P10909 (CLUS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.39 Ref.41 Ref.45 Ref.46 Ref.50 Ref.51 Ref.52
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. 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.41 Ref.43 Ref.45 Ref.51
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.39 Ref.43 Ref.46 Ref.51 Nucleus. Cytoplasm. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytosol. Microsome. Endoplasmic reticulum. Cytoplasmic vesicle › secretory vesicle › chromaffin 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.39 Ref.43 Ref.46 Ref.51
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.39 Ref.42 Ref.48
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.40
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.31 Ref.32 Ref.35 Ref.36 Ref.37 Ref.44 Ref.47 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 process	Apoptosis Complement pathway Immunity Innate immunity
Cellular component	Cytoplasm Cytoplasmic vesicle Endoplasmic reticulum Membrane Microsome Mitochondrion Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Chaperone
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chaperone-mediated protein folding Inferred from direct assay Ref.24. Source: UniProtKB complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW induction of apoptosis by intracellular signals Inferred from direct assay. Source: UniProtKB innate immune response Inferred from electronic annotation. Source: UniProtKB-KW lipid metabolic process Non-traceable author statement. Source: ProtInc 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.51. Source: UniProtKB positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.51. Source: UniProtKB positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.51. 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.50. Source: BHF-UCL response to virus Inferred from expression pattern Ref.34. Source: UniProtKB reverse cholesterol transport Traceable author statement. Source: BHF-UCL
Cellular component	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 microsome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from direct assay Ref.51. Source: UniProtKB platelet alpha granule lumen Traceable author statement. Source: Reactome spherical high-density lipoprotein particle Inferred from direct assay. Source: BHF-UCL
Molecular function	misfolded protein binding Inferred from direct assay Ref.24. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct ubiquitin protein ligase binding Inferred from direct assay Ref.51. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL2L1	Q07817-1	6	EBI-4322678,EBI-287195
DISC1	Q9NRI5	4	EBI-1104674,EBI-529989
FOS	P01100	2	EBI-1104674,EBI-852851
PPARG	P37231	3	EBI-1104674,EBI-781384

