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P10909 (CLUS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Clusterin beta chain
    Alternative name(s):
    ApoJalpha
    Complement cytolysis inhibitor a chain
  2. Clusterin alpha chain
    Alternative name(s):
    ApoJbeta
    Complement cytolysis inhibitor b chain
Gene names
Name:CLU
Synonyms:APOJ, CLI, KUB1
ORF Names:AAG4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.33 Ref.37 Ref.38 Ref.40 Ref.42 Ref.46 Ref.47 Ref.51 Ref.52 Ref.53

Subunit structure

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. Ref.1 Ref.9 Ref.10 Ref.11 Ref.14 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.30 Ref.33 Ref.37 Ref.39 Ref.40 Ref.42 Ref.44 Ref.46 Ref.52

Subcellular location

Isoform 1: Secreted. Note: Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Ref.1 Ref.10 Ref.11 Ref.13 Ref.22 Ref.24 Ref.27 Ref.33 Ref.37 Ref.38 Ref.40 Ref.44 Ref.47 Ref.52

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. Ref.1 Ref.10 Ref.11 Ref.13 Ref.22 Ref.24 Ref.27 Ref.33 Ref.37 Ref.38 Ref.40 Ref.44 Ref.47 Ref.52

Tissue specificity

Detected in blood plasma, cerebrospinal fluid, milk, seminal plasma and colon mucosa. Detected in the germinal center of colon lymphoid nodules and in colon parasympathetic ganglia of the Auerbach plexus (at protein level). Ubiquitous. Detected in brain, testis, ovary, liver and pancreas, and at lower levels in kidney, heart, spleen and lung. Ref.1 Ref.2 Ref.10 Ref.11 Ref.13 Ref.14 Ref.22 Ref.24 Ref.37 Ref.40 Ref.43

Induction

Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). Up-regulated by agents that induce apoptosis, both at mRNA and protein level. Isoform 1 is up-regulated by androgen. Isoform 2 is down-regulated by androgen. Ref.34 Ref.38 Ref.41

Post-translational modification

Isoform 1 is proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen. Ref.10

Polyubiquitinated, leading to proteasomal degradation.

Heavily N-glycosylated. About 30% of the protein mass is comprised of complex N-linked carbohydrate. Ref.10 Ref.18 Ref.23 Ref.29 Ref.37 Ref.49

Sequence similarities

Belongs to the clusterin family.

Sequence caution

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 AAB06508.1 differs from that shown. Reason: Contaminating sequence.

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 gene model prediction.

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.

Ontologies

Keywords
   Biological processApoptosis
Complement pathway
Immunity
Innate immunity
   Cellular componentCytoplasm
Cytoplasmic vesicle
Endoplasmic reticulum
Membrane
Microsome
Mitochondrion
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   Molecular functionChaperone
   PTMDisulfide bond
Glycoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchaperone-mediated protein folding

Inferred from direct assay Ref.24. Source: UniProtKB

complement activation

Traceable author statement PubMed 1585460. Source: ProtInc

complement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 21567405. Source: UniProtKB

lipid metabolic process

Non-traceable author statement Ref.10. Source: ProtInc

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype Ref.33. Source: BHF-UCL

negative regulation of protein homooligomerization

Inferred from mutant phenotype Ref.33. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.52. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 21567405. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21567405. Source: UniProtKB

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.52. Source: UniProtKB

positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.52. Source: UniProtKB

protein stabilization

Inferred from direct assay Ref.24. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred by curator Ref.33. Source: BHF-UCL

response to misfolded protein

Inferred from direct assay Ref.51. Source: BHF-UCL

response to virus

Inferred from expression pattern Ref.34. Source: UniProtKB

reverse cholesterol transport

Traceable author statement PubMed 16682745. Source: BHF-UCL

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

chromaffin granule

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay Ref.33. Source: BHF-UCL

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay Ref.52. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

spherical high-density lipoprotein particle

Inferred from direct assay PubMed 16682745. Source: BHF-UCL

   Molecular_functionmisfolded protein binding

Inferred from direct assay Ref.24. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from direct assay Ref.52. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P10909-1)

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.
Note: Major isoform.
Isoform 2 (identifier: P10909-2)

