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UniProtKB/Swiss-Prot entry P10909


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CLUS_HUMAN
Primary accession number P10909
Secondary accession numbers P11380 P11381 Q5HYC1 Q7Z5B9
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 105)
Name and origin of the protein
Protein name Clusterin [Precursor]
Synonyms Complement-associated protein SP-40,40
Complement cytolysis inhibitor
CLI
NA1/NA2
Apolipoprotein J
Apo-J
Testosterone-repressed prostate message 2
TRPM-2
Ku70-binding protein 1
Contains Clusterin beta chain
     (ApoJalpha)
     (Complement cytolysis inhibitor a chain)
Clusterin alpha chain
     (ApoJbeta)
     (Complement cytolysis inhibitor b chain)
Gene name
Name: CLU
Synonyms: APOJ, CLI, KUB1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=2721499 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00474a025; PubMed=1974459 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=8181474 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Small intestine;
The German cDNA consortium;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-317; ASN-328 AND LEU-396.
Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04406; PubMed=16421571 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-449.
PubMed=2780565 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
PROTEIN SEQUENCE OF 23-33; 229-242; 303-317 AND 397-403.
PubMed=1903064 [NCBI, ExPASy, EBI, Israel, Japan]
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.
PubMed=2387851 [NCBI, ExPASy, EBI, Israel, Japan]
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.
PubMed=8328966 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/0161-5890(89)90139-9; PubMed=2601725 [NCBI, ExPASy, EBI, Israel, Japan]
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.
PubMed=3154963 [NCBI, ExPASy, EBI, Israel, Japan]
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 61-449.
PubMed=1924317 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 140-449.
TISSUE=Liver;
Glew M.D., Kirszbaum L., Bozas S.E., Walker I.D.;
Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
[16]
PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374.
DOI=10.1016/0014-5793(92)80330-J; PubMed=1551440 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
DISULFIDE BONDS.
PubMed=1491011 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
GLYCOSYLATION AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374.
PubMed=9336835 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[19]
GLYCOSYLATION AT ASN-354.
DOI=10.1038/nbt827; PubMed=12754519 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
INTERACTION WITH CLUAP1.
DOI=10.1038/sj.onc.1208100; PubMed=15480429 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-354 AND ASN-374, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374, AND MASS SPECTROMETRY.
TISSUE=Saliva;
DOI=10.1021/pr050492k; PubMed=16740002 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1074/mcp.M500324-MCP200; PubMed=16263699 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X14723; CAA32847.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02908; AAA51765.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63379; AAB06507.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63376; AAB06507.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63377; AAB06507.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63378; AAB06507.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M64722; AAB06508.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX648414; CAI45990.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY341244; AAP88927.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF311103; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC010514; AAH10514.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019588; AAH19588.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M25915; AAA35692.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M74816; AAA60321.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00974; AAA60567.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S43646; A41386.
RefSeq NP_001822.2; -.
NP_976084.1; -.
UniGene Hs.436657
