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ATP-binding cassette sub-family A member 1 (ATP-binding cassette transporter 1) (ABC-1) (ATP-binding cassette 1) (Cholesterol efflux regulatory protein)

 ABCA1_HUMAN             Reviewed;        2261 AA.
O95477; Q5VX33; Q96S56; Q96T85; Q9NQV4; Q9UN06; Q9UN07; Q9UN08;
Q9UN09;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
22-NOV-2017, entry version 193.
RecName: Full=ATP-binding cassette sub-family A member 1;
AltName: Full=ATP-binding cassette transporter 1;
Short=ABC-1;
Short=ATP-binding cassette 1;
AltName: Full=Cholesterol efflux regulatory protein;
Name=ABCA1; Synonyms=ABC1, CERP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ARG-1587.
PubMed=10884428; DOI=10.1073/pnas.97.14.7987;
Santamarina-Fojo S., Peterson K.M., Knapper C.L., Qiu Y.,
Freeman L.A., Cheng J.-F., Osorio J., Remaley A.T., Yang X.-P.,
Haudenschild C.C., Prades C., Chimini G., Blackmon E.E.,
Francois T.L., Duverger N., Rubin E.M., Rosier M., Denefle P.,
Fredrickson D.S., Brewer H.B. Jr.;
"Complete genomic sequence of the human ABCA1 gene: analysis of the
human and mouse ATP-binding cassette A promoter.";
Proc. Natl. Acad. Sci. U.S.A. 97:7987-7992(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-1587.
TISSUE=Skin;
Schwartz K., Lawn R.M., Wade D.P.;
"ABCA1 gene expression and apoA-I-mediated cholesterol efflux are
regulated by LXR.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-1587.
PubMed=11352567; DOI=10.1006/geno.2000.6467;
Qiu Y., Cavelier L., Chiu S., Yang X., Rubin E., Cheng J.-F.;
"Human and mouse ABCA1 comparative sequencing and transgenesis studies
revealing novel regulatory sequences.";
Genomics 73:66-76(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Tanaka A.R., Abe-Dohmae S., Arakawa R., Sadanami K., Kidera A.,
Kioka N., Amachi T., Yokoyama S., Ueda K.;
"A new topological model of functional human ABCA1-signal peptide
cleavage and glycosylation of a large extracellular domain.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-2261, AND VARIANTS THR-1555;
ARG-1587; PRO-1648 AND PRO-2168.
PubMed=10092505; DOI=10.1006/bbrc.1999.0406;
Langmann T., Klucken J., Reil M., Liebisch G., Luciani M.-F.,
Chimini G., Kaminski W.E., Schmitz G.;
"Molecular cloning of the human ATP-binding cassette transporter 1
(hABC1): evidence for sterol-dependent regulation in macrophages.";
Biochem. Biophys. Res. Commun. 257:29-33(1999).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 21-2261, AND VARIANTS
THR-1555; ARG-1587; PRO-1648 AND PRO-2168.
PubMed=10431238; DOI=10.1038/11921;
Rust S., Rosier M., Funke H., Real J., Amoura Z., Piette J.-C.,
Deleuze J.-F., Brewer H.B. Jr., Duverger N., Denefle P., Assmann G.;
"Tangier disease is caused by mutations in the gene encoding ATP-
binding cassette transporter 1.";
Nat. Genet. 22:352-355(1999).
[8]
PHOSPHORYLATION AT SER-1042 AND SER-2054.
PubMed=12196520; DOI=10.1074/jbc.M204923200;
See R.H., Caday-Malcolm R.A., Singaraja R.R., Zhou S., Silverston A.,
Huber M.T., Moran J., James E.R., Janoo R., Savill J.M., Rigot V.,
Zhang L.H., Wang M., Chimini G., Wellington C.L., Tafuri S.R.,
Hayden M.R.;
"Protein kinase A site-specific phosphorylation regulates ATP-binding
cassette A1 (ABCA1)-mediated phospholipid efflux.";
J. Biol. Chem. 277:41835-41842(2002).
[9]
REPRESSION BY ZNF202.
PubMed=11279031; DOI=10.1074/jbc.M100218200;
Porsch-Oezcueruemez M., Langmann T., Heimerl S., Borsukova H.,
Kaminski W.E., Drobnik W., Honer C., Schumacher C., Schmitz G.;
"The zinc finger protein 202 (ZNF202) is a transcriptional repressor
of ATP binding cassette transporter A1 (ABCA1) and ABCG1 gene
expression and a modulator of cellular lipid efflux.";
J. Biol. Chem. 276:12427-12433(2001).
[10]
INDUCTION BY LPS.
PubMed=12032171;
Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.;
"Bacterial lipopolysaccharide induces expression of ABCA1 but not
ABCG1 via an LXR-independent pathway.";
J. Lipid Res. 43:952-959(2002).
[11]
INTERACTION WITH MEGF10.
PubMed=17205124; DOI=10.1371/journal.pone.0000120;
Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
Zhou Z., Chimini G.;
"Cooperation between engulfment receptors: the case of ABCA1 and
MEGF10.";
PLoS ONE 1:E120-E120(2006).
[12]
REVIEW ON VARIANTS.
PubMed=12763760; DOI=10.1161/01.ATV.0000078520.89539.77;
Singaraja R.R., Brunham L.R., Visscher H., Kastelein J.J.P.,
Hayden M.R.;
"Efflux and atherosclerosis: the clinical and biochemical impact of
variations in the ABCA1 gene.";
Arterioscler. Thromb. Vasc. Biol. 23:1322-1332(2003).
[13]
POLYMORPHISM, AND INVOLVEMENT IN HDLCQ13.
PubMed=18354102; DOI=10.1056/NEJMoa0706728;
Kathiresan S., Melander O., Anevski D., Guiducci C., Burtt N.P.,
Roos C., Hirschhorn J.N., Berglund G., Hedblad B., Groop L.,
Altshuler D.M., Newton-Cheh C., Orho-Melander M.;
"Polymorphisms associated with cholesterol and risk of cardiovascular
events.";
N. Engl. J. Med. 358:1240-1249(2008).
[14]
PALMITOYLATION AT CYS-3; CYS-23; CYS-1110 AND CYS-1111, AND
SUBCELLULAR LOCATION.
PubMed=19556522; DOI=10.1161/CIRCRESAHA.108.193011;
Singaraja R.R., Kang M.H., Vaid K., Sanders S.S., Vilas G.L.,
Arstikaitis P., Coutinho J., Drisdel R.C., El-Husseini Ael D.,
Green W.N., Berthiaume L., Hayden M.R.;
"Palmitoylation of ATP-binding cassette transporter A1 is essential
for its trafficking and function.";
Circ. Res. 105:138-147(2009).
