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P02649 (APOE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 191. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein E

Short name=Apo-E
Gene names
Name:APOE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subcellular location

Secreted.

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.

Post-translational modification

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 Thr-314 are minor glycosylation siteS compared to Ser-308. Ref.20

Glycated in plasma VLDL of normal subjects, and of hyperglycemic diabetic patients at a higher level (2-3 fold).

Phosphorylation sites are present in the extracellular medium.

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 isE3 and is present in 40-90% of the population. Common APOE variants influence lipoprotein metabolism in healthy individuals.

Involvement in disease

Hyperlipoproteinemia 3 (HLPP3) [MIM:107741]: 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.
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. Ref.16 Ref.26 Ref.27 Ref.29 Ref.39

Alzheimer disease 2 (AD2) [MIM:104310]: A late-onset 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 constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. The APOE*4 allele 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. Ref.16

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.33 Ref.36

Lipoprotein glomerulopathy (LPG) [MIM:611771]: Uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.30 Ref.32 Ref.37

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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.40

Sequence similarities

Belongs to the apolipoprotein A1/A4/E family.

Ontologies

Keywords
   Biological processCholesterol metabolism
Lipid metabolism
Lipid transport
Steroid metabolism
Sterol metabolism
Transport
   Cellular componentChylomicron
HDL
Secreted
VLDL
   Coding sequence diversityPolymorphism
   DiseaseAlzheimer disease
Amyloidosis
Disease mutation
Hyperlipidemia
Neurodegeneration
   DomainRepeat
Signal
   LigandHeparin-binding
   PTMGlycation
Glycoprotein
Oxidation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 16443932. Source: BHF-UCL

N-methyl-D-aspartate receptor clustering

Inferred from direct assay PubMed 24328732. Source: Alzheimers_University_of_Toronto

aging

Inferred from electronic annotation. Source: Ensembl

alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering

Inferred from direct assay PubMed 24328732. Source: Alzheimers_University_of_Toronto

artery morphogenesis

Inferred from electronic annotation. Source: Ensembl

cGMP-mediated signaling

Inferred from direct assay PubMed 8995232. Source: BHF-UCL

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to cholesterol

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cholesterol catabolic process

Inferred from electronic annotation. Source: Ensembl

cholesterol efflux

Inferred from direct assay PubMed 11162594PubMed 16443932. Source: BHF-UCL

cholesterol homeostasis

Inferred from direct assay PubMed 9649566. Source: BHF-UCL

cholesterol metabolic process

Inferred from direct assay PubMed 9649566. Source: BHF-UCL

chylomicron remnant clearance

Inferred from mutant phenotype PubMed 7175379. Source: BHF-UCL

cytoskeleton organization

Traceable author statement PubMed 9622609. Source: UniProtKB

fatty acid homeostasis

Inferred from direct assay PubMed 24345162. Source: Alzheimers_University_of_Toronto

high-density lipoprotein particle assembly

Inferred from direct assay PubMed 17305370. Source: BHF-UCL

high-density lipoprotein particle clearance

Inferred from direct assay PubMed 210175. Source: BHF-UCL

high-density lipoprotein particle remodeling

Inferred from genetic interaction PubMed 12401887. Source: BHF-UCL

intracellular transport

Traceable author statement PubMed 9622609. Source: UniProtKB

lipoprotein biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein catabolic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein metabolic process

