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Apolipoprotein E (Apo-E)

 APOE_HUMAN              Reviewed;         317 AA.
P02649; B2RC15; C0JYY5; Q9P2S4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 226.
RecName: Full=Apolipoprotein E;
Short=Apo-E;
Flags: Precursor;
Name=APOE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (VARIANT E3).
PubMed=6325438;
Zannis V.I., McPherson J., Goldberger G., Karathanasis S.K.,
Breslow J.L.;
"Synthesis, intracellular processing, and signal peptide of human
apolipoprotein E.";
J. Biol. Chem. 259:5495-5499(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (VARIANT E3).
PubMed=6327682;
McLean J.W., Elshourbagy N.A., Chang D.J., Mahley R.W., Taylor J.M.;
"Human apolipoprotein E mRNA. cDNA cloning and nucleotide sequencing
of a new variant.";
J. Biol. Chem. 259:6498-6504(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANT E4).
PubMed=2987927; DOI=10.1073/pnas.82.10.3445;
Paik Y.-K., Chang D.J., Reardon C.A., Davies G.E., Mahley R.W.,
Taylor J.M.;
"Nucleotide sequence and structure of the human apolipoprotein E
gene.";
Proc. Natl. Acad. Sci. U.S.A. 82:3445-3449(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANT E2).
PubMed=3243553; DOI=10.1016/0888-7543(88)90130-9;
Emi M., Wu L.L., Robertson M.A., Myers R.L., Hegele R.A.,
Williams R.R., White R., Lalouel J.-M.;
"Genotyping and sequence analysis of apolipoprotein E isoforms.";
Genomics 3:373-379(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10520737; DOI=10.3109/10425179809086433;
Freitas E.M., Zhang W.J., Lalonde J.P., Tay G.K., Gaudieri S.,
Ashworth L.K., Van Bockxmeer F.M., Dawkins R.L.;
"Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene:
PEREC1.";
DNA Seq. 9:89-100(1998).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-46; ARG-130;
CYS-163 AND CYS-176.
PubMed=11042151; DOI=10.1101/gr.146900;
Nickerson D.A., Taylor S.L., Fullerton S.M., Weiss K.M., Clark A.G.,
Stengard J.H., Salomaa V., Boerwinkle E., Sing C.F.;
"Sequence diversity and large-scale typing of SNPs in the human
apolipoprotein E gene.";
Genome Res. 10:1532-1545(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-78, AND VARIANT HIS-64.
TISSUE=Blood;
Imura T., Kimura H., Kawasaki M.;
"A new apolipoprotein E variant (Gln46-->His).";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 99-317 (VARIANT E3).
PubMed=6897404;
Breslow J.L., McPherson J., Nussbaum A.L., Williams H.W.,
Lofquist-Kahl F., Karathanasis S.K., Zannis V.I.;
"Identification and DNA sequence of a human apolipoprotein E cDNA
clone.";
J. Biol. Chem. 257:14639-14641(1982).
[12]
ERRATUM.
Breslow J.L., McPherson J., Nussbaum A.L., Williams H.W.,
Lofquist-Kahl F., Karathanasis S.K., Zannis V.I.;
J. Biol. Chem. 258:11422-11422(1983).
[13]
PROTEIN SEQUENCE OF 19-317 (VARIANT E2).
PubMed=7068630;
Rall S.C. Jr., Weisgraber K.H., Mahley R.W.;
"Human apolipoprotein E. The complete amino acid sequence.";
J. Biol. Chem. 257:4171-4178(1982).
[14]
REVIEW.
PubMed=3283935; DOI=10.1126/science.3283935;
Mahley R.W.;
"Apolipoprotein E: cholesterol transport protein with expanding role
in cell biology.";
Science 240:622-630(1988).
[15]
HEPARIN-BINDING SITES.
PubMed=3947350; DOI=10.1016/S0006-291X(86)80489-2;
Cardin A.D., Hirose N., Blankenship D.T., Jackson R.L.,
Harmony J.A.K., Sparrow D.A., Sparrow J.T.;
"Binding of a high reactive heparin to human apolipoprotein E:
identification of two heparin-binding domains.";
Biochem. Biophys. Res. Commun. 134:783-789(1986).
[16]
INVOLVEMENT IN AD2, AND VARIANT AD2 ARG-130.
PubMed=8346443; DOI=10.1126/science.8346443;
Corder E.H., Saunders A.M., Strittmatter W.J., Schmechel D.E.,
Gaskell P.C., Small G.W., Roses A.D., Haines J.L., Pericak-Vance M.A.;
"Gene dose of apolipoprotein E type 4 allele and the risk of
Alzheimer's disease in late onset families.";
Science 261:921-923(1993).
[17]
GLYCATION AT LYS-93, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10452964; DOI=10.1016/S0925-4439(99)00047-2;
Shuvaev V.V., Fujii J., Kawasaki Y., Itoh H., Hamaoka R., Barbier A.,
Ziegler O., Siest G., Taniguchi N.;
"Glycation of apolipoprotein E impairs its binding to heparin:
identification of the major glycation site.";
Biochim. Biophys. Acta 1454:296-308(1999).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-212; THR-307 AND SER-308,
AND STRUCTURE OF CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[21]
GLYCOSYLATION AT THR-26; THR-36 AND SER-314, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
PHOSPHORYLATION AT SER-147.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[24]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 41-184, AND LDL RECEPTOR
BINDING REGION.
PubMed=2063194; DOI=10.1126/science.2063194;
Wilson C., Wardell M.R., Weisgraber K.H., Mahley R.W., Agard D.A.;
"Three-dimensional structure of the LDL receptor-binding domain of
human apolipoprotein E.";
Science 252:1817-1822(1991).
[25]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 41-181.
PubMed=8756331; DOI=10.1038/nsb0896-718;
Dong L.-M., Parkin S., Trakhanov S.D., Rupp B., Simmons T.,
Arnold K.S., Newhouse Y.M., Innerarity T.L., Weisgraber K.H.;
"Novel mechanism for defective receptor binding of apolipoprotein E2
in type III hyperlipoproteinemia.";
Nat. Struct. Biol. 3:718-722(1996).
