskov K.S., Klokov D.Y., Li J., Kinsella T.J., Boothman D.A.;
"Synthesis and functional analyses of nuclear clusterin, a cell death
protein.";
J. Biol. Chem. 278:11590-11600(2003).
[28]
FUNCTION.
PubMed=12882985; DOI=10.1074/jbc.C300252200;
Santilli G., Aronow B.J., Sala A.;
"Essential requirement of apolipoprotein J (clusterin) signaling for
IkappaB expression and regulation of NF-kappaB activity.";
J. Biol. Chem. 278:38214-38219(2003).
[29]
GLYCOSYLATION AT ASN-354.
TISSUE=Serum;
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[30]
INTERACTION WITH CLUAP1.
PubMed=15480429; DOI=10.1038/sj.onc.1208100;
Takahashi M., Lin Y.-M., Nakamura Y., Furukawa Y.;
"Isolation and characterization of a novel gene CLUAP1 whose
expression is frequently upregulated in colon cancer.";
Oncogene 23:9289-9294(2004).
[31]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-354 AND ASN-374.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[32]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-103; ASN-145;
ASN-291; ASN-354 AND ASN-374.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[33]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BAX.
PubMed=16113678; DOI=10.1038/ncb1291;
Zhang H., Kim J.K., Edwards C.A., Xu Z., Taichman R., Wang C.Y.;
"Clusterin inhibits apoptosis by interacting with activated Bax.";
Nat. Cell Biol. 7:909-915(2005).
[34]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
Leong W.F., Chow V.T.;
"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
reveal differential cellular gene expression in response to
enterovirus 71 infection.";
Cell. Microbiol. 8:565-580(2006).
[35]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by
glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[36]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[37]
FUNCTION, SUBUNIT, INTERACTION WITH LRP2, GLYCOSYLATION, SUBCELLULAR
LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, CIRCULAR DICHROISM, AND
TISSUE SPECIFICITY.
PubMed=17260971; DOI=10.1021/bi062082v;
Stewart E.M., Aquilina J.A., Easterbrook-Smith S.B.,
Murphy-Durland D., Jacobsen C., Moestrup S., Wilson M.R.;
"Effects of glycosylation on the structure and function of the
extracellular chaperone clusterin.";
Biochemistry 46:1412-1422(2007).
[38]
FUNCTION, INDUCTION, PROTEASOMAL DEGRADATION, AND SUBCELLULAR
LOCATION.
PubMed=17689225; DOI=10.1016/j.bbadis.2007.06.004;
Ranney M.K., Ahmed I.S., Potts K.R., Craven R.J.;
"Multiple pathways regulating the anti-apoptotic protein clusterin in
breast cancer.";
Biochim. Biophys. Acta 1772:1103-1111(2007).
[39]
IDENTIFICATION IN A COMPLEX WITH LTF; SEMG1 AND EPPIN.
PubMed=17567961; DOI=10.1095/biolreprod.107.060194;
Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.;
"Characterization of an eppin protein complex from human semen and
spermatozoa.";
Biol. Reprod. 77:476-484(2007).
[40]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17412999; DOI=10.1096/fj.06-7986com;
Yerbury J.J., Poon S., Meehan S., Thompson B., Kumita J.R.,
Dobson C.M., Wilson M.R.;
"The extracellular chaperone clusterin influences amyloid formation
and toxicity by interacting with prefibrillar structures.";
FASEB J. 21:2312-2322(2007).
[41]
ALTERNATIVE SPLICING, IDENTIFICATION OF ISOFORMS 1 AND 2, AND
INDUCTION BY ANDROGEN.
PubMed=17148459; DOI=10.1074/jbc.M608162200;
Cochrane D.R., Wang Z., Muramaki M., Gleave M.E., Nelson C.C.;
"Differential regulation of clusterin and its isoforms by androgens in
prostate cells.";
J. Biol. Chem. 282:2278-2287(2007).
[42]
FUNCTION, AND SUBUNIT.
PubMed=17407782; DOI=10.1016/j.jmb.2007.02.095;
Kumita J.R., Poon S., Caddy G.L., Hagan C.L., Dumoulin M.,
Yerbury J.J., Stewart E.M., Robinson C.V., Wilson M.R., Dobson C.M.;
"The extracellular chaperone clusterin potently inhibits human
lysozyme amyloid formation by interacting with prefibrillar species.";
J. Mol. Biol. 369:157-167(2007).
[43]
ALTERNATIVE SPLICING, IDENTIFICATION OF ISOFORMS 1; 2 AND 5, AND
TISSUE SPECIFICITY.