Traceable author statement. Source: Reactome

long-chain fatty acid transport

Inferred from direct assay PubMed 24345162. Source: Alzheimers_University_of_Toronto

low-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

maintenance of location in cell

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAP kinase activity

Inferred from direct assay PubMed 9685360. Source: BHF-UCL

negative regulation of beta-amyloid formation

Inferred from direct assay PubMed 24154541PubMed 24259049. Source: Alzheimers_University_of_Toronto

negative regulation of blood coagulation

Inferred from direct assay PubMed 8995232. Source: BHF-UCL

negative regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 9685360. Source: BHF-UCL

negative regulation of cholesterol biosynthetic process

Inferred from direct assay PubMed 1917954. Source: BHF-UCL

negative regulation of cholesterol efflux

Inferred from direct assay PubMed 12042316. Source: Alzheimers_University_of_Toronto

negative regulation of dendritic spine development

Inferred from direct assay PubMed 24328732. Source: Alzheimers_University_of_Toronto

negative regulation of dendritic spine maintenance

Inferred from direct assay PubMed 24328732. Source: Alzheimers_University_of_Toronto

negative regulation of endothelial cell proliferation

Inferred from direct assay PubMed 9685360. Source: BHF-UCL

negative regulation of inflammatory response

Inferred by curator PubMed 8995232. Source: BHF-UCL

negative regulation of lipid biosynthetic process

Inferred from direct assay PubMed 12042316. Source: Alzheimers_University_of_Toronto

negative regulation of lipid transport across blood brain barrier

Inferred from direct assay PubMed 24345162. Source: Alzheimers_University_of_Toronto

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron death

Inferred from direct assay PubMed 24259049. Source: Alzheimers_University_of_Toronto

negative regulation of phospholipid efflux

Inferred from direct assay PubMed 12042316. Source: Alzheimers_University_of_Toronto

negative regulation of platelet activation

Inferred from direct assay PubMed 8995232. Source: BHF-UCL

negative regulation of postsynaptic membrane organization

Inferred from direct assay PubMed 24259049. Source: Alzheimers_University_of_Toronto

negative regulation of presynaptic membrane organization

Inferred from direct assay PubMed 24259049. Source: Alzheimers_University_of_Toronto

nitric oxide mediated signal transduction

Inferred from direct assay PubMed 8995232. Source: BHF-UCL

oligodendrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

peripheral nervous system axon regeneration

Inferred from electronic annotation. Source: Ensembl

phospholipid efflux

Inferred from direct assay PubMed 11162594. Source: BHF-UCL

phototransduction, visible light

Traceable author statement. Source: Reactome

positive regulation of axon extension

Inferred from electronic annotation. Source: Ensembl

positive regulation of beta-amyloid formation

Inferred from direct assay PubMed 24154541PubMed 24259049. Source: Alzheimers_University_of_Toronto

positive regulation of cGMP biosynthetic process

Inferred from direct assay PubMed 8995232. Source: BHF-UCL

positive regulation of cholesterol efflux

Inferred from direct assay PubMed 12042316. Source: Alzheimers_University_of_Toronto

positive regulation of cholesterol esterification

Inferred from direct assay PubMed 15654758. Source: BHF-UCL

positive regulation of dendritic spine development

Inferred from direct assay PubMed 24328732. Source: Alzheimers_University_of_Toronto

positive regulation of dendritic spine maintenance

Inferred from direct assay PubMed 24328732. Source: Alzheimers_University_of_Toronto

positive regulation of lipid biosynthetic process

Inferred from direct assay PubMed 12042316. Source: Alzheimers_University_of_Toronto

positive regulation of lipid transport across blood brain barrier

Inferred from direct assay PubMed 24345162. Source: Alzheimers_University_of_Toronto

positive regulation of low-density lipoprotein particle receptor catabolic process

Inferred from direct assay PubMed 15950758. Source: BHF-UCL

positive regulation of membrane protein ectodomain proteolysis

Inferred from direct assay PubMed 15950758. Source: BHF-UCL

positive regulation of neurofibrillary tangle assembly

Inferred from direct assay PubMed 24154541. Source: Alzheimers_University_of_Toronto

positive regulation of neuron death

Inferred from direct assay PubMed 24259049. Source: Alzheimers_University_of_Toronto