Also known as: 1; CLU34;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQVCSQPQRGCVREQSAINTAPPSAHNAASPGGARGHRVPLTEACKDSRIGGM
Isoform 3 (identifier: P10909-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-175: Missing.
Isoform 4 (identifier: P10909-4)

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.
Isoform 5 (identifier: P10909-5)

Also known as: CLU36;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Chain23 – 449427Clusterin
PRO_0000005529
Chain23 – 227205Clusterin beta chain Ref.14
PRO_0000005530
Chain228 – 449222Clusterin alpha chain Ref.14
PRO_0000005531

Regions

Motif78 – 814Nuclear localization signal By similarity
Motif443 – 4475Nuclear localization signal By similarity

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) (complex) Ref.18 Ref.23 Ref.32 Ref.48 Ref.49
Glycosylation1031N-linked (GlcNAc...) Ref.17 Ref.18 Ref.23 Ref.32 Ref.48
Glycosylation1451N-linked (GlcNAc...) Ref.17 Ref.18 Ref.23 Ref.32 Ref.48
Glycosylation2911N-linked (GlcNAc...) Ref.17 Ref.18 Ref.23 Ref.32 Ref.45
Glycosylation3171N-linked (GlcNAc...) Ref.45
Glycosylation3541N-linked (GlcNAc...) Ref.18 Ref.23 Ref.29 Ref.31 Ref.32 Ref.48
Glycosylation3741N-linked (GlcNAc...) (complex) Ref.18 Ref.23 Ref.31 Ref.32 Ref.35 Ref.36 Ref.45 Ref.48 Ref.49 Ref.50
Disulfide bond102 ↔ 313Interchain (between beta and alpha chains) Ref.1 Ref.10 Ref.11 Ref.18 Ref.21
Disulfide bond113 ↔ 305Interchain (between beta and alpha chains) Ref.1 Ref.10 Ref.11 Ref.18 Ref.21
Disulfide bond116 ↔ 302Interchain (between beta and alpha chains) Ref.1 Ref.10 Ref.11 Ref.18 Ref.21
Disulfide bond121 ↔ 295Interchain (between beta and alpha chains) Ref.1 Ref.10 Ref.11 Ref.18 Ref.21
Disulfide bond129 ↔ 285Interchain (between beta and alpha chains) Ref.1 Ref.10 Ref.11 Ref.18 Ref.21

Natural variations

Alternative sequence1 – 175175Missing in isoform 3.
VSP_041475
Alternative sequence1 – 3333Missing in isoform 4.
VSP_041476
Alternative sequence11M → MQVCSQPQRGCVREQSAINT APPSAHNAASPGGARGHRVP LTEACKDSRIGGM in isoform 2.
VSP_037661
Alternative sequence11M → MEACKDSRIGGM in isoform 5.
VSP_041477
Natural variant3171N → H. Ref.6
Corresponds to variant rs9331936 [ dbSNP | Ensembl ].
VAR_019366
Natural variant3281D → N. Ref.6
Corresponds to variant rs9331938 [ dbSNP | Ensembl ].
VAR_019367
Natural variant3961S → L. Ref.6
Corresponds to variant rs13494 [ dbSNP | Ensembl ].
VAR_019368

Experimental info

Sequence conflict281D → S AA sequence Ref.9
Sequence conflict281D → S AA sequence Ref.13
Sequence conflict471Q → H AA sequence Ref.10
Sequence conflict521G → Q AA sequence Ref.10
Sequence conflict1721M → V in CAI45990. Ref.5
Sequence conflict2241R → L in BAG36598. Ref.3
Sequence conflict3051C → M AA sequence Ref.9
Sequence conflict3881T → M in CAI45990. Ref.5
Sequence conflict4111D → G in BAG36598. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (2) (CLU35) (sCLU) [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 9583DE4CCECC169F

FASTA44952,495
        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 

« Hide

Isoform 2 (1) (CLU34) [UniParc].

Checksum: 1941842E61CD3464
Show »

FASTA50157,833
Isoform 3 [UniParc].

Checksum: 0917960A8B4D6857
Show »

FASTA27432,364
Isoform 4 (nCLU) [UniParc].

