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)

Protein symbol
ABCA1
UniProt ID
EVMP score
0.50
Frequency
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
Disease related genesEnzymesFDA approved drug targetsHuman disease related genesMetabolic proteinsPlasma proteinsPredicted intracellular proteinsPredicted membrane proteinsTransporters
Protein Function
  • 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
ABC1HDLDT1TGD
Gene Description
ATP binding cassette subfamily A member 1
Chromosome
9
Position
104781006-104928155
Frequency
3
EVMP Score
0.50
Fluorescence & Localization
Cell SpecificBergmann gliaSingle-Nuclei Brain Specificendothelial cellSecretome LocationIntracellular and membraneSecretome FunctionNo annotated function
Function & Pathway
Protein Function
  • 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
Clinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

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
Page 2 of 2Previous

Ligand-Receptor Signaling

32 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
extracellularextracellularDGIdbNoNoNoNoNo
extracellularextracellularOmniPathNoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
cell_surface_ligandcell_surface_ligandBaccin2019YesNoNoNoNo
cell_surface_ligandcell_surface_ligandCellPhoneDBYesNoNoNoNo
cell_surface_ligandcell_surface_ligandOmniPathYesNoNoNoNo
transportertransporterSurfaceomeNoYesNoNoNo
Page 1 of 4Next

Regulatory Interaction Network

8 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
ABCA1O95477MEG10Q96KG7YesYesNoSIGNORSIGNOR:17205124
MEG10Q96KG7ABCA1O95477YesYesNoCellTalkDBSIGNORCellTalkDB:17205124SIGNOR:17205124
EGFRP00533ABCA1O95477YesNoYesPhosphoSite_norefSIGNORiPTMnetProtMapperSIGNOR_ProtMapperPhosphoSite_ProtMapperSIGNOR:12196520ProtMapper:12196520
LNX1Q8TBB1ABCA1O95477YesNoYesSIGNORSIGNOR:22889411
ABCA1O95477APOA1P02647YesYesNoCellPhoneDBSIGNORHPRDHINTIntActInnateDBHPRD:12084722InnateDB:22271762IntAct:12084722SIGNOR:15347662HINT:12084722HINT:22271762IntAct:30458687
APOA1P02647ABCA1O95477YesYesNoCellChatDBCellTalkDBCellPhoneDBSIGNORHPRDHINTIntActInnateDBHPRD:12084722CellTalkDB:27100352InnateDB:22271762IntAct:12084722HINT:12084722HINT:22271762SIGNOR:12869555CellChatDB:20064972IntAct:30458687
KAPCAP17612ABCA1O95477YesYesNophosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperHPRDReactome_ProtMapperPhosphoSite_KEAKEAHPRD_KEASIGNOR_ProtMapperPhosphoSiteHPRD-phosPhosphoSite_ProtMapperKEA:12196520HPRD:12196520ProtMapper:12196520PhosphoSite:12196520HPRD-phos:12196520SIGNOR:12196520
CSK21P68400ABCA1O95477YesNoNoPhosphoNetworksphosphoELM_MIMPPhosphoSite_MIMPMIMPPhosphoSite_norefPhosphoPointiPTMnetProtMapperHPRDPhosphoSite_KEAKEAphosphoELM_KEAphosphoELMPhosphoSitePhosphoSite_ProtMapperHPRD:15218032PhosphoSite:15218032KEA:15218032phosphoELM:15218032

Protein Complex Composition

0 records.

Isolation & Detection Technology

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
  • ABC transporter superfamily
  • ABCA family
Sequence Similarities
Belongs to the ABC transporter superfamily. ABCA family.
Clinical Relevance
Disease Involvement
AtherosclerosisDisease variantFDA approved drug targets
Biomarker
Approved; Investigative; Discontinued in Phase 1
Drug Targets
FDA approved drug targets
Interaction Protein
ENSG00000118137ENSG00000168807
Interaction Count
2
Interaction Dataset
intact_biogrid