positive regulation of nitric-oxide synthase activity

Inferred from direct assay PubMed 8995232. Source: BHF-UCL

positive regulation of phospholipid efflux

Inferred from direct assay PubMed 12042316. Source: Alzheimers_University_of_Toronto

positive regulation of postsynaptic membrane organization

Inferred from direct assay PubMed 24259049. Source: Alzheimers_University_of_Toronto

positive regulation of presynaptic membrane organization

Inferred from direct assay PubMed 24259049. Source: Alzheimers_University_of_Toronto

protein import

Inferred from direct assay PubMed 24446231. Source: Alzheimers_University_of_Toronto

receptor-mediated endocytosis

Inferred from direct assay PubMed 1917954. Source: BHF-UCL

regulation of Cdc42 protein signal transduction

Inferred from direct assay PubMed 16443932. Source: BHF-UCL

regulation of axon extension

Traceable author statement PubMed 9622609. Source: UniProtKB

regulation of beta-amyloid clearance

Inferred from direct assay PubMed 24446231. Source: Alzheimers_University_of_Toronto

regulation of neuron death

Inferred from direct assay PubMed 24154541. Source: Alzheimers_University_of_Toronto

regulation of neuronal synaptic plasticity

Traceable author statement PubMed 9622609. Source: UniProtKB

regulation of tau-protein kinase activity

Inferred from direct assay PubMed 24154541. Source: Alzheimers_University_of_Toronto

response to dietary excess

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to reactive oxygen species

Non-traceable author statement PubMed 11743999. Source: UniProtKB

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Traceable author statement. Source: Reactome

reverse cholesterol transport

Inferred from direct assay PubMed 8127890. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission, cholinergic

Traceable author statement PubMed 9622609. Source: UniProtKB

triglyceride metabolic process

Inferred from direct assay PubMed 9649566. Source: BHF-UCL

vasodilation

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle clearance

Inferred from direct assay PubMed 1917954. Source: BHF-UCL

very-low-density lipoprotein particle remodeling

Inferred from direct assay PubMed 15654758. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

chylomicron

Inferred from direct assay PubMed 16935699PubMed 8245722. Source: BHF-UCL

cytoplasm

Traceable author statement PubMed 9622609. Source: UniProtKB

dendrite

Non-traceable author statement PubMed 8083695. Source: BHF-UCL

early endosome

Traceable author statement. Source: Reactome

endocytic vesicle lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

extrinsic component of external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle

Inferred from direct assay PubMed 210174. Source: BHF-UCL

intermediate-density lipoprotein particle

Inferred from direct assay PubMed 17336988. Source: BHF-UCL

late endosome

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein particle

Inferred from direct assay PubMed 8245722. Source: BHF-UCL

neuronal cell body

Non-traceable author statement PubMed 8083695. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

plasma membrane

Traceable author statement. Source: Reactome

very-low-density lipoprotein particle

Inferred from direct assay PubMed 17154273PubMed 8245722. Source: BHF-UCL

   Molecular_functionantioxidant activity

Inferred from direct assay PubMed 9685360. Source: BHF-UCL

beta-amyloid binding

Inferred from direct assay PubMed 11305869. Source: UniProtKB

cholesterol transporter activity

Inferred from electronic annotation. Source: Ensembl

heparin binding

Inferred from direct assay PubMed 2745454. Source: BHF-UCL

hydroxyapatite binding

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from direct assay PubMed 4066713. Source: BHF-UCL

lipid binding

Inferred from direct assay PubMed 4066713. Source: UniProtKB

lipid transporter activity

Inferred from direct assay PubMed 17305370. Source: BHF-UCL

lipoprotein particle binding

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein particle receptor binding