[26]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-165.
PubMed=10850798; DOI=10.1110/ps.9.5.886;
Segelke B.W., Forstner M., Knapp M., Trakhanov S.D., Parkin S.,
Newhouse Y.M., Bellamy H.D., Weisgraber K.H., Rupp B.;
"Conformational flexibility in the apolipoprotein E amino-terminal
domain structure determined from three new crystal forms: implications
for lipid binding.";
Protein Sci. 9:886-897(2000).
[27]
REVIEW ON VARIANTS.
PubMed=7833947; DOI=10.1002/humu.1380040303;
de Knijff P., van den Maagdenberg A.M.J.M., Frants R.R., Havekes L.M.;
"Genetic heterogeneity of apolipoprotein E and its influence on plasma
lipid and lipoprotein levels.";
Hum. Mutat. 4:178-194(1994).
[28]
VARIANT E5 LYS-21.
PubMed=2760009; DOI=10.1093/oxfordjournals.jbchem.a122692;
Maeda H., Nakamura H., Kobori S., Okada M., Niki H., Ogura T.,
Hiraga S.;
"Molecular cloning of a human apolipoprotein E variant: E5 (Glu-
3-->Lys).";
J. Biochem. 105:491-493(1989).
[29]
VARIANT HLPP3 E3 LEIDEN GLU-VAL-GLN-ALA-MET-LEU-GLY-145 INS.
PubMed=2556398;
Wardell M.R., Weisgraber K.H., Havekes L.M., Rall S.C. Jr.;
"Apolipoprotein E3-Leiden contains a seven-amino acid insertion that
is a tandem repeat of residues 121-127.";
J. Biol. Chem. 264:21205-21210(1989).
[30]
VARIANTS HLPP3 E4 PHILADELPHIA LYS-31 AND CYS-163.
PubMed=1674745;
Lohse P., Mann W.A., Stein E.A., Brewer H.B. Jr.;
"Apolipoprotein E-4 Philadelphia (Glu-13-->Lys,Arg-145-->Cys).
Homozygosity for two rare point mutations in the apolipoprotein E gene
combined with severe type III hyperlipoproteinemia.";
J. Biol. Chem. 266:10479-10484(1991).
[31]
VARIANTS GLU-254; GLY-269; GLU-270; HIS-292 AND ARG-314.
PubMed=8488843;
van den Maagdenberg A.M.J.M., Weng W., de Bruijn I.H., de Knijff P.,
Funke H., Smelt A.H.M., Leuven J.A.G., van 't Hooft F.M., Assmann G.,
Hofker M.H., Havekes L.M., Frants R.R.;
"Characterization of five new mutants in the carboxyl-terminal domain
of human apolipoprotein E: no cosegregation with severe
hyperlipidemia.";
Am. J. Hum. Genet. 52:937-946(1993).
[32]
VARIANTS HLPP3 ARG-130; ASP-145; SER-154; CYS-160 AND CYS-176.
PubMed=8287539;
Richard P., Thomas G., de Zulueta M.P., de Gennes J.-L., Thomas M.,
Cassaigne A., Bereziat G., Iron A.;
"Common and rare genotypes of human apolipoprotein E determined by
specific restriction profiles of polymerase chain reaction-amplified
DNA.";
Clin. Chem. 40:24-29(1994).
[33]
VARIANT LPG PRO-163.
PubMed=9176854;
Oikawa S., Matsunaga A., Saito T., Sato H., Seki T., Hoshi K.,
Hayasaka K., Kotake H., Midorikawa H., Sekikawa A., Hara S., Abe K.,
Toyota T., Jingami H., Nakamura H., Sasaki J.;
"Apolipoprotein E Sendai (arginine 145-->proline): a new variant
associated with lipoprotein glomerulopathy.";
J. Am. Soc. Nephrol. 8:820-823(1997).
[34]
VARIANTS E4/3 ARG-130 AND GLY-269.
PubMed=9360638; DOI=10.1016/S1383-5726(97)00009-5;
Kang A.K., Jenkins D.J.A., Wolever T.M.S., Huff M.W., Maguire G.F.,
Connelly P.W., Hegele R.A.;
"Apolipoprotein E R112; R251G: a carboxy-terminal variant found in
patients with hyperlipidemia and coronary heart disease.";
Mutat. Res. 382:57-65(1997).
[35]
VARIANT LPG CYS-43.
PubMed=10432380; DOI=10.1046/j.1523-1755.1999.00572.x;
Matsunaga A., Sasaki J., Komatsu T., Kanatsu K., Tsuji E.,
Moriyama K., Koga T., Arakawa K., Oikawa S., Saito T., Kita T.,
Doi T.;
"A novel apolipoprotein E mutation, E2 (Arg25Cys), in lipoprotein
glomerulopathy.";
Kidney Int. 56:421-427(1999).
[36]
VARIANT SBHD LEU-167 DEL.
PubMed=11095479; DOI=10.1210/jcem.85.11.6981;
Nguyen T.T., Kruckeberg K.E., O'Brien J.F., Ji Z.-S., Karnes P.S.,
Crotty T.B., Hay I.D., Mahley R.W., O'Brien T.;
"Familial splenomegaly: macrophage hypercatabolism of lipoproteins
associated with apolipoprotein E mutation [apolipoprotein E (delta149
Leu)].";
J. Clin. Endocrinol. Metab. 85:4354-4358(2000).
[37]
VARIANT E3 BASEL VAL-124.
PubMed=12864777; DOI=10.1046/j.1365-2362.2003.01180.x;
Miserez A.R., Scharnagl H., Muller P.Y., Mirsaidi R., Stahelin H.B.,
Monsch A., Marz W., Hoffmann M.M.;
"Apolipoprotein E3Basel: new insights into a highly conserved protein
region.";
Eur. J. Clin. Invest. 33:677-685(2003).
