Reviewed, UniProtKB/Swiss-Prot P10909 (CLUS_HUMAN)

Names and origin

Protein names

Recommended name:
    Clusterin
Alternative name(s):
    Complement-associated protein SP-40,40
    Complement cytolysis inhibitor
      Short name=CLI
    NA1/NA2
    Apolipoprotein J
      Short name=Apo-J
    Testosterone-repressed prostate message 2
      Short name=TRPM-2
    Ku70-binding protein 1
    Aging-associated gene 4 protein
Cleaved into the following 2 chains:
    1- Recommended name:
            Clusterin beta chain
        Alternative name(s):
            ApoJalpha
            Complement cytolysis inhibitor a chain
    2- Recommended name:
            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) [Complete proteome]

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	Not yet clear. It is known to be expressed in a variety of tissues and it seems to be able to bind to cells, membranes and hydrophobic proteins. It has been associated with programmed cell death (apoptosis).
Subunit structure	Antiparallel disulfide-linked heterodimer. Interacts with APOA1, CLUAP1 AND PON1. Ref.16 Ref.20 Ref.21 Ref.22 Ref.25
Subcellular location	Secreted.
Sequence similarities	Belongs to the clusterin family.
Sequence caution	The sequence AAP88927.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Apoptosis Complement pathway Immune response Innate immunity
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW lipid metabolic process Ref.8 Non-traceable author statement. Source: ProtInc negative regulation of protein homooligomerization Inferred from mutant phenotype. Source: UniProtKB release of cytochrome c from mitochondria Inferred by curator. Source: UniProtKB reverse cholesterol transport Traceable author statement. Source: UniProtKB
Cellular component	mitochondrion Inferred from direct assay. Source: UniProtKB platelet alpha granule lumen Inferred from Experiment. Source: Reactome spherical high-density lipoprotein particle Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DISC1	Q9NRI5	2	EBI-1104674,EBI-529989

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P10909-1)

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.

Isoform 2 (identifier: P10909-2)

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

Note: Ref.4 (AAB06508) sequence differs from that shown due to a frameshifts in position 37.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
	Chain	23 – 449	427	Clusterin		PRO_0000005529
	Chain	23 – 227	205	Clusterin beta chain Ref.12		PRO_0000005530
	Chain	228 – 449	222	Clusterin alpha chain Ref.12		PRO_0000005531
Amino acid modifications
	Glycosylation	86	1	N-linked (GlcNAc...) Ref.16 Ref.23 Ref.27 Ref.31 Ref.15
	Glycosylation	103	1	N-linked (GlcNAc...) Ref.16 Ref.23 Ref.27 Ref.31 Ref.15
	Glycosylation	145	1	N-linked (GlcNAc...) Ref.16 Ref.23 Ref.27 Ref.31 Ref.15
	Glycosylation	291	1	N-linked (GlcNAc...) Ref.16 Ref.23 Ref.27 Ref.30 Ref.15
	Glycosylation	317	1	N-linked (GlcNAc...) Ref.30
	Glycosylation	354	1	N-linked (GlcNAc...) Ref.16 Ref.23 Ref.27 Ref.31 Ref.24 Ref.26
	Glycosylation	374	1	N-linked (GlcNAc...) Ref.16 Ref.23 Ref.27 Ref.31 Ref.30 Ref.26 Ref.28 Ref.29
	Disulfide bond	102 ↔ 313		Interchain (between beta and alpha chains) Ref.16 Ref.21
	Disulfide bond	113 ↔ 305		Interchain (between beta and alpha chains) Ref.16 Ref.21
	Disulfide bond	116 ↔ 302		Interchain (between beta and alpha chains) Ref.16 Ref.21
	Disulfide bond	121 ↔ 295		Interchain (between beta and alpha chains) Ref.16 Ref.21
	Disulfide bond	129 ↔ 285		Interchain (between beta and alpha chains) Ref.16 Ref.21
Natural variations
	Alternative sequence	1	1	M → MQVCSQPQRGCVREQSAINT APPSAHNAASPGGARGHRVP LTEACKDSRIGGM in isoform 2.		VSP_037661
	Natural variant	317	1	N → H: dbSNP rs9331936. Ref.5		VAR_019366
	Natural variant	328	1	D → N: dbSNP rs9331938. Ref.5		VAR_019367
	Natural variant	396	1	S → L: dbSNP rs13494. Ref.5		VAR_019368
Experimental info
	Sequence conflict	28	1	D → S AA sequence Ref.7
	Sequence conflict	28	1	D → S AA sequence Ref.11
	Sequence conflict	31 – 33	3	LQE → PQD in AAA51765. Ref.3
	Sequence conflict	47	1	Q → H AA sequence Ref.8
	Sequence conflict	52	1	G → Q AA sequence Ref.8
	Sequence conflict	172	1	M → V in CAI45990. Ref.4
	Sequence conflict	224	1	R → L in BAG36598. Ref.18
	Sequence conflict	305	1	C → M AA sequence Ref.7
	Sequence conflict	388	1	T → M in CAI45990. Ref.4
	Sequence conflict	411	1	D → G in BAG36598. Ref.18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [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. 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