Inferred from direct assay PubMed 210175. Source: BHF-UCL

metal chelating activity

Inferred from direct assay PubMed 9685360. Source: BHF-UCL

phosphatidylcholine-sterol O-acyltransferase activator activity

Inferred from direct assay PubMed 15654758. Source: BHF-UCL

phospholipid binding

Inferred from direct assay PubMed 4066713. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 7566652. Source: IntAct

protein homodimerization activity

Inferred from physical interaction PubMed 8245722. Source: BHF-UCL

tau protein binding

Inferred from physical interaction PubMed 7566652. Source: BHF-UCL

very-low-density lipoprotein particle receptor binding

Inferred from direct assay PubMed 1384047. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.13
Chain19 – 317299Apolipoprotein E
PRO_0000001987

Regions

Repeat80 – 101221
Repeat102 – 123222
Repeat124 – 145223
Repeat146 – 167224
Repeat168 – 189225
Repeat190 – 211226
Repeat212 – 233227
Repeat234 – 255228
Region80 – 2551768 X 22 AA approximate tandem repeats
Region158 – 16811LDL receptor binding Potential
Region162 – 1654Heparin-binding
Region229 – 2368Heparin-binding

Amino acid modifications

Modified residue1431Methionine sulfoxide By similarity
Glycosylation261O-linked (GalNAc...) Ref.20
Glycosylation361O-linked (GalNAc...) Ref.20
Glycosylation931N-linked (Glc) (glycation) Ref.17
Glycosylation2121O-linked (GalNAc...) Ref.18
Glycosylation3071O-linked (GalNAc...) Ref.18
Glycosylation3081O-linked (GalNAc...) Ref.18
Glycosylation3141O-linked (GalNAc...) Ref.20

Natural variations

Natural variant211E → K in form E5; associated with hyperlipoproteinemia and atherosclerosis. Ref.25
VAR_000645
Natural variant311E → K in HLPP3; form E4 Philadelphia and form E5-type; only form E4 Philadelphia is disease-linked. Ref.27
Corresponds to variant rs201672011 [ dbSNP | Ensembl ].
VAR_000646
Natural variant431R → C in LPG; form E2 Kyoto. Ref.32 Ref.37
VAR_042734
Natural variant461L → P in form E4 Freiburg. Ref.6
Corresponds to variant rs769452 [ dbSNP | Ensembl ].
VAR_000647
Natural variant601T → A in form E3 Freiburg.
Corresponds to variant rs28931576 [ dbSNP | Ensembl ].
VAR_000648
Natural variant641Q → H Polymorphism confirmed at protein level. Ref.10 Ref.38
VAR_014114
Natural variant991Q → K in form E5 Frankfurt.
VAR_000649
Natural variant1021P → R in form E5-type; no hyperlipidemia.
Corresponds to variant rs28931578 [ dbSNP | Ensembl ].
VAR_000650
Natural variant1171A → T in form E3*.
Corresponds to variant rs28931577 [ dbSNP | Ensembl ].
VAR_000651
Natural variant1241A → V in form E3 Basel. Ref.34
VAR_016789
Natural variant1301C → R in HLPP3; form E3**, form E4, form E4/3 and some forms E5-type; only form E3** is disease-linked. Ref.6 Ref.29 Ref.31 Ref.35
Corresponds to variant rs429358 [ dbSNP | Ensembl ].
VAR_000652
Natural variant1451G → D in form E1 Weisgraber. Ref.29
VAR_000653
Natural variant1451G → GEVQAMLG in HLPP3; form E3 Leiden.
VAR_000654
Natural variant1521R → Q in form E2-type; no hyperlipidemia.
Corresponds to variant rs28931578 [ dbSNP | Ensembl ].
VAR_000655
Natural variant1541R → C in HLPP3; form E2-type.
VAR_000657
Natural variant1541R → S in HLPP3; form E2 Christchurch. Ref.29 Ref.39
VAR_000656
Natural variant1601R → C in HLPP3; form E3**. Ref.29
VAR_000658
Natural variant1631R → C in HLPP3; form E4 Philadelphia and form E2-type; only form E4 Philadelphia is disease-linked. Ref.6 Ref.27
Corresponds to variant rs769455 [ dbSNP | Ensembl ].
VAR_000659
Natural variant1631R → H in E3 Kochi.
VAR_000660
Natural variant1631R → P in LPG; form E2 Sendai. Ref.30
VAR_042735
Natural variant1641K → E in HLPP3; form E1 Harrisburg.
VAR_000662
Natural variant1641K → Q in HLPP3; form E2**.
VAR_000661
Natural variant1671Missing in SBHD and FH; also found in patients with a diagnosis of familial combined hyperlipidemia. Ref.33 Ref.36 Ref.39 Ref.40
VAR_035015
Natural variant1701A → P in form E3*.
VAR_000663
Natural variant1761R → C in HLPP3; forms E1 Weisgraber, form E2 and form E3**. Ref.6 Ref.29 Ref.35
Corresponds to variant rs7412 [ dbSNP | Ensembl ].
VAR_000664
Natural variant2421R → Q in form E2 Fukuoka.
VAR_000665
Natural variant2461R → C in form E2 Dunedin.
VAR_000666
Natural variant2541V → E in form E2 W.G.. Ref.28
VAR_000667
Natural variant262 – 2632EE → KK in HLPP3; form E7 Suita.
VAR_000668
Natural variant2691R → G in form E3 H.B. and isoform E4/3. Ref.28 Ref.31
VAR_000669
Natural variant2701L → E in form E1 H.E.; requires 2 nucleotide substitutions. Ref.28
VAR_000670
Natural variant2921R → H in form E4 P.D.. Ref.28
VAR_000671
Natural variant3141S → R in form E4 H.G.. Ref.28
Corresponds to variant rs28931579 [ dbSNP | Ensembl ].
VAR_000672

