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Multidrug resistance-associated protein 1 (ATP-binding cassette sub-family C member 1) (Leukotriene C(4) transporter) (LTC4 transporter)

 MRP1_HUMAN              Reviewed;        1531 AA.
P33527; A3RJX2; C9JPJ4; O14819; O43333; P78419; Q59GI9; Q9UQ97;
Q9UQ99; Q9UQA0;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
25-OCT-2017, entry version 189.
RecName: Full=Multidrug resistance-associated protein 1;
AltName: Full=ATP-binding cassette sub-family C member 1;
AltName: Full=Leukotriene C(4) transporter;
Short=LTC4 transporter;
Name=ABCC1; Synonyms=MRP, MRP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-117.
PubMed=1360704; DOI=10.1126/science.1360704;
Cole S.P.C., Bhardwaj G., Gerlach J.H., Mackie J.E., Grant C.E.,
Almquist K.C., Stewart A.J., Kurz E.U., Duncan A.M.V., Deeley R.G.;
"Overexpression of a transporter gene in a multidrug-resistant human
lung cancer cell line.";
Science 258:1650-1654(1992).
[2]
SEQUENCE REVISION.
PubMed=8098549; DOI=10.1126/science.8098549;
Cole S.P.C., Deeley R.G.;
"Multidrug resistance-associated protein: sequence correction.";
Science 260:879-879(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANT
THR-117.
PubMed=9344662; DOI=10.1006/geno.1997.4950;
Grant C.E., Kurz E.U., Cole S.P.C., Deeley R.G.;
"Analysis of the intron-exon organization of the human multidrug-
resistance protein gene (MRP) and alternative splicing of its mRNA.";
Genomics 45:368-378(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-671; GLN-723;
THR-861; SER-1047 AND ILE-1146.
NIEHS SNPs program;
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-1531 (ISOFORM 9).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 516-1531.
PubMed=10493829; DOI=10.1006/geno.1999.5927;
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
Harris P.C., Venter J.C., Adams M.D.;
"Genome duplications and other features in 12 Mb of DNA sequence from
human chromosome 16p and 16q.";
Genomics 60:295-308(1999).
[8]
TOPOLOGY, AND GLYCOSYLATION AT ASN-19; ASN-23 AND ASN-1006.
PubMed=9295302; DOI=10.1074/jbc.272.38.23623;
Hipfner D.R., Almquist K.C., Leslie E.M., Gerlach J.H., Grant C.E.,
Deeley R.G., Cole S.P.C.;
"Membrane topology of the multidrug resistance protein (MRP). A study
of glycosylation-site mutants reveals an extracytosolic NH2
terminus.";
J. Biol. Chem. 272:23623-23630(1997).
[9]
TOPOLOGY.
PubMed=9334225; DOI=10.1074/jbc.272.42.26479;
Kast C., Gros P.;
"Topology mapping of the amino-terminal half of multidrug resistance-
associated protein by epitope insertion and immunofluorescence.";
J. Biol. Chem. 272:26479-26487(1997).
[10]
TOPOLOGY.
PubMed=9485377; DOI=10.1021/bi972332v;
Kast C., Gros P.;
"Epitope insertion favors a six transmembrane domain model for the
carboxy-terminal portion of the multidrug resistance-associated
protein.";
Biochemistry 37:2305-2313(1998).
[11]
FUNCTION.
PubMed=10064732;
Sjoelinder M., Tornhamre S., Claesson H.-E., Hydman J., Lindgren J.A.;
"Characterization of a leukotriene C4 export mechanism in human
platelets: possible involvement of multidrug resistance-associated
protein 1.";
J. Lipid Res. 40:439-446(1999).
[12]
FUNCTION.
PubMed=11114332; DOI=10.1016/S0092-8674(00)00179-3;
Robbiani D.F., Finch R.A., Jaeger D., Muller W.A., Sartorelli A.C.,
Randolph G.J.;
"The leukotriene C(4) transporter MRP1 regulates CCL19 (MIP-3beta,
ELC)-dependent mobilization of dendritic cells to lymph nodes.";
Cell 103:757-768(2000).
[13]
MUTAGENESIS OF ASP-792; ASP-793; LYS-1333 AND 1454-ASP-GLU-1455.
PubMed=11469806; DOI=10.1006/abbi.2001.2441;
Cui L., Hou Y.-X., Riordan J.R., Chang X.-B.;
"Mutations of the Walker B motif in the first nucleotide binding
domain of multidrug resistance protein MRP1 prevent conformational
maturation.";
Arch. Biochem. Biophys. 392:153-161(2001).