[15]
DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
PubMed=19258317; DOI=10.1074/jbc.M900580200;
Hozoji M., Kimura Y., Kioka N., Ueda K.;
"Formation of two intramolecular disulfide bonds is necessary for
ApoA-I-dependent cholesterol efflux mediated by ABCA1.";
J. Biol. Chem. 284:11293-11300(2009).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98 AND ASN-244.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
VARIANTS HDLD2 THR-1091 AND 1893-GLU-ASP-1894 DEL.
PubMed=10533863; DOI=10.1016/S0140-6736(99)07026-9;
Marcil M., Brooks-Wilson A., Clee S.M., Roomp K., Zhang L.-H., Yu L.,
Collins J.A., van Dam M., Molhuizen H.O.F., Loubser O.,
Ouellette B.F.F., Sensen C.W., Fichter K., Mott S., Denis M.,
Boucher B., Pimstone S., Genest J. Jr., Kastelein J.J.P., Hayden M.R.;
"Mutations in the ABC1 gene in familial HDL deficiency with defective
cholesterol efflux.";
Lancet 354:1341-1346(1999).
[19]
VARIANTS HDLD1 ARG-597 AND ARG-1477, AND VARIANT HDLD2 LEU-693 DEL.
PubMed=10431236; DOI=10.1038/11905;
Brooks-Wilson A., Marcil M., Clee S.M., Zhang L.-H., Roomp K.,
van Dam M., Yu L., Brewer C., Collins J.A., Molhuizen H.O.F.,
Loubser O., Ouelette B.F.F., Fichter K., Ashbourne-Excoffon K.J.D.,
Sensen C.W., Scherer S., Mott S., Denis M., Martindale D.,
Frohlich J., Morgan K., Koop B., Pimstone S., Kastelein J.J.P.,
Hayden M.R.;
"Mutations in ABC1 in Tangier disease and familial high-density
lipoprotein deficiency.";
Nat. Genet. 22:336-345(1999).
[20]
VARIANTS HDLD1 SER-590; SER-935 AND VAL-937, AND VARIANTS ALA-399 AND
MET-883.
PubMed=10431237; DOI=10.1038/11914;
Bodzioch M., Orso E., Klucken J., Langmann T., Boettcher A.,
Diederich W., Drobnik W., Barlage S., Buechler C.,
Porsch-Oezcueruemez M., Kaminski W.E., Hahmann H.W., Oette K.,
Rothe G., Aslanidis C., Lackner K.J., Schmitz G.;
"The gene encoding ATP-binding cassette transporter 1 is mutated in
Tangier disease.";
Nat. Genet. 22:347-351(1999).
[21]
VARIANTS HDLD1 ARG-597; ILE-929 AND ARG-1477, AND VARIANTS HDLD2
LEU-693 DEL; THR-1091; 1893-GLU-ASP-1894 DEL AND LEU-2150.
PubMed=11086027; DOI=10.1172/JCI10727;
Clee S.M., Kastelein J.J.P., van Dam M., Marcil M., Roomp K.,
Zwarts K.Y., Collins J.A., Roelants R., Tamasawa N., Stulc T.,
Suda T., Ceska R., Boucher B., Rondeau C., DeSouich C.,
Brooks-Wilson A., Molhuizen H.O.F., Frohlich J., Genest J. Jr.,
Hayden M.R.;
"Age and residual cholesterol efflux affect HDL cholesterol levels and
coronary artery disease in ABCA1 heterozygotes.";
J. Clin. Invest. 106:1263-1270(2000).
[22]
VARIANTS HDLD1 ASN-1289 AND HIS-1800.
PubMed=10706591;
Brousseau M.E., Schaefer E.J., Dupuis J., Eustace B.,
Van Eerdewegh P., Goldkamp A.L., Thurston L.M., FitzGerald M.G.,
Yasek-McKenna D., O'Neill G., Eberhart G.P., Weiffenbach B.,
Ordovas J.M., Freeman M.W., Brown R.H. Jr., Gu J.Z.;
"Novel mutations in the gene encoding ATP-binding cassette 1 in four
tangier disease kindreds.";
J. Lipid Res. 41:433-441(2000).
[23]
VARIANT HDLD1 ASP-1046, AND VARIANTS LYS-219; CYS-230; ILE-825;
MET-883 AND ARG-1587.
PubMed=10938021; DOI=10.1161/01.ATV.20.8.1983;
Wang J., Burnett J.R., Near S., Young K., Zinman B., Hanley A.J.G.,
Connelly P.W., Harris S.B., Hegele R.A.;
"Common and rare ABCA1 variants affecting plasma HDL cholesterol.";
Arterioscler. Thromb. Vasc. Biol. 20:1983-1989(2000).
[24]
VARIANT HDLD1 TRP-587, AND VARIANT PRO-2168.
PubMed=11257260; DOI=10.1016/S0021-9150(00)00587-6;
Bertolini S., Pisciotta L., Seri M., Cusano R., Cantafora A.,
Calabresi L., Franceschini G., Ravazzolo R., Calandra S.;
"A point mutation in ABC1 gene in a patient with severe premature
coronary heart disease and mild clinical phenotype of Tangier
disease.";
Atherosclerosis 154:599-605(2001).
[25]
VARIANTS LYS-219; MET-883 AND ASP-1172.
PubMed=11257261; DOI=10.1016/S0021-9150(00)00722-X;
Brousseau M.E., Bodzioch M., Schaefer E.J., Goldkamp A.L., Kielar D.,
Probst M., Ordovas J.M., Aslanidis C., Lackner K.J.,
Bloomfield Rubins H., Collins D., Robins S.J., Wilson P.W.F.,
Schmitz G.;
"Common variants in the gene encoding ATP-binding cassette transporter
1 in men with low HDL cholesterol levels and coronary heart disease.";
Atherosclerosis 154:607-611(2001).
[26]
VARIANT HDLD1 LEU-1506.
PubMed=11476961; DOI=10.1016/S0925-4439(01)00053-9;
Lapicka-Bodzioch K., Bodzioch M., Kruell M., Kielar D., Probst M.,
Kiec B., Andrikovics H., Boettcher A., Hubacek J., Aslanidis C.,
Suttorp N., Schmitz G.;
"Homogeneous assay based on 52 primer sets to scan for mutations of
the ABCA1 gene and its application in genetic analysis of a new
patient with familial high-density lipoprotein deficiency syndrome.";
Biochim. Biophys. Acta 1537:42-48(2001).
[27]
VARIANTS HDLD1 ASN-1289 AND TRP-2081, AND VARIANT LYS-219.
PubMed=11476965; DOI=10.1016/S0925-4439(01)00058-8;
Huang W., Moriyama K., Koga T., Hua H., Ageta M., Kawabata S.,
Mawatari K., Imamura T., Eto T., Kawamura M., Teramoto T., Sasaki J.;
"Novel mutations in ABCA1 gene in Japanese patients with Tangier
disease and familial high density lipoprotein deficiency with coronary
heart disease.";
Biochim. Biophys. Acta 1537:71-78(2001).