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
	Chain	23 – 449	427	Clusterin		PRO_0000005529
	Chain	23 – 227	205	Clusterin beta chain Ref.14		PRO_0000005530
	Chain	228 – 449	222	Clusterin alpha chain Ref.14		PRO_0000005531
Regions
	Motif	78 – 81	4	Nuclear localization signal By similarity
	Motif	443 – 447	5	Nuclear localization signal By similarity
Amino acid modifications
	Modified residue	393	1	Phosphothreonine Ref.48
	Modified residue	394	1	Phosphoserine Ref.48
	Modified residue	396	1	Phosphoserine Ref.48
	Glycosylation	86	1	N-linked (GlcNAc...) Ref.17 Ref.18 Ref.23 Ref.32 Ref.47
	Glycosylation	103	1	N-linked (GlcNAc...) Ref.17 Ref.18 Ref.23 Ref.32 Ref.47
	Glycosylation	145	1	N-linked (GlcNAc...) Ref.17 Ref.18 Ref.23 Ref.32 Ref.47
	Glycosylation	291	1	N-linked (GlcNAc...) Ref.17 Ref.18 Ref.23 Ref.32 Ref.44
	Glycosylation	317	1	N-linked (GlcNAc...) Ref.44
	Glycosylation	354	1	N-linked (GlcNAc...) Ref.18 Ref.23 Ref.29 Ref.31 Ref.32 Ref.47
	Glycosylation	374	1	N-linked (GlcNAc...) (complex) Ref.18 Ref.23 Ref.31 Ref.32 Ref.35 Ref.36 Ref.44 Ref.47 Ref.49
	Disulfide bond	102 ↔ 313		Interchain (between beta and alpha chains) Ref.1 Ref.10 Ref.11 Ref.18 Ref.21
	Disulfide bond	113 ↔ 305		Interchain (between beta and alpha chains) Ref.1 Ref.10 Ref.11 Ref.18 Ref.21
	Disulfide bond	116 ↔ 302		Interchain (between beta and alpha chains) Ref.1 Ref.10 Ref.11 Ref.18 Ref.21
	Disulfide bond	121 ↔ 295		Interchain (between beta and alpha chains) Ref.1 Ref.10 Ref.11 Ref.18 Ref.21
	Disulfide bond	129 ↔ 285		Interchain (between beta and alpha chains) Ref.1 Ref.10 Ref.11 Ref.18 Ref.21
Natural variations
	Alternative sequence	1 – 175	175	Missing in isoform 3.		VSP_041475
	Alternative sequence	1 – 33	33	Missing in isoform 4.		VSP_041476
	Alternative sequence	1	1	M → MQVCSQPQRGCVREQSAINT APPSAHNAASPGGARGHRVP LTEACKDSRIGGM in isoform 2.		VSP_037661
	Alternative sequence	1	1	M → MEACKDSRIGGM in isoform 5.		VSP_041477
	Natural variant	317	1	N → H. Ref.6 Corresponds to variant rs9331936 [ dbSNP | Ensembl ].		VAR_019366
	Natural variant	328	1	D → N. Ref.6 Corresponds to variant rs9331938 [ dbSNP | Ensembl ].		VAR_019367
	Natural variant	396	1	S → L. Ref.6 Corresponds to variant rs13494 [ dbSNP | Ensembl ].		VAR_019368
Experimental info
	Sequence conflict	28	1	D → S AA sequence Ref.9
	Sequence conflict	28	1	D → S AA sequence Ref.13
	Sequence conflict	47	1	Q → H AA sequence Ref.10
	Sequence conflict	52	1	G → Q AA sequence Ref.10
	Sequence conflict	172	1	M → V in CAI45990. Ref.5
	Sequence conflict	224	1	R → L in BAG36598. Ref.3
	Sequence conflict	305	1	C → M AA sequence Ref.9
	Sequence conflict	388	1	T → M in CAI45990. Ref.5
	Sequence conflict	411	1	D → G in BAG36598. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (2) (CLU35) (sCLU) [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 9583DE4CCECC169F	FASTA	449	52,495
	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
	Isoform 2 (1) (CLU34) [UniParc]. Checksum: 1941842E61CD3464	FASTA	501	57,833
	10 20 30 40 50 60 MQVCSQPQRG CVREQSAINT APPSAHNAAS PGGARGHRVP LTEACKDSRI GGMMKTLLLF 70 80 90 100 110 120 VGLLLTWESG QVLGDQTVSD NELQEMSNQG SKYVNKEIQN AVNGVKQIKT LIEKTNEERK 130 140 150 160 170 180 TLLSNLEEAK KKKEDALNET RESETKLKEL PGVCNETMMA LWEECKPCLK QTCMKFYARV 190 200 210 220 230 240 CRSGSGLVGR QLEEFLNQSS PFYFWMNGDR IDSLLENDRQ QTHMLDVMQD HFSRASSIID 250 260 270 280 290 300 ELFQDRFFTR EPQDTYHYLP FSLPHRRPHF FFPKSRIVRS LMPFSPYEPL NFHAMFQPFL 310 320 330 340 350 360 EMIHEAQQAM DIHFHSPAFQ HPPTEFIREG DDDRTVCREI RHNSTGCLRM KDQCDKCREI 370 380 390 400 410 420 LSVDCSTNNP SQAKLRRELD ESLQVAERLT RKYNELLKSY QWKMLNTSSL LEQLNEQFNW 430 440 450 460 470 480 VSRLANLTQG EDQYYLRVTT VASHTSDSDV PSGVTEVVVK LFDSDPITVT VPVEVSRKNP 490 500 KFMETVAEKA LQEYRKKHRE E
	Isoform 3 [UniParc]. Checksum: 0917960A8B4D6857	FASTA	274	32,364
	10 20 30 40 50 60 MQDHFSRASS IIDELFQDRF FTREPQDTYH YLPFSLPHRR PHFFFPKSRI VRSLMPFSPY 70 80 90 100 110 120 EPLNFHAMFQ PFLEMIHEAQ QAMDIHFHSP AFQHPPTEFI REGDDDRTVC REIRHNSTGC 130 140 150 160 170 180 LRMKDQCDKC REILSVDCST NNPSQAKLRR ELDESLQVAE RLTRKYNELL KSYQWKMLNT 190 200 210 220 230 240 SSLLEQLNEQ FNWVSRLANL TQGEDQYYLR VTTVASHTSD SDVPSGVTEV VVKLFDSDPI 250 260 270 TVTVPVEVSR KNPKFMETVA EKALQEYRKK HREE
	Isoform 4 (nCLU) [UniParc]. Checksum: 77900AB70F7AC243	FASTA	416	48,803
	10 20 30 40 50 60 MSNQGSKYVN KEIQNAVNGV KQIKTLIEKT NEERKTLLSN LEEAKKKKED ALNETRESET 70 80 90 100 110 120 KLKELPGVCN ETMMALWEEC KPCLKQTCMK FYARVCRSGS GLVGRQLEEF LNQSSPFYFW 130 140 150 160 170 180 MNGDRIDSLL ENDRQQTHML DVMQDHFSRA SSIIDELFQD RFFTREPQDT YHYLPFSLPH 190 200 210 220 230 240 RRPHFFFPKS RIVRSLMPFS PYEPLNFHAM FQPFLEMIHE AQQAMDIHFH SPAFQHPPTE 250 260 270 280 290 300 FIREGDDDRT VCREIRHNST GCLRMKDQCD KCREILSVDC STNNPSQAKL RRELDESLQV 310 320 330 340 350 360 AERLTRKYNE LLKSYQWKML NTSSLLEQLN EQFNWVSRLA NLTQGEDQYY LRVTTVASHT 370 380 390 400 410 SDSDVPSGVT EVVVKLFDSD PITVTVPVEV SRKNPKFMET VAEKALQEYR KKHREE
	Isoform 5 (CLU36) [UniParc]. Checksum: 0B0A0165A6C5622A	FASTA	460	53,643
	10 20 30 40 50 60 MEACKDSRIG GMMKTLLLFV GLLLTWESGQ VLGDQTVSDN ELQEMSNQGS KYVNKEIQNA 70 80 90 100 110 120 VNGVKQIKTL IEKTNEERKT LLSNLEEAKK KKEDALNETR ESETKLKELP GVCNETMMAL 130 140 150 160 170 180 WEECKPCLKQ TCMKFYARVC RSGSGLVGRQ LEEFLNQSSP FYFWMNGDRI DSLLENDRQQ 190 200 210 220 230 240 THMLDVMQDH FSRASSIIDE LFQDRFFTRE PQDTYHYLPF SLPHRRPHFF FPKSRIVRSL 250 260 270 280 290 300 MPFSPYEPLN FHAMFQPFLE MIHEAQQAMD IHFHSPAFQH PPTEFIREGD DDRTVCREIR 310 320 330 340 350 360 HNSTGCLRMK DQCDKCREIL SVDCSTNNPS QAKLRRELDE SLQVAERLTR KYNELLKSYQ 370 380 390 400 410 420 WKMLNTSSLL EQLNEQFNWV SRLANLTQGE DQYYLRVTTV ASHTSDSDVP SGVTEVVVKL 430 440 450 460 FDSDPITVTV PVEVSRKNPK FMETVAEKAL QEYRKKHREE

References

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[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: 2780565] [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: 8181474] [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: 14702039] [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: 17974005] [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. , 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: 16421571] [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: 15489334] [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: 1903064] [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: 2387851] [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: 8328966] [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: 2601725] [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: 3154963] [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: 1974459] [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: 1924317] [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: 2721499] [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: 1551440] [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: 1742316] [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: 1491011] [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: 8292612] [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: 9336835] [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: 11123922] [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: 12047389] [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: 12176985] [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: 12551933] [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: 12882985] [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: 12754519] [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: 15480429] [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: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-354 AND ASN-374, MASS SPECTROMETRY. 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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374, MASS SPECTROMETRY. 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: 16113678] [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: 16548883] [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: 16740002] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374, MASS SPECTROMETRY. 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: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374, MASS SPECTROMETRY. 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: 17260971] [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: 17689225] [Abstract] Cited for: FUNCTION, INDUCTION, PROTEASOMAL DEGRADATION, SUBCELLULAR LOCATION.
[39]	"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: 17412999] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[40]	"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: 17148459] [Abstract] Cited for: ALTERNATIVE SPLICING, IDENTIFICATION OF ISOFORMS 1 AND 2, INDUCTION BY ANDROGEN.
[41]	"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: 17407782] [Abstract] Cited for: FUNCTION, SUBUNIT.
[42]	"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: 17322305] [Abstract] Cited for: ALTERNATIVE SPLICING, IDENTIFICATION OF ISOFORMS 1; 2 AND 5, TISSUE SPECIFICITY.
[43]	"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: 17451556] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SYVN1, UBIQUITINATION.
[44]	"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: 18780401] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-291; ASN-317 AND ASN-374, MASS SPECTROMETRY. Tissue: Milk.
[45]	"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: 19535339] [Abstract] Cited for: FUNCTION, SUBUNIT.
[46]	"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: 19137541] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION.
[47]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-103; ASN-145; ASN-354 AND ASN-374, MASS SPECTROMETRY. Tissue: Liver.
[48]	"An initial characterization of the serum phosphoproteome." Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A., Liotta L.A., Petricoin E.F. III J. Proteome Res. 8:5523-5531(2009) [PubMed: 19824718] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-393; SER-394 AND SER-396, TISSUE SPECIFICITY, MASS SPECTROMETRY. Tissue: Serum.
[49]	"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: 19838169] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[50]	"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: 19996109] [Abstract] Cited for: FUNCTION.
[51]	"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: 20068069] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COMMD1; UBIQUITIN; CUL1 ANDBTRC, IDENTIFICATION IN A E3 UBIQUITIN-PROTEIN LIGASE COMPLEX.
[52]	"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: 21505792] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00291262. IPI00400826. IPI00954954. IPI00976752. IPI00978715.
PIR	A41386. S43646.
RefSeq	NP_001822.3. NM_001831.3.
UniGene	Hs.436657.
3D structure databases
ProteinModelPortal	P10909.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10909. 27 interactions.
MINT	MINT-3007494.
STRING	P10909.
PTM databases
PhosphoSite	P10909.
Polymorphism databases
DMDM	116533.
2D gel databases
SWISS-2DPAGE	P10909.
Cornea-2DPAGE	P10909.
DOSAC-COBS-2DPAGE	P10909.
OGP	P10909.
REPRODUCTION-2DPAGE	IPI00291262.
Proteomic databases
PRIDE	P10909.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000316403; ENSP00000315130; ENSG00000120885. ENST00000380446; ENSP00000369812; ENSG00000120885. ENST00000405140; ENSP00000385419; ENSG00000120885.
GeneID	1191.
KEGG	hsa:1191.
UCSC	uc003xfw.1. human.
Organism-specific databases
CTD	1191.
GeneCards	GC08M027510.
H-InvDB	HIX0007408.
HGNC	HGNC:2095. CLU.
HPA	CAB000476. CAB016253. HPA000572.
MIM	185430. gene.
neXtProt	NX_P10909.
PharmGKB	PA26620.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG17094.
HOVERGEN	HBG006908.
InParanoid	P10909.
OMA	NGDRIDS.
OrthoDB	EOG447FTH.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P10909.
Bgee	P10909.
CleanEx	HS_CLU.
Genevestigator	P10909.
GermOnline	ENSG00000120885. Homo sapiens.
Family and domain databases
InterPro	IPR016016. Clusterin. IPR000753. Clusterin-like. IPR016015. Clusterin_C. IPR016014. Clusterin_N. [Graphical view]
Pfam	PF01093. Clusterin. 1 hit. [Graphical view]
PIRSF	PIRSF002368. Clusterin. 1 hit.
SMART	SM00035. CLa. 1 hit. SM00030. CLb. 1 hit. [Graphical view]
PROSITE	PS00492. CLUSTERIN_1. 1 hit. PS00493. CLUSTERIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	4922.
PMAP-CutDB	P10909.
SOURCE	Search...

Entry information

Entry name

CLUS_HUMAN

Accession

Primary (citable) accession number: P10909
Secondary accession number(s): B2R9Q1 , B3KSE6, P11380, P11381, Q2TU75, Q5HYC1, Q7Z5B9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 144 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.