[14]
MUTAGENESIS OF TRP-1246.
PubMed=11278867; DOI=10.1074/jbc.M011246200;
Ito K., Olsen S.L., Qiu W., Deeley R.G., Cole S.P.C.;
"Mutation of a single conserved tryptophan in multidrug resistance
protein 1 (MRP1/ABCC1) results in loss of drug resistance and
selective loss of organic anion transport.";
J. Biol. Chem. 276:15616-15624(2001).
[15]
MUTAGENESIS OF GLU-1089.
PubMed=11278596; DOI=10.1074/jbc.M010008200;
Zhang D.-W., Cole S.P.C., Deeley R.G.;
"Identification of an amino acid residue in multidrug resistance
protein 1 critical for conferring resistance to anthracyclines.";
J. Biol. Chem. 276:13231-13239(2001).
[16]
MUTAGENESIS OF ARG-1046; ASP-1084 AND ARG-1131.
PubMed=15208328; DOI=10.1074/jbc.M403832200;
Situ D., Haimeur A., Conseil G., Sparks K.E., Zhang D.-W.,
Deeley R.G., Cole S.P.C.;
"Mutational analysis of ionizable residues proximal to the cytoplasmic
interface of membrane spanning domain 3 of the multidrug resistance
protein, MRP1 (ABCC1): glutamate 1204 is important for both the
expression and catalytic activity of the transporter.";
J. Biol. Chem. 279:38871-38880(2004).
[17]
MUTAGENESIS OF GLN-580; THR-581; SER-585; ASN-597; SER-604 AND
SER-605.
PubMed=15260484; DOI=10.1021/bi0495230;
Zhang D.-W., Nunoya K., Vasa M., Gu H.-M., Theis A., Cole S.P.C.,
Deeley R.G.;
"Transmembrane helix 11 of multidrug resistance protein 1
(MRP1/ABCC1): identification of polar amino acids important for
substrate specificity and binding of ATP at nucleotide binding domain
1.";
Biochemistry 43:9413-9425(2004).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[19]
FUNCTION, MUTAGENESIS OF ARG-1138; LYS-1141 AND ARG-1142, AND
SUBCELLULAR LOCATION.
PubMed=16230346; DOI=10.1074/jbc.M510143200;
Conseil G., Deeley R.G., Cole S.P.;
"Functional importance of three basic residues clustered at the
cytosolic interface of transmembrane helix 15 in the multidrug and
organic anion transporter MRP1 (ABCC1).";
J. Biol. Chem. 281:43-50(2006).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905 AND SER-930, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
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).
[28]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 642-871 IN COMPLEX WITH
MG-ATP.
PubMed=16697012; DOI=10.1016/j.jmb.2006.04.005;
Ramaen O., Leulliot N., Sizun C., Ulryck N., Pamlard O.,
Lallemand J.-Y., Tilbeurgh H., Jacquet E.;
"Structure of the human multidrug resistance protein 1 nucleotide
binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic
site.";
J. Mol. Biol. 359:940-949(2006).
[29]
VARIANTS GLN-633 AND VAL-671.
PubMed=10835642; DOI=10.1038/76102;
Le Saux O., Urban Z., Tschuch C., Csiszar K., Bacchelli B.,
Quaglino D., Pasquali-Ronchetti I., Pope F.M., Richards A., Terry S.,
Bercovitch L., de Paepe A., Boyd C.D.;
"Mutations in a gene encoding an ABC transporter cause pseudoxanthoma
elasticum.";
Nat. Genet. 25:223-227(2000).
[30]
VARIANT VAL-671.
PubMed=10811882; DOI=10.1073/pnas.100041297;
Ringpfeil F., Lebwohl M.G., Christiano A.M., Uitto J.;
"Pseudoxanthoma elasticum: mutations in the MRP6 gene encoding a
transmembrane ATP-binding cassette (ABC) transporter.";
Proc. Natl. Acad. Sci. U.S.A. 97:6001-6006(2000).
[31]
VARIANT SER-433, AND CHARACTERIZATION OF VARIANT VAL-671.
PubMed=11721885; DOI=10.1007/s100380170017;
Conrad S., Kauffmann H.-M., Ito K., Deeley R.G., Cole S.P.C.,
Schrenk D.;
"Identification of human multidrug resistance protein 1 (MRP1)
mutations and characterization of a G671V substitution.";
J. Hum. Genet. 46:656-663(2001).
[32]
VARIANTS THR-117 AND LEU-1512.
PubMed=11139250;
DOI=10.1002/1098-1004(2001)17:1<74::AID-HUMU14>3.0.CO;2-F;
Perdu J., Germain D.P.;
"Identification of novel polymorphisms in the pM5 and MRP1 (ABCC1)
genes at locus 16p13.1 and exclusion of both genes as responsible for
pseudoxanthoma elasticum.";
Hum. Mutat. 17:74-75(2001).
[33]
VARIANTS SER-43; ILE-73; GLN-723 AND GLN-1058.
PubMed=11266082; DOI=10.1097/00008571-200103000-00008;
Ito S., Ieiri I., Tanabe M., Suzuki A., Higuchi S., Otsubo K.;
"Polymorphism of the ABC transporter genes, MDR1, MRP1 and MRP2/cMOAT,
in healthy Japanese subjects.";
Pharmacogenetics 11:175-184(2001).
[34]
VARIANT [LARGE SCALE ANALYSIS] SER-433.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
-!- FUNCTION: Mediates export of organic anions and drugs from the
cytoplasm. Mediates ATP-dependent transport of glutathione and
glutathione conjugates, leukotriene C4, estradiol-17-beta-o-
glucuronide, methotrexate, antiviral drugs and other xenobiotics.
Confers resistance to anticancer drugs. Hydrolyzes ATP with low
efficiency. {ECO:0000269|PubMed:10064732,
ECO:0000269|PubMed:11114332, ECO:0000269|PubMed:16230346}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16230346};
Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
ECO:0000269|PubMed:16230346}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Comment=Additional isoforms seem to exist. Experimental
confirmation may be lacking for some isoforms.;
Name=1; Synonyms=Allexons;
IsoId=P33527-1; Sequence=Displayed;
Name=2; Synonyms=Delexon-17;
IsoId=P33527-2; Sequence=VSP_000037;
Name=3; Synonyms=Delexon-18;
IsoId=P33527-3; Sequence=VSP_000038;
Name=4; Synonyms=Delexon-30;
IsoId=P33527-4; Sequence=VSP_000039;
Name=5; Synonyms=Delexon-17-18;
IsoId=P33527-5; Sequence=VSP_000037, VSP_000038;
Name=6; Synonyms=Delexon-17-30;
IsoId=P33527-6; Sequence=VSP_000037, VSP_000039;
Name=7; Synonyms=Delexon-18-30;
IsoId=P33527-7; Sequence=VSP_000038, VSP_000039;
Name=8; Synonyms=Delexon-17-18-30;
IsoId=P33527-8; Sequence=VSP_000037, VSP_000038, VSP_000039;
Name=9;
IsoId=P33527-9; Sequence=VSP_017014;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Lung, testis and peripheral blood mononuclear
cells.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. Conjugate transporter (TC 3.A.1.208) subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MRPID106.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/abcc1/";
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P33527";
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EMBL; L05628; AAB46616.1; -; mRNA.
EMBL; AF022853; AAB83979.1; -; Genomic_DNA.
EMBL; AF022827; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022828; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022829; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022831; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022833; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022835; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022837; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022839; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022841; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022850; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022849; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022848; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022847; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022846; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022845; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022844; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022843; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022842; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022852; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022851; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022840; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022838; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022836; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022834; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022832; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022826; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022825; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022824; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022830; AAB83979.1; JOINED; Genomic_DNA.
EMBL; AF022853; AAB83980.1; -; Genomic_DNA.
EMBL; AF022824; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022825; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022826; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022828; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022830; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022832; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022834; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022836; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022838; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022848; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022847; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022846; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022845; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022844; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022843; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022842; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022841; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022839; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022852; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022851; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022850; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022849; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022837; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022835; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022833; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022831; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022829; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022827; AAB83980.1; JOINED; Genomic_DNA.
EMBL; AF022853; AAB83981.1; -; Genomic_DNA.
EMBL; AF022824; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022825; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022826; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022827; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022829; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022831; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022833; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022835; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022837; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022847; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022846; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022845; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022844; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022843; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022842; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022841; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022840; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022838; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022852; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022851; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022850; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022849; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022848; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022836; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022834; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022832; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022830; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022828; AAB83981.1; JOINED; Genomic_DNA.
EMBL; AF022853; AAB83983.1; -; Genomic_DNA.
EMBL; AF022824; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022825; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022826; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022827; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022828; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022829; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022830; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022831; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022832; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022833; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022834; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022835; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022836; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022837; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022838; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022839; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022840; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022841; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022842; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022843; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022844; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022845; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022846; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022847; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022848; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022849; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022850; AAB83983.1; JOINED; Genomic_DNA.
EMBL; AF022851; AAB83983.1; JOINED; Genomic_DNA.
EMBL; EF419769; ABN79590.1; -; Genomic_DNA.
EMBL; AC025778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC130651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC136624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB209120; BAD92357.1; -; mRNA.
EMBL; U91318; AAC15784.1; -; Genomic_DNA.
EMBL; AC003026; AAC05808.1; -; Genomic_DNA.
CCDS; CCDS42122.1; -. [P33527-1]
PIR; A44231; DVHUAR.
RefSeq; NP_004987.2; NM_004996.3. [P33527-1]
UniGene; Hs.391464; -.
PDB; 2CBZ; X-ray; 1.50 A; A=642-871.
PDB; 4C3Z; X-ray; 2.10 A; A=628-881.
PDBsum; 2CBZ; -.
PDBsum; 4C3Z; -.
ProteinModelPortal; P33527; -.
SMR; P33527; -.
BioGrid; 110503; 56.
IntAct; P33527; 14.
MINT; MINT-2802626; -.
STRING; 9606.ENSP00000382342; -.
BindingDB; P33527; -.
ChEMBL; CHEMBL3004; -.
DrugBank; DB05812; Abiraterone.
DrugBank; DB00345; Aminohippuric acid.
DrugBank; DB00701; Amprenavir.
DrugBank; DB01072; Atazanavir.
DrugBank; DB01076; Atorvastatin.
DrugBank; DB04851; Biricodar dicitrate.
DrugBank; DB02659; Cholic Acid.
DrugBank; DB01394; Colchicine.
DrugBank; DB00286; Conjugated Equine Estrogens.
DrugBank; DB00091; Cyclosporine.
DrugBank; DB00970; Dactinomycin.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB00586; Diclofenac.
DrugBank; DB01248; Docetaxel.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB00445; Epirubicin.
DrugBank; DB00773; Etoposide.
DrugBank; DB00693; Fluorescein.
DrugBank; DB01645; Genistein.
DrugBank; DB00143; Glutathione.
DrugBank; DB01016; Glyburide.
DrugBank; DB00365; Grepafloxacin.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB01177; Idarubicin.
DrugBank; DB00224; Indinavir.
DrugBank; DB00328; Indomethacin.
DrugBank; DB00762; Irinotecan.
DrugBank; DB00602; Ivermectin.
DrugBank; DB00709; Lamivudine.
DrugBank; DB00563; Methotrexate.
DrugBank; DB00834; Mifepristone.
DrugBank; DB01204; Mitoxantrone.
DrugBank; DB02375; Myricetin.
DrugBank; DB03467; Naringenin.
DrugBank; DB01165; Ofloxacin.
DrugBank; DB01229; Paclitaxel.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB01032; Probenecid.
DrugBank; DB00396; Progesterone.
DrugBank; DB04216; Quercetin.
DrugBank; DB03825; Rhodamine 6G.
DrugBank; DB01045; Rifampicin.
DrugBank; DB00503; Ritonavir.
DrugBank; DB01098; Rosuvastatin.
DrugBank; DB01232; Saquinavir.
DrugBank; DB06335; Saxagliptin.
DrugBank; DB01138; Sulfinpyrazone.
DrugBank; DB04348; Taurocholic Acid.
DrugBank; DB09161; Technetium Tc-99m sestamibi.
DrugBank; DB05294; Vandetanib.
DrugBank; DB08881; Vemurafenib.
DrugBank; DB00661; Verapamil.
DrugBank; DB00570; Vinblastine.
DrugBank; DB00541; Vincristine.
DrugBank; DB00399; Zoledronic acid.
GuidetoPHARMACOLOGY; 779; -.
SwissLipids; SLP:000000404; -.
TCDB; 3.A.1.208.8; the atp-binding cassette (abc) superfamily.
iPTMnet; P33527; -.
PhosphoSitePlus; P33527; -.
SwissPalm; P33527; -.
BioMuta; ABCC1; -.
DMDM; 296439301; -.
EPD; P33527; -.
MaxQB; P33527; -.
PaxDb; P33527; -.
PeptideAtlas; P33527; -.
PRIDE; P33527; -.
Ensembl; ENST00000399410; ENSP00000382342; ENSG00000103222. [P33527-1]
Ensembl; ENST00000621144; ENSP00000483316; ENSG00000278183. [P33527-1]
GeneID; 4363; -.
KEGG; hsa:4363; -.
UCSC; uc010bvi.4; human. [P33527-1]
CTD; 4363; -.
DisGeNET; 4363; -.
EuPathDB; HostDB:ENSG00000103222.18; -.
GeneCards; ABCC1; -.
H-InvDB; HIX0134370; -.
HGNC; HGNC:51; ABCC1.
HPA; HPA002380; -.
MIM; 158343; gene.
neXtProt; NX_P33527; -.
OpenTargets; ENSG00000103222; -.
PharmGKB; PA244; -.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00880000137856; -.
HOVERGEN; HBG108314; -.
InParanoid; P33527; -.
KO; K05665; -.
OMA; ENEWRVD; -.
OrthoDB; EOG091G00IN; -.
PhylomeDB; P33527; -.
TreeFam; TF105199; -.
Reactome; R-HSA-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
SIGNOR; P33527; -.
ChiTaRS; ABCC1; human.
EvolutionaryTrace; P33527; -.
GeneWiki; ABCC1; -.
GenomeRNAi; 4363; -.
PRO; PR:P33527; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103222; -.
CleanEx; HS_ABCC1; -.
ExpressionAtlas; P33527; baseline and differential.
Genevisible; P33527; HS.
GO; GO:0016323; C:basolateral plasma membrane; IDA:CACAO.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; TAS:Reactome.
GO; GO:0043225; F:ATPase-coupled anion transmembrane transporter activity; TAS:Reactome.
GO; GO:0015420; F:cobalamin-transporting ATPase activity; TAS:Reactome.
GO; GO:0015431; F:glutathione S-conjugate-exporting ATPase activity; IBA:GO_Central.
GO; GO:0034634; F:glutathione transmembrane transporter activity; IBA:GO_Central.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IMP:BHF-UCL.
GO; GO:0046623; F:sphingolipid-translocating ATPase activity; IMP:BHF-UCL.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0008559; F:xenobiotic-transporting ATPase activity; IBA:GO_Central.
GO; GO:0060326; P:cell chemotaxis; ISS:BHF-UCL.
GO; GO:0009235; P:cobalamin metabolic process; TAS:Reactome.
GO; GO:0006855; P:drug transmembrane transport; IBA:GO_Central.
GO; GO:0034775; P:glutathione transmembrane transport; IBA:GO_Central.
GO; GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
GO; GO:0045332; P:phospholipid translocation; IMP:BHF-UCL.
GO; GO:0042493; P:response to drug; TAS:ProtInc.
GO; GO:0099039; P:sphingolipid translocation; IMP:BHF-UCL.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0006810; P:transport; TAS:ProtInc.
GO; GO:0042908; P:xenobiotic transport; IBA:GO_Central.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR005292; Multidrug-R_assoc.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
TIGRFAMs; TIGR00957; MRP_assoc_pro; 1.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Glycoprotein; Hydrolase; Membrane;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1531 Multidrug resistance-associated protein
1.
/FTId=PRO_0000093351.
TOPO_DOM 1 33 Extracellular.
TRANSMEM 34 54 Helical; Name=1.
TOPO_DOM 55 74 Cytoplasmic.
TRANSMEM 75 95 Helical; Name=2.
TOPO_DOM 96 100 Extracellular.
TRANSMEM 101 121 Helical; Name=3.
TOPO_DOM 122 133 Cytoplasmic.
TRANSMEM 134 154 Helical; Name=4.
TOPO_DOM 155 172 Extracellular.
TRANSMEM 173 193 Helical; Name=5.
TOPO_DOM 194 316 Cytoplasmic.
TRANSMEM 317 337 Helical; Name=6.
TOPO_DOM 338 363 Extracellular.
TRANSMEM 364 384 Helical; Name=7.
TOPO_DOM 385 440 Cytoplasmic.
TRANSMEM 441 461 Helical; Name=8.
TOPO_DOM 462 464 Extracellular.
TRANSMEM 465 485 Helical; Name=9.
TOPO_DOM 486 547 Cytoplasmic.
TRANSMEM 548 568 Helical; Name=10.
TOPO_DOM 569 590 Extracellular.
TRANSMEM 591 611 Helical; Name=11.
TOPO_DOM 612 967 Cytoplasmic.
TRANSMEM 968 988 Helical; Name=12.
TOPO_DOM 989 1025 Extracellular.
TRANSMEM 1026 1046 Helical; Name=13.
TOPO_DOM 1047 1089 Cytoplasmic.
TRANSMEM 1090 1110 Helical; Name=14.
TOPO_DOM 1111 1111 Extracellular.
TRANSMEM 1112 1132 Helical; Name=15.
TOPO_DOM 1133 1203 Cytoplasmic.
TRANSMEM 1204 1224 Helical; Name=16.
TOPO_DOM 1225 1226 Extracellular.
TRANSMEM 1227 1247 Helical; Name=17.
TOPO_DOM 1248 1531 Cytoplasmic.
DOMAIN 325 608 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 644 868 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 975 1256 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1293 1527 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 678 685 ATP 1.
NP_BIND 1327 1334 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
BINDING 653 653 ATP 1.
BINDING 713 713 ATP 1.
MOD_RES 277 277 Phosphotyrosine.
{ECO:0000250|UniProtKB:O35379}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000250|UniProtKB:O35379}.
MOD_RES 503 503 N6-succinyllysine.
{ECO:0000250|UniProtKB:O35379}.
MOD_RES 905 905 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 915 915 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 930 930 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CARBOHYD 19 19 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9295302}.
CARBOHYD 23 23 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9295302}.
CARBOHYD 1006 1006 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9295302}.
VAR_SEQ 706 764 Missing (in isoform 2, isoform 5, isoform
6 and isoform 8). {ECO:0000305}.
/FTId=VSP_000037.
VAR_SEQ 765 820 Missing (in isoform 3, isoform 5, isoform
7 and isoform 8). {ECO:0000305}.
/FTId=VSP_000038.
VAR_SEQ 882 882 G -> GSTVMDEEEAG (in isoform 9).
{ECO:0000303|Ref.6}.
/FTId=VSP_017014.
VAR_SEQ 1431 1495 Missing (in isoform 4, isoform 6, isoform
7 and isoform 8). {ECO:0000305}.
/FTId=VSP_000039.
VARIANT 43 43 C -> S (in dbSNP:rs41395947).
{ECO:0000269|PubMed:11266082}.
/FTId=VAR_013317.
VARIANT 73 73 T -> I (in dbSNP:rs41494447).
{ECO:0000269|PubMed:11266082}.
/FTId=VAR_013318.
VARIANT 117 117 M -> T. {ECO:0000269|PubMed:11139250,
ECO:0000269|PubMed:1360704,
ECO:0000269|PubMed:9344662}.
/FTId=VAR_013319.
VARIANT 433 433 R -> S (in dbSNP:rs60782127).
{ECO:0000269|PubMed:11721885,
ECO:0000269|PubMed:18987736}.
/FTId=VAR_013320.
VARIANT 633 633 R -> Q (in dbSNP:rs112282109).
{ECO:0000269|PubMed:10835642}.
/FTId=VAR_011488.
VARIANT 671 671 G -> V (no effect on leukotriene C4 and
estradiol glucuronide transport;
dbSNP:rs45511401).
{ECO:0000269|PubMed:10811882,
ECO:0000269|PubMed:10835642,
ECO:0000269|PubMed:11721885,
ECO:0000269|Ref.4}.
/FTId=VAR_011489.
VARIANT 723 723 R -> Q (in dbSNP:rs4148356).
{ECO:0000269|PubMed:11266082,
ECO:0000269|Ref.4}.
/FTId=VAR_013321.
VARIANT 861 861 A -> T (in dbSNP:rs45517537).
{ECO:0000269|Ref.4}.
/FTId=VAR_055384.
VARIANT 1047 1047 C -> S (in dbSNP:rs13337489).
{ECO:0000269|Ref.4}.
/FTId=VAR_055385.
VARIANT 1058 1058 R -> Q (in dbSNP:rs41410450).
{ECO:0000269|PubMed:11266082}.
/FTId=VAR_013322.
VARIANT 1146 1146 V -> I (in dbSNP:rs28706727).
{ECO:0000269|Ref.4}.
/FTId=VAR_055386.
VARIANT 1512 1512 S -> L (in dbSNP:rs369410659).
{ECO:0000269|PubMed:11139250}.
/FTId=VAR_013323.
MUTAGEN 580 580 Q->A: No effect.
{ECO:0000269|PubMed:15260484}.
MUTAGEN 581 581 T->A: No effect.
{ECO:0000269|PubMed:15260484}.
MUTAGEN 585 585 S->A: No effect.
{ECO:0000269|PubMed:15260484}.
MUTAGEN 597 597 N->A: Increases resistance to vincristine
and decreases resistance to VP-16.
{ECO:0000269|PubMed:15260484}.
MUTAGEN 604 604 S->A: Increases estradiol glucuronide
transport. {ECO:0000269|PubMed:15260484}.
MUTAGEN 605 605 S->A: Decreases resistance to
vincristine, VP-16 and doxorubicin.
{ECO:0000269|PubMed:15260484}.
MUTAGEN 792 792 D->A: Only partially affects protein
maturation; impairs leukotriene C4
transport. {ECO:0000269|PubMed:11469806}.
MUTAGEN 792 792 D->L: Impairs protein maturation and
leukotriene C4 transport.
{ECO:0000269|PubMed:11469806}.
MUTAGEN 793 793 D->L: No effect on protein maturation and
leukotriene C4 transport.
{ECO:0000269|PubMed:11469806}.
MUTAGEN 1046 1046 R->D: Slightly impairs leukotriene C4 and
estradiol glucuronide transport.
{ECO:0000269|PubMed:15208328}.
MUTAGEN 1084 1084 D->R: Impairs leukotriene C4 and
estradiol glucuronide transport.
{ECO:0000269|PubMed:15208328}.
MUTAGEN 1089 1089 E->A,L,N,Q: Decreases resistance to
anthracyclines.
{ECO:0000269|PubMed:11278596}.
MUTAGEN 1089 1089 E->D: No effect.
{ECO:0000269|PubMed:11278596}.
MUTAGEN 1089 1089 E->K: Abolishes resistance to
anthracyclines.
{ECO:0000269|PubMed:11278596}.
MUTAGEN 1131 1131 R->E: Slightly impairs leukotriene C4 and
estradiol glucuronide transport.
{ECO:0000269|PubMed:15208328}.
MUTAGEN 1138 1138 R->E,K: Strongly reduced transport of
leukotriene C4, estradiol glucuronide and
of glutathione.
{ECO:0000269|PubMed:16230346}.
MUTAGEN 1141 1141 K->E: Reduced transport of leukotriene C4
and of glutathione.
{ECO:0000269|PubMed:16230346}.
MUTAGEN 1141 1141 K->R: Reduced transport of glutathione.
{ECO:0000269|PubMed:16230346}.
MUTAGEN 1142 1142 R->E,K: Reduced transport of leukotriene
C4, estradiol glucuronide and of
glutathione.
{ECO:0000269|PubMed:16230346}.
MUTAGEN 1246 1246 W->A,F,Y: Impairs estradiol glucuronide
transport. {ECO:0000269|PubMed:11278867}.
MUTAGEN 1246 1246 W->C: Impairs estradiol glucuronide
transport; loss of resistance to alkaloid
vincristine, cationic anthracyclines,
epipodophyllotoxin VP-16, but not
potassium antimony tartrate; partial loss
of resistance to sodium arsenite.
{ECO:0000269|PubMed:11278867}.
MUTAGEN 1333 1333 K->L: Impairs leukotriene C4 transport.
{ECO:0000269|PubMed:11469806}.
MUTAGEN 1454 1455 DE->LL: Impairs leukotriene C4 transport.
{ECO:0000269|PubMed:11469806}.
STRAND 644 653 {ECO:0000244|PDB:2CBZ}.
STRAND 660 668 {ECO:0000244|PDB:2CBZ}.
STRAND 673 677 {ECO:0000244|PDB:2CBZ}.
HELIX 684 691 {ECO:0000244|PDB:2CBZ}.
STRAND 695 704 {ECO:0000244|PDB:2CBZ}.
STRAND 708 711 {ECO:0000244|PDB:2CBZ}.
STRAND 719 721 {ECO:0000244|PDB:2CBZ}.
HELIX 722 727 {ECO:0000244|PDB:2CBZ}.
HELIX 736 743 {ECO:0000244|PDB:2CBZ}.
HELIX 747 750 {ECO:0000244|PDB:2CBZ}.
HELIX 756 758 {ECO:0000244|PDB:2CBZ}.
STRAND 759 762 {ECO:0000244|PDB:2CBZ}.
HELIX 770 784 {ECO:0000244|PDB:2CBZ}.
STRAND 787 793 {ECO:0000244|PDB:2CBZ}.
TURN 794 797 {ECO:0000244|PDB:2CBZ}.
HELIX 800 809 {ECO:0000244|PDB:2CBZ}.
TURN 816 819 {ECO:0000244|PDB:2CBZ}.
STRAND 820 825 {ECO:0000244|PDB:2CBZ}.
HELIX 832 834 {ECO:0000244|PDB:2CBZ}.
STRAND 835 842 {ECO:0000244|PDB:2CBZ}.
STRAND 845 850 {ECO:0000244|PDB:2CBZ}.
HELIX 852 858 {ECO:0000244|PDB:2CBZ}.
HELIX 861 868 {ECO:0000244|PDB:2CBZ}.
SEQUENCE 1531 AA; 171591 MW; 46A7CB643B9478C4 CRC64;
MALRGFCSAD GSDPLWDWNV TWNTSNPDFT KCFQNTVLVW VPCFYLWACF PFYFLYLSRH
DRGYIQMTPL NKTKTALGFL LWIVCWADLF YSFWERSRGI FLAPVFLVSP TLLGITMLLA
TFLIQLERRK GVQSSGIMLT FWLVALVCAL AILRSKIMTA LKEDAQVDLF RDITFYVYFS
LLLIQLVLSC FSDRSPLFSE TIHDPNPCPE SSASFLSRIT FWWITGLIVR GYRQPLEGSD
LWSLNKEDTS EQVVPVLVKN WKKECAKTRK QPVKVVYSSK DPAQPKESSK VDANEEVEAL
IVKSPQKEWN PSLFKVLYKT FGPYFLMSFF FKAIHDLMMF SGPQILKLLI KFVNDTKAPD
WQGYFYTVLL FVTACLQTLV LHQYFHICFV SGMRIKTAVI GAVYRKALVI TNSARKSSTV
GEIVNLMSVD AQRFMDLATY INMIWSAPLQ VILALYLLWL NLGPSVLAGV AVMVLMVPVN
AVMAMKTKTY QVAHMKSKDN RIKLMNEILN GIKVLKLYAW ELAFKDKVLA IRQEELKVLK
KSAYLSAVGT FTWVCTPFLV ALCTFAVYVT IDENNILDAQ TAFVSLALFN ILRFPLNILP
MVISSIVQAS VSLKRLRIFL SHEELEPDSI ERRPVKDGGG TNSITVRNAT FTWARSDPPT
LNGITFSIPE GALVAVVGQV GCGKSSLLSA LLAEMDKVEG HVAIKGSVAY VPQQAWIQND
SLRENILFGC QLEEPYYRSV IQACALLPDL EILPSGDRTE IGEKGVNLSG GQKQRVSLAR
AVYSNADIYL FDDPLSAVDA HVGKHIFENV IGPKGMLKNK TRILVTHSMS YLPQVDVIIV
MSGGKISEMG SYQELLARDG AFAEFLRTYA STEQEQDAEE NGVTGVSGPG KEAKQMENGM
LVTDSAGKQL QRQLSSSSSY SGDISRHHNS TAELQKAEAK KEETWKLMEA DKAQTGQVKL
SVYWDYMKAI GLFISFLSIF LFMCNHVSAL ASNYWLSLWT DDPIVNGTQE HTKVRLSVYG
ALGISQGIAV FGYSMAVSIG GILASRCLHV DLLHSILRSP MSFFERTPSG NLVNRFSKEL
DTVDSMIPEV IKMFMGSLFN VIGACIVILL ATPIAAIIIP PLGLIYFFVQ RFYVASSRQL
KRLESVSRSP VYSHFNETLL GVSVIRAFEE QERFIHQSDL KVDENQKAYY PSIVANRWLA
VRLECVGNCI VLFAALFAVI SRHSLSAGLV GLSVSYSLQV TTYLNWLVRM SSEMETNIVA
VERLKEYSET EKEAPWQIQE TAPPSSWPQV GRVEFRNYCL RYREDLDFVL RHINVTINGG
EKVGIVGRTG AGKSSLTLGL FRINESAEGE IIIDGINIAK IGLHDLRFKI TIIPQDPVLF
SGSLRMNLDP FSQYSDEEVW TSLELAHLKD FVSALPDKLD HECAEGGENL SVGQRQLVCL
ARALLRKTKI LVLDEATAAV DLETDDLIQS TIRTQFEDCT VLTIAHRLNT IMDYTRVIVL
DKGEIQEYGA PSDLLQQRGL FYSMAKDAGL V


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