References

	« Hide 'large scale' referencesShow '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: 2780565] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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).
[3]	"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.
[4]	"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.
[5]	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.
[6]	"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].
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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 31-449 (ISOFORMS 1/2).
[13]	"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.
[14]	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.
[15]	"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.
[16]	"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.
[17]	"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).
[18]	"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: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[19]	"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: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[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.
[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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	M25915 mRNA. Translation: AAA35692.1. Different initiation. M63379 , M63376, M63377, M63378 Genomic DNA. Translation: AAB06507.1. M64722 mRNA. Translation: AAB06508.1. Sequence problems. CR599675 mRNA. No translation available. BX648414 mRNA. Translation: CAI45990.1. AY341244 Genomic DNA. Translation: AAP88927.1. Different initiation. AF311103 Genomic DNA. No translation available. J02908 mRNA. Translation: AAA51765.1. Different initiation. 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. AK313870 mRNA. Translation: BAG36598.1. Different initiation. BC010514 mRNA. Translation: AAH10514.1. Different initiation. BC019588 mRNA. Translation: AAH19588.1. Different initiation.
IPI	IPI00291262. IPI00400826.
PIR	A41386. S43646.
RefSeq	NP_001822.2. NP_976084.1.
UniGene	Hs.436657
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P10909. 6 interactions.
STRING	P10909.
2-D gel databases
SWISS-2DPAGE	P10909.
Cornea-2DPAGE	P10909.
DOSAC-COBS-2DPAGE	P10909.
OGP	P10909.
REPRODUCTION-2DPAGE	IPI00291262.
Proteomic databases
PRIDE	P10909.
Genome annotation databases
Ensembl	ENST00000316403; ENSP00000315130; ENSG00000120885; Homo sapiens. [Genome view] ENST00000380446; ENSP00000369812; ENSG00000120885; Homo sapiens. [Genome view] ENST00000405140; ENSP00000385419; ENSG00000120885; Homo sapiens. [Genome view]
GeneID	1191.
KEGG	hsa:1191.
UCSC	uc003xfw.1. human. uc003xfy.1. human.
Organism-specific databases
CTD	1191.
GeneCards	GC08M027510.
H-InvDB	HIX0007408.
HGNC	HGNC:2095. CLU.
HPA	CAB000476. CAB016253. HPA000572.
MIM	185430. gene.
PharmGKB	PA26620.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P10909.
HOVERGEN	P10909.
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]
PANTHER	PTHR10970:SF1. Clusterin. 1 hit.
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 Resources
NextBio	4922.
PMAP-CutDB	P10909.
SOURCE	Search...

Entry information

Entry name

CLUS_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	October 13, 2009
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.