Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 170 (07 Oct 2020)
Sequence version 2 (01 Oct 1996)
Previous versions | rss
Add a publicationFeedback
Protein

Apolipoprotein E

Gene

Apoe

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells.By similarity

Miscellaneous

The mature protein has no cysteine residues; however, in different allelic variants where cysteine residues replace arginine at positions 155 or 168, binding of Apo-E to cell membrane receptors is decreased. The amino end of this protein is therefore thought to interact with the receptor.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHeparin-binding
Biological processLipid transport, Transport
LigandLipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-3000480, Scavenging by Class A Receptors
R-RNO-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-RNO-8957275, Post-translational protein phosphorylation
R-RNO-8963888, Chylomicron assembly
R-RNO-8963901, Chylomicron remodeling
R-RNO-8964026, Chylomicron clearance
R-RNO-8964058, HDL remodeling
R-RNO-975634, Retinoid metabolism and transport

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Apolipoprotein E
Short name:
Apo-E
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Apoe
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Rat genome database

More...
RGDi
2138, Apoe

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chylomicron, Extracellular matrix, HDL, Secreted, VLDL

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18Sequence analysisAdd BLAST18
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000199619 – 312Apolipoprotein EAdd BLAST294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei135Methionine sulfoxideBy similarity1
Modified residuei139PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific.By similarity
Glycated in plasma VLDL.By similarity
Phosphorylated by FAM20C in the extracellular medium.By similarity

Keywords - PTMi

Glycoprotein, Oxidation, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P02650

PRoteomics IDEntifications database

More...
PRIDEi
P02650

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P02650

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P02650

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000018454, Expressed in liver and 21 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P02650, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P02650, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
247757, 3 interactors

Protein interaction database and analysis system

More...
IntActi
P02650, 4 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000050968

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P02650

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati72 – 931Add BLAST22
Repeati94 – 1152Add BLAST22
Repeati116 – 1373Add BLAST22
Repeati138 – 1594Add BLAST22
Repeati160 – 1815Add BLAST22
Repeati182 – 2036Add BLAST22
Repeati204 – 2257Add BLAST22
Repeati226 – 2478Add BLAST22

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni72 – 2478 X 22 AA approximate tandem repeatsAdd BLAST176
Regioni150 – 160LDL and other lipoprotein receptors bindingBy similarityAdd BLAST11
Regioni150 – 160LDL receptor bindingBy similarityAdd BLAST11
Regioni154 – 157Heparin-bindingBy similarity4
Regioni202 – 282Lipid-binding and lipoprotein associationBy similarityAdd BLAST81
Regioni221 – 228Heparin-bindingBy similarity8
Regioni258 – 312HomooligomerizationBy similarityAdd BLAST55
Regioni270 – 282Specificity for association with VLDLBy similarityAdd BLAST13

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the apolipoprotein A1/A4/E family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QVD6, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182929

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P02650

KEGG Orthology (KO)

More...
KOi
K04524

Database of Orthologous Groups

More...
OrthoDBi
1314660at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P02650

TreeFam database of animal gene trees

More...
TreeFami
TF334458

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000074, ApoA_E

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01442, Apolipoprotein, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P02650-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKALWALLLV PLLTGCLAEG ELEVTDQLPG QSDQPWEQAL NRFWDYLRWV
60 70 80 90 100
QTLSDQVQEE LQSSQVTQEL TVLMEDTMTE VKAYKKELEE QLGPVAEETR
110 120 130 140 150
ARLAKEVQAA QARLGADMED LRNRLGQYRN EVNTMLGQST EELRSRLSTH
160 170 180 190 200
LRKMRKRLMR DADDLQKRLA VYKAGAQEGA ERGVSAIRER LGPLVEQGRQ
210 220 230 240 250
RTANLGAGAA QPLRDRAQAL SDRIRGRLEE VGNQARDRLE EVREQMEEVR
260 270 280 290 300
SKMEEQTQQI RLQAEIFQAR IKGWFEPLVE DMQRQWANLM EKIQASVATN
310
SIASTTVPLE NQ
Length:312
Mass (Da):35,753
Last modified:October 1, 1996 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8180EEE933378D92
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K151A0A0G2K151_RAT
Apolipoprotein E
Apoe
359Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti104A → T in CAA28650 (PubMed:3797247).Curated1
Sequence conflicti110A → T no nucleotide entry (PubMed:6190813).Curated1
Sequence conflicti110A → T in AAC60703 (PubMed:7766086).Curated1
Sequence conflicti141E → D no nucleotide entry (PubMed:6190813).Curated1
Sequence conflicti141E → D in AAC60703 (PubMed:7766086).Curated1
Sequence conflicti206 – 213GAGAAQPL → RWRRPAP in CAA28650 (PubMed:3797247).Curated8
Sequence conflicti206 – 213GAGAAQPL → RWRRPAP no nucleotide entry (PubMed:6190813).Curated8
Sequence conflicti309 – 310LE → WR no nucleotide entry (PubMed:6190813).Curated2
Sequence conflicti309 – 310LE → WR in AAC60703 (PubMed:7766086).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X04979 Genomic DNA Translation: CAA28650.1
J02582 Genomic DNA Translation: AAA40755.1
S76779 mRNA Translation: AAC60703.1
BC086581 mRNA Translation: AAH86581.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A26189, LPRTE

NCBI Reference Sequences

More...
RefSeqi
NP_001257610.1, NM_001270681.1
NP_001257611.1, NM_001270682.1
NP_001257612.1, NM_001270683.1
NP_001257613.1, NM_001270684.1
NP_620183.2, NM_138828.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000041891; ENSRNOP00000050968; ENSRNOG00000018454
ENSRNOT00000091574; ENSRNOP00000068937; ENSRNOG00000018454

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25728

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25728

UCSC genome browser

More...
UCSCi
RGD:2138, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04979 Genomic DNA Translation: CAA28650.1
J02582 Genomic DNA Translation: AAA40755.1
S76779 mRNA Translation: AAC60703.1
BC086581 mRNA Translation: AAH86581.1
PIRiA26189, LPRTE
RefSeqiNP_001257610.1, NM_001270681.1
NP_001257611.1, NM_001270682.1
NP_001257612.1, NM_001270683.1
NP_001257613.1, NM_001270684.1
NP_620183.2, NM_138828.3

3D structure databases

SMRiP02650
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi247757, 3 interactors
IntActiP02650, 4 interactors
STRINGi10116.ENSRNOP00000050968

PTM databases

iPTMnetiP02650
PhosphoSitePlusiP02650

Proteomic databases

PaxDbiP02650
PRIDEiP02650

Genome annotation databases

EnsembliENSRNOT00000041891; ENSRNOP00000050968; ENSRNOG00000018454
ENSRNOT00000091574; ENSRNOP00000068937; ENSRNOG00000018454
GeneIDi25728
KEGGirno:25728
UCSCiRGD:2138, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
348
RGDi2138, Apoe

Phylogenomic databases

eggNOGiENOG502QVD6, Eukaryota
GeneTreeiENSGT00950000182929
InParanoidiP02650
KOiK04524
OrthoDBi1314660at2759
PhylomeDBiP02650
TreeFamiTF334458

Enzyme and pathway databases

ReactomeiR-RNO-3000480, Scavenging by Class A Receptors
R-RNO-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-RNO-8957275, Post-translational protein phosphorylation
R-RNO-8963888, Chylomicron assembly
R-RNO-8963901, Chylomicron remodeling
R-RNO-8964026, Chylomicron clearance
R-RNO-8964058, HDL remodeling
R-RNO-975634, Retinoid metabolism and transport

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P02650

Gene expression databases

BgeeiENSRNOG00000018454, Expressed in liver and 21 other tissues
ExpressionAtlasiP02650, baseline and differential
GenevisibleiP02650, RN

Family and domain databases

InterProiView protein in InterPro
IPR000074, ApoA_E
PfamiView protein in Pfam
PF01442, Apolipoprotein, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAPOE_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P02650
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: October 7, 2020
This is version 170 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again