Secondary structure

................................... 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02649 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 91AFC04210A30689

FASTA31736,154
        10         20         30         40         50         60 
MKVLWAALLV TFLAGCQAKV EQAVETEPEP ELRQQTEWQS GQRWELALGR FWDYLRWVQT 

        70         80         90        100        110        120 
LSEQVQEELL SSQVTQELRA LMDETMKELK AYKSELEEQL TPVAEETRAR LSKELQAAQA 

       130        140        150        160        170        180 
RLGADMEDVC GRLVQYRGEV QAMLGQSTEE LRVRLASHLR KLRKRLLRDA DDLQKRLAVY 

       190        200        210        220        230        240 
QAGAREGAER GLSAIRERLG PLVEQGRVRA ATVGSLAGQP LQERAQAWGE RLRARMEEMG 

       250        260        270        280        290        300 
SRTRDRLDEV KEQVAEVRAK LEEQAQQIRL QAEAFQARLK SWFEPLVEDM QRQWAGLVEK 

       310 
VQAAVGTSAA PVPSDNH 

« Hide

References

« Hide 'large scale' references
[1]"Synthesis, intracellular processing, and signal peptide of human apolipoprotein E."
Zannis V.I., McPherson J., Goldberger G., Karathanasis S.K., Breslow J.L.
J. Biol. Chem. 259:5495-5499(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT E3).
[2]"Human apolipoprotein E mRNA. cDNA cloning and nucleotide sequencing of a new variant."
McLean J.W., Elshourbagy N.A., Chang D.J., Mahley R.W., Taylor J.M.
J. Biol. Chem. 259:6498-6504(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT E3).
[3]"Nucleotide sequence and structure of the human apolipoprotein E gene."
Paik Y.-K., Chang D.J., Reardon C.A., Davies G.E., Mahley R.W., Taylor J.M.
Proc. Natl. Acad. Sci. U.S.A. 82:3445-3449(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANT E4).
[4]"Genotyping and sequence analysis of apolipoprotein E isoforms."
Emi M., Wu L.L., Robertson M.A., Myers R.L., Hegele R.A., Williams R.R., White R., Lalouel J.-M.
Genomics 3:373-379(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANT E2).
[5]"Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene: PEREC1."
Freitas E.M., Zhang W.J., Lalonde J.P., Tay G.K., Gaudieri S., Ashworth L.K., Van Bockxmeer F.M., Dawkins R.L.
DNA Seq. 9:89-100(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Sequence diversity and large-scale typing of SNPs in the human apolipoprotein E gene."
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.
Genome Res. 10:1532-1545(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-46; ARG-130; CYS-163 AND CYS-176.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[8]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[10]"A new apolipoprotein E variant (Gln46-->His)."
Imura T., Kimura H., Kawasaki M.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-78, VARIANT HIS-64.
Tissue: Blood.
[11]"Identification and DNA sequence of a human apolipoprotein E cDNA clone."
Breslow J.L., McPherson J., Nussbaum A.L., Williams H.W., Lofquist-Kahl F., Karathanasis S.K., Zannis V.I.
J. Biol. Chem. 257:14639-14641(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-317 (VARIANT E3).
[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]"Human apolipoprotein E. The complete amino acid sequence."
Rall S.C. Jr., Weisgraber K.H., Mahley R.W.
J. Biol. Chem. 257:4171-4178(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-317 (VARIANT E2).
[14]"Apolipoprotein E: cholesterol transport protein with expanding role in cell biology."
Mahley R.W.