[38]
VARIANTS ARG-130 AND CYS-176.
PubMed=12966036; DOI=10.1093/hmg/ddg314;
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
Alvin G.B., Das K., Gilliam T.C.;
"Association of extreme blood lipid profile phenotypic variation with
11 reverse cholesterol transport genes and 10 non-genetic
cardiovascular disease risk factors.";
Hum. Mol. Genet. 12:2733-2743(2003).
[39]
VARIANT SBHD LEU-167 DEL.
PubMed=16094309; DOI=10.1038/sj.ejhg.5201480;
Faivre L., Saugier-Veber P., Pais de Barros J.-P., Verges B.,
Couret B., Lorcerie B., Thauvin C., Charbonnier F., Huet F.,
Gambert P., Frebourg T., Duvillard L.;
"Variable expressivity of the clinical and biochemical phenotype
associated with the apolipoprotein E p.Leu149del mutation.";
Eur. J. Hum. Genet. 13:1186-1191(2005).
[40]
VARIANT LPG CYS-43.
PubMed=18077821; DOI=10.1056/NEJMc072088;
Rovin B.H., Roncone D., McKinley A., Nadasdy T., Korbet S.M.,
Schwartz M.M.;
"APOE Kyoto mutation in European Americans with lipoprotein
glomerulopathy.";
N. Engl. J. Med. 357:2522-2524(2007).
[41]
VARIANT HIS-64, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22028381; DOI=10.1093/jmcb/mjr024;
Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H.,
Lin X., Zeng R., Wu J.R.;
"Quantitative detection of single amino acid polymorphisms by targeted
proteomics.";
J. Mol. Cell Biol. 3:309-315(2011).
[42]
VARIANT HLPP3 SER-154, AND VARIANT LEU-167 DEL.
PubMed=22481068; DOI=10.1016/j.atherosclerosis.2012.03.011;
Solanas-Barca M., de Castro-Oros I., Mateo-Gallego R., Cofan M.,
Plana N., Puzo J., Burillo E., Martin-Fuentes P., Ros E., Masana L.,
Pocovi M., Civeira F., Cenarro A.;
"Apolipoprotein E gene mutations in subjects with mixed hyperlipidemia
and a clinical diagnosis of familial combined hyperlipidemia.";
Atherosclerosis 222:449-455(2012).
[43]
POSSIBLE INVOLVEMENT IN FH, AND VARIANT FH LEU-167 DEL.
PubMed=24267230; DOI=10.1016/j.atherosclerosis.2013.09.007;
Awan Z., Choi H.Y., Stitziel N., Ruel I., Bamimore M.A., Husa R.,
Gagnon M.H., Wang R.H., Peloso G.M., Hegele R.A., Seidah N.G.,
Kathiresan S., Genest J.;
"APOE p.Leu167del mutation in familial hypercholesterolemia.";
Atherosclerosis 231:218-222(2013).
[44]
POSSIBLE INVOLVEMENT IN FH, AND VARIANT FH LEU-167 DEL.
PubMed=22949395; DOI=10.1002/humu.22215;
Marduel M., Ouguerram K., Serre V., Bonnefont-Rousselot D.,
Marques-Pinheiro A., Erik Berge K., Devillers M., Luc G., Lecerf J.M.,
Tosolini L., Erlich D., Peloso G.M., Stitziel N., Nitchke P.,
Jais J.P., Abifadel M., Kathiresan S., Leren T.P., Rabes J.P.,
Boileau C., Varret M.;
"Description of a large family with autosomal dominant
hypercholesterolemia associated with the APOE p.Leu167del mutation.";
Hum. Mutat. 34:83-87(2013).
[45]
POSSIBLE INVOLVEMENT IN FH, AND VARIANTS FH PRO-46; ASP-145; CYS-163
AND LEU-167 DEL.
PubMed=26802169; DOI=10.1194/jlr.P055699;
Wintjens R., Bozon D., Belabbas K., Mbou F., Girardet J.P.,
Tounian P., Jolly M., Boccara F., Cohen A., Karsenty A., Dubern B.,
Carel J.C., Azar-Kolakez A., Feillet F., Labarthe F., Gorsky A.M.,
Horovitz A., Tamarindi C., Kieffer P., Lienhardt A., Lascols O.,
Di Filippo M., Dufernez F.;
"Global molecular analysis and APOE mutations in a cohort of autosomal
dominant hypercholesterolemia patients in France.";
J. Lipid Res. 57:482-491(2016).
-!- FUNCTION: Mediates the binding, internalization, and catabolism of
lipoprotein particles. It can serve as a ligand for the LDL (apo
B/E) receptor and for the specific apo-E receptor (chylomicron
remnant) of hepatic tissues. {ECO:0000303|PubMed:3283935}.
-!- INTERACTION:
P27958:- (xeno); NbExp=4; IntAct=EBI-1222467, EBI-6904269;
Q16543:CDC37; NbExp=3; IntAct=EBI-1222467, EBI-295634;
Q9BQ95:ECSIT; NbExp=4; IntAct=EBI-1222467, EBI-712452;
P00738:HP; NbExp=7; IntAct=EBI-1222467, EBI-1220767;
P01130:LDLR; NbExp=2; IntAct=EBI-1222467, EBI-988319;
Q14114:LRP8; NbExp=2; IntAct=EBI-1222467, EBI-2681187;
P10636:MAPT; NbExp=3; IntAct=EBI-9209835, EBI-366182;
Q53EL6:PDCD4; NbExp=3; IntAct=EBI-1222467, EBI-935824;
P50502:ST13; NbExp=3; IntAct=EBI-1222467, EBI-357285;
O75069:TMCC2; NbExp=5; IntAct=EBI-1222467, EBI-726731;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:3283935}.
-!- TISSUE SPECIFICITY: Occurs in all lipoprotein fractions in plasma.
It constitutes 10-20% of very low density lipoproteins (VLDL) and
1-2% of high density lipoproteins (HDL). APOE is produced in most
organs. Significant quantities are produced in liver, brain,
spleen, lung, adrenal, ovary, kidney and muscle.
-!- PTM: Synthesized with the sialic acid attached by O-glycosidic
linkage and is subsequently desialylated in plasma. O-glycosylated
with core 1 or possibly core 8 glycans. Thr-307 and Ser-314 are
minor glycosylation sites compared to Ser-308.
{ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23234360}.
-!- PTM: Glycated in plasma VLDL of normal subjects, and of
hyperglycemic diabetic patients at a higher level (2-3 fold).
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- POLYMORPHISM: Three common APOE alleles have been identified:
APOE*2, APOE*3, and APOE*4. The corresponding three major
isoforms, E2, E3, and E4, are recognized according to their
relative position after isoelectric focusing. Different mutations
causing the same migration pattern after isoelectric focusing
define different isoform subtypes. The most common isoform is E3
and is present in 40-90% of the population. Common APOE variants
influence lipoprotein metabolism in healthy individuals.
{ECO:0000305}.
-!- DISEASE: Hyperlipoproteinemia 3 (HLPP3) [MIM:617347]: A disorder
characterized by the accumulation of intermediate-density
lipoprotein particles (IDL or broad-beta-lipoprotein) rich in
cholesterol. Clinical features include xanthomas, yellowish lipid
deposits in the palmar crease, or less specific on tendons and on
elbows. The disorder rarely manifests before the third decade in
men. In women, it is usually expressed only after the menopause.
{ECO:0000269|PubMed:1674745, ECO:0000269|PubMed:22481068,
ECO:0000269|PubMed:2556398, ECO:0000269|PubMed:8287539}. Note=The
disease is caused by mutations affecting the gene represented in
this entry. The vast majority of the patients are homozygous for
APOE*2 alleles. More severe cases of HLPP3 have also been observed
in individuals heterozygous for rare APOE variants. The influence
of APOE on lipid levels is often suggested to have major
implications for the risk of coronary artery disease (CAD).
Individuals carrying the common APOE*4 variant are at higher risk
of CAD.
-!- DISEASE: Alzheimer disease 2 (AD2) [MIM:104310]: A late-onset form
of Alzheimer disease. Alzheimer disease is a neurodegenerative
disorder characterized by progressive dementia, loss of cognitive
abilities, and deposition of fibrillar amyloid proteins as
intraneuronal neurofibrillary tangles, extracellular amyloid
plaques and vascular amyloid deposits. The major constituents of
these plaques are neurotoxic amyloid-beta protein 40 and amyloid-
beta protein 42, that are produced by the proteolysis of the
transmembrane APP protein. The cytotoxic C-terminal fragments
(CTFs) and the caspase-cleaved products, such as C31, are also
implicated in neuronal death. {ECO:0000269|PubMed:8346443}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry. The APOE*4 allele
(APOE form E4) is genetically associated with the common late
onset familial and sporadic forms of Alzheimer disease. Risk for
AD increased from 20% to 90% and mean age at onset decreased from
84 to 68 years with increasing number of APOE*4 alleles in 42
families with late onset AD. Thus APOE*4 gene dose is a major risk
factor for late onset AD and, in these families, homozygosity for
APOE*4 was virtually sufficient to cause AD by age 80. The
mechanism by which APOE*4 participates in pathogenesis is not
known. {ECO:0000269|PubMed:8346443}.
-!- DISEASE: Sea-blue histiocyte disease (SBHD) [MIM:269600]:
Characterized by splenomegaly, mild thrombocytopenia and, in the
bone marrow, numerous histiocytes containing cytoplasmic granules
which stain bright blue with the usual hematologic stains. The
syndrome is the consequence of an inherited metabolic defect
analogous to Gaucher disease and other sphingolipidoses.
{ECO:0000269|PubMed:11095479, ECO:0000269|PubMed:16094309}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Lipoprotein glomerulopathy (LPG) [MIM:611771]: Uncommon
kidney disease characterized by proteinuria, progressive kidney
failure, and distinctive lipoprotein thrombi in glomerular
capillaries. {ECO:0000269|PubMed:10432380,
ECO:0000269|PubMed:18077821, ECO:0000269|PubMed:9176854}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Familial hypercholesterolemia (FH) [MIM:143890]: Common
autosomal semi-dominant disease that affects about 1 in 500
individuals. The receptor defect impairs the catabolism of LDL,
and the resultant elevation in plasma LDL-cholesterol promotes
deposition of cholesterol in the skin (xanthelasma), tendons
(xanthomas), and coronary arteries (atherosclerosis).
{ECO:0000269|PubMed:22949395, ECO:0000269|PubMed:24267230,
ECO:0000269|PubMed:26802169}. Note=The disease may be caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=APOE";
-!- WEB RESOURCE: Name=Wikipedia; Note=Apolipoprotein E entry;
URL="https://en.wikipedia.org/wiki/Apolipoprotein_E";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Tangled - Issue 83 of
June 2007;
URL="https://web.expasy.org/spotlight/back_issues/083";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M12529; AAB59518.1; -; mRNA.
EMBL; K00396; AAB59546.1; -; mRNA.
EMBL; M10065; AAB59397.1; -; Genomic_DNA.
EMBL; AF050154; AAD02505.1; -; Genomic_DNA.
EMBL; AF261279; AAG27089.1; -; Genomic_DNA.
EMBL; AK314898; BAG37412.1; -; mRNA.
EMBL; FJ525876; ACN81314.1; -; Genomic_DNA.
EMBL; BC003557; AAH03557.1; -; mRNA.
EMBL; AB035149; BAA96080.1; -; Genomic_DNA.
CCDS; CCDS12647.1; -.
PIR; A92478; LPHUE.
RefSeq; NP_000032.1; NM_000041.3.
RefSeq; NP_001289617.1; NM_001302688.1.
RefSeq; NP_001289618.1; NM_001302689.1.
RefSeq; NP_001289619.1; NM_001302690.1.
RefSeq; NP_001289620.1; NM_001302691.1.
UniGene; Hs.654439; -.
PDB; 1B68; X-ray; 2.00 A; A=19-209.
PDB; 1BZ4; X-ray; 1.85 A; A=40-183.
PDB; 1EA8; X-ray; 1.95 A; A=19-209.
PDB; 1GS9; X-ray; 1.70 A; A=19-183.
PDB; 1H7I; X-ray; 1.90 A; A=19-209.
PDB; 1LE2; X-ray; 3.00 A; A=41-184.
PDB; 1LE4; X-ray; 2.50 A; A=41-184.
PDB; 1LPE; X-ray; 2.25 A; A=41-184.
PDB; 1NFN; X-ray; 1.80 A; A=19-209.
PDB; 1NFO; X-ray; 2.00 A; A=19-209.
PDB; 1OEF; NMR; -; A=281-304.
PDB; 1OEG; NMR; -; A=285-307.
PDB; 1OR2; X-ray; 2.50 A; A=19-183.
PDB; 1OR3; X-ray; 1.73 A; A=19-183.
PDB; 2KC3; NMR; -; A=19-201.
PDB; 2KNY; NMR; -; A=147-167.
PDB; 2L7B; NMR; -; A=19-317.
PDBsum; 1B68; -.
PDBsum; 1BZ4; -.
PDBsum; 1EA8; -.
PDBsum; 1GS9; -.
PDBsum; 1H7I; -.
PDBsum; 1LE2; -.
PDBsum; 1LE4; -.
PDBsum; 1LPE; -.
PDBsum; 1NFN; -.
PDBsum; 1NFO; -.
PDBsum; 1OEF; -.
PDBsum; 1OEG; -.
PDBsum; 1OR2; -.
PDBsum; 1OR3; -.
PDBsum; 2KC3; -.
PDBsum; 2KNY; -.
PDBsum; 2L7B; -.
ProteinModelPortal; P02649; -.
SMR; P02649; -.
BioGrid; 106845; 63.
DIP; DIP-1120N; -.
IntAct; P02649; 33.
MINT; MINT-4999641; -.
STRING; 9606.ENSP00000252486; -.
DrugBank; DB00062; Human Serum Albumin.
DrugBank; DB00064; Serum albumin iodonated.
iPTMnet; P02649; -.
PhosphoSitePlus; P02649; -.
SwissPalm; P02649; -.
UniCarbKB; P02649; -.
BioMuta; APOE; -.
DMDM; 114039; -.
DOSAC-COBS-2DPAGE; P02649; -.
SWISS-2DPAGE; P02649; -.
EPD; P02649; -.
MaxQB; P02649; -.
PaxDb; P02649; -.
PeptideAtlas; P02649; -.
PRIDE; P02649; -.
DNASU; 348; -.
Ensembl; ENST00000252486; ENSP00000252486; ENSG00000130203.
GeneID; 348; -.
KEGG; hsa:348; -.
UCSC; uc002pab.4; human.
CTD; 348; -.
DisGeNET; 348; -.
EuPathDB; HostDB:ENSG00000130203.9; -.
GeneCards; APOE; -.
HGNC; HGNC:613; APOE.
HPA; CAB008363; -.
HPA; CAB069921; -.
HPA; HPA065539; -.
HPA; HPA068768; -.
MalaCards; APOE; -.
MIM; 104310; phenotype.
MIM; 107741; gene.
MIM; 143890; phenotype.
MIM; 269600; phenotype.
MIM; 611771; phenotype.
MIM; 617347; phenotype.
neXtProt; NX_P02649; -.
OpenTargets; ENSG00000130203; -.
Orphanet; 238616; Alzheimer disease.
Orphanet; 1648; Dementia with Lewy body.
Orphanet; 406; Heterozygous familial hypercholesterolemia.
Orphanet; 412; Hyperlipoproteinemia type 3.
Orphanet; 329481; Lipoprotein glomerulopathy.
Orphanet; 158029; Sea-blue histiocytosis.
PharmGKB; PA55; -.
eggNOG; ENOG410IVK0; Eukaryota.
eggNOG; ENOG4111MYC; LUCA.
GeneTree; ENSGT00730000111315; -.
HOGENOM; HOG000034006; -.
HOVERGEN; HBG010582; -.
InParanoid; P02649; -.
KO; K04524; -.
OMA; MGSRTRD; -.
OrthoDB; EOG091G0IA5; -.
PhylomeDB; P02649; -.
TreeFam; TF334458; -.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8864260; Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-8963888; Chylomicron assembly.
Reactome; R-HSA-8963901; Chylomicron remodeling.
Reactome; R-HSA-8964026; Chylomicron clearance.
Reactome; R-HSA-8964058; HDL remodeling.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SIGNOR; P02649; -.
ChiTaRS; APOE; human.
EvolutionaryTrace; P02649; -.
GeneWiki; Apolipoprotein_E; -.
GenomeRNAi; 348; -.
PMAP-CutDB; P02649; -.
PRO; PR:P02649; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130203; -.
CleanEx; HS_APOE; -.
ExpressionAtlas; P02649; baseline and differential.
Genevisible; P02649; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0042627; C:chylomicron; IDA:BHF-UCL.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0030425; C:dendrite; NAS:BHF-UCL.
GO; GO:0034365; C:discoidal high-density lipoprotein particle; TAS:ARUK-UCL.
GO; GO:0005769; C:early endosome; TAS:Reactome.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:ARUK-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:AgBase.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:1990777; C:lipoprotein particle; IDA:ARUK-UCL.
GO; GO:0034362; C:low-density lipoprotein particle; IDA:ARUK-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; NAS:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0001540; F:amyloid-beta binding; IDA:UniProtKB.
GO; GO:0016209; F:antioxidant activity; IDA:BHF-UCL.
GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
GO; GO:0017127; F:cholesterol transporter activity; IBA:GO_Central.
GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL.
GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
GO; GO:0005319; F:lipid transporter activity; IDA:BHF-UCL.
GO; GO:0071813; F:lipoprotein particle binding; IEA:Ensembl.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:BHF-UCL.
