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Entry version 216 (07 Oct 2020)
Sequence version 3 (05 Oct 2010)
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Protein

Phospholipid-transporting ATPase ABCA1

Gene

ABCA1

Organism
Homo sapiens (Human)
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

Catalyzes the translocation of specific phospholipids from the cytoplasmic to the extracellular/lumenal leaflet of membrane coupled to the hydrolysis of ATP (PubMed:24097981). Thereby, participates in phospholipid transfer to apoliproteins to form nascent high density lipoproteins/HDLs (PubMed:14754908). Transports preferentially phosphatidylcholine over phosphatidylserine (PubMed:24097981). May play a similar role in the efflux of intracellular cholesterol to apoliproteins and the formation of nascent high density lipoproteins/HDLs (PubMed:10533863, PubMed:14754908, PubMed:24097981).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • ATP + H(2)O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).1 Publication EC:7.6.2.1

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

ATPase activity is decreased by cholesterol and ceramide. ATPase activity is stimulated by phosphatidylcholine and to a lesser degree by phosphatidylserine and sphingomyelin. Phospholipid translocase activity is highly reduced by berylium fluoride and aluminum flouride and reduced by N-ethylmaleimide.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi933 – 940ATP 1PROSITE-ProRule annotation8
Nucleotide bindingi1946 – 1953ATP 2PROSITE-ProRule annotation8

<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 functionTranslocase
Biological processCholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
O95477

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1989781, PPARA activates gene expression
R-HSA-5682113, Defective ABCA1 causes Tangier disease
R-HSA-8963896, HDL assembly
R-HSA-9029569, NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
O95477

SIGNOR Signaling Network Open Resource

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SIGNORi
O95477

Protein family/group databases

Transport Classification Database

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TCDBi
3.A.1.211.14, the atp-binding cassette (abc) superfamily

Chemistry databases

SwissLipids knowledge resource for lipid biology

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SwissLipidsi
SLP:000000345

<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:
Phospholipid-transporting ATPase ABCA1Curated (EC:7.6.2.11 Publication)
Alternative name(s):
ATP-binding cassette sub-family A member 1
ATP-binding cassette transporter 1
Short name:
ABC-1
Short name:
ATP-binding cassette 1
Cholesterol efflux regulatory protein
<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:ABCA1Imported
Synonyms:ABC1, CERP
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000165029.15

Human Gene Nomenclature Database

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HGNCi
HGNC:29, ABCA1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600046, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O95477