[28]
VARIANTS LYS-219; ALA-399; MET-771; PRO-774; ASN-776; ILE-825;
MET-883; ASP-1172; ARG-1587 AND CYS-1731.
PubMed=11238261; DOI=10.1161/01.CIR.103.9.1198;
Clee S.M., Zwinderman A.H., Engert J.C., Zwarts K.Y.,
Molhuizen H.O.F., Roomp K., Jukema J.W., van Wijland M., van Dam M.,
Hudson T.J., Brooks-Wilson A., Genest J. Jr., Kastelein J.J.P.,
Hayden M.R.;
"Common genetic variation in ABCA1 is associated with altered
lipoprotein levels and a modified risk for coronary artery disease.";
Circulation 103:1198-1205(2001).
[29]
VARIANT HDLD2 LEU-85.
PubMed=12204794; DOI=10.1016/S0021-9150(02)00106-5;
Hong S.H., Rhyne J., Zeller K., Miller M.;
"ABCA1(Alabama): a novel variant associated with HDL deficiency and
premature coronary artery disease.";
Atherosclerosis 164:245-250(2002).
[30]
VARIANTS HDLD2 TYR-1099 AND SER-2009.
PubMed=12009425; DOI=10.1016/S0925-4439(02)00066-2;
Hong S.H., Rhyne J., Zeller K., Miller M.;
"Novel ABCA1 compound variant associated with HDL cholesterol
deficiency.";
Biochim. Biophys. Acta 1587:60-64(2002).
[31]
VARIANT HDLD1 THR-255, AND VARIANT ATHEROSCLEROSIS ASP-1611.
PubMed=11785958; DOI=10.1006/bbrc.2001.6219;
Nishida Y., Hirano K., Tsukamoto K., Nagano M., Ikegami C., Roomp K.,
Ishihara M., Sakane N., Zhang Z., Tsujii K., Matsuyama A., Ohama T.,
Matsuura F., Ishigami M., Sakai N., Hiraoka H., Hattori H.,
Wellington C., Yoshida Y., Misugi S., Hayden M.R., Egashira T.,
Yamashita S., Matsuzawa Y.;
"Expression and functional analyses of novel mutations of ATP-binding
cassette transporter-1 in Japanese patients with high-density
lipoprotein deficiency.";
Biochem. Biophys. Res. Commun. 290:713-721(2002).
[32]
VARIANT HDLD1 LEU-590.
PubMed=12407001;
Hong S.H., Riley W., Rhyne J., Friel G., Miller M.;
"Lack of association between increased carotid intima-media thickening
and decreased HDL-cholesterol in a family with a novel ABCA1 variant,
G2265T.";
Clin. Chem. 48:2066-2070(2002).
[33]
VARIANTS HDLD1 HIS-935 AND SER-935.
PubMed=12111381; DOI=10.1007/s100380200044;
Guo Z., Inazu A., Yu W., Suzumura T., Okamoto M., Nohara A.,
Higashikata T., Sano R., Wakasugi K., Hayakawa T., Yoshida K.,
Suehiro T., Schmitz G., Mabuchi H.;
"Double deletions and missense mutations in the first nucleotide-
binding fold of the ATP-binding cassette transporter A1 (ABCA1) gene
in Japanese patients with Tangier disease.";
J. Hum. Genet. 47:325-329(2002).
[34]
VARIANT HDLD1 TRP-1680.
PubMed=12111371; DOI=10.1007/s100380200051;
Ishii J., Nagano M., Kujiraoka T., Ishihara M., Egashira T.,
Takada D., Tsuji M., Hattori H., Emi M.;
"Clinical variant of Tangier disease in Japan: mutation of the ABCA1
gene in hypoalphalipoproteinemia with corneal lipidosis.";
J. Hum. Genet. 47:366-369(2002).
[35]
VARIANT HDLD1 GLN-1851.
PubMed=14576201; DOI=10.1161/01.RES.0000102957.84247.8F;
Hong S.H., Rhyne J., Miller M.;
"Novel polypyrimidine variation (IVS46: del T -39._.-46) in ABCA1
causes exon skipping and contributes to HDL cholesterol deficiency in
a family with premature coronary disease.";
Circ. Res. 93:1006-1012(2003).
[36]
VARIANTS ILE-825 AND MET-883, AND ASSOCIATION OF VARIANTS ILE-825 AND
MET-883 WITH HIGHER PLASMA HDL CHOLESTEROL.
PubMed=12709788; DOI=10.1007/s00439-003-0943-3;
Tan J.H., Low P.S., Tan Y.S., Tong M.C., Saha N., Yang H., Heng C.K.;
"ABCA1 gene polymorphisms and their associations with coronary artery
disease and plasma lipids in males from three ethnic populations in
Singapore.";
Hum. Genet. 113:106-117(2003).
[37]
VARIANTS LYS-219; MET-771; ILE-825; MET-883; ASP-1172; PHE-1181 AND
ARG-1587.
PubMed=12966036; DOI=10.1093/hmg/ddg314;
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
Alvin G.B., Das K., Gilliam T.C.;
"Association of extreme blood lipid profile phenotypic variation with
11 reverse cholesterol transport genes and 10 non-genetic
cardiovascular disease risk factors.";
Hum. Mol. Genet. 12:2733-2743(2003).
[38]
VARIANT LYS-219.
PubMed=12624133; DOI=10.1136/jmg.40.3.163;
Cenarro A., Artieda M., Castillo S., Mozas P., Reyes G., Tejedor D.,
Alonso R., Mata P., Pocovi M., Civeira F.;
"A common variant in the ABCA1 gene is associated with a lower risk
for premature coronary heart disease in familial
hypercholesterolaemia.";
J. Med. Genet. 40:163-168(2003).
[39]
VARIANTS HDLD1 LEU-590; ARG-840 AND CYS-1068, AND VARIANTS MET-771;
SER-2163 AND ILE-2244.
PubMed=15262183; DOI=10.1016/j.atherosclerosis.2004.02.019;
Probst M.C., Thumann H., Aslanidis C., Langmann T., Buechler C.,
Patsch W., Baralle F.E., Dallinga-Thie G.M., Geisel J., Keller C.,
Menys V.C., Schmitz G.;
"Screening for functional sequence variations and mutations in
ABCA1.";
Atherosclerosis 175:269-279(2004).
[40]
VARIANTS HDLD1 LYS-284; CYS-482; HIS-1800; SER-1901 AND HIS-2196.
PubMed=15019541; DOI=10.1016/j.atherosclerosis.2003.11.009;
Pisciotta L., Hamilton-Craig I., Tarugi P., Bellocchio A., Fasano T.,
Alessandrini P., Bon G.B., Siepi D., Mannarino E., Cattin L.,
Averna M., Cefalu A.B., Cantafora A., Calandra S., Bertolini S.;
"Familial HDL deficiency due to ABCA1 gene mutations with or without
other genetic lipoprotein disorders.";
Atherosclerosis 172:309-320(2004).
[41]
VARIANTS HDLD1 PHE-1379 AND ASP-1704, AND CHARACTERIZATION OF VARIANTS
HDLD1 PHE-1379 AND ASP-1704.
PubMed=15158913; DOI=10.1016/j.bbadis.2004.01.007;
Albrecht C., Baynes K., Sardini A., Schepelmann S., Eden E.R.,
Davies S.W., Higgins C.F., Feher M.D., Owen J.S., Soutar A.K.;
"Two novel missense mutations in ABCA1 result in altered trafficking
and cause severe autosomal recessive HDL deficiency.";
Biochim. Biophys. Acta 1689:47-57(2004).
[42]
VARIANT HDLD1 HIS-1800, AND VARIANTS LYS-219; CYS-364; MET-771;
PRO-774; ASN-776; ILE-825; MET-883; SER-1065; ASP-1172; VAL-1216 AND
ARG-1587.
PubMed=15520867; DOI=10.1172/JCI200420361;
Frikke-Schmidt R., Nordestgaard B.G., Jensen G.B., Tybjaerg-Hansen A.;
"Genetic variation in ABC transporter A1 contributes to HDL
cholesterol in the general population.";
J. Clin. Invest. 114:1343-1353(2004).
[43]
VARIANT HDLD1 HIS-1800, AND VARIANTS ALA-248; GLN-401; TRP-496;
SER-590; GLN-638; SER-774; GLY-815; PHE-1181; THR-1341; GLY-1376;
GLN-1615; THR-1670; GLN-1680 AND GLU-2243.
PubMed=15297675; DOI=10.1126/science.1099870;
Cohen J.C., Kiss R.S., Pertsemlidis A., Marcel Y.L., McPherson R.,
Hobbs H.H.;
"Multiple rare alleles contribute to low plasma levels of HDL
cholesterol.";
Science 305:869-872(2004).
[44]
VARIANT SCOTT SYNDROME GLN-1925, AND CHARACTERIZATION OF VARIANT SCOTT
SYNDROME GLN-1925.
PubMed=15790791; DOI=10.1182/blood-2004-05-2056;
Albrecht C., McVey J.H., Elliott J.I., Sardini A., Kasza I.,
Mumford A.D., Naoumova R.P., Tuddenham E.G., Szabo K., Higgins C.F.;
"A novel missense mutation in ABCA1 results in altered protein
trafficking and reduced phosphatidylserine translocation in a patient
with Scott syndrome.";
Blood 106:542-549(2005).
[45]
VARIANT ASN-776, AND ASSOCIATION OF VARIANT ASN-776 WITH INCREASED
RISK OF ISCHEMIC HEART DISEASE.
PubMed=16226177; DOI=10.1016/j.jacc.2005.06.066;
Frikke-Schmidt R., Nordestgaard B.G., Schnohr P., Steffensen R.,
Tybjaerg-Hansen A.;
"Mutation in ABCA1 predicted risk of ischemic heart disease in the
Copenhagen City Heart Study Population.";
J. Am. Coll. Cardiol. 46:1516-1520(2005).
[46]
VARIANT HDLD2 TRP-1897.
PubMed=15722566; DOI=10.1194/jlr.D400038-JLR200;
Fasano T., Bocchi L., Pisciotta L., Bertolini S., Calandra S.;
"Denaturing high-performance liquid chromatography in the detection of
ABCA1 gene mutations in familial HDL deficiency.";
J. Lipid Res. 46:817-822(2005).
[47]
VARIANTS [LARGE SCALE ANALYSIS] ASP-210; TYR-917; THR-1407 AND
THR-2109.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[48]
VARIANT CYS-230.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: cAMP-dependent and sulfonylurea-sensitive anion
transporter. Key gatekeeper influencing intracellular cholesterol
transport.
-!- SUBUNIT: Interacts with MEGF10. {ECO:0000269|PubMed:17205124}.
-!- INTERACTION:
Q86UK0:ABCA12; NbExp=4; IntAct=EBI-784112, EBI-9541582;
P02647:APOA1; NbExp=4; IntAct=EBI-784112, EBI-701692;
P27824:CANX; NbExp=8; IntAct=EBI-784112, EBI-355947;
P60953:CDC42; NbExp=2; IntAct=EBI-784112, EBI-81752;
P55055:NR1H2; NbExp=2; IntAct=EBI-784112, EBI-745354;
Q13424:SNTA1; NbExp=2; IntAct=EBI-784112, EBI-717191;
Q13884:SNTB1; NbExp=3; IntAct=EBI-784112, EBI-295843;
Q86Y82:STX12; NbExp=9; IntAct=EBI-784112, EBI-2691717;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19258317,
ECO:0000269|PubMed:19556522}; Multi-pass membrane protein
{ECO:0000269|PubMed:19258317, ECO:0000269|PubMed:19556522}.
-!- TISSUE SPECIFICITY: Widely expressed, but most abundant in
macrophages.
-!- INDUCTION: By bacterial lipopolysaccharides (LPS). LPS regulates
expression through a liver X receptor (LXR) -independent
mechanism. Repressed by ZNF202. {ECO:0000269|PubMed:11279031,
ECO:0000269|PubMed:12032171}.
-!- DOMAIN: Multifunctional polypeptide with two homologous halves,
each containing a hydrophobic membrane-anchoring domain and an ATP
binding cassette (ABC) domain.
-!- PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux.
{ECO:0000269|PubMed:12196520}.
-!- PTM: Palmitoylation by DHHC8 is essential for membrane
localization. {ECO:0000269|PubMed:19556522}.
-!- POLYMORPHISM: Genetic variations in ABCA1 define the high density
lipoprotein cholesterol level quantitative trait locus 13
(HDLCQ13) [MIM:600046]. {ECO:0000269|PubMed:18354102}.
-!- DISEASE: High density lipoprotein deficiency 1 (HDLD1)
[MIM:205400]: Recessive disorder characterized by absence of high
density lipoprotein (HDL) cholesterol from plasma, accumulation of
cholesteryl esters, premature coronary artery disease (CAD),
hepatosplenomegaly, recurrent peripheral neuropathy and
progressive muscle wasting and weakness.
{ECO:0000269|PubMed:10431236, ECO:0000269|PubMed:10431237,
ECO:0000269|PubMed:10706591, ECO:0000269|PubMed:10938021,
ECO:0000269|PubMed:11086027, ECO:0000269|PubMed:11257260,
ECO:0000269|PubMed:11476961, ECO:0000269|PubMed:11476965,
ECO:0000269|PubMed:11785958, ECO:0000269|PubMed:12111371,
ECO:0000269|PubMed:12111381, ECO:0000269|PubMed:12407001,
ECO:0000269|PubMed:14576201, ECO:0000269|PubMed:15019541,
ECO:0000269|PubMed:15158913, ECO:0000269|PubMed:15262183,
ECO:0000269|PubMed:15297675, ECO:0000269|PubMed:15520867}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: High density lipoprotein deficiency 2 (HDLD2)
[MIM:604091]: Inherited as autosomal dominant trait. It is
characterized by moderately low HDL cholesterol, predilection
toward premature coronary artery disease (CAD) and a reduction in
cellular cholesterol efflux. {ECO:0000269|PubMed:10431236,
ECO:0000269|PubMed:10533863, ECO:0000269|PubMed:11086027,
ECO:0000269|PubMed:12009425, ECO:0000269|PubMed:12204794,
ECO:0000269|PubMed:15722566}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD49849.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA10005.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=ABCA1";
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=O95477";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF275948; AAF86276.1; -; Genomic_DNA.
EMBL; AL353685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF285167; AAF98175.1; -; mRNA.
EMBL; AF287262; AAK43526.1; -; Genomic_DNA.
EMBL; AB055982; BAB63210.1; -; mRNA.
EMBL; AJ012376; CAA10005.1; ALT_INIT; mRNA.
EMBL; AF165281; AAD49849.1; ALT_INIT; mRNA.
EMBL; AF165286; AAD49851.1; -; Genomic_DNA.
EMBL; AF165282; AAD49851.1; JOINED; Genomic_DNA.
EMBL; AF165283; AAD49851.1; JOINED; Genomic_DNA.
EMBL; AF165284; AAD49851.1; JOINED; Genomic_DNA.
EMBL; AF165285; AAD49851.1; JOINED; Genomic_DNA.
EMBL; AF165306; AAD49852.1; -; Genomic_DNA.
EMBL; AF165287; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165288; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165289; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165290; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165291; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165292; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165293; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165294; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165295; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165296; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165297; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165298; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165299; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165300; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165301; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165302; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165303; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165304; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165305; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165309; AAD49854.1; -; Genomic_DNA.
EMBL; AF165307; AAD49854.1; JOINED; Genomic_DNA.
EMBL; AF165308; AAD49854.1; JOINED; Genomic_DNA.
EMBL; AF165310; AAD49853.1; -; Genomic_DNA.
CCDS; CCDS6762.1; -.
RefSeq; NP_005493.2; NM_005502.3.
UniGene; Hs.659274; -.
PDB; 5XJY; EM; 4.10 A; A=1-2261.
PDBsum; 5XJY; -.
ProteinModelPortal; O95477; -.
SMR; O95477; -.
BioGrid; 106537; 24.
DIP; DIP-29211N; -.
IntAct; O95477; 29.
MINT; MINT-239561; -.
STRING; 9606.ENSP00000363868; -.
ChEMBL; CHEMBL2362986; -.
DrugBank; DB00171; Adenosine triphosphate.
DrugBank; DB01016; Glyburide.
DrugBank; DB01599; Probucol.
SwissLipids; SLP:000000345; -.
TCDB; 3.A.1.211.14; the atp-binding cassette (abc) superfamily.
iPTMnet; O95477; -.
PhosphoSitePlus; O95477; -.
SwissPalm; O95477; -.
BioMuta; ABCA1; -.
EPD; O95477; -.
MaxQB; O95477; -.
PaxDb; O95477; -.
PeptideAtlas; O95477; -.
PRIDE; O95477; -.
Ensembl; ENST00000374736; ENSP00000363868; ENSG00000165029.
GeneID; 19; -.
KEGG; hsa:19; -.
UCSC; uc004bcl.4; human.
CTD; 19; -.
DisGeNET; 19; -.
EuPathDB; HostDB:ENSG00000165029.15; -.
GeneCards; ABCA1; -.
HGNC; HGNC:29; ABCA1.
HPA; CAB069889; -.
HPA; HPA057283; -.
MalaCards; ABCA1; -.
MIM; 205400; phenotype.
MIM; 600046; gene+phenotype.
MIM; 604091; phenotype.
neXtProt; NX_O95477; -.
OpenTargets; ENSG00000165029; -.
Orphanet; 425; Apolipoprotein A-I deficiency.
Orphanet; 31150; Tangier disease.
PharmGKB; PA24373; -.
eggNOG; KOG0059; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00760000118965; -.
HOVERGEN; HBG050436; -.
InParanoid; O95477; -.
KO; K05641; -.
OMA; IQTISRF; -.
OrthoDB; EOG091G007E; -.
PhylomeDB; O95477; -.
TreeFam; TF105191; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-5682113; Defective ABCA1 causes Tangier disease.
Reactome; R-HSA-8963896; HDL assembly.
SignaLink; O95477; -.
SIGNOR; O95477; -.
ChiTaRS; ABCA1; human.
GeneWiki; ABCA1; -.
GenomeRNAi; 19; -.
PRO; PR:O95477; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165029; -.
ExpressionAtlas; O95477; baseline and differential.
Genevisible; O95477; HS.
GO; GO:0030139; C:endocytic vesicle; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0045335; C:phagocytic vesicle; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0008509; F:anion transmembrane transporter activity; ISS:BHF-UCL.
GO; GO:0034186; F:apolipoprotein A-I binding; IPI:BHF-UCL.
GO; GO:0034188; F:apolipoprotein A-I receptor activity; IDA:BHF-UCL.
GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
GO; GO:0016887; F:ATPase activity; IDA:BHF-UCL.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
GO; GO:0015485; F:cholesterol binding; IC:BHF-UCL.
GO; GO:0017127; F:cholesterol transporter activity; IDA:BHF-UCL.
GO; GO:0090554; F:phosphatidylcholine-translocating ATPase activity; IDA:BHF-UCL.
GO; GO:0090556; F:phosphatidylserine-translocating ATPase activity; IDA:BHF-UCL.
GO; GO:0005543; F:phospholipid binding; IC:BHF-UCL.
GO; GO:0005548; F:phospholipid transporter activity; IDA:BHF-UCL.
GO; GO:0005102; F:receptor binding; IPI:BHF-UCL.
GO; GO:0031267; F:small GTPase binding; IPI:BHF-UCL.
GO; GO:0019905; F:syntaxin binding; IPI:BHF-UCL.
GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
GO; GO:0016197; P:endosomal transport; IDA:BHF-UCL.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IMP:BHF-UCL.
GO; GO:0050702; P:interleukin-1 beta secretion; IMP:BHF-UCL.
GO; GO:0032367; P:intracellular cholesterol transport; IMP:BHF-UCL.
GO; GO:0007040; P:lysosome organization; IDA:BHF-UCL.
GO; GO:0010887; P:negative regulation of cholesterol storage; TAS:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; TAS:BHF-UCL.
GO; GO:0006911; P:phagocytosis, engulfment; IEA:Ensembl.
GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
GO; GO:0055091; P:phospholipid homeostasis; IMP:BHF-UCL.
GO; GO:0045332; P:phospholipid translocation; IDA:BHF-UCL.
GO; GO:0060155; P:platelet dense granule organization; IMP:BHF-UCL.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IMP:BHF-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
GO; GO:0006497; P:protein lipidation; IEA:Ensembl.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IMP:BHF-UCL.
GO; GO:0090107; P:regulation of high-density lipoprotein particle assembly; TAS:BHF-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0034616; P:response to laminar fluid shear stress; IEP:BHF-UCL.
GO; GO:0055098; P:response to low-density lipoprotein particle stimulus; IEP:BHF-UCL.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR026082; ABC_A.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR19229; PTHR19229; 1.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
3D-structure; Atherosclerosis; ATP-binding; Cholesterol metabolism;
Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
Lipid metabolism; Lipoprotein; Membrane; Nucleotide-binding;
Palmitate; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Steroid metabolism; Sterol metabolism; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 2261 ATP-binding cassette sub-family A member
1.
/FTId=PRO_0000093288.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 639 Extracellular.
TRANSMEM 640 660 Helical. {ECO:0000255}.
TRANSMEM 683 703 Helical. {ECO:0000255}.
TRANSMEM 716 736 Helical. {ECO:0000255}.
TRANSMEM 745 765 Helical. {ECO:0000255}.
TRANSMEM 777 797 Helical. {ECO:0000255}.
TRANSMEM 827 847 Helical. {ECO:0000255}.
TRANSMEM 1041 1057 Helical. {ECO:0000255}.
TRANSMEM 1351 1371 Helical. {ECO:0000255}.
TOPO_DOM 1372 1656 Extracellular.
TRANSMEM 1657 1677 Helical. {ECO:0000255}.
TRANSMEM 1703 1723 Helical. {ECO:0000255}.
TRANSMEM 1735 1755 Helical. {ECO:0000255}.
TRANSMEM 1768 1788 Helical. {ECO:0000255}.
TRANSMEM 1802 1822 Helical. {ECO:0000255}.
TRANSMEM 1852 1872 Helical. {ECO:0000255}.
DOMAIN 899 1131 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 1912 2144 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 933 940 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1946 1953 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 1042 1042 Phosphoserine; by PKA.
{ECO:0000269|PubMed:12196520}.
MOD_RES 1296 1296 Phosphoserine.
{ECO:0000250|UniProtKB:P41233}.
MOD_RES 2054 2054 Phosphoserine; by PKA.
{ECO:0000269|PubMed:12196520}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000269|PubMed:19556522}.
LIPID 23 23 S-palmitoyl cysteine.
{ECO:0000269|PubMed:19556522}.
LIPID 1110 1110 S-palmitoyl cysteine.
{ECO:0000269|PubMed:19556522}.
LIPID 1111 1111 S-palmitoyl cysteine.
{ECO:0000269|PubMed:19556522}.
CARBOHYD 14 14 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 489 489 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 521 521 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 820 820 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1144 1144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1294 1294 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1453 1453 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1504 1504 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1637 1637 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2044 2044 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2238 2238 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 75 309 {ECO:0000269|PubMed:19258317}.
DISULFID 1463 1477 {ECO:0000269|PubMed:19258317}.
VARIANT 85 85 P -> L (in HDLD2; Alabama;
dbSNP:rs145183203).
{ECO:0000269|PubMed:12204794}.
/FTId=VAR_017529.
VARIANT 210 210 E -> D (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035724.
VARIANT 219 219 R -> K (common polymorphism; associated
with a decreased severity of CAD;
dbSNP:rs2230806).
{ECO:0000269|PubMed:10938021,
ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:11257261,
ECO:0000269|PubMed:11476965,
ECO:0000269|PubMed:12624133,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15520867}.
/FTId=VAR_012618.
VARIANT 230 230 R -> C (in dbSNP:rs9282541).
{ECO:0000269|PubMed:10938021,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_012619.
VARIANT 248 248 P -> A (in dbSNP:rs142625938).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062481.
VARIANT 255 255 A -> T (in HDLD1; deficient cellular
cholesterol efflux; dbSNP:rs758100110).
{ECO:0000269|PubMed:11785958}.
/FTId=VAR_012620.
VARIANT 284 284 E -> K (in HDLD1).
{ECO:0000269|PubMed:15019541}.
/FTId=VAR_062482.
VARIANT 364 364 S -> C (in dbSNP:rs775035559).
{ECO:0000269|PubMed:15520867}.
/FTId=VAR_062483.
VARIANT 399 399 V -> A (in dbSNP:rs9282543).
{ECO:0000269|PubMed:10431237,
ECO:0000269|PubMed:11238261}.
/FTId=VAR_009145.
VARIANT 401 401 K -> Q (in dbSNP:rs138487227).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062484.
VARIANT 482 482 Y -> C (in HDLD1).
{ECO:0000269|PubMed:15019541}.
/FTId=VAR_062485.
VARIANT 496 496 R -> W (associated with increased plasma
HDL cholesterol; dbSNP:rs147675550).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062486.
VARIANT 587 587 R -> W (in HDLD1; dbSNP:rs2853574).
{ECO:0000269|PubMed:11257260}.
/FTId=VAR_009146.
VARIANT 590 590 W -> L (in HDLD1; dbSNP:rs137854496).
{ECO:0000269|PubMed:12407001,
ECO:0000269|PubMed:15262183}.
/FTId=VAR_062487.
VARIANT 590 590 W -> S (in HDLD1; dbSNP:rs137854496).
{ECO:0000269|PubMed:10431237,
ECO:0000269|PubMed:15297675}.
/FTId=VAR_009147.
VARIANT 597 597 Q -> R (in HDLD1; dbSNP:rs2853578).
{ECO:0000269|PubMed:10431236,
ECO:0000269|PubMed:11086027}.
/FTId=VAR_009148.
VARIANT 638 638 R -> Q (associated with reduced plasma
HDL cholesterol; dbSNP:rs374190304).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062488.
VARIANT 693 693 Missing (in HDLD2).
{ECO:0000269|PubMed:10431236,
ECO:0000269|PubMed:11086027}.
/FTId=VAR_009149.
VARIANT 771 771 V -> M (associated with HDL cholesterol;
dbSNP:rs2066718).
{ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15262183,
ECO:0000269|PubMed:15520867}.
/FTId=VAR_012621.
VARIANT 774 774 T -> P (in dbSNP:rs35819696).
{ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:15520867}.
/FTId=VAR_012622.
VARIANT 774 774 T -> S. {ECO:0000269|PubMed:15297675}.
/FTId=VAR_062489.
VARIANT 776 776 K -> N (may be associated with increased
risk of ischemic heart disease;
dbSNP:rs138880920).
{ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:15520867,
ECO:0000269|PubMed:16226177}.
/FTId=VAR_012623.
VARIANT 815 815 E -> G (associated with reduced plasma
HDL cholesterol; dbSNP:rs145582736).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062490.
VARIANT 825 825 V -> I (associated with higher plasma
cholesterol; dbSNP:rs2066715).
{ECO:0000269|PubMed:10938021,
ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:12709788,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15520867}.
/FTId=VAR_012624.
VARIANT 840 840 W -> R (in HDLD1).
{ECO:0000269|PubMed:15262183}.
/FTId=VAR_062491.
VARIANT 883 883 I -> M (associated with higher plasma
cholesterol; dbSNP:rs2066714).
{ECO:0000269|PubMed:10431237,
ECO:0000269|PubMed:10938021,
ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:11257261,
ECO:0000269|PubMed:12709788,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15520867}.
/FTId=VAR_012625.
VARIANT 917 917 D -> Y (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035725.
VARIANT 929 929 T -> I (in HDLD1).
{ECO:0000269|PubMed:11086027}.
/FTId=VAR_012626.
VARIANT 935 935 N -> H (in HDLD1; dbSNP:rs28937314).
{ECO:0000269|PubMed:12111381}.
/FTId=VAR_037968.
VARIANT 935 935 N -> S (in HDLD1; dbSNP:rs28937313).
{ECO:0000269|PubMed:10431237,
ECO:0000269|PubMed:12111381}.
/FTId=VAR_009150.
VARIANT 937 937 A -> V (in HDLD1; dbSNP:rs137854495).
{ECO:0000269|PubMed:10431237}.
/FTId=VAR_009151.
VARIANT 1046 1046 A -> D (in HDLD1; dbSNP:rs141021096).
{ECO:0000269|PubMed:10938021}.
/FTId=VAR_012627.
VARIANT 1054 1054 V -> I (in dbSNP:rs13306072).
/FTId=VAR_037969.
VARIANT 1065 1065 P -> S. {ECO:0000269|PubMed:15520867}.
/FTId=VAR_062492.
VARIANT 1068 1068 R -> C (in HDLD1; dbSNP:rs745593394).
{ECO:0000269|PubMed:15262183}.
/FTId=VAR_062493.
VARIANT 1091 1091 M -> T (in HDLD2).
{ECO:0000269|PubMed:10533863,
ECO:0000269|PubMed:11086027}.
/FTId=VAR_012628.
VARIANT 1099 1099 D -> Y (in HDLD2; dbSNP:rs28933692).
{ECO:0000269|PubMed:12009425}.
/FTId=VAR_017530.
VARIANT 1172 1172 E -> D (associated with premature
coronary heart disease;
dbSNP:rs33918808).
{ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:11257261,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15520867}.
/FTId=VAR_012629.
VARIANT 1181 1181 S -> F (associated with reduced plasma
HDL cholesterol; dbSNP:rs76881554).
{ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15297675}.
/FTId=VAR_017016.
VARIANT 1216 1216 G -> V (in dbSNP:rs562403512).
{ECO:0000269|PubMed:15520867}.
/FTId=VAR_062494.
VARIANT 1289 1289 D -> N (in HDLD1; dbSNP:rs137854500).
{ECO:0000269|PubMed:10706591,
ECO:0000269|PubMed:11476965}.
/FTId=VAR_009152.
VARIANT 1341 1341 R -> T (associated with reduced plasma
HDL cholesterol; dbSNP:rs147743782).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062495.
VARIANT 1376 1376 S -> G (in dbSNP:rs145689805).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062496.
VARIANT 1379 1379 L -> F (in HDLD1; the mutant protein is
retained in the endoplasmic reticulum
while the wild-type protein is located at
the plasma membrane).
{ECO:0000269|PubMed:15158913}.
/FTId=VAR_062497.
VARIANT 1407 1407 A -> T (in a colorectal cancer sample;
somatic mutation; dbSNP:rs189206655).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035726.
VARIANT 1477 1477 C -> R (in HDLD1; dbSNP:rs137854494).
{ECO:0000269|PubMed:10431236,
ECO:0000269|PubMed:11086027}.
/FTId=VAR_009153.
VARIANT 1506 1506 S -> L (in HDLD1; dbSNP:rs137854497).
{ECO:0000269|PubMed:11476961}.
/FTId=VAR_012630.
VARIANT 1517 1517 I -> R (in HDLD1).
/FTId=VAR_009154.
VARIANT 1555 1555 I -> T (in dbSNP:rs1997618).
{ECO:0000269|PubMed:10092505,
ECO:0000269|PubMed:10431238}.
/FTId=VAR_012638.
VARIANT 1587 1587 K -> R (associated with HDL cholesterol;
dbSNP:rs2230808).
{ECO:0000269|PubMed:10092505,
ECO:0000269|PubMed:10431238,
ECO:0000269|PubMed:10884428,
ECO:0000269|PubMed:10938021,
ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:11352567,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15520867,
ECO:0000269|Ref.2}.
/FTId=VAR_012631.
VARIANT 1611 1611 N -> D (probable disease-associated
mutation; associated with
atherosclerosis; deficient cellular
cholesterol efflux).
{ECO:0000269|PubMed:11785958}.
/FTId=VAR_012632.
VARIANT 1615 1615 R -> Q (associated with reduced plasma
HDL cholesterol).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062498.
VARIANT 1648 1648 L -> P (in dbSNP:rs1883024).
{ECO:0000269|PubMed:10092505,
ECO:0000269|PubMed:10431238}.
/FTId=VAR_012639.
VARIANT 1670 1670 A -> T (associated with reduced plasma
HDL cholesterol).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062499.
VARIANT 1680 1680 R -> Q (associated with increased plasma
HDL cholesterol; dbSNP:rs150125857).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062500.
VARIANT 1680 1680 R -> W (in HDLD1; dbSNP:rs137854498).
{ECO:0000269|PubMed:12111371}.
/FTId=VAR_037970.
VARIANT 1704 1704 V -> D (in HDLD1; the mutant protein is
retained in the endoplasmic reticulum
while the wild-type protein is located at
the plasma membrane).
{ECO:0000269|PubMed:15158913}.
/FTId=VAR_062501.
VARIANT 1731 1731 S -> C (in dbSNP:rs760507032).
{ECO:0000269|PubMed:11238261}.
/FTId=VAR_012633.
VARIANT 1800 1800 N -> H (in HDLD1; dbSNP:rs146292819).
{ECO:0000269|PubMed:10706591,
ECO:0000269|PubMed:15019541,
ECO:0000269|PubMed:15297675,
ECO:0000269|PubMed:15520867}.
/FTId=VAR_009155.
VARIANT 1851 1851 R -> Q (in HDLD1).
{ECO:0000269|PubMed:14576201}.
/FTId=VAR_062502.
VARIANT 1893 1894 Missing (in HDLD2).
{ECO:0000269|PubMed:10533863,
ECO:0000269|PubMed:11086027}.
/FTId=VAR_012634.
VARIANT 1897 1897 R -> W (in HDLD2; uncertain pathological
significance; dbSNP:rs760768125).
{ECO:0000269|PubMed:15722566}.
/FTId=VAR_062503.
VARIANT 1901 1901 R -> S (in HDLD1).
{ECO:0000269|PubMed:15019541}.
/FTId=VAR_062504.
VARIANT 1925 1925 R -> Q (in Scott syndrome; shows impaired
trafficking of the mutant protein to the
plasma membrane; dbSNP:rs142688906).
{ECO:0000269|PubMed:15790791}.
/FTId=VAR_062505.
VARIANT 2009 2009 F -> S (in HDLD2; dbSNP:rs137854499).
{ECO:0000269|PubMed:12009425}.
/FTId=VAR_037971.
VARIANT 2081 2081 R -> W (in HDLD1; dbSNP:rs137854501).
{ECO:0000269|PubMed:11476965}.
/FTId=VAR_012635.
VARIANT 2109 2109 A -> T (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035727.
VARIANT 2150 2150 P -> L (in HDLD2; dbSNP:rs369098049).
{ECO:0000269|PubMed:11086027}.
/FTId=VAR_012636.
VARIANT 2163 2163 F -> S (could be associated with reduced
plasma HDL cholesterol).
{ECO:0000269|PubMed:15262183}.
/FTId=VAR_062506.
VARIANT 2168 2168 L -> P (in dbSNP:rs2853577).
{ECO:0000269|PubMed:10092505,
ECO:0000269|PubMed:10431238,
ECO:0000269|PubMed:11257260}.
/FTId=VAR_012637.
VARIANT 2196 2196 Q -> H (in HDLD1; dbSNP:rs564764153).
{ECO:0000269|PubMed:15019541}.
/FTId=VAR_062507.
VARIANT 2243 2243 D -> E (in dbSNP:rs34879708).
{ECO:0000269|PubMed:15297675}.
/FTId=VAR_062508.
VARIANT 2244 2244 V -> I (could be associated with reduced
plasma HDL cholesterol;
dbSNP:rs144588452).
{ECO:0000269|PubMed:15262183}.
/FTId=VAR_062509.
CONFLICT 793 793 Y -> C (in Ref. 3; AAK43526).
{ECO:0000305}.
CONFLICT 831 831 D -> N (in Ref. 3; AAK43526).
{ECO:0000305}.
CONFLICT 1005 1005 E -> K (in Ref. 3; AAK43526).
{ECO:0000305}.
CONFLICT 1745 1746 Missing (in Ref. 7; AAD49852).
{ECO:0000305}.
SEQUENCE 2261 AA; 254302 MW; 21A2CF8F3F518D6D CRC64;
MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE QHECHFPNKA
MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS IVARLFSDAR RLLLYSQKDT
SMKDMRKVLR TLQQIKKSSS NLKLQDFLVD NETFSGFLYH NLSLPKSTVD KMLRADVILH
KVFLQGYQLH LTSLCNGSKS EEMIQLGDQE VSELCGLPRE KLAAAERVLR SNMDILKPIL
RTLNSTSPFP SKELAEATKT LLHSLGTLAQ ELFSMRSWSD MRQEVMFLTN VNSSSSSTQI
YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNGTE EDAETFYDNS TTPYCNDLMK
NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN KTFQELAVFH DLEGMWEELS
PKIWTFMENS QEMDLVRMLL DSRDNDHFWE QQLDGLDWTA QDIVAFLAKH PEDVQSSNGS
VYTWREAFNE TNQAIRTISR FMECVNLNKL EPIATEVWLI NKSMELLDER KFWAGIVFTG
ITPGSIELPH HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV
EQAIIRVLTG TEKKTGVYMQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY SVAVIIKGIV
YEKEARLKET MRIMGLDNSI LWFSWFISSL IPLLVSAGLL VVILKLGNLL PYSDPSVVFV
FLSVFAVVTI LQCFLISTLF SRANLAAACG GIIYFTLYLP YVLCVAWQDY VGFTLKIFAS
LLSPVAFGFG CEYFALFEEQ GIGVQWDNLF ESPVEEDGFN LTTSVSMMLF DTFLYGVMTW
YIEAVFPGQY GIPRPWYFPC TKSYWFGEES DEKSHPGSNQ KRISEICMEE EPTHLKLGVS
IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF PPTSGTAYIL
GKDIRSEMST IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL KGLSEKHVKA EMEQMALDVG
LPSSKLKSKT SQLSGGMQRK LSVALAFVGG SKVVILDEPT AGVDPYSRRG IWELLLKYRQ
GRTIILSTHH MDEADVLGDR IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS
SCRNSSSTVS YLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI
GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK VAEESGVDAE
TSDGTLPARR NRRAFGDKQS CLRPFTEDDA ADPNDSDIDP ESRETDLLSG MDGKGSYQVK
GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ
PWMYNEQYTF VSNDAPEDTG TLELLNALTK DPGFGTRCME GNPIPDTPCQ AGEEEWTTAP
VPQTIMDLFQ NGNWTMQNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QNTADILQDL
TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NTQALPPSQE VNDAIKQMKK
HLKLAKDSSA DRFLNSLGRF MTGLDTKNNV KVWFNNKGWH AISSFLNVIN NAILRANLQK
GENPSHYGIT AFNHPLNLTK QQLSEVALMT TSVDVLVSIC VIFAMSFVPA SFVVFLIQER
VSKAKHLQFI SGVKPVIYWL SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL
LLLLYGWSIT PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTDNKLNNIN
DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG RNLFAMAVEG
VVFFLITVLI QYRFFIRPRP VNAKLSPLND EDEDVRRERQ RILDGGGQND ILEIKELTKI
YRRKRKPAVD RICVGIPPGE CFGLLGVNGA GKSSTFKMLT GDTTVTRGDA FLNKNSILSN
IHEVHQNMGY CPQFDAITEL LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK
YAGNYSGGNK RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSV VKEGRSVVLT
SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP DLKPVQDFFG
LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR LHIEDYSVSQ TTLDQVFVNF
AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF LQDEKVKESY V


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