3D structure databases
ModBase P10909.
Protein-protein interaction databases
IntAct P10909; -.
Polymorphism databases
NIEHS-SNPs CLU.
2D gel databases
SWISS-2DPAGE P10909; -.
Cornea-2DPAGE P10909; -.
DOSAC-COBS-2DPAGE P10909; -.
OGP P10909; -.
REPRODUCTION-2DPAGE IPI00291262; -.
Organism-specific databases
H-InvDB HIX0007408; -.
HGNC HGNC:2095; CLU.
GenAtlas CLU.
HPA CAB000476; -.
CAB016253; -.
HPA000572; -.
MIM 185430; gene. [NCBI / EBI]
PharmGKB PA26620; -.
GeneCards P10909.
Gene expression databases
ArrayExpress P10909; -.
CleanEx HS_CLU; -.
GermOnline ENSG00000120885; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006956; Biological process: complement activation (traceable author statement from ProtInc).
GO:0006629; Biological process: lipid metabolic process (non-traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR016016; Clusterin.
IPR000753; Clusterin-like.
IPR016015; Clusterin_C.
IPR016014; Clusterin_N.
Graphical view of domain structure.
PANTHER PTHR10970:SF1; Clusterin; 1.
Pfam PF01093; Clusterin; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF002368; Clusterin; 1.
SMART SM00035; CLa; 1.
SM00030; CLb; 1.
SMART graphical view of domain structure.
PROSITE PS00492; CLUSTERIN_1; 1.
PS00493; CLUSTERIN_2; 1.
BLOCKS P10909.
Genome annotation databases
Ensembl ENSG00000120885; Homo sapiens. [Contig view]
GeneID 1191; -.
KEGG hsa:1191; -.
Phylogenomic databases
HOGENOM P10909; -.
HOVERGEN P10909; -.
Other
SOURCE CLU; Homo sapiens.
ProtoNet P10909.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoptosis; Complement pathway; Direct protein sequencing; Glycoprotein; Immune response; Innate immunity; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    22  22      
CHAIN   23   449  427     Clusterin. PRO_0000005529
CHAIN   23   227  205     Clusterin beta chain. PRO_0000005530
CHAIN   228   449  222     Clusterin alpha chain. PRO_0000005531
CARBOHYD   86    86        N-linked (GlcNAc...). 
CARBOHYD   103   103        N-linked (GlcNAc...). 
CARBOHYD   145   145        N-linked (GlcNAc...). 
CARBOHYD   291   291        N-linked (GlcNAc...). 
CARBOHYD   354   354        N-linked (GlcNAc...). 
CARBOHYD   374   374        N-linked (GlcNAc...). 
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). 
VARIANT   317   317  1     N -> H (in dbSNP:rs9331936 [NCBI]). VAR_019366 
VARIANT   328   328  1     D -> N (in dbSNP:rs9331938 [NCBI]). VAR_019367 
VARIANT   396   396  1     S -> L (in dbSNP:rs9331940 [NCBI]). VAR_019368 
CONFLICT   28    28        D -> S (in Ref. 9 and 13). 
CONFLICT   47    47        Q -> H (in Ref. 10; AA sequence). 
CONFLICT   52    52        G -> Q (in Ref. 10; AA sequence). 
CONFLICT   172   172        M -> V (in Ref. 7; CAI45990). 
CONFLICT   305   305        C -> M (in Ref. 9; AA sequence). 
CONFLICT   388   388        T -> M (in Ref. 7; CAI45990). 
Sequence information
Length: 449 AA [This is the length of the unprocessed precursor] Molecular weight: 52495 Da [This is the MW of the unprocessed precursor] CRC64: 9583DE4CCECC169F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMKTLLLFVG LLLTWESGQV LGDQTVSDNE LQEMSNQGSK YVNKEIQNAV NGVKQIKTLI 

        70         80         90        100        110        120 
EKTNEERKTL LSNLEEAKKK KEDALNETRE SETKLKELPG VCNETMMALW EECKPCLKQT 

       130        140        150        160        170        180 
CMKFYARVCR SGSGLVGRQL EEFLNQSSPF YFWMNGDRID SLLENDRQQT HMLDVMQDHF 

       190        200        210        220        230        240 
SRASSIIDEL FQDRFFTREP QDTYHYLPFS LPHRRPHFFF PKSRIVRSLM PFSPYEPLNF 

       250        260        270        280        290        300 
HAMFQPFLEM IHEAQQAMDI HFHSPAFQHP PTEFIREGDD DRTVCREIRH NSTGCLRMKD 

       310        320        330        340        350        360 
QCDKCREILS VDCSTNNPSQ AKLRRELDES LQVAERLTRK YNELLKSYQW KMLNTSSLLE 

       370        380        390        400        410        420 
QLNEQFNWVS RLANLTQGED QYYLRVTTVA SHTSDSDVPS GVTEVVVKLF DSDPITVTVP 

       430        440 
VEVSRKNPKF METVAEKALQ EYRKKHREE 

P10909 in FASTA format

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View entry in raw text format (no links)
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