Protein detail

ABCA1

Phospholipid-transporting ATPase ABCA1 (EC 7.6.2.1) (ATP-binding cassette sub-family A member 1) (ATP-binding cassette transporter 1) (ABC-1) (ATP-binding cassette 1) (Cholesterol efflux regulatory protein)

Entry name
ABCA1
UniProt ID
EVMP confidence score
0.53
Supporting publications (n)
3
Transmembrane count
15
Protein classification
Disease related genesEnzymesFDA approved drug targetsHuman disease related genesMetabolic proteinsPlasma proteinsPredicted intracellular proteinsPredicted membrane proteinsTransporters
Basic Information
Protein Names
Phospholipid-transporting ATPase ABCA1 (EC 7.6.2.1) (ATP-binding cassette sub-family A member 1) (ATP-binding cassette transporter 1) (ABC-1) (ATP-binding cassette 1) (Cholesterol efflux regulatory protein)
Protein Class (9)
Disease related genesEnzymesFDA approved drug targetsHuman disease related genesMetabolic proteinsPlasma proteinsPredicted intracellular proteinsPredicted membrane proteinsTransporters
Protein Function (8)
  • Human disease related genes:Cardiovascular diseases:Vascular diseases
  • Predicted intracellular proteins
  • Human disease related genes:Congenital disorders of metabolism:Congenital disorders of lipid/glycolipid metabolism
  • Enzymes
  • ENZYME proteins
  • Transporters:Primary Active Transporters
  • Disease related genes
  • FDA approved drug targets:Small molecule drugs
Transmembrane
22..42; Helical; 640..660; Helical; 683..703; Helical; 716..736; Helical; 745..765; Helical; 777..797; Helical; 827..847; Helical; 1041..1057; Helical; 1351..1371; Helical; 1657..1677; Helical; 1703..1723; Helical; 1735..1755; Helical; 1768..1788; Helical; 1802..1822; Helical; 1852..1872; Helical
Transmembrane Count
15
Entrez Gene Symbol
Gene Synonym (3)
ABC1HDLDT1TGD
Gene Description
ATP binding cassette subfamily A member 1
Chromosome
9
Position
104781006-104928155
Supporting publications (n)
3
EVMP confidence score
0.53
Fluorescence & Localization
ABCA1 fluorescence
Cell SpecificBergmann gliaSingle-Nuclei Brain Specificendothelial cellSecretome LocationIntracellular and membraneSecretome FunctionNo annotated function
Function & Pathway
Protein Function (8)
  • Human disease related genes:Cardiovascular diseases:Vascular diseases
  • Predicted intracellular proteins
  • Human disease related genes:Congenital disorders of metabolism:Congenital disorders of lipid/glycolipid metabolism
  • Enzymes
  • ENZYME proteins
  • Transporters:Primary Active Transporters
  • Disease related genes
  • FDA approved drug targets:Small molecule drugs
Mediation Categories (5)
Clinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence59

Enzyme-Mediated Modification (18)

18 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
ABCA1PRKYO43930S2,054phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
ABCA1PRKACBP22694S2,054phosphorylationReactome_ProtMapperProtMapper
ABCA1PRKACBP22694S1,042phosphorylationReactome_ProtMapperProtMapper
ABCA1PRKACGP22612S2,054phosphorylationReactome_ProtMapperProtMapper
ABCA1PRKACGP22612S1,042phosphorylationReactome_ProtMapperProtMapper
ABCA1PRKCBP05771S1,042phosphorylationKEAKEA:17570479
ABCA1PRKG1Q13976S2,054phosphorylationKEAKEA:17570479
ABCA1RPS6KA3P51812S1,042phosphorylationKEAKEA:17570479
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Ligand-Receptor Signaling (32)

32 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
extracellularextracellularDGIdb
extracellularextracellularOmniPath
intracellularintracellularComPPI
intracellularintracellularGO_Intercell
intracellularintracellularUniProt_location
intracellularintracellularOmniPath
cell_surface_ligandcell_surface_ligandBaccin2019Yes
cell_surface_ligandcell_surface_ligandCellPhoneDBYes
cell_surface_ligandcell_surface_ligandOmniPathYes
transportertransporterSurfaceomeYes
Page 1 of 4Next

Regulatory Interaction Network (8)

8 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
ABCA1O95477MEG10Q96KG7YesYesSIGNORSIGNOR:17205124
MEG10Q96KG7ABCA1O95477YesYesCellTalkDBSIGNORCellTalkDB:17205124SIGNOR:17205124
EGFRP00533ABCA1O95477YesYesPhosphoSite_norefSIGNORiPTMnetProtMapperSIGNOR_ProtMapperPhosphoSite_ProtMapperSIGNOR:12196520ProtMapper:12196520
LNX1Q8TBB1ABCA1O95477YesYesSIGNORSIGNOR:22889411
ABCA1O95477APOA1P02647YesYesCellPhoneDBSIGNORHPRDHINTIntActInnateDBHPRD:12084722InnateDB:22271762IntAct:12084722SIGNOR:15347662HINT:12084722HINT:22271762IntAct:30458687
APOA1P02647ABCA1O95477YesYesCellChatDBCellTalkDBCellPhoneDBSIGNORHPRDHINTIntActInnateDBHPRD:12084722CellTalkDB:27100352InnateDB:22271762IntAct:12084722HINT:12084722HINT:22271762SIGNOR:12869555CellChatDB:20064972IntAct:30458687
KAPCAP17612ABCA1O95477YesYesphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperHPRDReactome_ProtMapperPhosphoSite_KEAKEAHPRD_KEASIGNOR_ProtMapperPhosphoSiteHPRD-phosPhosphoSite_ProtMapperKEA:12196520HPRD:12196520ProtMapper:12196520PhosphoSite:12196520HPRD-phos:12196520SIGNOR:12196520
CSK21P68400ABCA1O95477YesPhosphoNetworksphosphoELM_MIMPPhosphoSite_MIMPMIMPPhosphoSite_norefPhosphoPointiPTMnetProtMapperHPRDPhosphoSite_KEAKEAphosphoELM_KEAphosphoELMPhosphoSitePhosphoSite_ProtMapperHPRD:15218032PhosphoSite:15218032KEA:15218032phosphoELM:15218032

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometry22677501328590090
Sequence, Structure & Domains

Sequences

Length
2,261
Mass
254,302
Sequence
MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILHKVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPILRTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGSVYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTGITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAPVPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDAIKQMKKHLKLAKDSSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFGLAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV

3D Structural Models

Turn
240..245; 560..562; 582..585; 909..911; 964..966; 1000..1002; 1214..1216; 1229..1231; 1561..1563; 1568..1570; 1727..1729; 1732..1734; 1755..1759; 1846..1848; 1872..1875; 1922..1924; 1977..1979; 2197..2200
Helix
4..20; 22..44; 62..64; 66..75; 87..89; 101..117; 121..135; 200..209; 216..226; 230..233; 236..239; 253..274; 278..288; 299..308; 353..363; 369..379; 390..404; 405..409; 412..416; 419..426; 431..440; 445..453; 460..467; 484..501; 516..528; 587..590; 593..608; 631..643; 646..664; 667..674; 678..706; 715..737; 743..756; 759..767; 768..770; 773..779; 785..799; 821..845; 940..946; 968..972; 990..999; 1005..1019; 1030..1032; 1035..1045; 1065..1077; 1091..1096; 1115..1121; 1182..1190; 1218..1227; 1244..1253; 1322..1341; 1344..1350; 1352..1364; 1381..1383; 1401..1408; 1446..1449; 1505..1522; 1548..1560; 1571..1582; 1601..1617; 1644..1667; 1669..1671; 1672..1680; 1684..1690; 1695..1723; 1735..1753; 1763..1789; 1796..1807; 1811..1833; 1849..1871; 1893..1904; 1952..1960; 1981..1985; 2003..2014; 2018..2020; 2021..2030; 2042..2044; 2047..2058; 2077..2092; 2104..2109; 2128..2134; 2153..2162; 2187..2196; 2213..2223
Beta Strand
58..60; 90..92; 98..100; 212..215; 384..386; 441..444; 535..537; 541..545; 550..557; 616..621; 709..713; 782..784; 805..808; 849..851; 893..895; 899..906; 920..924; 929..933; 937..939; 948..950; 953..959; 975..978; 986..989; 1023..1025; 1052..1059; 1060..1062; 1080..1082; 1084..1087; 1099..1105; 1108..1113; 1126..1129; 1191..1193; 1195..1198; 1200..1202; 1205..1208; 1210..1213; 1239..1241; 1384..1386; 1388..1393; 1398..1400; 1414..1421; 1456..1458; 1487..1490; 1492..1494; 1496..1499; 1533..1539; 1587..1594; 1624..1626; 1628..1633; 1681..1683; 1911..1919; 1934..1936; 1940..1946; 1967..1974; 1989..1991; 2035..2037; 2038..2041; 2064..2070; 2071..2074; 2096..2100; 2112..2118; 2121..2123; 2140..2144; 2168..2170; 2173..2179; 2205..2211
3D Structure
Electron microscopy (7)

Domain & Motif Annotations

Compositional Bias
1287..1299; Acidic residues
Domain (CC)
Multifunctional polypeptide with two homologous halves, each containing a hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain.
Domain (FT)
899..1131; ABC transporter 1; 1912..2144; ABC transporter 2
Region
69..80; Annulus domain 1; 368..379; Annulus domain 2; 564..594; Gateway domain; 1283..1312; Disordered
Protein Families (2)
  • ABC transporter superfamily
  • ABCA family
Sequence Similarities
Belongs to the ABC transporter superfamily. ABCA family.
Clinical Relevance
Disease Involvement (3)
AtherosclerosisDisease variantFDA approved drug targets
Biomarker
Approved; Investigative; Discontinued in Phase 1
Drug Targets
FDA approved drug targets
Antibody (2)
Interaction Protein (2)
ENSG00000118137ENSG00000168807
Interaction Count
2
Interaction Dataset
intact_biogrid
Supporting Publications3
PMIDTitleRelated sentences
38113368In-Depth Proteome Profiling of Small Extracellular Vesicles Isolated from Cancer Cell Lines and Patient Serum.No related sentences available
38207106Proteomic, Metabolomic, and Fatty Acid Profiling of Small Extracellular Vesicles from Glioblastoma Stem-Like Cells and Their Role in Tumor Heterogeneity.No related sentences available
40189497Small extracellular vesicle-based one-step high-throughput microfluidic platform for epithelial ovarian cancer diagnosis.No related sentences available