Science 240:622-630(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[15]"Binding of a high reactive heparin to human apolipoprotein E: identification of two heparin-binding domains."
Cardin A.D., Hirose N., Blankenship D.T., Jackson R.L., Harmony J.A.K., Sparrow D.A., Sparrow J.T.
Biochem. Biophys. Res. Commun. 134:783-789(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: HEPARIN-BINDING SITES.
[16]"Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families."
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.
Science 261:921-923(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF APOE*4 WITH ALZHEIMER DISEASE.
[17]"Glycation of apolipoprotein E impairs its binding to heparin: identification of the major glycation site."
Shuvaev V.V., Fujii J., Kawasaki Y., Itoh H., Hamaoka R., Barbier A., Ziegler O., Siest G., Taniguchi N.
Biochim. Biophys. Acta 1454:296-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCATION AT LYS-93, IDENTIFICATION BY MASS SPECTROMETRY.
[18]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-212; THR-307 AND SER-308, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-26; THR-36 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY.
[21]"Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E."
Wilson C., Wardell M.R., Weisgraber K.H., Mahley R.W., Agard D.A.
Science 252:1817-1822(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 41-184.
[22]"Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia."
Dong L.-M., Parkin S., Trakhanov S.D., Rupp B., Simmons T., Arnold K.S., Newhouse Y.M., Innerarity T.L., Weisgraber K.H.
Nat. Struct. Biol. 3:718-722(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 41-181.
[23]"Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding."
Segelke B.W., Forstner M., Knapp M., Trakhanov S.D., Parkin S., Newhouse Y.M., Bellamy H.D., Weisgraber K.H., Rupp B.
Protein Sci. 9:886-897(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-165.
[24]"Genetic heterogeneity of apolipoprotein E and its influence on plasma lipid and lipoprotein levels."
de Knijff P., van den Maagdenberg A.M.J.M., Frants R.R., Havekes L.M.
Hum. Mutat. 4:178-194(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[25]"Molecular cloning of a human apolipoprotein E variant: E5 (Glu-3-->Lys)."
Maeda H., Nakamura H., Kobori S., Okada M., Niki H., Ogura T., Hiraga S.
J. Biochem. 105:491-493(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT E5 LYS-21.
[26]"Apolipoprotein E3-Leiden contains a seven-amino acid insertion that is a tandem repeat of residues 121-127."
Wardell M.R., Weisgraber K.H., Havekes L.M., Rall S.C. Jr.
J. Biol. Chem. 264:21205-21210(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP3 E3 LEIDEN GLU-VAL-GLN-ALA-MET-LEU-GLY-145 INS.
[27]"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."
Lohse P., Mann W.A., Stein E.A., Brewer H.B. Jr.
J. Biol. Chem. 266:10479-10484(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP3 E4 PHILADELPHIA LYS-31 AND CYS-163.
[28]"Characterization of five new mutants in the carboxyl-terminal domain of human apolipoprotein E: no cosegregation with severe hyperlipidemia."
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.
Am. J. Hum. Genet. 52:937-946(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLU-254; GLY-269; GLU-270; HIS-292 AND ARG-314.
[29]"Common and rare genotypes of human apolipoprotein E determined by specific restriction profiles of polymerase chain reaction-amplified DNA."
