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P10909

- CLUS_HUMAN

UniProt

P10909 - CLUS_HUMAN

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Protein

Clusterin

Gene

CLU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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. cytoplasm Source: Alzheimers_University_of_Toronto
  4. endoplasmic reticulum Source: UniProtKB-KW
  5. extracellular matrix Source: UniProtKB
  6. extracellular region Source: Reactome
  7. extracellular space Source: UniProtKB
  8. extracellular vesicular exosome Source: UniProtKB
  9. membrane Source: UniProtKB-KW
  10. mitochondrion Source: BHF-UCL
  11. neurofibrillary tangle Source: Alzheimers_University_of_Toronto
  12. nucleus Source: UniProtKB-KW
  13. perinuclear region of cytoplasm Source: UniProtKB
  14. platelet alpha granule lumen Source: Reactome
  15. spherical high-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

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

BgeeiP10909.
CleanExiHS_CLU.
ExpressionAtlasiP10909. baseline and differential.
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. 89 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.
GeneTreeiENSGT00530000063668.
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

        10         20         30         40         50
MMKTLLLFVG LLLTWESGQV LGDQTVSDNE LQEMSNQGSK YVNKEIQNAV
60 70 80 90 100
NGVKQIKTLI EKTNEERKTL LSNLEEAKKK KEDALNETRE SETKLKELPG
110 120 130 140 150
VCNETMMALW EECKPCLKQT CMKFYARVCR SGSGLVGRQL EEFLNQSSPF
160 170 180 190 200
YFWMNGDRID SLLENDRQQT HMLDVMQDHF SRASSIIDEL FQDRFFTREP
210 220 230 240 250
QDTYHYLPFS LPHRRPHFFF PKSRIVRSLM PFSPYEPLNF HAMFQPFLEM
260 270 280 290 300
IHEAQQAMDI HFHSPAFQHP PTEFIREGDD DRTVCREIRH NSTGCLRMKD
310 320 330 340 350
QCDKCREILS VDCSTNNPSQ AKLRRELDES LQVAERLTRK YNELLKSYQW
360 370 380 390 400
KMLNTSSLLE QLNEQFNWVS RLANLTQGED QYYLRVTTVA SHTSDSDVPS
410 420 430 440
GVTEVVVKLF DSDPITVTVP VEVSRKNPKF METVAEKALQ EYRKKHREE

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. 89 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.
GeneTreei ENSGT00530000063668.
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

Bgeei P10909.
CleanExi HS_CLU.
ExpressionAtlasi P10909. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 173 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