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei22 – 42HelicalSequence analysisAdd BLAST21
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini43 – 639ExtracellularAdd BLAST597
Transmembranei640 – 660HelicalSequence analysisAdd BLAST21
Transmembranei683 – 703HelicalSequence analysisAdd BLAST21
Transmembranei716 – 736HelicalSequence analysisAdd BLAST21
Transmembranei745 – 765HelicalSequence analysisAdd BLAST21
Transmembranei777 – 797HelicalSequence analysisAdd BLAST21
Transmembranei827 – 847HelicalSequence analysisAdd BLAST21
Transmembranei1041 – 1057HelicalSequence analysisAdd BLAST17
Transmembranei1351 – 1371HelicalSequence analysisAdd BLAST21
Topological domaini1372 – 1656ExtracellularAdd BLAST285
Transmembranei1657 – 1677HelicalSequence analysisAdd BLAST21
Transmembranei1703 – 1723HelicalSequence analysisAdd BLAST21
Transmembranei1735 – 1755HelicalSequence analysisAdd BLAST21
Transmembranei1768 – 1788HelicalSequence analysisAdd BLAST21
Transmembranei1802 – 1822HelicalSequence analysisAdd BLAST21
Transmembranei1852 – 1872HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Tangier disease (TGD)20 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by near absence of plasma high density lipoproteins, low serum HDL cholesterol, and massive tissue deposition of cholesterol esters. Clinical features include large yellow-orange tonsils, hepatomegaly, splenomegaly, enlarged lymph nodes, and often sensory polyneuropathy.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_012620255A → T in TGD; deficient cellular cholesterol efflux. 1 PublicationCorresponds to variant dbSNP:rs758100110Ensembl.1
Natural variantiVAR_062482284E → K in TGD. 1 Publication1
Natural variantiVAR_062485482Y → C in TGD. 1 Publication1
Natural variantiVAR_009146587R → W in TGD. 1 PublicationCorresponds to variant dbSNP:rs2853574EnsemblClinVar.1
Natural variantiVAR_062487590W → L in TGD. 2 PublicationsCorresponds to variant dbSNP:rs137854496EnsemblClinVar.1
Natural variantiVAR_009147590W → S in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity. 3 PublicationsCorresponds to variant dbSNP:rs137854496EnsemblClinVar.1
Natural variantiVAR_009148597Q → R in TGD. 2 PublicationsCorresponds to variant dbSNP:rs2853578EnsemblClinVar.1
Natural variantiVAR_062491840W → R in TGD. 1 PublicationCorresponds to variant dbSNP:rs1322998567Ensembl.1
Natural variantiVAR_012626929T → I in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane. 2 Publications1
Natural variantiVAR_037968935N → H in TGD. 1 PublicationCorresponds to variant dbSNP:rs28937314EnsemblClinVar.1
Natural variantiVAR_009150935N → S in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity. 3 PublicationsCorresponds to variant dbSNP:rs28937313EnsemblClinVar.1
Natural variantiVAR_009151937A → V in TGD. 1 PublicationCorresponds to variant dbSNP:rs137854495EnsemblClinVar.1
Natural variantiVAR_0126271046A → D in TGD. 1 PublicationCorresponds to variant dbSNP:rs141021096Ensembl.1
Natural variantiVAR_0624931068R → C in TGD. 1 PublicationCorresponds to variant dbSNP:rs745593394Ensembl.1
Natural variantiVAR_0091521289D → N in TGD. 2 PublicationsCorresponds to variant dbSNP:rs137854500EnsemblClinVar.1
Natural variantiVAR_0624971379L → F in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane. 1 Publication1
Natural variantiVAR_0091531477C → R in TGD; loss of interaction with APOE; unable to generate APOE-containing high density lipoproteins; moderately decreased protein abundance; moderately decreased ATPase activity; moderately decreased phospholipid translocase activity. 4 PublicationsCorresponds to variant dbSNP:rs137854494EnsemblClinVar.1
Natural variantiVAR_0126301506S → L in TGD. 1 PublicationCorresponds to variant dbSNP:rs137854497EnsemblClinVar.1
Natural variantiVAR_0091541517I → R in TGD. 1
Natural variantiVAR_0379701680R → W in TGD. 1 PublicationCorresponds to variant dbSNP:rs137854498EnsemblClinVar.1
Natural variantiVAR_0625011704V → D in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane. 1 Publication1
Natural variantiVAR_0091551800N → H in TGD. 4 PublicationsCorresponds to variant dbSNP:rs146292819EnsemblClinVar.1
Natural variantiVAR_0625021851R → Q in TGD. 1 PublicationCorresponds to variant dbSNP:rs1055285452Ensembl.1
Natural variantiVAR_0625041901R → S in TGD. 1 Publication1
Natural variantiVAR_0126352081R → W in TGD; highly decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane. 2 PublicationsCorresponds to variant dbSNP:rs137854501EnsemblClinVar.1
Natural variantiVAR_0625072196Q → H in TGD. 1 PublicationCorresponds to variant dbSNP:rs564764153Ensembl.1
Hypoalphalipoproteinemia, primary, 1 (FHA1)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by decreased plasma high density lipoproteins, moderately low HDL cholesterol, a reduction in cellular cholesterol efflux, and susceptibility to premature coronary artery disease.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01752985P → L in FHA1; Alabama. 1 PublicationCorresponds to variant dbSNP:rs145183203EnsemblClinVar.1
Natural variantiVAR_009149693Missing in FHA1. 2 Publications1
Natural variantiVAR_0126281091M → T in FHA1; loss of localization to plasma membrane; decreased cholesterol efflux; decreased phospholipid efflux. 3 Publications1
Natural variantiVAR_0175301099D → Y in FHA1. 1 PublicationCorresponds to variant dbSNP:rs28933692EnsemblClinVar.1
Natural variantiVAR_0126341893 – 1894Missing in FHA1. 2 Publications2
Natural variantiVAR_0625031897R → W in FHA1; uncertain pathological significance. 1 PublicationCorresponds to variant dbSNP:rs760768125Ensembl.1
Natural variantiVAR_0379712009F → S in FHA1. 1 PublicationCorresponds to variant dbSNP:rs137854499EnsemblClinVar.1
Natural variantiVAR_0126362150P → L in FHA1; moderately decreased protein abundance; does not affect ATPase activity; moderately decreased phospholipid translocase activity. 2 PublicationsCorresponds to variant dbSNP:rs369098049Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi3C → S: Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased cholesterol efflux. Decreased phospholipid efflux. Decreased palmitoylation; when associated with S-23, S-1110 and S-1111. 1 Publication1
Mutagenesisi23C → S: Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased palmitoylation; when associated with S-3, S-1110 and S-1111. 1 Publication1
Mutagenesisi100S → C: Highly decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity. 1 Publication1
Mutagenesisi593F → L: Moderately decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity. 1 Publication1
Mutagenesisi939K → M: Inhibits ATPase activity; when associated with M-1952. Decreases translocase activity; when associated with M-1952. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-1952. 1 Publication1
Mutagenesisi1110C → S: Decreased palmitoylation; when associated with S-3, S-23 and S-1111. 1 Publication1
Mutagenesisi1111C → S: Decreased palmitoylation; when associated with S-3, S-23 and S-1110. 1 Publication1
Mutagenesisi1512T → M: Moderately decreased protein abundance. Does not affect ATPase activity. Moderately decreased phospholipid translocase activity. 1 Publication1
Mutagenesisi1952K → M: Inhibits ATPase activity; when associated with M-939. Decreases translocase activity; when associated with M-939. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-939. 1 Publication1