GO; GO:0046911; F:metal chelating activity; IDA:BHF-UCL.
GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IDA:BHF-UCL.
GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
GO; GO:0046983; F:protein dimerization activity; IDA:ARUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
GO; GO:0005198; F:structural molecule activity; TAS:ARUK-UCL.
GO; GO:0048156; F:tau protein binding; IPI:BHF-UCL.
GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; IDA:BHF-UCL.
GO; GO:0097113; P:AMPA glutamate receptor clustering; IDA:Alzheimers_University_of_Toronto.
GO; GO:0042982; P:amyloid precursor protein metabolic process; IDA:UniProtKB.
GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0019934; P:cGMP-mediated signaling; IDA:BHF-UCL.
GO; GO:0006707; P:cholesterol catabolic process; IBA:GO_Central.
GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
GO; GO:0034378; P:chylomicron assembly; TAS:Reactome.
GO; GO:0034382; P:chylomicron remnant clearance; IMP:BHF-UCL.
GO; GO:0034371; P:chylomicron remodeling; TAS:Reactome.
GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
GO; GO:0055089; P:fatty acid homeostasis; IDA:Alzheimers_University_of_Toronto.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IDA:BHF-UCL.
GO; GO:0034384; P:high-density lipoprotein particle clearance; IDA:BHF-UCL.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IGI:BHF-UCL.
GO; GO:0046907; P:intracellular transport; TAS:UniProtKB.
GO; GO:0010877; P:lipid transport involved in lipid storage; ISS:BHF-UCL.
GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
GO; GO:0042159; P:lipoprotein catabolic process; IBA:GO_Central.
GO; GO:0035641; P:locomotory exploration behavior; IMP:ARUK-UCL.
GO; GO:0015909; P:long-chain fatty acid transport; IDA:Alzheimers_University_of_Toronto.
GO; GO:0007616; P:long-term memory; IGI:ARUK-UCL.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; IEA:Ensembl.
GO; GO:0051651; P:maintenance of location in cell; IEA:Ensembl.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IDA:Alzheimers_University_of_Toronto.
GO; GO:0030195; P:negative regulation of blood coagulation; IDA:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:ARUK-UCL.
GO; GO:0032269; P:negative regulation of cellular protein metabolic process; IGI:ARUK-UCL.
GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IDA:BHF-UCL.
GO; GO:0090370; P:negative regulation of cholesterol efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:0061000; P:negative regulation of dendritic spine development; IDA:Alzheimers_University_of_Toronto.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IDA:Alzheimers_University_of_Toronto.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:BHF-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; IDA:Alzheimers_University_of_Toronto.
GO; GO:1903001; P:negative regulation of lipid transport across blood brain barrier; IDA:Alzheimers_University_of_Toronto.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IDA:ARUK-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IBA:GO_Central.
GO; GO:1901215; P:negative regulation of neuron death; IDA:Alzheimers_University_of_Toronto.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:ARUK-UCL.
GO; GO:1902999; P:negative regulation of phospholipid efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:0010544; P:negative regulation of platelet activation; IDA:BHF-UCL.
GO; GO:1901627; P:negative regulation of postsynaptic membrane organization; IDA:Alzheimers_University_of_Toronto.
GO; GO:1901630; P:negative regulation of presynaptic membrane organization; IDA:Alzheimers_University_of_Toronto.
GO; GO:0090209; P:negative regulation of triglyceride metabolic process; IEA:Ensembl.
GO; GO:0031102; P:neuron projection regeneration; IBA:GO_Central.
GO; GO:0007263; P:nitric oxide mediated signal transduction; IDA:BHF-UCL.
GO; GO:0097114; P:NMDA glutamate receptor clustering; IDA:Alzheimers_University_of_Toronto.
GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
GO; GO:0044794; P:positive regulation by host of viral process; IMP:AgBase.
GO; GO:1905908; P:positive regulation of amyloid fibril formation; TAS:ARUK-UCL.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IDA:Alzheimers_University_of_Toronto.
GO; GO:0030828; P:positive regulation of cGMP biosynthetic process; IDA:BHF-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:0010873; P:positive regulation of cholesterol esterification; IDA:BHF-UCL.
GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:Alzheimers_University_of_Toronto.
GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IDA:Alzheimers_University_of_Toronto.
GO; GO:0045807; P:positive regulation of endocytosis; IDA:ARUK-UCL.
GO; GO:1905855; P:positive regulation of heparan sulfate binding; IDA:ARUK-UCL.
GO; GO:1905860; P:positive regulation of heparan sulfate proteoglycan binding; IDA:ARUK-UCL.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IDA:Alzheimers_University_of_Toronto.
GO; GO:1903002; P:positive regulation of lipid transport across blood brain barrier; IDA:Alzheimers_University_of_Toronto.
GO; GO:0032805; P:positive regulation of low-density lipoprotein particle receptor catabolic process; IDA:BHF-UCL.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:1902998; P:positive regulation of neurofibrillary tangle assembly; IDA:Alzheimers_University_of_Toronto.
GO; GO:1901216; P:positive regulation of neuron death; IDA:Alzheimers_University_of_Toronto.
GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ARUK-UCL.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:1902995; P:positive regulation of phospholipid efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:1901628; P:positive regulation of postsynaptic membrane organization; IDA:Alzheimers_University_of_Toronto.
GO; GO:1901631; P:positive regulation of presynaptic membrane organization; IDA:Alzheimers_University_of_Toronto.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0017038; P:protein import; IDA:Alzheimers_University_of_Toronto.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:BHF-UCL.
GO; GO:1905906; P:regulation of amyloid fibril formation; IDA:ARUK-UCL.
GO; GO:1900221; P:regulation of amyloid-beta clearance; IDA:Alzheimers_University_of_Toronto.
GO; GO:0030516; P:regulation of axon extension; TAS:UniProtKB.
GO; GO:2000822; P:regulation of behavioral fear response; IMP:ARUK-UCL.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IDA:BHF-UCL.
GO; GO:1905890; P:regulation of cellular response to very-low-density lipoprotein particle stimulus; IDA:ARUK-UCL.
GO; GO:0090181; P:regulation of cholesterol metabolic process; IGI:ARUK-UCL.
GO; GO:1901214; P:regulation of neuron death; IDA:Alzheimers_University_of_Toronto.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; TAS:UniProtKB.
GO; GO:0032462; P:regulation of protein homooligomerization; IDA:ARUK-UCL.
GO; GO:0051246; P:regulation of protein metabolic process; IGI:ARUK-UCL.
GO; GO:1902947; P:regulation of tau-protein kinase activity; IDA:Alzheimers_University_of_Toronto.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0061771; P:response to caloric restriction; IGI:ARUK-UCL.
GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
GO; GO:0000302; P:response to reactive oxygen species; NAS:UniProtKB.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0043691; P:reverse cholesterol transport; IDA:BHF-UCL.
GO; GO:0007271; P:synaptic transmission, cholinergic; TAS:UniProtKB.
GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
GO; GO:0070328; P:triglyceride homeostasis; ISS:BHF-UCL.
GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL.
GO; GO:0042311; P:vasodilation; IEA:Ensembl.
GO; GO:0034447; P:very-low-density lipoprotein particle clearance; IDA:BHF-UCL.
GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
GO; GO:0019068; P:virion assembly; IMP:AgBase.
InterPro; IPR000074; ApoA_E.
Pfam; PF01442; Apolipoprotein; 1.
1: Evidence at protein level;
3D-structure; Alzheimer disease; Amyloidosis; Cholesterol metabolism;
Chylomicron; Complete proteome; Direct protein sequencing;
Disease mutation; Glycation; Glycoprotein; HDL; Heparin-binding;
Hyperlipidemia; Lipid metabolism; Lipid transport; Neurodegeneration;
Oxidation; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Secreted; Signal; Steroid metabolism; Sterol metabolism; Transport;
VLDL.
SIGNAL 1 18 {ECO:0000269|PubMed:7068630}.
CHAIN 19 317 Apolipoprotein E.
/FTId=PRO_0000001987.
REPEAT 80 101 1.
REPEAT 102 123 2.
REPEAT 124 145 3.
REPEAT 146 167 4.
REPEAT 168 189 5.
REPEAT 190 211 6.
REPEAT 212 233 7.
REPEAT 234 255 8.
REGION 80 255 8 X 22 AA approximate tandem repeats.
REGION 158 168 LDL receptor binding.
{ECO:0000269|PubMed:2063194}.
REGION 162 165 Heparin-binding.
{ECO:0000269|PubMed:3947350}.
REGION 229 236 Heparin-binding.
{ECO:0000269|PubMed:3947350}.
MOD_RES 143 143 Methionine sulfoxide.
{ECO:0000250|UniProtKB:P08226}.
MOD_RES 147 147 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
CARBOHYD 26 26 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:23234360}.
CARBOHYD 36 36 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:23234360}.
CARBOHYD 93 93 N-linked (Glc) (glycation) lysine.
CARBOHYD 212 212 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19838169}.
CARBOHYD 307 307 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19838169}.
CARBOHYD 308 308 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:19838169}.
CARBOHYD 314 314 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:23234360}.
VARIANT 21 21 E -> K (in form E5; associated with
hyperlipoproteinemia and atherosclerosis;
dbSNP:rs121918392).
{ECO:0000269|PubMed:2760009}.
/FTId=VAR_000645.
VARIANT 31 31 E -> K (in HLPP3; form E4 Philadelphia
and form E5-type; only form E4
Philadelphia is associated with HLPP3;
dbSNP:rs201672011).
{ECO:0000269|PubMed:1674745}.
/FTId=VAR_000646.
VARIANT 43 43 R -> C (in LPG; form E2 Kyoto;
dbSNP:rs121918399).
{ECO:0000269|PubMed:10432380,
ECO:0000269|PubMed:18077821}.
/FTId=VAR_042734.
VARIANT 46 46 L -> P (in FH; unknown pathological
significance; form E4 Freiburg;
dbSNP:rs769452).
{ECO:0000269|PubMed:11042151,
ECO:0000269|PubMed:26802169}.
/FTId=VAR_000647.
VARIANT 60 60 T -> A (in form E3 Freiburg;
dbSNP:rs28931576).
/FTId=VAR_000648.
VARIANT 64 64 Q -> H (polymorphism; confirmed at
protein level; dbSNP:rs370594287).
{ECO:0000269|PubMed:22028381,
ECO:0000269|Ref.10}.
/FTId=VAR_014114.
VARIANT 99 99 Q -> K (in form E5 Frankfurt).
/FTId=VAR_000649.
VARIANT 102 102 P -> R (in form E5-type; no
hyperlipidemia; dbSNP:rs28931578).
/FTId=VAR_000650.
VARIANT 117 117 A -> T (in form E3*; dbSNP:rs28931577).
/FTId=VAR_000651.
VARIANT 124 124 A -> V (in form E3 Basel).
{ECO:0000269|PubMed:12864777}.
/FTId=VAR_016789.
VARIANT 130 130 C -> R (in HLPP3 and AD2; form E3**, form
E4, form E4/3 and some forms E5-type;
form E3** is associated with HLPP3; form
E4 is associated with AD2;
dbSNP:rs429358).
{ECO:0000269|PubMed:11042151,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:8287539,
ECO:0000269|PubMed:8346443,
ECO:0000269|PubMed:9360638}.
/FTId=VAR_000652.
VARIANT 145 145 G -> D (in FH; unknown pathological
significance; form E1 Weisgraber;
dbSNP:rs267606664).
{ECO:0000269|PubMed:26802169,
ECO:0000269|PubMed:8287539}.
/FTId=VAR_000653.
VARIANT 145 145 G -> GEVQAMLG (in HLPP3; form E3 Leiden).
{ECO:0000269|PubMed:2556398}.
/FTId=VAR_000654.
VARIANT 152 152 R -> Q (in form E2-type; no
hyperlipidemia; dbSNP:rs28931578).
/FTId=VAR_000655.
VARIANT 154 154 R -> C (in HLPP3; form E2-type;
dbSNP:rs121918393).
/FTId=VAR_000657.
VARIANT 154 154 R -> S (in HLPP3; form E2 Christchurch;
dbSNP:rs121918393).
{ECO:0000269|PubMed:22481068,
ECO:0000269|PubMed:8287539}.
/FTId=VAR_000656.
VARIANT 160 160 R -> C (in HLPP3; form E3**;
dbSNP:rs387906567).
{ECO:0000269|PubMed:8287539}.
/FTId=VAR_000658.
VARIANT 163 163 R -> C (in HLPP3 and FH; form E4
Philadelphia and form E2-type;
dbSNP:rs769455).
{ECO:0000269|PubMed:11042151,
ECO:0000269|PubMed:1674745,
ECO:0000269|PubMed:26802169}.
/FTId=VAR_000659.
VARIANT 163 163 R -> H (in E3 Kochi; dbSNP:rs121918397).
/FTId=VAR_000660.
VARIANT 163 163 R -> P (in LPG; form E2 Sendai;
dbSNP:rs121918397).
{ECO:0000269|PubMed:9176854}.
/FTId=VAR_042735.
VARIANT 164 164 K -> E (in HLPP3; form E1 Harrisburg;
dbSNP:rs121918394).
/FTId=VAR_000662.
VARIANT 164 164 K -> Q (in HLPP3; form E2**;
dbSNP:rs121918394).
/FTId=VAR_000661.
VARIANT 167 167 Missing (in SBHD and FH; also found in
patients with a diagnosis of familial
combined hyperlipidemia).
{ECO:0000269|PubMed:11095479,
ECO:0000269|PubMed:16094309,
ECO:0000269|PubMed:22481068,
ECO:0000269|PubMed:22949395,
ECO:0000269|PubMed:24267230,
ECO:0000269|PubMed:26802169}.
/FTId=VAR_035015.
VARIANT 170 170 A -> P (in form E3*; dbSNP:rs267606662).
/FTId=VAR_000663.
VARIANT 176 176 R -> C (in HLPP3; forms E1 Weisgraber,
form E2 and form E3**; form E3** is
associated with HLPP; dbSNP:rs7412).
{ECO:0000269|PubMed:11042151,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:8287539}.
/FTId=VAR_000664.
VARIANT 242 242 R -> Q (in form E2 Fukuoka;
dbSNP:rs267606663).
/FTId=VAR_000665.
VARIANT 246 246 R -> C (in form E2 Dunedin;
dbSNP:rs121918395).
/FTId=VAR_000666.
VARIANT 254 254 V -> E (in form E2 WG;
dbSNP:rs199768005).
{ECO:0000269|PubMed:8488843}.
/FTId=VAR_000667.
VARIANT 262 263 EE -> KK (in HLPP3; form E7 Suita).
/FTId=VAR_000668.
VARIANT 269 269 R -> G (in form E3 HB and form E4/3;
dbSNP:rs267606661).
{ECO:0000269|PubMed:8488843,
ECO:0000269|PubMed:9360638}.
/FTId=VAR_000669.
VARIANT 270 270 L -> E (in form E1 HE; requires 2
nucleotide substitutions).
{ECO:0000269|PubMed:8488843}.
/FTId=VAR_000670.
VARIANT 292 292 R -> H (in form E4 PD;
dbSNP:rs121918398).
{ECO:0000269|PubMed:8488843}.
/FTId=VAR_000671.
VARIANT 314 314 S -> R (in form E4 HG; dbSNP:rs28931579).
{ECO:0000269|PubMed:8488843}.
/FTId=VAR_000672.
STRAND 22 24 {ECO:0000244|PDB:2KC3}.
HELIX 31 39 {ECO:0000244|PDB:2KC3}.
TURN 40 42 {ECO:0000244|PDB:2KC3}.
HELIX 43 60 {ECO:0000244|PDB:1GS9}.
HELIX 63 70 {ECO:0000244|PDB:1GS9}.
HELIX 73 96 {ECO:0000244|PDB:1GS9}.
TURN 97 99 {ECO:0000244|PDB:1LE4}.
HELIX 106 141 {ECO:0000244|PDB:1GS9}.
TURN 143 145 {ECO:0000244|PDB:1NFN}.
HELIX 149 179 {ECO:0000244|PDB:1GS9}.
TURN 180 182 {ECO:0000244|PDB:1BZ4}.
TURN 187 190 {ECO:0000244|PDB:2KC3}.
HELIX 193 198 {ECO:0000244|PDB:2KC3}.
STRAND 200 202 {ECO:0000244|PDB:2L7B}.
HELIX 209 217 {ECO:0000244|PDB:2L7B}.
HELIX 228 241 {ECO:0000244|PDB:2L7B}.
HELIX 257 283 {ECO:0000244|PDB:2L7B}.
HELIX 286 303 {ECO:0000244|PDB:1OEF}.
STRAND 307 309 {ECO:0000244|PDB:2L7B}.
SEQUENCE 317 AA; 36154 MW; 91AFC04210A30689 CRC64;
MKVLWAALLV TFLAGCQAKV EQAVETEPEP ELRQQTEWQS GQRWELALGR FWDYLRWVQT
LSEQVQEELL SSQVTQELRA LMDETMKELK AYKSELEEQL TPVAEETRAR LSKELQAAQA
RLGADMEDVC GRLVQYRGEV QAMLGQSTEE LRVRLASHLR KLRKRLLRDA DDLQKRLAVY
QAGAREGAER GLSAIRERLG PLVEQGRVRA ATVGSLAGQP LQERAQAWGE RLRARMEEMG
SRTRDRLDEV KEQVAEVRAK LEEQAQQIRL QAEAFQARLK SWFEPLVEDM QRQWAGLVEK
VQAAVGTSAA PVPSDNH


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