Richard P., Thomas G., de Zulueta M.P., de Gennes J.-L., Thomas M., Cassaigne A., Bereziat G., Iron A.
Clin. Chem. 40:24-29(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP3 ARG-130; ASP-145; SER-154; CYS-160 AND CYS-176.
[30]"Apolipoprotein E Sendai (arginine 145-->proline): a new variant associated with lipoprotein glomerulopathy."
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.
J. Am. Soc. Nephrol. 8:820-823(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LPG PRO-163.
[31]"Apolipoprotein E R112; R251G: a carboxy-terminal variant found in patients with hyperlipidemia and coronary heart disease."
Kang A.K., Jenkins D.J.A., Wolever T.M.S., Huff M.W., Maguire G.F., Connelly P.W., Hegele R.A.
Mutat. Res. 382:57-65(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS E4/3 ARG-130 AND GLY-269.
[32]"A novel apolipoprotein E mutation, E2 (Arg25Cys), in lipoprotein glomerulopathy."
Matsunaga A., Sasaki J., Komatsu T., Kanatsu K., Tsuji E., Moriyama K., Koga T., Arakawa K., Oikawa S., Saito T., Kita T., Doi T.
Kidney Int. 56:421-427(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LPG CYS-43.
[33]"Familial splenomegaly: macrophage hypercatabolism of lipoproteins associated with apolipoprotein E mutation [apolipoprotein E (delta149 Leu)]."
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.
J. Clin. Endocrinol. Metab. 85:4354-4358(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SBHD LEU-167 DEL.
[34]"Apolipoprotein E3Basel: new insights into a highly conserved protein region."
Miserez A.R., Scharnagl H., Muller P.Y., Mirsaidi R., Stahelin H.B., Monsch A., Marz W., Hoffmann M.M.
Eur. J. Clin. Invest. 33:677-685(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT E3 BASEL VAL-124.
[35]"Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors."
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.
Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-130 AND CYS-176.
[36]"Variable expressivity of the clinical and biochemical phenotype associated with the apolipoprotein E p.Leu149del mutation."
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.
Eur. J. Hum. Genet. 13:1186-1191(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SBHD LEU-167 DEL.
[37]"APOE Kyoto mutation in European Americans with lipoprotein glomerulopathy."
Rovin B.H., Roncone D., McKinley A., Nadasdy T., Korbet S.M., Schwartz M.M.
N. Engl. J. Med. 357:2522-2524(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LPG CYS-43.
[38]"Quantitative detection of single amino acid polymorphisms by targeted proteomics."
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.
J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-64, IDENTIFICATION BY MASS SPECTROMETRY.
[39]"Apolipoprotein E gene mutations in subjects with mixed hyperlipidemia and a clinical diagnosis of familial combined hyperlipidemia."
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.
Atherosclerosis 222:449-455(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP3 SER-154, VARIANT LEU-167 DEL.
[40]"Description of a large family with autosomal dominant hypercholesterolemia associated with the APOE p.Leu167del mutation."
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. expand/collapse author list , Rabes J.P., Boileau C., Varret M.
Hum. Mutat. 34:83-87(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH LEU-167 DEL.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Apolipoprotein E entry