Keywords - Diseasei

Atherosclerosis, Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
19

MalaCards human disease database

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MalaCardsi
ABCA1
MIMi205400, phenotype
604091, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000165029

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
425, Apolipoprotein A-I deficiency
31150, Tangier disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24373

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
O95477, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2362986

Drug and drug target database

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DrugBanki
DB00171, ATP
DB01016, Glyburide
DB01599, Probucol
DB00675, Tamoxifen
DB11635, Tocofersolan
DB00163, Vitamin E

DrugCentral

More...
DrugCentrali
O95477

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ABCA1

<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 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_00000932881 – 2261Phospholipid-transporting ATPase ABCA1Add BLAST2261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi3S-palmitoyl cysteine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi14N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi23S-palmitoyl cysteine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi75 ↔ 3091 Publication
Glycosylationi98N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi151N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi161N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi196N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi244N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi292N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi337N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi349N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi400N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi478N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi489N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi521N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi820N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei1042Phosphoserine; by PKA1 Publication1
Lipidationi1110S-palmitoyl cysteine1 Publication1
Lipidationi1111S-palmitoyl cysteine1 Publication1
Glycosylationi1144N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1294N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1296PhosphoserineBy similarity1
Glycosylationi1453N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1463 ↔ 14771 Publication
Glycosylationi1504N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1637N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2044N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei2054Phosphoserine; by PKA1 Publication1
Glycosylationi2238N-linked (GlcNAc...) asparagineSequence analysis1

<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

Phosphorylation on Ser-2054 regulates phospholipid efflux.1 Publication
Palmitoylated by ZDHHC8 (PubMed:19556522). Palmitoylation is essential for localization to the plasma membrane (PubMed:19556522).1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O95477

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O95477

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
O95477

MaxQB - The MaxQuant DataBase

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MaxQBi
O95477

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

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PaxDbi
O95477

PeptideAtlas

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PeptideAtlasi
O95477

PRoteomics IDEntifications database

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PRIDEi
O95477

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
50908

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1020, 1 N-Linked glycan (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
O95477, 21 sites

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O95477

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

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PhosphoSitePlusi
O95477

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O95477

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed, but most abundant in macrophages.

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By bacterial lipopolysaccharides (LPS). LPS regulates expression through a liver X receptor (LXR) -independent mechanism. Repressed by ZNF202.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000165029, Expressed in liver and 233 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O95477, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O95477, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000165029, Low tissue specificity

<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

Interacts with MEGF10 (PubMed:17205124). May interact with APOE1; functionally associated with APOE1 in the biogenesis of HDLs (PubMed:14754908).

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
106537, 25 interactors

Database of interacting proteins

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DIPi
DIP-29211N

Protein interaction database and analysis system

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IntActi
O95477, 32 interactors

Molecular INTeraction database

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MINTi
O95477

STRING: functional protein association networks

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STRINGi
9606.ENSP00000363868

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
O95477, protein

<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

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SMRi
O95477

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
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 <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini899 – 1131ABC transporter 1PROSITE-ProRule annotationAdd BLAST233
Domaini1912 – 2144ABC transporter 2PROSITE-ProRule annotationAdd BLAST233

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Multifunctional polypeptide with two homologous halves, each containing a hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain.

<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

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0059, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000154658

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000604_19_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O95477

KEGG Orthology (KO)

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KOi
K05641

Identification of Orthologs from Complete Genome Data

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OMAi
ICIAFTY

Database of Orthologous Groups

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OrthoDBi
131191at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O95477

TreeFam database of animal gene trees

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TreeFami
TF105191

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003593, AAA+_ATPase
IPR003439, ABC_transporter-like
IPR017871, ABC_transporter_CS
IPR026082, ABCA
IPR027417, P-loop_NTPase

The PANTHER Classification System

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PANTHERi
PTHR19229, PTHR19229, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00005, ABC_tran, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00382, AAA, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540, SSF52540, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00211, ABC_TRANSPORTER_1, 1 hit
PS50893, ABC_TRANSPORTER_2, 2 hits

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

O95477-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE
60 70 80 90 100
QHECHFPNKA MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS
110 120 130 140 150
IVARLFSDAR RLLLYSQKDT SMKDMRKVLR TLQQIKKSSS NLKLQDFLVD
160 170 180 190 200
NETFSGFLYH NLSLPKSTVD KMLRADVILH KVFLQGYQLH LTSLCNGSKS
210 220 230 240 250
EEMIQLGDQE VSELCGLPRE KLAAAERVLR SNMDILKPIL RTLNSTSPFP
260 270 280 290 300
SKELAEATKT LLHSLGTLAQ ELFSMRSWSD MRQEVMFLTN VNSSSSSTQI
310 320 330 340 350
YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNGTE EDAETFYDNS
360 370 380 390 400
TTPYCNDLMK NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN
410 420 430 440 450
KTFQELAVFH DLEGMWEELS PKIWTFMENS QEMDLVRMLL DSRDNDHFWE
460 470 480 490 500
QQLDGLDWTA QDIVAFLAKH PEDVQSSNGS VYTWREAFNE TNQAIRTISR
510 520 530 540 550
FMECVNLNKL EPIATEVWLI NKSMELLDER KFWAGIVFTG ITPGSIELPH
560 570 580 590 600
HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV
610 620 630 640 650
EQAIIRVLTG TEKKTGVYMQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY
660 670 680 690 700
SVAVIIKGIV YEKEARLKET MRIMGLDNSI LWFSWFISSL IPLLVSAGLL
710 720 730 740 750
VVILKLGNLL PYSDPSVVFV FLSVFAVVTI LQCFLISTLF SRANLAAACG
760 770 780 790 800
GIIYFTLYLP YVLCVAWQDY VGFTLKIFAS LLSPVAFGFG CEYFALFEEQ
810 820 830 840 850
GIGVQWDNLF ESPVEEDGFN LTTSVSMMLF DTFLYGVMTW YIEAVFPGQY
860 870 880 890 900
GIPRPWYFPC TKSYWFGEES DEKSHPGSNQ KRISEICMEE EPTHLKLGVS
910 920 930 940 950
IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF
960 970 980 990 1000
PPTSGTAYIL GKDIRSEMST IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL
1010 1020 1030 1040 1050
KGLSEKHVKA EMEQMALDVG LPSSKLKSKT SQLSGGMQRK LSVALAFVGG
1060 1070 1080 1090 1100
SKVVILDEPT AGVDPYSRRG IWELLLKYRQ GRTIILSTHH MDEADVLGDR
1110 1120 1130 1140 1150
IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS SCRNSSSTVS
1160 1170 1180 1190 1200
YLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI
1210 1220 1230 1240 1250
GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK
1260 1270 1280 1290 1300
VAEESGVDAE TSDGTLPARR NRRAFGDKQS CLRPFTEDDA ADPNDSDIDP
1310 1320 1330 1340 1350
ESRETDLLSG MDGKGSYQVK GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ
1360 1370 1380 1390 1400
IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ PWMYNEQYTF VSNDAPEDTG
1410 1420 1430 1440 1450
TLELLNALTK DPGFGTRCME GNPIPDTPCQ AGEEEWTTAP VPQTIMDLFQ
1460 1470 1480 1490 1500
NGNWTMQNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QNTADILQDL
1510 1520 1530 1540 1550
TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NTQALPPSQE
1560 1570 1580 1590 1600
VNDAIKQMKK HLKLAKDSSA DRFLNSLGRF MTGLDTKNNV KVWFNNKGWH
1610 1620 1630 1640 1650
AISSFLNVIN NAILRANLQK GENPSHYGIT AFNHPLNLTK QQLSEVALMT
1660 1670 1680 1690 1700
TSVDVLVSIC VIFAMSFVPA SFVVFLIQER VSKAKHLQFI SGVKPVIYWL
1710 1720 1730 1740 1750
SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL LLLLYGWSIT
1760 1770 1780 1790 1800
PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTDNKLNNIN
1810 1820 1830 1840 1850
DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG
1860 1870 1880 1890 1900
RNLFAMAVEG VVFFLITVLI QYRFFIRPRP VNAKLSPLND EDEDVRRERQ
1910 1920 1930 1940 1950
RILDGGGQND ILEIKELTKI YRRKRKPAVD RICVGIPPGE CFGLLGVNGA
1960 1970 1980 1990 2000
GKSSTFKMLT GDTTVTRGDA FLNKNSILSN IHEVHQNMGY CPQFDAITEL
2010 2020 2030 2040 2050
LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK YAGNYSGGNK
2060 2070 2080 2090 2100
RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSV VKEGRSVVLT
2110 2120 2130 2140 2150
SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP
2160 2170 2180 2190 2200
DLKPVQDFFG LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR
2210 2220 2230 2240 2250
LHIEDYSVSQ TTLDQVFVNF AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF
2260
LQDEKVKESY V
Length:2,261
Mass (Da):254,302
Last modified:October 5, 2010 - v3
<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:i21A2CF8F3F518D6D
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1AMI2B1AMI2_HUMAN
ATP-binding cassette, sub-family A ...
ABCA1 hCG_1789838
363Annotation score:

Annotation score:1 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>
B1AMI1B1AMI1_HUMAN
Phospholipid-transporting ATPase AB...
ABCA1
123Annotation score:

Annotation score:1 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD49849 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence CAA10005 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

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 conflicti793Y → C in AAK43526 (PubMed:11352567).Curated1
Sequence conflicti831D → N in AAK43526 (PubMed:11352567).Curated1
Sequence conflicti1005E → K in AAK43526 (PubMed:11352567).Curated1
Sequence conflicti1745 – 1746Missing in AAD49852 (PubMed:10431238).Curated2

