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Canalicular multispecific organic anion transporter 1 (ATP-binding cassette sub-family C member 2) (Canalicular multidrug resistance protein) (Multidrug resistance-associated protein 2)

 MRP2_HUMAN              Reviewed;        1545 AA.
Q92887; B2RMT8; Q14022; Q5T2B1; Q92500; Q92798; Q99663; Q9UMS2;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
25-OCT-2017, entry version 179.
RecName: Full=Canalicular multispecific organic anion transporter 1;
AltName: Full=ATP-binding cassette sub-family C member 2;
AltName: Full=Canalicular multidrug resistance protein;
AltName: Full=Multidrug resistance-associated protein 2;
Name=ABCC2; Synonyms=CMOAT, CMOAT1, CMRP, MRP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-39.
PubMed=8797578;
Taniguchi K., Wada M., Kohno K., Nakamura T., Kawabe T., Kawakami M.,
Kagotani K., Okumura K., Akiyama S., Kuwano M.;
"A human canalicular multispecific organic anion transporter (cMOAT)
gene is overexpressed in cisplatin-resistant human cancer cell lines
with decreased drug accumulation.";
Cancer Res. 56:4124-4129(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PHE-39; GLU-1188 AND
TYR-1515.
Kool M., de Haas M., Ponne N.J., Paulusma C.C., Oude-Elferink R.P.J.,
Baas F., Borst P.;
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-39.
PubMed=8662992; DOI=10.1074/jbc.271.25.15091;
Buechler M., Koenig J., Brom M., Kartenbeck J., Spring H., Horie T.,
Keppler D.;
"cDNA cloning of the hepatocyte canalicular isoform of the multidrug
resistance protein, cMrp, reveals a novel conjugate export pump
deficient in hyperbilirubinemic mutant rats.";
J. Biol. Chem. 271:15091-15098(1996).
[4]
SEQUENCE REVISION.
Keppler D.;
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-39 AND DJS
1392-ARG-MET-1393 DEL.
PubMed=10464142; DOI=10.1016/S0016-5085(99)70459-2;
Tsujii H., Koenig J., Rost D., Stoeckel B., Leuschner U., Keppler D.;
"Exon-intron organization of the human multidrug-resistance protein 2
(MRP2) gene mutated in Dubin-Johnson syndrome.";
Gastroenterology 117:653-660(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-39.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-39.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
REVIEW.
PubMed=11076395; DOI=10.1055/s-2000-9391;
Keppler D., Koenig J.;
"Hepatic secretion of conjugated drugs and endogenous substances.";
Semin. Liver Dis. 20:265-272(2000).
[10]
MUTAGENESIS OF TRP-1254.
PubMed=11500505; DOI=10.1074/jbc.M105160200;
Ito K., Oleschuk C.J., Westlake C., Vasa M.Z., Deeley R.G.,
Cole S.P.C.;
"Mutation of Trp1254 in the multispecific organic anion transporter,
multidrug resistance protein 2 (MRP2) (ABCC2), alters substrate
specificity and results in loss of methotrexate transport activity.";
J. Biol. Chem. 276:38108-38114(2001).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-878, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
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).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-926; SER-930 AND
SER-938, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878 AND SER-1438, AND
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).
[17]
VARIANT DJS TRP-768.
PubMed=9425227; DOI=10.1093/hmg/7.2.203;
Wada M., Toh S., Taniguchi K., Nakamura T., Uchiumi T., Kohno K.,
Yoshida I., Kimura A., Sakisaka S., Adachi Y., Kuwano M.;
"Mutations in the canalicular multispecific organic anion transporter
(cMOAT) gene, a novel ABC transporter, in patients with
hyperbilirubinemia II/Dubin-Johnson syndrome.";
Hum. Mol. Genet. 7:203-207(1998).
[18]
VARIANTS DJS TRP-768 AND ARG-1382.
PubMed=10053008; DOI=10.1086/302292;
Toh S., Wada M., Uchiumi T., Inokuchi A., Makino Y., Horie Y.,
Adachi Y., Sakisaka S., Kuwano M.;
"Genomic structure of the canalicular multispecific organic anion-
transporter gene (MRP2/cMOAT) and mutations in the ATP-binding-
cassette region in Dubin-Johnson syndrome.";
Am. J. Hum. Genet. 64:739-746(1999).
[19]
CHARACTERIZATION OF VARIANT DJS 1392-ARG-MET-1393 DEL, AND SUBCELLULAR
LOCATION.
PubMed=11093739; DOI=10.1053/jhep.2000.19791;
Keitel V., Kartenbeck J., Nies A.T., Spring H., Brom M., Keppler D.;
"Impaired protein maturation of the conjugate export pump multidrug
resistance protein 2 as a consequence of a deletion mutation in Dubin-
Johnson syndrome.";
Hepatology 32:1317-1328(2000).
[20]
VARIANTS DJS HIS-1150 AND PHE-1173, AND VARIANTS ASN-281 AND ILE-417.
PubMed=11477083; DOI=10.1074/jbc.M105047200;
Mor-Cohen R., Zivelin A., Rosenberg N., Shani M., Muallem S.,
Seligsohn U.;
"Identification and functional analysis of two novel mutations in the
multidrug resistance protein 2 gene in Israeli patients with Dubin-
Johnson syndrome.";
J. Biol. Chem. 276:36923-36930(2001).
[21]
VARIANT DJS TRP-768, AND VARIANTS ILE-417; PHE-789 AND THR-1450.
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).
[22]
VARIANTS PHE-39; GLY-333; HIS-353; ILE-486; THR-670; SER-921;
THR-1036; HIS-1174; LEU-1181; GLU-1188; LEU-1291 AND TYR-1515,
CHARACTERIZATION OF VARIANTS DJS PHE-1173, AND CHARACTERIZATION OF
VARIANTS GLY-333; HIS-353; ILE-486; SER-921; THR-1036; HIS-1174;
LEU-1181; LYS-1244 AND LEU-1291.
PubMed=22290738; DOI=10.1002/humu.22041;
Arlanov R., Porter A., Strand D., Brough R., Karpova D., Kerb R.,
Wojnowski L., Schwab M., Lang T.;
"Functional characterization of protein variants of the human
multidrug transporter ABCC2 by a novel targeted expression system in
fibrosarcoma cells.";
Hum. Mutat. 33:750-762(2012).
[23]
VARIANT DJS TRP-768, AND VARIANT ILE-417.
PubMed=25336012; DOI=10.1111/ped.12404;
Okada H., Kusaka T., Fuke N., Kunikata J., Kondo S., Iwase T., Nan W.,
Hirota T., Ieiri I., Itoh S.;
"Neonatal Dubin-Johnson syndrome: novel compound heterozygous mutation
in the ABCC2 gene.";
Pediatr. Int. 56:E62-E62(2014).
-!- FUNCTION: Mediates hepatobiliary excretion of numerous organic
anions. May function as a cellular cisplatin transporter.
-!- INTERACTION:
P19838:NFKB1; NbExp=3; IntAct=EBI-3916193, EBI-300010;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:11093739}; Multi-pass membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00441,
ECO:0000269|PubMed:11093739}.
-!- TISSUE SPECIFICITY: Expressed by polarized cells in liver, kidney
and intestine. The highest expression is found in liver.
-!- DISEASE: Dubin-Johnson syndrome (DJS) [MIM:237500]: Autosomal
recessive disorder characterized by conjugated hyperbilirubinemia,
an increase in the urinary excretion of coproporphyrin isomer I,
deposition of melanin-like pigment in hepatocytes, and prolonged
retention of sulfobromophthalein, but otherwise normal liver
function. {ECO:0000269|PubMed:10053008,
ECO:0000269|PubMed:10464142, ECO:0000269|PubMed:11093739,
ECO:0000269|PubMed:11266082, ECO:0000269|PubMed:11477083,
ECO:0000269|PubMed:22290738, ECO:0000269|PubMed:25336012,
ECO:0000269|PubMed:9425227}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. Conjugate transporter (TC 3.A.1.208) subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q92887";
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EMBL; U63970; AAB39892.1; -; mRNA.
EMBL; U49248; AAB09422.1; -; mRNA.
EMBL; X96395; CAA65259.2; -; mRNA.
EMBL; AJ132244; CAB45309.1; -; Genomic_DNA.
EMBL; AJ132287; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ245625; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132288; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132289; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132290; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132291; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132292; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132293; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132294; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132295; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132296; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132297; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132298; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132299; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132300; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132301; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132302; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132303; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ245626; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132304; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132305; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132306; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132307; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132308; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ245627; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132309; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132310; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132311; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132312; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132313; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AJ132314; CAB45309.1; JOINED; Genomic_DNA.
EMBL; AL392107; CAI11010.1; -; Genomic_DNA.
EMBL; AL133353; CAI11010.1; JOINED; Genomic_DNA.
EMBL; AL133353; CAI14502.1; -; Genomic_DNA.
EMBL; AL392107; CAI14502.1; JOINED; Genomic_DNA.
EMBL; CH471066; EAW49853.1; -; Genomic_DNA.
EMBL; BC136419; AAI36420.1; -; mRNA.
CCDS; CCDS7484.1; -.
PIR; S71841; S71841.
RefSeq; NP_000383.1; NM_000392.4.
UniGene; Hs.368243; -.
ProteinModelPortal; Q92887; -.
SMR; Q92887; -.
BioGrid; 107647; 48.
IntAct; Q92887; 5.
MINT; MINT-5004989; -.
STRING; 9606.ENSP00000359478; -.
BindingDB; Q92887; -.
ChEMBL; CHEMBL5748; -.
DrugBank; DB04789; 5-methyltetrahydrofolic acid.
DrugBank; DB00171; Adenosine triphosphate.
DrugBank; DB00345; Aminohippuric acid.
DrugBank; DB01169; Arsenic trioxide.
DrugBank; DB01076; Atorvastatin.
DrugBank; DB09060; Avibactam.
DrugBank; DB08907; Canagliflozin.
DrugBank; DB00564; Carbamazepine.
DrugBank; DB00958; Carboplatin.
DrugBank; DB00439; Cerivastatin.
DrugBank; DB02659; Cholic Acid.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00257; Clotrimazole.
DrugBank; DB00286; Conjugated Equine Estrogens.
DrugBank; DB00091; Cyclosporine.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB01248; Docetaxel.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB09272; Eluxadoline.
DrugBank; DB00876; Eprosartan.
DrugBank; DB00977; Ethinyl Estradiol.
DrugBank; DB00773; Etoposide.
DrugBank; DB00973; Ezetimibe.
DrugBank; DB00695; Furosemide.
DrugBank; DB02703; Fusidic Acid.
DrugBank; DB08884; Gadoxetic acid.
DrugBank; DB00143; Glutathione.
DrugBank; DB01016; Glyburide.
DrugBank; DB00365; Grepafloxacin.
DrugBank; DB01892; Hyperforin.
DrugBank; DB00224; Indinavir.
DrugBank; DB09374; Indocyanine green.
DrugBank; DB00328; Indomethacin.
DrugBank; DB00762; Irinotecan.
DrugBank; DB00602; Ivermectin.
DrugBank; DB00709; Lamivudine.
DrugBank; DB01202; Levetiracetam.
DrugBank; DB11256; Levomefolic acid.
DrugBank; DB00978; Lomefloxacin.
DrugBank; DB00227; Lovastatin.
DrugBank; DB00563; Methotrexate.
DrugBank; DB00688; Mycophenolate mofetil.
DrugBank; DB01115; Nifedipine.
DrugBank; DB00957; Norgestimate.
DrugBank; DB01165; Ofloxacin.
DrugBank; DB00275; Olmesartan.
DrugBank; DB00526; Oxaliplatin.
DrugBank; DB01229; Paclitaxel.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB00252; Phenytoin.
DrugBank; DB08860; Pitavastatin.
DrugBank; DB01411; Pranlukast.
DrugBank; DB00175; Pravastatin.
DrugBank; DB01032; Probenecid.
DrugBank; DB04216; Quercetin.
DrugBank; DB00908; Quinidine.
DrugBank; DB00206; Reserpine.
DrugBank; DB01045; Rifampicin.
DrugBank; DB00503; Ritonavir.
DrugBank; DB01232; Saquinavir.
DrugBank; DB00641; Simvastatin.
DrugBank; DB00398; Sorafenib.
DrugBank; DB01208; Sparfloxacin.
DrugBank; DB00421; Spironolactone.
DrugBank; DB00795; Sulfasalazine.
DrugBank; DB01138; Sulfinpyrazone.
DrugBank; DB01268; Sunitinib.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB04348; Taurocholic Acid.
DrugBank; DB00966; Telmisartan.
DrugBank; DB00300; Tenofovir.
DrugBank; DB00116; Tetrahydrofolic acid.
DrugBank; DB01586; Ursodeoxycholic acid.
DrugBank; DB00067; Vasopressin.
DrugBank; DB00661; Verapamil.
DrugBank; DB00570; Vinblastine.
DrugBank; DB00541; Vincristine.
GuidetoPHARMACOLOGY; 780; -.
SwissLipids; SLP:000001599; -.
TCDB; 3.A.1.208.2; the atp-binding cassette (abc) superfamily.
iPTMnet; Q92887; -.
PhosphoSitePlus; Q92887; -.
BioMuta; ABCC2; -.
DMDM; 308153583; -.
EPD; Q92887; -.
MaxQB; Q92887; -.
PaxDb; Q92887; -.
PeptideAtlas; Q92887; -.
PRIDE; Q92887; -.
Ensembl; ENST00000370449; ENSP00000359478; ENSG00000023839.
GeneID; 1244; -.
KEGG; hsa:1244; -.
UCSC; uc001kqf.3; human.
CTD; 1244; -.
DisGeNET; 1244; -.
EuPathDB; HostDB:ENSG00000023839.10; -.
GeneCards; ABCC2; -.
HGNC; HGNC:53; ABCC2.
HPA; CAB037271; -.
HPA; HPA004860; -.
MalaCards; ABCC2; -.
MIM; 237500; phenotype.
MIM; 601107; gene.
neXtProt; NX_Q92887; -.
OpenTargets; ENSG00000023839; -.
Orphanet; 234; Dubin-Johnson syndrome.
PharmGKB; PA116; -.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00880000137856; -.
HOVERGEN; HBG108314; -.
InParanoid; Q92887; -.
KO; K05666; -.
OMA; DLPLCFE; -.
OrthoDB; EOG091G00IN; -.
PhylomeDB; Q92887; -.
TreeFam; TF105199; -.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
SABIO-RK; Q92887; -.
ChiTaRS; ABCC2; human.
GeneWiki; Multidrug_resistance-associated_protein_2; -.
GenomeRNAi; 1244; -.
PRO; PR:Q92887; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000023839; -.
CleanEx; HS_ABCC2; -.
ExpressionAtlas; Q92887; baseline and differential.
Genevisible; Q92887; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0046581; C:intercellular canaliculus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; TAS:ProtInc.
GO; GO:0043225; F:ATPase-coupled anion transmembrane transporter activity; TAS:Reactome.
GO; GO:0015127; F:bilirubin transmembrane transporter activity; TAS:Reactome.
GO; GO:0008514; F:organic anion transmembrane transporter activity; TAS:ProtInc.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:1901086; P:benzylpenicillin metabolic process; IEA:Ensembl.
GO; GO:0015722; P:canalicular bile acid transport; IEA:Ensembl.
GO; GO:0030644; P:cellular chloride ion homeostasis; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0006855; P:drug transmembrane transport; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0015694; P:mercury ion transport; IEA:Ensembl.
GO; GO:0015732; P:prostaglandin transport; IEA:Ensembl.
GO; GO:0097327; P:response to antineoplastic agent; IEA:Ensembl.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0009408; P:response to heat; IEA:Ensembl.
GO; GO:0031427; P:response to methotrexate; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0070327; P:thyroid hormone transport; IEA:Ensembl.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0006810; P:transport; TAS:ProtInc.
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; IPR030247; ABCC2.
InterPro; IPR005292; Multidrug-R_assoc.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24223:SF176; PTHR24223:SF176; 1.
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; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Disease mutation;
Glycoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1545 Canalicular multispecific organic anion
transporter 1.
/FTId=PRO_0000093356.
TOPO_DOM 1 27 Extracellular. {ECO:0000250}.
TRANSMEM 28 48 Helical; Name=1. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 49 68 Cytoplasmic. {ECO:0000250}.
TRANSMEM 69 89 Helical; Name=2. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 90 93 Extracellular. {ECO:0000250}.
TRANSMEM 94 114 Helical; Name=3. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 115 126 Cytoplasmic. {ECO:0000250}.
TRANSMEM 127 147 Helical; Name=4. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 148 165 Extracellular. {ECO:0000250}.
TRANSMEM 166 186 Helical; Name=5. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 187 313 Cytoplasmic. {ECO:0000250}.
TRANSMEM 314 334 Helical; Name=6. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 335 360 Extracellular. {ECO:0000250}.
TRANSMEM 361 381 Helical; Name=7. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 382 437 Cytoplasmic. {ECO:0000250}.
TRANSMEM 438 458 Helical; Name=8. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 459 461 Extracellular. {ECO:0000250}.
TRANSMEM 462 482 Helical; Name=9. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 483 544 Cytoplasmic. {ECO:0000250}.
TRANSMEM 545 565 Helical; Name=10. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 566 587 Extracellular. {ECO:0000250}.
TRANSMEM 588 608 Helical; Name=11. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 609 971 Cytoplasmic. {ECO:0000250}.
TRANSMEM 972 992 Helical; Name=12. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 993 1033 Extracellular. {ECO:0000250}.
TRANSMEM 1034 1054 Helical; Name=13. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1055 1097 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1098 1118 Helical; Name=14. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1119 1119 Extracellular. {ECO:0000250}.
TRANSMEM 1120 1140 Helical; Name=15. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1141 1211 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1212 1232 Helical; Name=16. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1233 1234 Extracellular. {ECO:0000250}.
TRANSMEM 1235 1255 Helical; Name=17. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1256 1545 Cytoplasmic. {ECO:0000250}.
DOMAIN 322 605 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 637 861 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 979 1264 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1300 1534 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 671 678 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1334 1341 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 281 281 Phosphoserine.
{ECO:0000250|UniProtKB:Q63120}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 878 878 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 926 926 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 930 930 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 938 938 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1438 1438 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 7 7 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 12 12 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1011 1011 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 39 39 Y -> F (in dbSNP:rs927344).
{ECO:0000269|PubMed:10464142,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:22290738,
ECO:0000269|PubMed:8662992,
ECO:0000269|PubMed:8797578,
ECO:0000269|Ref.2, ECO:0000269|Ref.7}.
/FTId=VAR_047152.
VARIANT 246 246 M -> L (in dbSNP:rs17222744).
/FTId=VAR_029113.
VARIANT 281 281 S -> N (in dbSNP:rs56131651).
{ECO:0000269|PubMed:11477083}.
/FTId=VAR_013324.
VARIANT 333 333 D -> G (decreased expression; altered
subcellular localization; altered
transporter activity; dbSNP:rs17222674).
{ECO:0000269|PubMed:22290738}.
/FTId=VAR_020226.
VARIANT 353 353 R -> H (altered transporter activity;
dbSNP:rs7080681).
{ECO:0000269|PubMed:22290738}.
/FTId=VAR_020227.
VARIANT 417 417 V -> I (in dbSNP:rs2273697).
{ECO:0000269|PubMed:11266082,
ECO:0000269|PubMed:11477083,
ECO:0000269|PubMed:25336012}.
/FTId=VAR_013325.
VARIANT 486 486 T -> I (altered transporter activity;
dbSNP:rs17222589).
{ECO:0000269|PubMed:22290738}.
/FTId=VAR_070607.
VARIANT 495 495 K -> E (in dbSNP:rs17222561).
/FTId=VAR_029115.
VARIANT 562 562 F -> L (in dbSNP:rs17216233).
/FTId=VAR_029116.
VARIANT 670 670 I -> T (in dbSNP:rs17222632).
{ECO:0000269|PubMed:22290738}.
/FTId=VAR_020228.
VARIANT 768 768 R -> W (in DJS; dbSNP:rs56199535).
{ECO:0000269|PubMed:10053008,
ECO:0000269|PubMed:11266082,
ECO:0000269|PubMed:25336012,
ECO:0000269|PubMed:9425227}.
/FTId=VAR_000099.
VARIANT 789 789 S -> F (in dbSNP:rs56220353).
{ECO:0000269|PubMed:11266082}.
/FTId=VAR_013326.
VARIANT 849 849 L -> R (in dbSNP:rs17222617).
/FTId=VAR_020229.
VARIANT 921 921 G -> S (altered transporter activity;
dbSNP:rs41318029).
{ECO:0000269|PubMed:22290738}.
/FTId=VAR_070608.
VARIANT 982 982 I -> V (in dbSNP:rs17222554).
/FTId=VAR_029117.
VARIANT 1036 1036 I -> T (polymorphism; no effect on
transporter activity; dbSNP:rs45441199).
{ECO:0000269|PubMed:22290738}.
/FTId=VAR_020230.
VARIANT 1063 1063 N -> S (in dbSNP:rs17222540).
/FTId=VAR_029118.
VARIANT 1150 1150 R -> H (in DJS; protein is properly
localized at the plasma membrane, but
transporter activity is impaired;
dbSNP:rs72558200).
{ECO:0000269|PubMed:11477083}.
/FTId=VAR_013327.
VARIANT 1173 1173 I -> F (in DJS; decreased expression and
mislocation to the endoplasmic reticulum;
dbSNP:rs72558201).
{ECO:0000269|PubMed:11477083,
ECO:0000269|PubMed:22290738}.
/FTId=VAR_013328.
VARIANT 1174 1174 R -> H (decreased expression; altered
subcellular localization; decreased
transporter activity; dbSNP:rs139188247).
{ECO:0000269|PubMed:22290738}.
/FTId=VAR_070609.
VARIANT 1181 1181 R -> L (decreased expression;
dbSNP:rs8187692).
{ECO:0000269|PubMed:22290738}.
/FTId=VAR_020231.
VARIANT 1188 1188 V -> E (in dbSNP:rs17222723).
{ECO:0000269|PubMed:22290738,
ECO:0000269|Ref.2}.
/FTId=VAR_020232.
VARIANT 1244 1244 N -> K (decreased transporter activity;
dbSNP:rs757141905).
{ECO:0000269|PubMed:22290738}.
/FTId=VAR_070610.
VARIANT 1273 1273 T -> A (in dbSNP:rs8187699).
/FTId=VAR_024360.
VARIANT 1291 1291 P -> L (altered transporter activity;
dbSNP:rs17216317).
{ECO:0000269|PubMed:22290738}.
/FTId=VAR_020233.
VARIANT 1382 1382 Q -> R (in DJS; dbSNP:rs72558202).
{ECO:0000269|PubMed:10053008}.
/FTId=VAR_010756.
VARIANT 1392 1393 Missing (in DJS; impaired transport from
the endoplasmic reticulum to the apical
plasma membrane associated with impaired
maturation).
{ECO:0000269|PubMed:10464142,
ECO:0000269|PubMed:11093739}.
/FTId=VAR_013329.
VARIANT 1450 1450 A -> T (in dbSNP:rs56296335).
{ECO:0000269|PubMed:11266082}.
/FTId=VAR_013330.
VARIANT 1515 1515 C -> Y (in dbSNP:rs8187710).
{ECO:0000269|PubMed:22290738,
ECO:0000269|Ref.2}.
/FTId=VAR_020234.
MUTAGEN 1254 1254 W->A,C: Fails to transport methotrexate,
leukotriene C4 and estradiol glucuronide.
{ECO:0000269|PubMed:11500505}.
MUTAGEN 1254 1254 W->F: Fails to transport methotrexate and
leukotriene C4. Does not affect estradiol
glucuronide transport.
{ECO:0000269|PubMed:11500505}.
MUTAGEN 1254 1254 W->Y: Fails to transport methotrexate;
reduces leukotriene C4 transport. Does
not affect estradiol glucuronide
transport. {ECO:0000269|PubMed:11500505}.
CONFLICT 1430 1430 V -> G (in Ref. 5; CAB45309).
{ECO:0000305}.
SEQUENCE 1545 AA; 174207 MW; C5F8984FFCDF9799 CRC64;
MLEKFCNSTF WNSSFLDSPE ADLPLCFEQT VLVWIPLGYL WLLAPWQLLH VYKSRTKRSS
TTKLYLAKQV FVGFLLILAA IELALVLTED SGQATVPAVR YTNPSLYLGT WLLVLLIQYS
RQWCVQKNSW FLSLFWILSI LCGTFQFQTL IRTLLQGDNS NLAYSCLFFI SYGFQILILI
FSAFSENNES SNNPSSIASF LSSITYSWYD SIILKGYKRP LTLEDVWEVD EEMKTKTLVS
KFETHMKREL QKARRALQRR QEKSSQQNSG ARLPGLNKNQ SQSQDALVLE DVEKKKKKSG
TKKDVPKSWL MKALFKTFYM VLLKSFLLKL VNDIFTFVSP QLLKLLISFA SDRDTYLWIG
YLCAILLFTA ALIQSFCLQC YFQLCFKLGV KVRTAIMASV YKKALTLSNL ARKEYTVGET
VNLMSVDAQK LMDVTNFMHM LWSSVLQIVL SIFFLWRELG PSVLAGVGVM VLVIPINAIL
STKSKTIQVK NMKNKDKRLK IMNEILSGIK ILKYFAWEPS FRDQVQNLRK KELKNLLAFS
QLQCVVIFVF QLTPVLVSVV TFSVYVLVDS NNILDAQKAF TSITLFNILR FPLSMLPMMI
SSMLQASVST ERLEKYLGGD DLDTSAIRHD CNFDKAMQFS EASFTWEHDS EATVRDVNLD
IMAGQLVAVI GPVGSGKSSL ISAMLGEMEN VHGHITIKGT TAYVPQQSWI QNGTIKDNIL
FGTEFNEKRY QQVLEACALL PDLEMLPGGD LAEIGEKGIN LSGGQKQRIS LARATYQNLD
IYLLDDPLSA VDAHVGKHIF NKVLGPNGLL KGKTRLLVTH SMHFLPQVDE IVVLGNGTIV
EKGSYSALLA KKGEFAKNLK TFLRHTGPEE EATVHDGSEE EDDDYGLISS VEEIPEDAAS
ITMRRENSFR RTLSRSSRSN GRHLKSLRNS LKTRNVNSLK EDEELVKGQK LIKKEFIETG
KVKFSIYLEY LQAIGLFSIF FIILAFVMNS VAFIGSNLWL SAWTSDSKIF NSTDYPASQR
DMRVGVYGAL GLAQGIFVFI AHFWSAFGFV HASNILHKQL LNNILRAPMR FFDTTPTGRI
VNRFAGDIST VDDTLPQSLR SWITCFLGII STLVMICMAT PVFTIIVIPL GIIYVSVQMF
YVSTSRQLRR LDSVTRSPIY SHFSETVSGL PVIRAFEHQQ RFLKHNEVRI DTNQKCVFSW
ITSNRWLAIR LELVGNLTVF FSALMMVIYR DTLSGDTVGF VLSNALNITQ TLNWLVRMTS
EIETNIVAVE RITEYTKVEN EAPWVTDKRP PPDWPSKGKI QFNNYQVRYR PELDLVLRGI
TCDIGSMEKI GVVGRTGAGK SSLTNCLFRI LEAAGGQIII DGVDIASIGL HDLREKLTII
PQDPILFSGS LRMNLDPFNN YSDEEIWKAL ELAHLKSFVA SLQLGLSHEV TEAGGNLSIG
QRQLLCLGRA LLRKSKILVL DEATAAVDLE TDNLIQTTIQ NEFAHCTVIT IAHRLHTIMD
SDKVMVLDNG KIIECGSPEE LLQIPGPFYF MAKEAGIENV NSTKF


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