Protein Spotlight

Tangled - Issue 83 of June 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12529 mRNA. Translation: AAB59518.1.
K00396 mRNA. Translation: AAB59546.1.
M10065 Genomic DNA. Translation: AAB59397.1.
AF050154 Genomic DNA. Translation: AAD02505.1.
AF261279 Genomic DNA. Translation: AAG27089.1.
AK314898 mRNA. Translation: BAG37412.1.
FJ525876 Genomic DNA. Translation: ACN81314.1.
BC003557 mRNA. Translation: AAH03557.1.
AB035149 Genomic DNA. Translation: BAA96080.1.
CCDSCCDS12647.1.
PIRLPHUE. A92478.
RefSeqNP_000032.1. NM_000041.2.
UniGeneHs.654439.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B68X-ray2.00A19-209[»]
1BZ4X-ray1.85A40-183[»]
1EA8X-ray1.95A19-209[»]
1GS9X-ray1.70A19-183[»]
1H7IX-ray1.90A19-209[»]
1LE2X-ray3.00A41-184[»]
1LE4X-ray2.50A41-184[»]
1LPEX-ray2.25A41-184[»]
1NFNX-ray1.80A19-209[»]
1NFOX-ray2.00A19-209[»]
1OEFNMR-A281-304[»]
1OEGNMR-A285-307[»]
1OR2X-ray2.50A19-183[»]
1OR3X-ray1.73A19-183[»]
2KC3NMR-A19-201[»]
2KNYNMR-A147-167[»]
2L7BNMR-A19-317[»]
DisProtDP00355.
ProteinModelPortalP02649.
SMRP02649. Positions 19-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106845. 49 interactions.
DIPDIP-1120N.
IntActP02649. 26 interactions.
MINTMINT-4999641.
STRING9606.ENSP00000252486.

Chemistry

DrugBankDB00062. Human Serum Albumin.
DB00064. Serum albumin iodonated.

PTM databases

PhosphoSiteP02649.

Polymorphism databases

DMDM114039.

2D gel databases

DOSAC-COBS-2DPAGEP02649.
SWISS-2DPAGEP02649.

Proteomic databases

MaxQBP02649.
PaxDbP02649.
PeptideAtlasP02649.
PRIDEP02649.

Protocols and materials databases

DNASU348.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252486; ENSP00000252486; ENSG00000130203.
GeneID348.
KEGGhsa:348.
UCSCuc002pab.3. human.

Organism-specific databases

CTD348.
GeneCardsGC19P045408.
HGNCHGNC:613. APOE.
HPACAB008363.
MIM104310. phenotype.
107741. gene+phenotype.
143890. phenotype.
269600. phenotype.
611771. phenotype.
neXtProtNX_P02649.
Orphanet238616. Alzheimer disease.
1648. Dementia with Lewy body.
406. Heterozygous familial hypercholesterolemia.
412. Hyperlipoproteinemia type 3.
329481. Lipoprotein glomerulopathy.
158029. Sea-blue histiocytosis.
PharmGKBPA55.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44867.
HOGENOMHOG000034006.
HOVERGENHBG010582.
InParanoidP02649.
KOK04524.
OMAPLQERAQ.
OrthoDBEOG793B87.
PhylomeDBP02649.
TreeFamTF334458.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP02649.
BgeeP02649.
CleanExHS_APOE.
GenevestigatorP02649.

Family and domain databases

InterProIPR000074. ApoA1_A4_E.
[Graphical view]
PfamPF01442. Apolipoprotein. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPOE. human.
EvolutionaryTraceP02649.
GeneWikiApolipoprotein_E.
GenomeRNAi348.
NextBio1435.
PMAP-CutDBP02649.
PROP02649.
SOURCESearch...

Entry information

Entry nameAPOE_HUMAN
AccessionPrimary (citable) accession number: P02649
Secondary accession number(s): B2RC15, C0JYY5, Q9P2S4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 191 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM