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P10909

- CLUS_HUMAN

UniProt

P10909 - CLUS_HUMAN

Protein

Clusterin

Gene

CLU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    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.15 Publications

    GO - Molecular functioni

    1. misfolded protein binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell morphogenesis Source: Alzheimers_University_of_Toronto
    3. central nervous system myelin maintenance Source: Alzheimers_University_of_Toronto
    4. chaperone-mediated protein complex assembly Source: Alzheimers_University_of_Toronto
    5. chaperone-mediated protein folding Source: UniProtKB
    6. complement activation Source: ProtInc
    7. complement activation, classical pathway Source: UniProtKB-KW
    8. innate immune response Source: UniProtKB-KW
    9. intrinsic apoptotic signaling pathway Source: UniProtKB
    10. lipid metabolic process Source: ProtInc
    11. microglial cell activation Source: Alzheimers_University_of_Toronto
    12. microglial cell proliferation Source: Alzheimers_University_of_Toronto
    13. negative regulation of beta-amyloid formation Source: Alzheimers_University_of_Toronto
    14. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: BHF-UCL
    15. negative regulation of protein homooligomerization Source: BHF-UCL
    16. platelet activation Source: Reactome
    17. platelet degranulation Source: Reactome
    18. positive regulation of apoptotic process Source: UniProtKB
    19. positive regulation of beta-amyloid formation Source: Alzheimers_University_of_Toronto
    20. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    21. positive regulation of neurofibrillary tangle assembly Source: Alzheimers_University_of_Toronto
    22. positive regulation of neuron death Source: Alzheimers_University_of_Toronto
    23. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    24. positive regulation of nitric oxide biosynthetic process Source: Alzheimers_University_of_Toronto
    25. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    26. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    27. positive regulation of tau-protein kinase activity Source: Alzheimers_University_of_Toronto
    28. positive regulation of tumor necrosis factor production Source: Alzheimers_University_of_Toronto
    29. protein import Source: Alzheimers_University_of_Toronto
    30. protein stabilization Source: UniProtKB
    31. regulation of beta-amyloid clearance Source: Alzheimers_University_of_Toronto
    32. regulation of neuronal signal transduction Source: Alzheimers_University_of_Toronto
    33. regulation of neuron death Source: Alzheimers_University_of_Toronto
    34. release of cytochrome c from mitochondria Source: BHF-UCL
    35. response to misfolded protein Source: BHF-UCL
    36. response to virus Source: UniProtKB
    37. reverse cholesterol transport Source: BHF-UCL

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Apoptosis, Complement pathway, Immunity, Innate immunity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Clusterin
    Alternative name(s):
    Aging-associated gene 4 protein
    Apolipoprotein J
    Short name:
    Apo-J
    Complement cytolysis inhibitor
    Short name:
    CLI
    Complement-associated protein SP-40,40
    Ku70-binding protein 1
    NA1/NA2
    Testosterone-repressed prostate message 2
    Short name:
    TRPM-2
    Cleaved into the following 2 chains:
    Alternative name(s):
    ApoJalpha
    Complement cytolysis inhibitor a chain
    Alternative name(s):
    ApoJbeta
    Complement cytolysis inhibitor b chain
    Gene namesi
    Name:CLU
    Synonyms:APOJ, CLI, KUB1
    ORF Names:AAG4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:2095. CLU.

    Subcellular locationi

    Isoform 1 : Secreted
    Note: Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress.
    Nucleus. Cytoplasm. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytosol. Microsome. Endoplasmic reticulum. Cytoplasmic vesiclesecretory vesiclechromaffin granule By similarity
    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.

    GO - Cellular componenti

    1. apical dendrite Source: Alzheimers_University_of_Toronto
    2. blood microparticle Source: UniProt
    3. chromaffin granule Source: UniProtKB-SubCell
    4. cytoplasm Source: Alzheimers_University_of_Toronto
    5. cytosol Source: UniProtKB-SubCell
    6. endoplasmic reticulum Source: UniProtKB-SubCell
    7. extracellular region Source: Reactome
    8. extracellular space Source: UniProtKB
    9. extracellular vesicular exosome Source: UniProt
    10. mitochondrial membrane Source: UniProtKB-SubCell
    11. mitochondrion Source: BHF-UCL
    12. neurofibrillary tangle Source: Alzheimers_University_of_Toronto
    13. nucleus Source: UniProtKB-SubCell
    14. perinuclear region of cytoplasm Source: UniProtKB
    15. platelet alpha granule lumen Source: Reactome
    16. spherical high-density lipoprotein particle Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Nucleus, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26620.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22226 PublicationsAdd
    BLAST
    Chaini23 – 449427ClusterinPRO_0000005529Add
    BLAST
    Chaini23 – 227205Clusterin beta chain1 PublicationPRO_0000005530Add
    BLAST
    Chaini228 – 449222Clusterin alpha chain1 PublicationPRO_0000005531Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi86 – 861N-linked (GlcNAc...) (complex)5 Publications
    Disulfide bondi102 ↔ 313Interchain (between beta and alpha chains)
    Glycosylationi103 – 1031N-linked (GlcNAc...)5 Publications
    Disulfide bondi113 ↔ 305Interchain (between beta and alpha chains)
    Disulfide bondi116 ↔ 302Interchain (between beta and alpha chains)
    Disulfide bondi121 ↔ 295Interchain (between beta and alpha chains)
    Disulfide bondi129 ↔ 285Interchain (between beta and alpha chains)
    Glycosylationi145 – 1451N-linked (GlcNAc...)5 Publications
    Glycosylationi291 – 2911N-linked (GlcNAc...)5 Publications
    Glycosylationi317 – 3171N-linked (GlcNAc...)1 Publication
    Glycosylationi354 – 3541N-linked (GlcNAc...)6 Publications
    Glycosylationi374 – 3741N-linked (GlcNAc...) (complex)10 Publications

    Post-translational modificationi

    Isoform 1 is proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen.1 Publication
    Polyubiquitinated, leading to proteasomal degradation.2 Publications
    Heavily N-glycosylated. About 30% of the protein mass is comprised of complex N-linked carbohydrate.13 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP10909.
    PaxDbiP10909.
    PRIDEiP10909.

    2D gel databases

    DOSAC-COBS-2DPAGEP10909.
    OGPiP10909.
    REPRODUCTION-2DPAGEIPI00291262.
    SWISS-2DPAGEP10909.

    PTM databases

    PhosphoSiteiP10909.

    Miscellaneous databases

    PMAP-CutDBP10909.

    Expressioni

    Tissue specificityi

    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.11 Publications

    Inductioni

    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.3 Publications

    Gene expression databases

    ArrayExpressiP10909.
    BgeeiP10909.
    CleanExiHS_CLU.
    GenevestigatoriP10909.

    Organism-specific databases

    HPAiCAB000476.
    CAB016253.
    HPA000572.

    Interactioni

    Subunit structurei

    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 SEMG1.21 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL2L1Q07817-16EBI-4322678,EBI-287195
    DISC1Q9NRI54EBI-1104674,EBI-529989
    FOSP011002EBI-1104674,EBI-852851
    PPARGP372313EBI-1104674,EBI-781384

    Protein-protein interaction databases

    BioGridi107603. 70 interactions.
    DIPiDIP-37546N.
    IntActiP10909. 28 interactions.
    MINTiMINT-3007494.
    STRINGi9606.ENSP00000315130.

    Structurei

    3D structure databases

    ProteinModelPortaliP10909.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi78 – 814Nuclear localization signalBy similarity
    Motifi443 – 4475Nuclear localization signalBy similarity

    Sequence similaritiesi

    Belongs to the clusterin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG26650.
    HOVERGENiHBG006908.
    InParanoidiP10909.
    KOiK17252.
    OMAiKFYARVC.
    OrthoDBiEOG7K6PV4.
    PhylomeDBiP10909.
    TreeFamiTF333030.

    Family and domain databases

    InterProiIPR016016. Clusterin.
    IPR000753. Clusterin-like.
    IPR016015. Clusterin_C.
    IPR016014. Clusterin_N.
    [Graphical view]
    PANTHERiPTHR10970:SF1. PTHR10970:SF1. 1 hit.
    PfamiPF01093. Clusterin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002368. Clusterin. 1 hit.
    SMARTiSM00035. CLa. 1 hit.
    SM00030. CLb. 1 hit.
    [Graphical view]
    PROSITEiPS00492. CLUSTERIN_1. 1 hit.
    PS00493. CLUSTERIN_2. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P10909-1) [UniParc]FASTAAdd to Basket

    Also known as: 2, CLU35, sCLU

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MMKTLLLFVG LLLTWESGQV LGDQTVSDNE LQEMSNQGSK YVNKEIQNAV    50
    NGVKQIKTLI EKTNEERKTL LSNLEEAKKK KEDALNETRE SETKLKELPG 100
    VCNETMMALW EECKPCLKQT CMKFYARVCR SGSGLVGRQL EEFLNQSSPF 150
    YFWMNGDRID SLLENDRQQT HMLDVMQDHF SRASSIIDEL FQDRFFTREP 200
    QDTYHYLPFS LPHRRPHFFF PKSRIVRSLM PFSPYEPLNF HAMFQPFLEM 250
    IHEAQQAMDI HFHSPAFQHP PTEFIREGDD DRTVCREIRH NSTGCLRMKD 300
    QCDKCREILS VDCSTNNPSQ AKLRRELDES LQVAERLTRK YNELLKSYQW 350
    KMLNTSSLLE QLNEQFNWVS RLANLTQGED QYYLRVTTVA SHTSDSDVPS 400
    GVTEVVVKLF DSDPITVTVP VEVSRKNPKF METVAEKALQ EYRKKHREE 449

    Note: Major isoform.

    Length:449
    Mass (Da):52,495
    Last modified:July 1, 1989 - v1
    Checksum:i9583DE4CCECC169F
    GO
    Isoform 2 (identifier: P10909-2) [UniParc]FASTAAdd to Basket

    Also known as: 1, CLU34

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MQVCSQPQRGCVREQSAINTAPPSAHNAASPGGARGHRVPLTEACKDSRIGGM

    Show »
    Length:501
    Mass (Da):57,833
    Checksum:i1941842E61CD3464
    GO
    Isoform 3 (identifier: P10909-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-175: Missing.

    Show »
    Length:274
    Mass (Da):32,364
    Checksum:i0917960A8B4D6857
    GO
    Isoform 4 (identifier: P10909-4) [UniParc]FASTAAdd to Basket

    Also known as: nCLU

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.

    Note: Minor isoform that has been detected in a breast cancer cell line, but not in any other tissues or cell lines.

    Show »
    Length:416
    Mass (Da):48,803
    Checksum:i77900AB70F7AC243
    GO
    Isoform 5 (identifier: P10909-5) [UniParc]FASTAAdd to Basket

    Also known as: CLU36

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEACKDSRIGGM

    Show »
    Length:460
    Mass (Da):53,643
    Checksum:i0B0A0165A6C5622A
    GO

    Sequence cautioni

    The sequence AAB06508.1 differs from that shown. Reason: Contaminating sequence.
    The sequence AAA35692.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAB06508.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH10514.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH19588.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAP88927.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAT08041.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAG36598.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA32847.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAP88927.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281D → S AA sequence (PubMed:1903064)Curated
    Sequence conflicti28 – 281D → S AA sequence (PubMed:3154963)Curated
    Sequence conflicti47 – 471Q → H AA sequence (PubMed:2387851)Curated
    Sequence conflicti52 – 521G → Q AA sequence (PubMed:2387851)Curated
    Sequence conflicti172 – 1721M → V in CAI45990. (PubMed:17974005)Curated
    Sequence conflicti224 – 2241R → L in BAG36598. (PubMed:14702039)Curated
    Sequence conflicti305 – 3051C → M AA sequence (PubMed:1903064)Curated
    Sequence conflicti388 – 3881T → M in CAI45990. (PubMed:17974005)Curated
    Sequence conflicti411 – 4111D → G in BAG36598. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti317 – 3171N → H.1 Publication
    Corresponds to variant rs9331936 [ dbSNP | Ensembl ].
    VAR_019366
    Natural varianti328 – 3281D → N.1 Publication
    Corresponds to variant rs9331938 [ dbSNP | Ensembl ].
    VAR_019367
    Natural varianti396 – 3961S → L.1 Publication
    Corresponds to variant rs13494 [ dbSNP | Ensembl ].
    VAR_019368

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 175175Missing in isoform 3. 1 PublicationVSP_041475Add
    BLAST
    Alternative sequencei1 – 3333Missing in isoform 4. CuratedVSP_041476Add
    BLAST
    Alternative sequencei1 – 11M → MQVCSQPQRGCVREQSAINT APPSAHNAASPGGARGHRVP LTEACKDSRIGGM in isoform 2. 3 PublicationsVSP_037661
    Alternative sequencei1 – 11M → MEACKDSRIGGM in isoform 5. 1 PublicationVSP_041477

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25915 mRNA. Translation: AAA35692.1. Different initiation.
    M63379
    , M63376, M63377, M63378 Genomic DNA. Translation: AAB06507.1.
    M64722 mRNA. Translation: AAB06508.1. Sequence problems.
    AK093399 mRNA. Translation: BAG52708.1.
    AK313870 mRNA. Translation: BAG36598.1. Different initiation.
    CR599675 mRNA. No translation available.
    BX648414 mRNA. Translation: CAI45990.1.
    AY341244 Genomic DNA. Translation: AAP88927.1. Different initiation.
    AF311103 Genomic DNA. No translation available.
    BC010514 mRNA. Translation: AAH10514.1. Different initiation.
    BC019588 mRNA. Translation: AAH19588.1. Different initiation.
    BU150467 mRNA. No translation available.
    J02908 mRNA. Translation: AAA51765.1.
    M74816 mRNA. Translation: AAA60321.1.
    L00974 Genomic DNA. Translation: AAA60567.1.
    X14723 mRNA. Translation: CAA32847.1. Different initiation.
    AY513288 mRNA. Translation: AAT08041.1. Different initiation.
    CCDSiCCDS47832.1. [P10909-1]
    PIRiS43646. A41386.
    RefSeqiNP_001822.3. NM_001831.3. [P10909-1]
    XP_006716347.1. XM_006716284.1. [P10909-2]
    UniGeneiHs.436657.

    Genome annotation databases

    EnsembliENST00000316403; ENSP00000315130; ENSG00000120885. [P10909-1]
    ENST00000405140; ENSP00000385419; ENSG00000120885. [P10909-1]
    ENST00000523500; ENSP00000429620; ENSG00000120885. [P10909-1]
    GeneIDi1191.
    KEGGihsa:1191.
    UCSCiuc003xfw.2. human. [P10909-1]
    uc003xfy.2. human. [P10909-5]

    Polymorphism databases

    DMDMi116533.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25915 mRNA. Translation: AAA35692.1 . Different initiation.
    M63379
    , M63376 , M63377 , M63378 Genomic DNA. Translation: AAB06507.1 .
    M64722 mRNA. Translation: AAB06508.1 . Sequence problems.
    AK093399 mRNA. Translation: BAG52708.1 .
    AK313870 mRNA. Translation: BAG36598.1 . Different initiation.
    CR599675 mRNA. No translation available.
    BX648414 mRNA. Translation: CAI45990.1 .
    AY341244 Genomic DNA. Translation: AAP88927.1 . Different initiation.
    AF311103 Genomic DNA. No translation available.
    BC010514 mRNA. Translation: AAH10514.1 . Different initiation.
    BC019588 mRNA. Translation: AAH19588.1 . Different initiation.
    BU150467 mRNA. No translation available.
    J02908 mRNA. Translation: AAA51765.1 .
    M74816 mRNA. Translation: AAA60321.1 .
    L00974 Genomic DNA. Translation: AAA60567.1 .
    X14723 mRNA. Translation: CAA32847.1 . Different initiation.
    AY513288 mRNA. Translation: AAT08041.1 . Different initiation.
    CCDSi CCDS47832.1. [P10909-1 ]
    PIRi S43646. A41386.
    RefSeqi NP_001822.3. NM_001831.3. [P10909-1 ]
    XP_006716347.1. XM_006716284.1. [P10909-2 ]
    UniGenei Hs.436657.

    3D structure databases

    ProteinModelPortali P10909.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107603. 70 interactions.
    DIPi DIP-37546N.
    IntActi P10909. 28 interactions.
    MINTi MINT-3007494.
    STRINGi 9606.ENSP00000315130.

    PTM databases

    PhosphoSitei P10909.

    Polymorphism databases

    DMDMi 116533.

    2D gel databases

    DOSAC-COBS-2DPAGE P10909.
    OGPi P10909.
    REPRODUCTION-2DPAGE IPI00291262.
    SWISS-2DPAGE P10909.

    Proteomic databases

    MaxQBi P10909.
    PaxDbi P10909.
    PRIDEi P10909.

    Protocols and materials databases

    DNASUi 1191.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316403 ; ENSP00000315130 ; ENSG00000120885 . [P10909-1 ]
    ENST00000405140 ; ENSP00000385419 ; ENSG00000120885 . [P10909-1 ]
    ENST00000523500 ; ENSP00000429620 ; ENSG00000120885 . [P10909-1 ]
    GeneIDi 1191.
    KEGGi hsa:1191.
    UCSCi uc003xfw.2. human. [P10909-1 ]
    uc003xfy.2. human. [P10909-5 ]

    Organism-specific databases

    CTDi 1191.
    GeneCardsi GC08M027454.
    HGNCi HGNC:2095. CLU.
    HPAi CAB000476.
    CAB016253.
    HPA000572.
    MIMi 185430. gene.
    neXtProti NX_P10909.
    PharmGKBi PA26620.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG26650.
    HOVERGENi HBG006908.
    InParanoidi P10909.
    KOi K17252.
    OMAi KFYARVC.
    OrthoDBi EOG7K6PV4.
    PhylomeDBi P10909.
    TreeFami TF333030.

    Miscellaneous databases

    ChiTaRSi CLU. human.
    GeneWikii Clusterin.
    GenomeRNAii 1191.
    NextBioi 4922.
    PMAP-CutDB P10909.
    PROi P10909.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10909.
    Bgeei P10909.
    CleanExi HS_CLU.
    Genevestigatori P10909.

    Family and domain databases

    InterProi IPR016016. Clusterin.
    IPR000753. Clusterin-like.
    IPR016015. Clusterin_C.
    IPR016014. Clusterin_N.
    [Graphical view ]
    PANTHERi PTHR10970:SF1. PTHR10970:SF1. 1 hit.
    Pfami PF01093. Clusterin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002368. Clusterin. 1 hit.
    SMARTi SM00035. CLa. 1 hit.
    SM00030. CLb. 1 hit.
    [Graphical view ]
    PROSITEi PS00492. CLUSTERIN_1. 1 hit.
    PS00493. CLUSTERIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Jenne D.E., Tschopp J.
      Proc. Natl. Acad. Sci. U.S.A. 86:7123-7127(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF N-TERMINUS, SUBUNIT, DISULFIDE BONDS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "Molecular characterization of human TRPM-2/clusterin, a gene associated with sperm maturation, apoptosis and neurodegeneration."
      Wong P., Taillefer D., Lakins J., Pineault J., Chader G., Tenniswood M.
      Eur. J. Biochem. 221:917-925(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Stomach and Testis.
    4. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Small intestine.
    6. NIEHS SNPs program
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-317; ASN-328 AND LEU-396.
    7. "DNA sequence and analysis of human chromosome 8."
      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.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain and Spinal ganglion.
    9. "Characterization of a human high density lipoprotein-associated protein, NA1/NA2. Identity with SP-40,40, an inhibitor of complement-mediated cytolysis."
      James R.W., Hochstrasser A.-C., Borghini I., Martin B.M., Pometta D., Hochstrasser D.F.
      Arterioscler. Thromb. 11:645-652(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-33; 229-242; 303-317 AND 397-403, SUBUNIT, INTERACTION WITH APOA1.
    10. "Purification and characterization of apolipoprotein J."
      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.
      J. Biol. Chem. 265:14292-14297(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-52 AND 228-257, SUBUNIT, DISULFIDE BOND, PROTEOLYTIC PROCESSING, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "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."
      Ghiso J., Matsubara E., Koudinov A., Choi-Miura N.-H., Tomita M., Wisniewski T., Frangione B.
      Biochem. J. 293:27-30(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-41 AND 228-246, INTERACTION WITH APP, SUBCELLULAR LOCATION, DISULFIDE BOND, TISSUE SPECIFICITY.
    12. "A serum protein SP40,40 modulates the formation of membrane attack complex of complement on erythrocytes."
      Choi N.H., Mazda T., Tomita M.
      Mol. Immunol. 26:835-840(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-37 AND 228-242.
    13. "HDL particle associated proteins in plasma and cerebrospinal fluid: identification and partial sequencing."
      Hochstrasser A.-C., James R.W., Martin B.M., Harrington M., Hochstrasser D.F., Pometta D., Merril C.R.
      Appl. Theor. Electrophor. 1:73-76(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-33 AND 228-240, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    14. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-449 (ISOFORMS 1/2/4), PARTIAL PROTEIN SEQUENCE, SUBUNIT, TISSUE SPECIFICITY.
    15. "Human gliomas and epileptic foci express high levels of a mRNA related to rat testicular sulfated glycoprotein 2, a purported marker of cell death."
      Danik M., Chabot J.G., Mercier C., Benabid A.L., Chauvin C., Quirion R., Suh M.
      Proc. Natl. Acad. Sci. U.S.A. 88:8577-8581(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 61-449.
      Tissue: Astrocytoma.
    16. Glew M.D., Kirszbaum L., Bozas S.E., Walker I.D.
      Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 140-449.
      Tissue: Fetal liver.
    17. "Molecular cloning and characterization of the novel, human complement-associated protein, SP-40,40: a link between the complement and reproductive systems."
      Kirszbaum L., Sharpe J.A., Murphy B., D'Apice J.F.A., Classon B., Hudson P., Walker I.D.
      EMBO J. 8:711-718(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    18. "SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges."
      Kirszbaum L., Bozas S.E., Walker I.D.
      FEBS Lett. 297:70-76(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374.
    19. "Identification of human aging-associated gene."
      Kim J.W.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    20. "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."
      Ehnholm C., Bozas S.E., Tenkanen H., Kirszbaum L., Metso J., Murphy B., Walker I.D.
      Biochim. Biophys. Acta 1086:255-260(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APOA1.
    21. "Identification of the disulfide bonds in human plasma protein SP-40,40 (apolipoprotein-J)."
      Choi-Miura N.H., Takahashi Y., Nakano Y., Tobe T., Tomita M.
      J. Biochem. 112:557-561(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    22. Cited for: INTERACTION WITH PON1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    23. "Identification and characterization of glycosylation sites in human serum clusterin."
      Kapron J.T., Hilliard G.M., Lakins J.N., Tenniswood M.P., West K.A., Carr S.A., Crabb J.W.
      Protein Sci. 6:2120-2133(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374.
      Tissue: Serum.
    24. "Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state."
      Poon S., Easterbrook-Smith S.B., Rybchyn M.S., Carver J.A., Wilson M.R.
      Biochemistry 39:15953-15960(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, ABSENCE OF ATPASE ACTIVITY, TISSUE SPECIFICITY.
    25. "Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterin."
      Hatters D.M., Wilson M.R., Easterbrook-Smith S.B., Howlett G.J.
      Eur. J. Biochem. 269:2789-2794(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    26. "Mildly acidic pH activates the extracellular molecular chaperone clusterin."
      Poon S., Rybchyn M.S., Easterbrook-Smith S.B., Carver J.A., Pankhurst G.J., Wilson M.R.
      J. Biol. Chem. 277:39532-39540(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, CIRCULAR DICHROISM.
    27. "Synthesis and functional analyses of nuclear clusterin, a cell death protein."
      Leskov K.S., Klokov D.Y., Li J., Kinsella T.J., Boothman D.A.
      J. Biol. Chem. 278:11590-11600(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, IDENTIFICATION OF ISOFORM 4, FUNCTION, INTERACTION WITH XRCC6, SUBCELLULAR LOCATION.
    28. "Essential requirement of apolipoprotein J (clusterin) signaling for IkappaB expression and regulation of NF-kappaB activity."
      Santilli G., Aronow B.J., Sala A.
      J. Biol. Chem. 278:38214-38219(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-354.
      Tissue: Serum.
    30. "Isolation and characterization of a novel gene CLUAP1 whose expression is frequently upregulated in colon cancer."
      Takahashi M., Lin Y.-M., Nakamura Y., Furukawa Y.
      Oncogene 23:9289-9294(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLUAP1.
    31. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-354 AND ASN-374.
      Tissue: Plasma.
    32. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374.
      Tissue: Plasma.
    33. "Clusterin inhibits apoptosis by interacting with activated Bax."
      Zhang H., Kim J.K., Edwards C.A., Xu Z., Taichman R., Wang C.Y.
      Nat. Cell Biol. 7:909-915(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BAX.
    34. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
      Leong W.F., Chow V.T.
      Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    35. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
      Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
      J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374.
      Tissue: Saliva.
    36. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
      Lewandrowski U., Moebius J., Walter U., Sickmann A.
      Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374.
      Tissue: Platelet.
    37. "Effects of glycosylation on the structure and function of the extracellular chaperone clusterin."
      Stewart E.M., Aquilina J.A., Easterbrook-Smith S.B., Murphy-Durland D., Jacobsen C., Moestrup S., Wilson M.R.
      Biochemistry 46:1412-1422(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH LRP2, GLYCOSYLATION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, CIRCULAR DICHROISM, TISSUE SPECIFICITY.
    38. "Multiple pathways regulating the anti-apoptotic protein clusterin in breast cancer."
      Ranney M.K., Ahmed I.S., Potts K.R., Craven R.J.
      Biochim. Biophys. Acta 1772:1103-1111(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, PROTEASOMAL DEGRADATION, SUBCELLULAR LOCATION.
    39. "Characterization of an eppin protein complex from human semen and spermatozoa."
      Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.
      Biol. Reprod. 77:476-484(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH LTF; SEMG1 AND EPPIN.
    40. "The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures."
      Yerbury J.J., Poon S., Meehan S., Thompson B., Kumita J.R., Dobson C.M., Wilson M.R.
      FASEB J. 21:2312-2322(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    41. "Differential regulation of clusterin and its isoforms by androgens in prostate cells."
      Cochrane D.R., Wang Z., Muramaki M., Gleave M.E., Nelson C.C.
      J. Biol. Chem. 282:2278-2287(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, IDENTIFICATION OF ISOFORMS 1 AND 2, INDUCTION BY ANDROGEN.
    42. "The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species."
      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.
      J. Mol. Biol. 369:157-167(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    43. Cited for: ALTERNATIVE SPLICING, IDENTIFICATION OF ISOFORMS 1; 2 AND 5, TISSUE SPECIFICITY.
    44. "Stress-induced retrotranslocation of clusterin/ApoJ into the cytosol."
      Nizard P., Tetley S., Le Drean Y., Watrin T., Le Goff P., Wilson M.R., Michel D.
      Traffic 8:554-565(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SYVN1, UBIQUITINATION.
    45. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
      Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
      Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-291; ASN-317 AND ASN-374.
      Tissue: Milk.
    46. "Structural characterization of clusterin-chaperone client protein complexes."
      Wyatt A.R., Yerbury J.J., Wilson M.R.
      J. Biol. Chem. 284:21920-21927(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    47. "Clusterin is a short half-life, poly-ubiquitinated protein, which controls the fate of prostate cancer cells."
      Rizzi F., Caccamo A.E., Belloni L., Bettuzzi S.
      J. Cell. Physiol. 219:314-323(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION.
    48. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-103; ASN-145; ASN-354 AND ASN-374.
      Tissue: Liver.
    49. Cited for: GLYCOSYLATION AT ASN-86 AND ASN-374.
    50. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    51. "Identification of human plasma proteins as major clients for the extracellular chaperone clusterin."
      Wyatt A.R., Wilson M.R.
      J. Biol. Chem. 285:3532-3539(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    52. "Clusterin facilitates COMMD1 and I-kappaB degradation to enhance NF-kappaB activity in prostate cancer cells."
      Zoubeidi A., Ettinger S., Beraldi E., Hadaschik B., Zardan A., Klomp L.W., Nelson C.C., Rennie P.S., Gleave M.E.
      Mol. Cancer Res. 8:119-130(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COMMD1; UBIQUITIN; CUL1 ANDBTRC, IDENTIFICATION IN A E3 UBIQUITIN-PROTEIN LIGASE COMPLEX.
    53. "Clusterin facilitates in vivo clearance of extracellular misfolded proteins."
      Wyatt A.R., Yerbury J.J., Berghofer P., Greguric I., Katsifis A., Dobson C.M., Wilson M.R.
      Cell. Mol. Life Sci. 68:3919-3931(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiCLUS_HUMAN
    AccessioniPrimary (citable) accession number: P10909
    Secondary accession number(s): B2R9Q1
    , B3KSE6, P11380, P11381, Q2TU75, Q5HYC1, Q7Z5B9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 172 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3