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Genetic variations in ABCA1 define the high density lipoprotein cholesterol level quantitative trait locus 13 (HDLCQ13) [MIMi:600046].1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01752985P → L in FHA1; Alabama. 1 PublicationCorresponds to variant dbSNP:rs145183203EnsemblClinVar.1
Natural variantiVAR_035724210E → D in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_012618219R → K Common polymorphism; associated with a decreased severity of CAD. 7 PublicationsCorresponds to variant dbSNP:rs2230806EnsemblClinVar.1
Natural variantiVAR_012619230R → C2 PublicationsCorresponds to variant dbSNP:rs9282541EnsemblClinVar.1
Natural variantiVAR_062481248P → A1 PublicationCorresponds to variant dbSNP:rs142625938Ensembl.1
Natural variantiVAR_012620255A → T in TGD; deficient cellular cholesterol efflux. 1 PublicationCorresponds to variant dbSNP:rs758100110Ensembl.1
Natural variantiVAR_062482284E → K in TGD. 1 Publication1
Natural variantiVAR_062483364S → C1 PublicationCorresponds to variant dbSNP:rs775035559Ensembl.1
Natural variantiVAR_009145399V → A2 PublicationsCorresponds to variant dbSNP:rs9282543EnsemblClinVar.1
Natural variantiVAR_062484401K → Q1 PublicationCorresponds to variant dbSNP:rs138487227Ensembl.1
Natural variantiVAR_062485482Y → C in TGD. 1 Publication1
Natural variantiVAR_062486496R → W Associated with increased plasma HDL cholesterol. 1 PublicationCorresponds to variant dbSNP:rs147675550EnsemblClinVar.1
Natural variantiVAR_009146587R → W in TGD. 1 PublicationCorresponds to variant dbSNP:rs2853574EnsemblClinVar.1
Natural variantiVAR_062487590W → L in TGD. 2 PublicationsCorresponds to variant dbSNP:rs137854496EnsemblClinVar.1
Natural variantiVAR_009147590W → S in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity. 3 PublicationsCorresponds to variant dbSNP:rs137854496EnsemblClinVar.1
Natural variantiVAR_009148597Q → R in TGD. 2 PublicationsCorresponds to variant dbSNP:rs2853578EnsemblClinVar.1
Natural variantiVAR_062488638R → Q Associated with reduced plasma HDL cholesterol. 1 PublicationCorresponds to variant dbSNP:rs374190304EnsemblClinVar.1
Natural variantiVAR_009149693Missing in FHA1. 2 Publications1
Natural variantiVAR_012621771V → M Associated with HDL cholesterol. 4 PublicationsCorresponds to variant dbSNP:rs2066718EnsemblClinVar.1
Natural variantiVAR_012622774T → P2 PublicationsCorresponds to variant dbSNP:rs35819696EnsemblClinVar.1
Natural variantiVAR_062489774T → S1 Publication1
Natural variantiVAR_012623776K → N May be associated with increased risk of ischemic heart disease. 3 PublicationsCorresponds to variant dbSNP:rs138880920EnsemblClinVar.1
Natural variantiVAR_062490815E → G Associated with reduced plasma HDL cholesterol. 1 PublicationCorresponds to variant dbSNP:rs145582736Ensembl.1
Natural variantiVAR_012624825V → I Associated with higher plasma cholesterol. 5 PublicationsCorresponds to variant dbSNP:rs2066715EnsemblClinVar.1
Natural variantiVAR_062491840W → R in TGD. 1 PublicationCorresponds to variant dbSNP:rs1322998567Ensembl.1
Natural variantiVAR_012625883I → M Associated with higher plasma cholesterol. 7 PublicationsCorresponds to variant dbSNP:rs2066714EnsemblClinVar.1
Natural variantiVAR_035725917D → Y in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_012626929T → I in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane. 2 Publications1
Natural variantiVAR_037968935N → H in TGD. 1 PublicationCorresponds to variant dbSNP:rs28937314EnsemblClinVar.1
Natural variantiVAR_009150935N → S in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity. 3 PublicationsCorresponds to variant dbSNP:rs28937313EnsemblClinVar.1
Natural variantiVAR_009151937A → V in TGD. 1 PublicationCorresponds to variant dbSNP:rs137854495EnsemblClinVar.1
Natural variantiVAR_0126271046A → D in TGD. 1 PublicationCorresponds to variant dbSNP:rs141021096Ensembl.1
Natural variantiVAR_0379691054V → I. Corresponds to variant dbSNP:rs13306072Ensembl.1
Natural variantiVAR_0624921065P → S1 Publication1
Natural variantiVAR_0624931068R → C in TGD. 1 PublicationCorresponds to variant dbSNP:rs745593394Ensembl.1
Natural variantiVAR_0126281091M → T in FHA1; loss of localization to plasma membrane; decreased cholesterol efflux; decreased phospholipid efflux. 3 Publications1
Natural variantiVAR_0175301099D → Y in FHA1. 1 PublicationCorresponds to variant dbSNP:rs28933692EnsemblClinVar.1
Natural variantiVAR_0126291172E → D Associated with premature coronary heart disease. 4 PublicationsCorresponds to variant dbSNP:rs33918808EnsemblClinVar.1
Natural variantiVAR_0170161181S → F Associated with reduced plasma HDL cholesterol. 2 PublicationsCorresponds to variant dbSNP:rs76881554EnsemblClinVar.1
Natural variantiVAR_0624941216G → V1 PublicationCorresponds to variant dbSNP:rs562403512Ensembl.1
Natural variantiVAR_0091521289D → N in TGD. 2 PublicationsCorresponds to variant dbSNP:rs137854500EnsemblClinVar.1
Natural variantiVAR_0624951341R → T Associated with reduced plasma HDL cholesterol. 1 PublicationCorresponds to variant dbSNP:rs147743782Ensembl.1
Natural variantiVAR_0624961376S → G1 PublicationCorresponds to variant dbSNP:rs145689805Ensembl.1
Natural variantiVAR_0624971379L → F in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane. 1 Publication1
Natural variantiVAR_0357261407A → T in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs189206655Ensembl.1
Natural variantiVAR_0091531477C → R in TGD; loss of interaction with APOE; unable to generate APOE-containing high density lipoproteins; moderately decreased protein abundance; moderately decreased ATPase activity; moderately decreased phospholipid translocase activity. 4 PublicationsCorresponds to variant dbSNP:rs137854494EnsemblClinVar.1
Natural variantiVAR_0126301506S → L in TGD. 1 PublicationCorresponds to variant dbSNP:rs137854497EnsemblClinVar.1
Natural variantiVAR_0091541517I → R in TGD. 1
Natural variantiVAR_0126381555I → T2 PublicationsCorresponds to variant dbSNP:rs1997618Ensembl.1
Natural variantiVAR_0126311587K → R Associated with HDL cholesterol. 9 PublicationsCorresponds to variant dbSNP:rs2230808EnsemblClinVar.1
Natural variantiVAR_0126321611N → D Probable disease-associated variant; associated with atherosclerosis; deficient cellular cholesterol efflux. 1 Publication1
Natural variantiVAR_0624981615R → Q Associated with reduced plasma HDL cholesterol. 1 PublicationCorresponds to variant dbSNP:rs1251839800Ensembl.1
Natural variantiVAR_0126391648L → P2 PublicationsCorresponds to variant dbSNP:rs1883024Ensembl.1
Natural variantiVAR_0624991670A → T Associated with reduced plasma HDL cholesterol. 1 PublicationCorresponds to variant dbSNP:rs1203589782Ensembl.1
Natural variantiVAR_0625001680R → Q Associated with increased plasma HDL cholesterol. 1 PublicationCorresponds to variant dbSNP:rs150125857EnsemblClinVar.1
Natural variantiVAR_0379701680R → W in TGD. 1 PublicationCorresponds to variant dbSNP:rs137854498EnsemblClinVar.1
Natural variantiVAR_0625011704V → D in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane. 1 Publication