PubMed=17322305; DOI=10.1074/mcp.M600261-MCP200;
Andersen C.L., Schepeler T., Thorsen K., Birkenkamp-Demtroder K.,
Mansilla F., Aaltonen L.A., Laurberg S., Orntoft T.F.;
"Clusterin expression in normal mucosa and colorectal cancer.";
Mol. Cell. Proteomics 6:1039-1048(2007).
[44]
SUBCELLULAR LOCATION, INTERACTION WITH SYVN1, AND UBIQUITINATION.
PubMed=17451556; DOI=10.1111/j.1600-0854.2007.00549.x;
Nizard P., Tetley S., Le Drean Y., Watrin T., Le Goff P., Wilson M.R.,
Michel D.;
"Stress-induced retrotranslocation of clusterin/ApoJ into the
cytosol.";
Traffic 8:554-565(2007).
[45]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-291; ASN-317 AND ASN-374.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[46]
FUNCTION, AND SUBUNIT.
PubMed=19535339; DOI=10.1074/jbc.M109.033688;
Wyatt A.R., Yerbury J.J., Wilson M.R.;
"Structural characterization of clusterin-chaperone client protein
complexes.";
J. Biol. Chem. 284:21920-21927(2009).
[47]
FUNCTION, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=19137541; DOI=10.1002/jcp.21671;
Rizzi F., Caccamo A.E., Belloni L., Bettuzzi S.;
"Clusterin is a short half-life, poly-ubiquitinated protein, which
controls the fate of prostate cancer cells.";
J. Cell. Physiol. 219:314-323(2009).
[48]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-103; ASN-145;
ASN-354 AND ASN-374.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[49]
GLYCOSYLATION AT ASN-86 AND ASN-374.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[50]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374, AND STRUCTURE OF
CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[51]
FUNCTION.
PubMed=19996109; DOI=10.1074/jbc.M109.079566;
Wyatt A.R., Wilson M.R.;
"Identification of human plasma proteins as major clients for the
extracellular chaperone clusterin.";
J. Biol. Chem. 285:3532-3539(2010).
[52]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COMMD1; UBIQUITIN;
CUL1 ANDBTRC, AND IDENTIFICATION IN A E3 UBIQUITIN-PROTEIN LIGASE
COMPLEX.
PubMed=20068069; DOI=10.1158/1541-7786.MCR-09-0277;
Zoubeidi A., Ettinger S., Beraldi E., Hadaschik B., Zardan A.,
Klomp L.W., Nelson C.C., Rennie P.S., Gleave M.E.;
"Clusterin facilitates COMMD1 and I-kappaB degradation to enhance NF-
kappaB activity in prostate cancer cells.";
Mol. Cancer Res. 8:119-130(2010).
[53]
FUNCTION.
PubMed=21505792; DOI=10.1007/s00018-011-0684-8);
Wyatt A.R., Yerbury J.J., Berghofer P., Greguric I., Katsifis A.,
Dobson C.M., Wilson M.R.;
"Clusterin facilitates in vivo clearance of extracellular misfolded
proteins.";
Cell. Mol. Life Sci. 68:3919-3931(2011).
[54]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-396, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:12047389,
ECO:0000269|PubMed:12176985, ECO:0000269|PubMed:12551933,
ECO:0000269|PubMed:12882985, ECO:0000269|PubMed:16113678,
ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17407782,
ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:17689225,
ECO:0000269|PubMed:19137541, ECO:0000269|PubMed:19535339,
ECO:0000269|PubMed:19996109, ECO:0000269|PubMed:20068069,
ECO:0000269|PubMed:21505792}.
-!- SUBUNIT: Antiparallel disulfide-linked heterodimer of an alpha
chain and a beta chain. Self-associates and forms higher
oligomers. Interacts with a broad range of misfolded proteins,
including APP, APOC2 and LYZ. Slightly acidic pH promotes
interaction with misfolded proteins. Forms high-molecular weight
oligomers upon interaction with misfolded proteins. Interacts with
APOA1, LRP2, CLUAP1 AND PON1. Interacts with the complement
complex. Interacts (via alpha chain) with XRCC6. Interacts with
SYVN1, COMMD1, BTRC, CUL1 and with ubiquitin and SCF (SKP1-CUL1-F-
box protein) E3 ubiquitin-protein ligase complexes. Interacts (via
alpha chain) with BAX in stressed cells, where BAX undergoes a
conformation change leading to association with the mitochondrial
membrane. Does not interact with BAX in unstressed cells. Found in
a complex with LTF, CLU, EPPIN and SEMG1.
{ECO:0000269|PubMed:12047389, ECO:0000269|PubMed:12176985,
ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:1491011,
ECO:0000269|PubMed:15480429, ECO:0000269|PubMed:1551440,
ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:17260971,
ECO:0000269|PubMed:17407782, ECO:0000269|PubMed:17412999,
ECO:0000269|PubMed:1742316, ECO:0000269|PubMed:17451556,
ECO:0000269|PubMed:17567961, ECO:0000269|PubMed:1903064,
ECO:0000269|PubMed:19535339, ECO:0000269|PubMed:1974459,
ECO:0000269|PubMed:20068069, ECO:0000269|PubMed:2387851,
ECO:0000269|PubMed:2780565, ECO:0000269|PubMed:8292612,
ECO:0000269|PubMed:8328966}.
-!- INTERACTION:
P18509:ADCYAP1; NbExp=4; IntAct=EBI-1104674, EBI-8588930;
Q07817-1:BCL2L1; NbExp=6; IntAct=EBI-4322678, EBI-287195;
Q9NRI5:DISC1; NbExp=4; IntAct=EBI-1104674, EBI-529989;
P01100:FOS; NbExp=2; IntAct=EBI-1104674, EBI-852851;
P30101:PDIA3; NbExp=2; IntAct=EBI-1104674, EBI-979862;
P37231:PPARG; NbExp=3; IntAct=EBI-1104674, EBI-781384;
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted. Note=Can
retrotranslocate from the secretory compartments to the cytosol
upon cellular stress.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion membrane;
Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytosol.
Microsome. Endoplasmic reticulum. Cytoplasmic vesicle, secretory
vesicle, chromaffin granule {ECO:0000250}. Note=Isoforms lacking
the N-terminal signal sequence have been shown to be cytoplasmic
and/or nuclear. Secreted isoforms can retrotranslocate from the
secretory compartments to the cytosol upon cellular stress.
Detected in perinuclear foci that may be aggresomes containing
misfolded, ubiquitinated proteins. Detected at the mitochondrion
membrane upon induction of apoptosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=2, CLU35, sCLU;
IsoId=P10909-1; Sequence=Displayed;
Note=Major isoform.;
Name=2; Synonyms=1, CLU34;
IsoId=P10909-2; Sequence=VSP_037661;
Name=3;
IsoId=P10909-3; Sequence=VSP_041475;
Name=4; Synonyms=nCLU;
IsoId=P10909-4; Sequence=VSP_041476;
Note=Minor isoform that has been detected in a breast cancer
cell line, but not in any other tissues or cell lines.;
Name=5; Synonyms=CLU36;
IsoId=P10909-5; Sequence=VSP_041477;
-!- TISSUE SPECIFICITY: Detected in blood plasma, cerebrospinal fluid,
milk, seminal plasma and colon mucosa. Detected in the germinal
center of colon lymphoid nodules and in colon parasympathetic
ganglia of the Auerbach plexus (at protein level). Ubiquitous.
Detected in brain, testis, ovary, liver and pancreas, and at lower
levels in kidney, heart, spleen and lung.
{ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:17260971,
ECO:0000269|PubMed:17322305, ECO:0000269|PubMed:17412999,
ECO:0000269|PubMed:1974459, ECO:0000269|PubMed:2387851,
ECO:0000269|PubMed:2780565, ECO:0000269|PubMed:3154963,
ECO:0000269|PubMed:8181474, ECO:0000269|PubMed:8292612,
ECO:0000269|PubMed:8328966}.
-!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71)
infection (at protein level). Up-regulated by agents that induce
apoptosis, both at mRNA and protein level. Isoform 1 is up-
regulated by androgen. Isoform 2 is down-regulated by androgen.
{ECO:0000269|PubMed:16548883, ECO:0000269|PubMed:17148459,
ECO:0000269|PubMed:17689225}.
-!- PTM: Isoform 1 is proteolytically cleaved on its way through the
secretory system, probably within the Golgi lumen.
{ECO:0000269|PubMed:2387851}.
-!- PTM: Polyubiquitinated, leading to proteasomal degradation.
{ECO:0000269|PubMed:17451556, ECO:0000269|PubMed:19137541}.
-!- PTM: Heavily N-glycosylated. About 30% of the protein mass is
comprised of complex N-linked carbohydrate.
{ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:1551440, ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:2387851,
ECO:0000269|PubMed:9336835}.
-!- SIMILARITY: Belongs to the clusterin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA35692.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAB06508.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAB06508.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
Sequence=AAH10514.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH19588.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAP88927.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAP88927.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT08041.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG36598.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA32847.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/clu/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CLUID40107ch8p21.html";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M25915; AAA35692.1; ALT_INIT; mRNA.
EMBL; M63379; AAB06507.1; -; Genomic_DNA.
EMBL; M63376; AAB06507.1; JOINED; Genomic_DNA.
EMBL; M63377; AAB06507.1; JOINED; Genomic_DNA.
EMBL; M63378; AAB06507.1; JOINED; Genomic_DNA.
EMBL; M64722; AAB06508.1; ALT_SEQ; mRNA.
EMBL; AK093399; BAG52708.1; -; mRNA.
EMBL; AK313870; BAG36598.1; ALT_INIT; mRNA.
EMBL; CR599675; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BX648414; CAI45990.1; -; mRNA.
EMBL; AY341244; AAP88927.1; ALT_INIT; Genomic_DNA.
EMBL; AF311103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010514; AAH10514.1; ALT_INIT; mRNA.
EMBL; BC019588; AAH19588.1; ALT_INIT; mRNA.
EMBL; BU150467; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; J02908; AAA51765.1; -; mRNA.
EMBL; M74816; AAA60321.1; -; mRNA.
EMBL; L00974; AAA60567.1; -; Genomic_DNA.
EMBL; X14723; CAA32847.1; ALT_INIT; mRNA.
EMBL; AY513288; AAT08041.1; ALT_INIT; mRNA.
CCDS; CCDS47832.1; -. [P10909-1]
PIR; S43646; A41386.
RefSeq; NP_001822.3; NM_001831.3. [P10909-1]
RefSeq; XP_006716347.1; XM_006716284.2. [P10909-2]
UniGene; Hs.436657; -.
ProteinModelPortal; P10909; -.
BioGrid; 107603; 152.
DIP; DIP-37546N; -.
IntAct; P10909; 52.
MINT; MINT-3007494; -.
STRING; 9606.ENSP00000315130; -.
iPTMnet; P10909; -.
PhosphoSitePlus; P10909; -.
BioMuta; CLU; -.
DMDM; 116533; -.
DOSAC-COBS-2DPAGE; P10909; -.
OGP; P10909; -.
REPRODUCTION-2DPAGE; IPI00291262; -.
SWISS-2DPAGE; P10909; -.
EPD; P10909; -.
MaxQB; P10909; -.
PaxDb; P10909; -.
PeptideAtlas; P10909; -.
PRIDE; P10909; -.
DNASU; 1191; -.
Ensembl; ENST00000316403; ENSP00000315130; ENSG00000120885. [P10909-1]
Ensembl; ENST00000405140; ENSP00000385419; ENSG00000120885. [P10909-1]
Ensembl; ENST00000523500; ENSP00000429620; ENSG00000120885. [P10909-1]
GeneID; 1191; -.
KEGG; hsa:1191; -.
UCSC; uc003xfw.3; human. [P10909-1]
CTD; 1191; -.
DisGeNET; 1191; -.
EuPathDB; HostDB:ENSG00000120885.19; -.
GeneCards; CLU; -.
HGNC; HGNC:2095; CLU.
HPA; CAB000476; -.
HPA; CAB016253; -.
HPA; HPA000572; -.
MIM; 185430; gene.
neXtProt; NX_P10909; -.
OpenTargets; ENSG00000120885; -.
PharmGKB; PA26620; -.
eggNOG; ENOG410IHRB; Eukaryota.
eggNOG; ENOG410YYKB; LUCA.
GeneTree; ENSGT00530000063668; -.
HOVERGEN; HBG006908; -.
InParanoid; P10909; -.
KO; K17252; -.
OMA; MKFYARV; -.
OrthoDB; EOG091G05R5; -.
PhylomeDB; P10909; -.
TreeFam; TF333030; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-166665; Terminal pathway of complement.
Reactome; R-HSA-6803157; Antimicrobial peptides.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SIGNOR; P10909; -.
ChiTaRS; CLU; human.
GeneWiki; Clusterin; -.
GenomeRNAi; 1191; -.
PMAP-CutDB; P10909; -.
PRO; PR:P10909; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000120885; -.
CleanEx; HS_CLU; -.
ExpressionAtlas; P10909; baseline and differential.
Genevisible; P10909; HS.
GO; GO:0097440; C:apical dendrite; IDA:Alzheimers_University_of_Toronto.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:ParkinsonsUK-UCL.
GO; GO:0005622; C:intracellular; TAS:ARUK-UCL.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
GO; GO:0097418; C:neurofibrillary tangle; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0034366; C:spherical high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
GO; GO:0051087; F:chaperone binding; ISS:ParkinsonsUK-UCL.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:ARUK-UCL.
GO; GO:0051787; F:misfolded protein binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IPI:ARUK-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0000902; P:cell morphogenesis; IDA:Alzheimers_University_of_Toronto.
GO; GO:0032286; P:central nervous system myelin maintenance; IMP:Alzheimers_University_of_Toronto.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:Alzheimers_University_of_Toronto.
GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
GO; GO:0061741; P:chaperone-mediated protein transport involved in chaperone-mediated autophagy; IC:ARUK-UCL.
GO; GO:0006956; P:complement activation; TAS:ProtInc.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc.
GO; GO:0001774; P:microglial cell activation; IDA:Alzheimers_University_of_Toronto.
GO; GO:0061518; P:microglial cell proliferation; IDA:Alzheimers_University_of_Toronto.
GO; GO:1905907; P:negative regulation of amyloid fibril formation; IDA:ARUK-UCL.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IDA:Alzheimers_University_of_Toronto.
GO; GO:0060548; P:negative regulation of cell death; IMP:ARUK-UCL.
GO; GO:1905892; P:negative regulation of cellular response to thapsigargin; IMP:ARUK-UCL.
GO; GO:1905895; P:negative regulation of cellular response to tunicamycin; IMP:ARUK-UCL.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:BHF-UCL.
GO; GO:0032463; P:negative regulation of protein homooligomerization; IDA:ARUK-UCL.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; TAS:ARUK-UCL.
GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; IMP:ARUK-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:1905908; P:positive regulation of amyloid fibril formation; TAS:ARUK-UCL.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:1902998; P:positive regulation of neurofibrillary tangle assembly; IMP:Alzheimers_University_of_Toronto.
GO; GO:1901216; P:positive regulation of neuron death; IDA:Alzheimers_University_of_Toronto.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:Alzheimers_University_of_Toronto.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0032464; P:positive regulation of protein homooligomerization; IDA:ARUK-UCL.
GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IGI:ARUK-UCL.
GO; GO:1902949; P:positive regulation of tau-protein kinase activity; IMP:Alzheimers_University_of_Toronto.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:Alzheimers_University_of_Toronto.
GO; GO:0017038; P:protein import; IDA:Alzheimers_University_of_Toronto.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; IC:ARUK-UCL.
GO; GO:1900221; P:regulation of amyloid-beta clearance; IDA:Alzheimers_University_of_Toronto.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:1901214; P:regulation of neuron death; IDA:Alzheimers_University_of_Toronto.
GO; GO:1902847; P:regulation of neuronal signal transduction; IMP:Alzheimers_University_of_Toronto.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IC:BHF-UCL.
GO; GO:0051788; P:response to misfolded protein; IDA:BHF-UCL.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0043691; P:reverse cholesterol transport; TAS:BHF-UCL.
InterPro; IPR016016; Clusterin.
InterPro; IPR000753; Clusterin-like.
InterPro; IPR016015; Clusterin_C.
InterPro; IPR033986; Clusterin_CS.
InterPro; IPR016014; Clusterin_N.
PANTHER; PTHR10970; PTHR10970; 1.
PANTHER; PTHR10970:SF1; PTHR10970:SF1; 1.
Pfam; PF01093; Clusterin; 1.
PIRSF; PIRSF002368; Clusterin; 1.
SMART; SM00035; CLa; 1.
SMART; SM00030; CLb; 1.
PROSITE; PS00492; CLUSTERIN_1; 1.
PROSITE; PS00493; CLUSTERIN_2; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Chaperone; Complement pathway;
Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Immunity; Innate immunity; Membrane; Microsome;
Mitochondrion; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Secreted; Signal; Ubl conjugation.
SIGNAL 1 22 {ECO:0000269|PubMed:1903064,
ECO:0000269|PubMed:2387851,
ECO:0000269|PubMed:2601725,
ECO:0000269|PubMed:2780565,
ECO:0000269|PubMed:3154963,
ECO:0000269|PubMed:8328966}.
CHAIN 23 449 Clusterin.
/FTId=PRO_0000005529.
CHAIN 23 227 Clusterin beta chain.
{ECO:0000269|PubMed:1974459}.
/FTId=PRO_0000005530.
CHAIN 228 449 Clusterin alpha chain.
{ECO:0000269|PubMed:1974459}.
/FTId=PRO_0000005531.
MOTIF 78 81 Nuclear localization signal.
{ECO:0000250}.
MOTIF 443 447 Nuclear localization signal.
{ECO:0000250}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 86 86 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:1551440,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9336835}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1551440,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:2721499,
ECO:0000269|PubMed:9336835}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1551440,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:2721499,
ECO:0000269|PubMed:9336835}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1551440,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:2721499,
ECO:0000269|PubMed:9336835}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:1551440,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9336835}.
CARBOHYD 374 374 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:1551440,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:9336835}.
DISULFID 102 313 Interchain (between beta and alpha
chains).
DISULFID 113 305 Interchain (between beta and alpha
chains).
DISULFID 116 302 Interchain (between beta and alpha
chains).
DISULFID 121 295 Interchain (between beta and alpha
chains).
DISULFID 129 285 Interchain (between beta and alpha
chains).
VAR_SEQ 1 175 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041475.
VAR_SEQ 1 33 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_041476.
VAR_SEQ 1 1 M -> MQVCSQPQRGCVREQSAINTAPPSAHNAASPGGARG
HRVPLTEACKDSRIGGM (in isoform 2).
{ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:2780565,
ECO:0000303|Ref.4}.
/FTId=VSP_037661.
VAR_SEQ 1 1 M -> MEACKDSRIGGM (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041477.
VARIANT 317 317 N -> H (in dbSNP:rs9331936).
{ECO:0000269|Ref.6}.
/FTId=VAR_019366.
VARIANT 328 328 D -> N (in dbSNP:rs9331938).
{ECO:0000269|Ref.6}.
/FTId=VAR_019367.
VARIANT 396 396 S -> L (in dbSNP:rs13494).
{ECO:0000269|Ref.6}.
/FTId=VAR_019368.
CONFLICT 28 28 D -> S (in Ref. 9; AA sequence and 13; AA
sequence). {ECO:0000305}.
CONFLICT 47 47 Q -> H (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 52 52 G -> Q (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 172 172 M -> V (in Ref. 5; CAI45990).
{ECO:0000305}.
CONFLICT 224 224 R -> L (in Ref. 3; BAG36598).
{ECO:0000305}.
CONFLICT 305 305 C -> M (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 388 388 T -> M (in Ref. 5; CAI45990).
{ECO:0000305}.
CONFLICT 411 411 D -> G (in Ref. 3; BAG36598).
{ECO:0000305}.
SEQUENCE 449 AA; 52495 MW; 9583DE4CCECC169F CRC64;
MMKTLLLFVG LLLTWESGQV LGDQTVSDNE LQEMSNQGSK YVNKEIQNAV NGVKQIKTLI
EKTNEERKTL LSNLEEAKKK KEDALNETRE SETKLKELPG VCNETMMALW EECKPCLKQT
CMKFYARVCR SGSGLVGRQL EEFLNQSSPF YFWMNGDRID SLLENDRQQT HMLDVMQDHF
SRASSIIDEL FQDRFFTREP QDTYHYLPFS LPHRRPHFFF PKSRIVRSLM PFSPYEPLNF
HAMFQPFLEM IHEAQQAMDI HFHSPAFQHP PTEFIREGDD DRTVCREIRH NSTGCLRMKD
QCDKCREILS VDCSTNNPSQ AKLRRELDES LQVAERLTRK YNELLKSYQW KMLNTSSLLE
QLNEQFNWVS RLANLTQGED QYYLRVTTVA SHTSDSDVPS GVTEVVVKLF DSDPITVTVP
VEVSRKNPKF METVAEKALQ EYRKKHREE


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