Checksum: 77900AB70F7AC243
Show »

FASTA41648,803
Isoform 5 (CLU36) [UniParc].

Checksum: 0B0A0165A6C5622A
Show »

FASTA46053,643

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Apolipoprotein J: structure and tissue distribution."
de Silva H.V., Harmony J.A.K., Stuart W.D., Gil C.M., Robbins J.
Biochemistry 29:5380-5389(1990) [PubMed] [Europe PMC] [Abstract]
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]"Apolipoprotein J is associated with paraoxonase in human plasma."
Kelso G.J., Stuart W.D., Richter R.J., Furlong C.E., Jordan-Starck T.C., Harmony J.A.K.
Biochemistry 33:832-839(1994) [PubMed] [Europe PMC] [Abstract]
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, 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, 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]"Clusterin expression in normal mucosa and colorectal cancer."
Andersen C.L., Schepeler T., Thorsen K., Birkenkamp-Demtroder K., Mansilla F., Aaltonen L.A., Laurberg S., Orntoft T.F.
Mol. Cell. Proteomics 6:1039-1048(2007) [PubMed] [Europe PMC] [Abstract]
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]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25915 mRNA. Translation: AAA35692.1. Different initiation.
M63379 expand/collapse EMBL AC list , 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.
PIRA41386. S43646.
RefSeqNP_001822.3. NM_001831.3.
UniGeneHs.436657.

3D structure databases

ProteinModelPortalP10909.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107603. 71 interactions.
DIPDIP-37546N.
IntActP10909. 28 interactions.
MINTMINT-3007494.
STRING9606.ENSP00000315130.

PTM databases

PhosphoSiteP10909.

Polymorphism databases

DMDM116533.

2D gel databases

DOSAC-COBS-2DPAGEP10909.
OGPP10909.
REPRODUCTION-2DPAGEIPI00291262.
SWISS-2DPAGEP10909.

Proteomic databases

PaxDbP10909.
PRIDEP10909.

Protocols and materials databases

DNASU1191.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316403; ENSP00000315130; ENSG00000120885. [P10909-1]
ENST00000405140; ENSP00000385419; ENSG00000120885. [P10909-1]
ENST00000523500; ENSP00000429620; ENSG00000120885. [P10909-1]
ENST00000546343; ENSP00000446413; ENSG00000120885. [P10909-5]
ENST00000560366; ENSP00000453939; ENSG00000120885. [P10909-2]
GeneID1191.
KEGGhsa:1191.
UCSCuc003xfw.2. human. [P10909-1]
uc003xfy.2. human. [P10909-5]

Organism-specific databases

CTD1191.
GeneCardsGC08M027454.
HGNCHGNC:2095. CLU.
HPACAB000476.
CAB016253.
HPA000572.
MIM185430. gene.
neXtProtNX_P10909.
PharmGKBPA26620.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26650.
HOVERGENHBG006908.
InParanoidP10909.
KOK17252.
OMAKFYARVC.
OrthoDBEOG7K6PV4.
TreeFamTF333030.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP10909.
BgeeP10909.
CleanExHS_CLU.
GenevestigatorP10909.

Family and domain databases

InterProIPR016016. Clusterin.
IPR000753. Clusterin-like.
IPR016015. Clusterin_C.
IPR016014. Clusterin_N.
[Graphical view]
PANTHERPTHR10970:SF1. PTHR10970:SF1. 1 hit.
PfamPF01093. Clusterin. 1 hit.
[Graphical view]
PIRSFPIRSF002368. Clusterin. 1 hit.
SMARTSM00035. CLa. 1 hit.
SM00030. CLb. 1 hit.
[Graphical view]
PROSITEPS00492. CLUSTERIN_1. 1 hit.
PS00493. CLUSTERIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCLU. human.
GeneWikiClusterin.
GenomeRNAi1191.
NextBio4922.
PMAP-CutDBP10909.
PROP10909.
SOURCESearch...

Entry information

Entry nameCLUS_HUMAN
AccessionPrimary (citable) accession number: P10909
Secondary accession number(s): B2R9Q1 expand/collapse secondary AC list , B3KSE6, P11380, P11381, Q2TU75, Q5HYC1, Q7Z5B9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 19, 2014
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM