Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

ATP-binding cassette sub-family G member 2 (Breast cancer resistance protein) (CDw338) (Mitoxantrone resistance-associated protein) (Placenta-specific ATP-binding cassette transporter) (Urate exporter) (CD antigen CD338)

 ABCG2_HUMAN             Reviewed;         655 AA.
Q9UNQ0; A0A1W3; A8K1T5; O95374; Q4W5I3; Q53ZQ1; Q569L4; Q5YLG4;
Q86V64; Q8IX16; Q96LD6; Q96TA8; Q9BY73; Q9NUS0;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 3.
30-AUG-2017, entry version 176.
RecName: Full=ATP-binding cassette sub-family G member 2;
AltName: Full=Breast cancer resistance protein;
AltName: Full=CDw338;
AltName: Full=Mitoxantrone resistance-associated protein;
AltName: Full=Placenta-specific ATP-binding cassette transporter;
AltName: Full=Urate exporter;
AltName: CD_antigen=CD338;
Name=ABCG2; Synonyms=ABCP, BCRP, BCRP1, MXR;
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), VARIANTS GLU-166 AND SER-208,
AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=9850061;
Allikmets R., Schriml L.M., Hutchinson A., Romano-Spica V., Dean M.;
"A human placenta-specific ATP-binding cassette gene (ABCP) on
chromosome 4q22 that is involved in multidrug resistance.";
Cancer Res. 58:5337-5339(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Mammary cancer;
PubMed=9861027; DOI=10.1073/pnas.95.26.15665;
Doyle L.A., Yang W., Abruzzo L.V., Krogmann T., Gao Y., Rishi A.K.,
Ross D.D.;
"A multidrug resistance transporter from human MCF-7 breast cancer
cells.";
Proc. Natl. Acad. Sci. U.S.A. 95:15665-15670(1998).
[3]
ERRATUM.
Doyle L.A., Yang W., Abruzzo L.V., Krogmann T., Gao Y., Rishi A.K.,
Ross D.D.;
Proc. Natl. Acad. Sci. U.S.A. 96:2569-2569(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kage K., Tsukahara S., Sugiyama T., Asada S., Ishikawa E., Tsuruo T.,
Sugimoto Y.;
"Breast cancer resistance protein constitutes a 140-kDa complex as a
homodimer.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11306452;
Komatani H., Kotani H., Hara Y., Nakagawa R., Matsumoto M.,
Arakawa H., Nishimura S.;
"Identification of breast cancer resistant protein/mitoxantrone
resistance/placenta-specific, ATP-binding cassette transporter as a
transporter of NB-506 and J-107088, topoisomerase I inhibitors with an
indolocarbazole structure.";
Cancer Res. 61:2827-2832(2001).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11533706; DOI=10.1038/nm0901-1028;
Zhou S., Schuetz J.D., Bunting K.D., Colapietro A.M., Sampath J.,
Morris J.J., Lagutina I., Grosveld G.C., Osawa M., Nakauchi H.,
Sorrentino B.P.;
"The ABC transporter Bcrp1/ABCG2 is expressed in a wide variety of
stem cells and is a molecular determinant of the side-population
phenotype.";
Nat. Med. 7:1028-1034(2001).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANTS GLU-166
AND SER-208.
TISSUE=Brain endothelium;
PubMed=12958161; DOI=10.1096/fj.02-1131fje;
Zhang W., Mojsilovic-Petrovic J., Andrade M.F., Zhang H., Ball M.,
Stanimirovic D.B.;
"The expression and functional characterization of ABCG2 in brain
endothelial cells and vessels.";
FASEB J. 17:2085-2087(2003).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-141.
Yoshikawa M., Yabuuchi H., Ikegami Y., Ishikawa T.;
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-316.
Sudarikov A., Makarik T., Andreeff M.;
"Cell line K562 resistant to Hoechst 33342.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hippocampus, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-12; LYS-141;
HIS-296 AND THR-528.
SeattleSNPs variation discovery resource;
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
LYS-141.
TISSUE=Pancreas, and PNS;
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).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 294-655 (ISOFORM 1).
PubMed=9892175;
Miyake K., Mickley L., Litman T., Zhan Z., Robey R.W., Cristensen B.,
Brangi M., Greenberger L., Dean M., Fojo T., Bates S.E.;
"Molecular cloning of cDNAs which are highly overexpressed in
mitoxantrone-resistant cells: demonstration of homology to ABC
transport genes.";
Cancer Res. 59:8-13(1999).
[15]
REVIEW.
PubMed=11590207;
Schmitz G., Langmann T., Heimerl S.;
"Role of ABCG1 and other ABCG family members in lipid metabolism.";
J. Lipid Res. 42:1513-1520(2001).
[16]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15001581; DOI=10.1074/jbc.M310785200;
Xu J., Liu Y., Yang Y., Bates S., Zhang J.T.;
"Characterization of oligomeric human half-ABC transporter ATP-binding
cassette G2.";
J. Biol. Chem. 279:19781-19789(2004).
[17]
SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-596, LACK OF GLYCOSYLATION
AT ASN-418 AND ASN-557, AND MUTAGENESIS OF ASN-418; ASN-557 AND
ASN-596.
PubMed=15807535; DOI=10.1021/bi0479858;
Diop N.K., Hrycyna C.A.;
"N-linked glycosylation of the human ABC transporter ABCG2 on
asparagine 596 is not essential for expression, transport activity, or
trafficking to the plasma membrane.";
Biochemistry 44:5420-5429(2005).
[18]
MUTAGENESIS OF ARG-482.
PubMed=15670731; DOI=10.1016/j.bbamem.2004.11.005;
Oezvegy-Laczka C., Koebloes G., Sarkadi B., Varadi A.;
"Single amino acid (482) variants of the ABCG2 multidrug transporter:
major differences in transport capacity and substrate recognition.";
Biochim. Biophys. Acta 1668:53-63(2005).
[19]
MUTAGENESIS OF LYS-86, SUBCELLULAR LOCATION, AND HOMODIMERIZATION.
PubMed=15769853; DOI=10.1242/jcs.01729;
Henriksen U., Gether U., Litman T.;
"Effect of Walker A mutation (K86M) on oligomerization and surface
targeting of the multidrug resistance transporter ABCG2.";
J. Cell Sci. 118:1417-1426(2005).
[20]
SUBUNIT, AND DISULFIDE BONDS.
PubMed=17686774; DOI=10.1074/jbc.C700133200;
Wakabayashi K., Nakagawa H., Tamura A., Koshiba S., Hoshijima K.,
Komada M., Ishikawa T.;
"Intramolecular disulfide bond is a critical check point determining
degradative fates of ATP-binding cassette (ABC) transporter ABCG2
protein.";
J. Biol. Chem. 282:27841-27846(2007).
[21]
POLYMORPHISM, AND INVOLVEMENT IN UAQTL1 AND GOUT.
PubMed=18834626; DOI=10.1016/S0140-6736(08)61343-4;
Dehghan A., Kottgen A., Yang Q., Hwang S.J., Kao W.L., Rivadeneira F.,
Boerwinkle E., Levy D., Hofman A., Astor B.C., Benjamin E.J.,
van Duijn C.M., Witteman J.C., Coresh J., Fox C.S.;
"Association of three genetic loci with uric acid concentration and
risk of gout: a genome-wide association study.";
Lancet 372:1953-1961(2008).
[22]
POLYMORPHISM, INVOLVEMENT IN UAQTL1, ASSOCIATION OF VARIANT LYS-141
WITH GOUT, AND CHARACTERIZATION OF VARIANT LYS-141.
PubMed=19506252; DOI=10.1073/pnas.0901249106;
Woodward O.M., Kottgen A., Coresh J., Boerwinkle E., Guggino W.B.,
Kottgen M.;
"Identification of a urate transporter, ABCG2, with a common
functional polymorphism causing gout.";
Proc. Natl. Acad. Sci. U.S.A. 106:10338-10342(2009).
[23]
POLYMORPHISM, INVOLVEMENT IN UAQTL1, AND ASSOCIATION OF VARIANT
LYS-141 WITH GOUT.
PubMed=20368174; DOI=10.1126/scitranslmed.3000237;
Matsuo H., Takada T., Ichida K., Nakamura T., Nakayama A.,
Ikebuchi Y., Ito K., Kusanagi Y., Chiba T., Tadokoro S., Takada Y.,
Oikawa Y., Inoue H., Suzuki K., Okada R., Nishiyama J., Domoto H.,
Watanabe S., Fujita M., Morimoto Y., Naito M., Nishio K., Hishida A.,
Wakai K., Asai Y., Niwa K., Kamakura K., Nonoyama S., Sakurai Y.,
Hosoya T., Kanai Y., Suzuki H., Hamajima N., Shinomiya N.;
"Common defects of ABCG2, a high-capacity urate exporter, cause gout:
a function-based genetic analysis in a Japanese population.";
Sci. Transl. Med. 1:5ra11-5ra11(2009).
[24]
FUNCTION, DOMAIN, AND MUTAGENESIS OF HIS-583; CYS-603 AND TYR-605.
PubMed=20705604; DOI=10.1074/jbc.M110.139170;
Desuzinges-Mandon E., Arnaud O., Martinez L., Huche F., Di Pietro A.,
Falson P.;
"ABCG2 transports and transfers heme to albumin through its large
extracellular loop.";
J. Biol. Chem. 285:33123-33133(2010).
[25]
FUNCTION.
PubMed=22132962; DOI=10.1080/15257770.2011.633953;
Nakayama A., Matsuo H., Takada T., Ichida K., Nakamura T.,
Ikebuchi Y., Ito K., Hosoya T., Kanai Y., Suzuki H., Shinomiya N.;
"ABCG2 is a high-capacity urate transporter and its genetic impairment
increases serum uric acid levels in humans.";
Nucleosides Nucleotides Nucleic Acids 30:1091-1097(2011).
[26]
REVIEW.
PubMed=22509477;
Mo W., Zhang J.T.;
"Human ABCG2: structure, function, and its role in multidrug
resistance.";
Int. J. Biochem. Mol. Biol. 3:1-27(2012).
[27]
POLYMORPHISM, INVOLVEMENT IN JR, AND VARIANT MET-12.
PubMed=22246507; DOI=10.1038/ng.1075;
Zelinski T., Coghlan G., Liu X.Q., Reid M.E.;
"ABCG2 null alleles define the Jr(a-) blood group phenotype.";
Nat. Genet. 44:131-132(2012).
[28]
POLYMORPHISM, AND INVOLVEMENT IN JR.
PubMed=22246505; DOI=10.1038/ng.1070;
Saison C., Helias V., Ballif B.A., Peyrard T., Puy H., Miyazaki T.,
Perrot S., Vayssier-Taussat M., Waldner M., Le Pennec P.Y.,
Cartron J.P., Arnaud L.;
"Null alleles of ABCG2 encoding the breast cancer resistance protein
define the new blood group system Junior.";
Nat. Genet. 44:174-177(2012).
[29]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23189181; DOI=10.1371/journal.pone.0050082;
Kobuchi H., Moriya K., Ogino T., Fujita H., Inoue K., Shuin T.,
Yasuda T., Utsumi K., Utsumi T.;
"Mitochondrial localization of ABC transporter ABCG2 and its function
in 5-aminolevulinic acid-mediated protoporphyrin IX accumulation.";
PLoS ONE 7:E50082-E50082(2012).
[30]
VARIANTS MET-12 AND LYS-141.
PubMed=12111378; DOI=10.1007/s100380200041;
Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K.,
Harigae S., Osawa S., Nakamura Y.;
"Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes
encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8,
ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and
ABCG8.";
J. Hum. Genet. 47:285-310(2002).
[31]
VARIANTS LEU-431 AND LEU-489.
PubMed=15618737; DOI=10.2133/dmpk.18.212;
Itoda M., Saito Y., Shirao K., Minami H., Ohtsu A., Yoshida T.,
Saijo N., Suzuki H., Sugiyama Y., Ozawa S., Sawada J.;
"Eight novel single nucleotide polymorphisms in ABCG2/BCRP in Japanese
cancer patients administered irinotacan.";
Drug Metab. Pharmacokinet. 18:212-217(2003).
[32]
VARIANTS MET-12; LYS-141; LEU-206 AND TYR-590.
PubMed=12544509; DOI=10.1097/00008571-200301000-00004;
Zamber C.P., Lamba J.K., Yasuda K., Farnum J., Thummel K.,
Schuetz J.D., Schuetz E.G.;
"Natural allelic variants of breast cancer resistance protein (BCRP)
and their relationship to BCRP expression in human intestine.";
Pharmacogenetics 13:19-28(2003).
[33]
CHARACTERIZATION OF VARIANTS MET-12; LYS-141 AND ASN-620.
PubMed=15838659; DOI=10.1007/s00280-004-0931-x;
Morisaki K., Robey R.W., Oezvegy-Laczka C., Honjo Y., Polgar O.,
Steadman K., Sarkadi B., Bates S.E.;
"Single nucleotide polymorphisms modify the transporter activity of
ABCG2.";
Cancer Chemother. Pharmacol. 56:161-172(2005).
[34]
VARIANTS MET-12; LEU-13; LYS-141; GLN-160; ARG-354; LEU-431; ASN-441
AND LEU-489.
PubMed=16702730; DOI=10.2133/dmpk.21.109;
Maekawa K., Itoda M., Sai K., Saito Y., Kaniwa N., Shirao K.,
Hamaguchi T., Kunitoh H., Yamamoto N., Tamura T., Minami H.,
Kubota K., Ohtsu A., Yoshida T., Saijo N., Kamatani N., Ozawa S.,
Sawada J.;
"Genetic variation and haplotype structure of the ABC transporter gene
ABCG2 in a Japanese population.";
Drug Metab. Pharmacokinet. 21:109-121(2006).
-!- FUNCTION: High-capacity urate exporter functioning in both renal
and extrarenal urate excretion. Plays a role in porphyrin
homeostasis as it is able to mediates the export of protoporhyrin
IX (PPIX) both from mitochondria to cytosol and from cytosol to
extracellular space, and cellular export of hemin, and heme.
Xenobiotic transporter that may play an important role in the
exclusion of xenobiotics from the brain. Appears to play a major
role in the multidrug resistance phenotype of several cancer cell
lines. Implicated in the efflux of numerous drugs and xenobiotics:
mitoxantrone, the photosensitizer pheophorbide, camptothecin,
methotrexate, azidothymidine (AZT), and the anthracyclines
daunorubicin and doxorubicin. {ECO:0000269|PubMed:12958161,
ECO:0000269|PubMed:20705604, ECO:0000269|PubMed:22132962,
ECO:0000269|PubMed:23189181}.
-!- SUBUNIT: Monomer under reducing conditions, the minimal functional
units is a homodimer; disulfide-linked, but the major oligomeric
form in plasma membranes is a homotetramer with possibility of
higher order oligomerization up to homododecamers.
{ECO:0000269|PubMed:15001581, ECO:0000269|PubMed:17686774}.
-!- INTERACTION:
P11309-1:PIM1; NbExp=9; IntAct=EBI-1569435, EBI-1018629;
P0CG48:UBC; NbExp=2; IntAct=EBI-1569435, EBI-3390054;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15001581,
ECO:0000269|PubMed:15769853, ECO:0000269|PubMed:15807535}; Multi-
pass membrane protein {ECO:0000255}. Mitochondrion membrane
{ECO:0000269|PubMed:23189181}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UNQ0-1; Sequence=Displayed;
Name=2;
IsoId=Q9UNQ0-2; Sequence=VSP_014232, VSP_014233;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in placenta. Low expression
in small intestine, liver and colon. {ECO:0000269|PubMed:9850061,
ECO:0000269|PubMed:9861027}.
-!- INDUCTION: Up-regulated in brain tumors.
-!- DOMAIN: The extracellular loop 3 (ECL3) is involved in binding
porphyrins and transfer them to other carriers, probably albumin.
{ECO:0000269|PubMed:20705604}.
-!- PTM: Glycosylation-deficient ABCG2 is normally expressed and
functional. {ECO:0000269|PubMed:15807535}.
-!- POLYMORPHISM: Genetic variations in ABCG2 define the blood group
Junior system (JR) [MIM:614490]. Individuals with Jr(a-) blood
group lack the Jr(a) antigen on their red blood cells. These
individuals may have anti-Jr(a) antibodies in their serum, which
can cause transfusion reactions or hemolytic disease of the fetus
or newborn. Although the clinical significance of the Jr(a-) blood
group has been controversial, severe fatal hemolytic disease of
the newborn has been reported. The Jr(a-) phenotype has a higher
frequency in individuals of Asian descent, compared to those of
European descent. The Jr(a-) phenotype is inherited as an
autosomal recessive trait. {ECO:0000269|PubMed:22246505,
ECO:0000269|PubMed:22246507}.
-!- POLYMORPHISM: Genetic variations in ABCG2 influence the variance
in serum uric acid concentrations and define the serum uric acid
concentration quantitative trait locus 1 (UAQTL1) [MIM:138900].
Excess serum accumulation of uric acid can lead to the development
of gout, a common disorder characterized by tissue deposition of
monosodium urate crystals as a consequence of hyperuricemia
(PubMed:18834626, PubMed:19506252, PubMed:20368174).
{ECO:0000269|PubMed:18834626, ECO:0000269|PubMed:19506252,
ECO:0000269|PubMed:20368174}.
-!- MISCELLANEOUS: When overexpressed, the transfected cells become
resistant to mitoxantrone, daunorubicin and doxorubicin.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AF093771; Type=Frameshift; Positions=486, 586; Evidence={ECO:0000305};
Sequence=AF093772; Type=Frameshift; Positions=386, 502, 586; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/abcg2/";
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q9UNQ0";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF103796; AAD09188.1; -; mRNA.
EMBL; AF098951; AAC97367.1; -; mRNA.
EMBL; AB056867; BAB39212.1; -; mRNA.
EMBL; AB051855; BAB46933.1; -; mRNA.
EMBL; AY017168; AAG52982.1; -; mRNA.
EMBL; AY289766; AAP44087.1; -; mRNA.
EMBL; AY288307; AAP31310.1; -; mRNA.
EMBL; AF463519; AAO14617.1; -; mRNA.
EMBL; AY333755; AAQ92941.1; -; mRNA.
EMBL; AY333756; AAQ92942.1; -; mRNA.
EMBL; AK002040; BAA92050.1; -; mRNA.
EMBL; AK290000; BAF82689.1; -; mRNA.
EMBL; DQ996467; ABI97388.1; -; Genomic_DNA.
EMBL; AC084732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC097484; AAY40902.1; -; Genomic_DNA.
EMBL; BC021281; AAH21281.1; -; mRNA.
EMBL; BC092408; AAH92408.1; -; mRNA.
EMBL; AF093771; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF093772; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS3628.1; -. [Q9UNQ0-1]
CCDS; CCDS58910.1; -. [Q9UNQ0-2]
RefSeq; NP_001244315.1; NM_001257386.1. [Q9UNQ0-2]
RefSeq; NP_004818.2; NM_004827.2. [Q9UNQ0-1]
RefSeq; XP_005263412.1; XM_005263355.3. [Q9UNQ0-1]
RefSeq; XP_011530722.1; XM_011532420.2. [Q9UNQ0-1]
UniGene; Hs.480218; -.
PDB; 5NJ3; EM; 3.78 A; A/B=2-655.
PDB; 5NJG; EM; 3.78 A; A/B=2-655.
PDBsum; 5NJ3; -.
PDBsum; 5NJG; -.
ProteinModelPortal; Q9UNQ0; -.
SMR; Q9UNQ0; -.
BioGrid; 114821; 18.
DIP; DIP-29162N; -.
IntAct; Q9UNQ0; 19.
MINT; MINT-2840423; -.
STRING; 9606.ENSP00000237612; -.
BindingDB; Q9UNQ0; -.
ChEMBL; CHEMBL5393; -.
DrugBank; DB08916; Afatinib.
DrugBank; DB11363; Alectinib.
DrugBank; DB06605; Apixaban.
DrugBank; DB04851; Biricodar dicitrate.
DrugBank; DB00921; Buprenorphine.
DrugBank; DB06772; Cabazitaxel.
DrugBank; DB04690; Camptothecin.
DrugBank; DB00958; Carboplatin.
DrugBank; DB00439; Cerivastatin.
DrugBank; DB04540; Cholesterol.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00242; Cladribine.
DrugBank; DB00631; Clofarabine.
DrugBank; DB09065; Cobicistat.
DrugBank; DB05239; Cobimetinib.
DrugBank; DB00286; Conjugated Equine Estrogens.
DrugBank; DB00091; Cyclosporine.
DrugBank; DB08912; Dabrafenib.
DrugBank; DB09102; Daclatasvir.
DrugBank; DB00970; Dactinomycin.
DrugBank; DB02115; Daidzin.
DrugBank; DB09183; Dasabuvir.
DrugBank; DB01254; Dasatinib.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB00255; Diethylstilbestrol.
DrugBank; DB01248; Docetaxel.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB00470; Dronabinol.
DrugBank; DB04881; Elacridar.
DrugBank; DB11574; Elbasvir.
DrugBank; DB00530; Erlotinib.
DrugBank; DB00783; Estradiol.
DrugBank; DB00655; Estrone.
DrugBank; DB00773; Etoposide.
DrugBank; DB00973; Ezetimibe.
DrugBank; DB03496; Flavopiridol.
DrugBank; DB00544; Fluorouracil.
DrugBank; DB00158; Folic Acid.
DrugBank; DB00317; Gefitinib.
DrugBank; DB01645; Genistein.
DrugBank; DB01016; Glyburide.
DrugBank; DB01094; Hesperetin.
DrugBank; DB00741; Hydrocortisone.
DrugBank; DB09054; Idelalisib.
DrugBank; DB00619; Imatinib.
DrugBank; DB00762; Irinotecan.
DrugBank; DB00602; Ivermectin.
DrugBank; DB00709; Lamivudine.
DrugBank; DB00448; Lansoprazole.
DrugBank; DB01097; Leflunomide.
DrugBank; DB09078; Lenvatinib.
DrugBank; DB00563; Methotrexate.
DrugBank; DB01204; Mitoxantrone.
DrugBank; DB00688; Mycophenolate mofetil.
DrugBank; DB03467; Naringenin.
DrugBank; DB00220; Nelfinavir.
DrugBank; DB04868; Nilotinib.
DrugBank; DB00698; Nitrofurantoin.
DrugBank; DB01051; Novobiocin.
DrugBank; DB00338; Omeprazole.
DrugBank; DB09330; Osimertinib.
DrugBank; DB00526; Oxaliplatin.
DrugBank; DB01229; Paclitaxel.
DrugBank; DB00213; Pantoprazole.
DrugBank; DB06589; Pazopanib.
DrugBank; DB08860; Pitavastatin.
DrugBank; DB08901; Ponatinib.
DrugBank; DB00175; Pravastatin.
DrugBank; DB00457; Prazosin.
DrugBank; DB04216; Quercetin.
DrugBank; DB01129; Rabeprazole.
DrugBank; DB08896; Regorafenib.
DrugBank; DB08864; Rilpivirine.
DrugBank; DB00740; Riluzole.
DrugBank; DB08931; Riociguat.
DrugBank; DB00503; Ritonavir.
DrugBank; DB09291; Rolapitant.
DrugBank; DB01098; Rosuvastatin.
DrugBank; DB06654; Safinamide.
DrugBank; DB01232; Saquinavir.
DrugBank; DB08934; Sofosbuvir.
DrugBank; DB00398; Sorafenib.
DrugBank; DB00795; Sulfasalazine.
DrugBank; DB00669; Sumatriptan.
DrugBank; DB01268; Sunitinib.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB04348; Taurocholic Acid.
DrugBank; DB00966; Telmisartan.
DrugBank; DB00444; Teniposide.
DrugBank; DB08880; Teriflunomide.
DrugBank; DB00624; Testosterone.
DrugBank; DB01030; Topotecan.
DrugBank; DB05294; Vandetanib.
DrugBank; DB08881; Vemurafenib.
DrugBank; DB11581; Venetoclax.
DrugBank; DB00285; Venlafaxine.
DrugBank; DB00661; Verapamil.
DrugBank; DB00541; Vincristine.
DrugBank; DB08828; Vismodegib.
DrugBank; DB00549; Zafirlukast.
DrugBank; DB00495; Zidovudine.
GuidetoPHARMACOLOGY; 792; -.
TCDB; 3.A.1.204.2; the atp-binding cassette (abc) superfamily.
iPTMnet; Q9UNQ0; -.
PhosphoSitePlus; Q9UNQ0; -.
BioMuta; ABCG2; -.
DMDM; 67462103; -.
PaxDb; Q9UNQ0; -.
PeptideAtlas; Q9UNQ0; -.
PRIDE; Q9UNQ0; -.
DNASU; 9429; -.
Ensembl; ENST00000237612; ENSP00000237612; ENSG00000118777. [Q9UNQ0-1]
Ensembl; ENST00000515655; ENSP00000426917; ENSG00000118777. [Q9UNQ0-2]
GeneID; 9429; -.
KEGG; hsa:9429; -.
UCSC; uc003hrg.4; human. [Q9UNQ0-1]
CTD; 9429; -.
DisGeNET; 9429; -.
GeneCards; ABCG2; -.
HGNC; HGNC:74; ABCG2.
HPA; CAB037299; -.
HPA; HPA054719; -.
MIM; 138900; phenotype.
MIM; 603756; gene.
MIM; 614490; phenotype.
neXtProt; NX_Q9UNQ0; -.
OpenTargets; ENSG00000118777; -.
PharmGKB; PA390; -.
eggNOG; ENOG410IN8P; Eukaryota.
eggNOG; COG0842; LUCA.
GeneTree; ENSGT00740000114855; -.
HOVERGEN; HBG050441; -.
InParanoid; Q9UNQ0; -.
KO; K05681; -.
OMA; CEAYNNP; -.
OrthoDB; EOG091G08QB; -.
PhylomeDB; Q9UNQ0; -.
TreeFam; TF105211; -.
Reactome; R-HSA-2161517; Abacavir transmembrane transport.
Reactome; R-HSA-917937; Iron uptake and transport.
SABIO-RK; Q9UNQ0; -.
ChiTaRS; ABCG2; human.
GeneWiki; ABCG2; -.
GenomeRNAi; 9429; -.
PRO; PR:Q9UNQ0; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000118777; -.
ExpressionAtlas; Q9UNQ0; baseline and differential.
Genevisible; Q9UNQ0; HS.
GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; TAS:ProtInc.
GO; GO:0015232; F:heme transporter activity; TAS:Reactome.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0008559; F:xenobiotic-transporting ATPase activity; TAS:ProtInc.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
GO; GO:0042493; P:response to drug; TAS:ProtInc.
GO; GO:0006810; P:transport; TAS:ProtInc.
GO; GO:0046415; P:urate metabolic process; IMP:UniProtKB.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR013525; ABC_2_trans.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR030256; ABCG2.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR19241:SF422; PTHR19241:SF422; 1.
Pfam; PF01061; ABC2_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Membrane;
Mitochondrion; Nucleotide-binding; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 655 ATP-binding cassette sub-family G member
2.
/FTId=PRO_0000093386.
TOPO_DOM 1 395 Cytoplasmic. {ECO:0000255}.
TRANSMEM 396 416 Helical. {ECO:0000255}.
TOPO_DOM 417 428 Extracellular. {ECO:0000255}.
TRANSMEM 429 449 Helical. {ECO:0000255}.
TOPO_DOM 450 477 Cytoplasmic. {ECO:0000255}.
TRANSMEM 478 498 Helical. {ECO:0000255}.
TOPO_DOM 499 506 Extracellular. {ECO:0000255}.
TRANSMEM 507 527 Helical. {ECO:0000255}.
TOPO_DOM 528 535 Cytoplasmic. {ECO:0000255}.
TRANSMEM 536 556 Helical. {ECO:0000255}.
TOPO_DOM 557 630 Extracellular. {ECO:0000255}.
TRANSMEM 631 651 Helical. {ECO:0000255}.
TOPO_DOM 652 655 Cytoplasmic. {ECO:0000255}.
DOMAIN 37 286 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 389 651 ABC transmembrane type-2.
NP_BIND 80 87 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
SITE 418 418 Not glycosylated.
{ECO:0000269|PubMed:15807535}.
SITE 557 557 Not glycosylated.
{ECO:0000269|PubMed:15807535}.
CARBOHYD 596 596 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15807535}.
DISULFID 592 608 {ECO:0000269|PubMed:17686774}.
DISULFID 603 603 Interchain.
{ECO:0000269|PubMed:17686774}.
VAR_SEQ 550 611 IFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQN
FCPGLNATGNNPCNYATCTGE -> VCWSISQPLHLGCHGF
STSAFHDMDLRLCSIMNFWDKTSAQDSMQQETILVTMQHVL
AKNIW (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014232.
VAR_SEQ 612 655 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014233.
VARIANT 12 12 V -> M (found in Jr(a-) blood group
phenotype; dbSNP:rs2231137).
{ECO:0000269|PubMed:12111378,
ECO:0000269|PubMed:12544509,
ECO:0000269|PubMed:15838659,
ECO:0000269|PubMed:16702730,
ECO:0000269|PubMed:22246507,
ECO:0000269|Ref.11}.
/FTId=VAR_020779.
VARIANT 13 13 S -> L. {ECO:0000269|PubMed:16702730}.
/FTId=VAR_067363.
VARIANT 141 141 Q -> K (polymorphism associated with high
serum levels of uric acid and increased
risk of gout; results in lower urate
transport rates compared to wild-type;
dbSNP:rs2231142).
{ECO:0000269|PubMed:12111378,
ECO:0000269|PubMed:12544509,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15838659,
ECO:0000269|PubMed:16702730,
ECO:0000269|PubMed:19506252,
ECO:0000269|Ref.11, ECO:0000269|Ref.8}.
/FTId=VAR_020780.
VARIANT 160 160 R -> Q (in dbSNP:rs528655917).
{ECO:0000269|PubMed:16702730}.
/FTId=VAR_067364.
VARIANT 166 166 Q -> E (in dbSNP:rs1061017).
{ECO:0000269|PubMed:12958161,
ECO:0000269|PubMed:9850061}.
/FTId=VAR_022704.
VARIANT 206 206 I -> L (in dbSNP:rs12721643).
{ECO:0000269|PubMed:12544509}.
/FTId=VAR_022705.
VARIANT 208 208 F -> S (in dbSNP:rs1061018).
{ECO:0000269|PubMed:12958161,
ECO:0000269|PubMed:9850061}.
/FTId=VAR_022706.
VARIANT 248 248 S -> P (in dbSNP:rs3116448).
/FTId=VAR_022707.
VARIANT 296 296 D -> H (in dbSNP:rs41282401).
{ECO:0000269|Ref.11}.
/FTId=VAR_030357.
VARIANT 316 316 T -> P. {ECO:0000269|Ref.9}.
/FTId=VAR_022443.
VARIANT 354 354 G -> R (in dbSNP:rs138606116).
{ECO:0000269|PubMed:16702730}.
/FTId=VAR_067365.
VARIANT 431 431 F -> L. {ECO:0000269|PubMed:15618737,
ECO:0000269|PubMed:16702730}.
/FTId=VAR_018349.
VARIANT 441 441 S -> N. {ECO:0000269|PubMed:16702730}.
/FTId=VAR_067366.
VARIANT 489 489 F -> L (in dbSNP:rs192169063).
{ECO:0000269|PubMed:15618737,
ECO:0000269|PubMed:16702730}.
/FTId=VAR_018350.
VARIANT 528 528 A -> T (in dbSNP:rs45605536).
{ECO:0000269|Ref.11}.
/FTId=VAR_030358.
VARIANT 571 571 F -> I (in dbSNP:rs9282571).
/FTId=VAR_022708.
VARIANT 590 590 N -> Y (in dbSNP:rs34264773).
{ECO:0000269|PubMed:12544509}.
/FTId=VAR_035355.
VARIANT 620 620 D -> N (in dbSNP:rs34783571).
{ECO:0000269|PubMed:15838659}.
/FTId=VAR_022709.
MUTAGEN 86 86 K->M: Inactive and altered subcellular
location. {ECO:0000269|PubMed:15769853}.
MUTAGEN 418 418 N->Q: No effect.
{ECO:0000269|PubMed:15807535}.
MUTAGEN 482 482 R->D: Decreases ATPase activity.
{ECO:0000269|PubMed:15670731}.
MUTAGEN 482 482 R->G,N,S,T: Increases ATPase activity.
{ECO:0000269|PubMed:15670731}.
MUTAGEN 482 482 R->K,I,M,Y: No change in ATPase activity.
{ECO:0000269|PubMed:15670731}.
MUTAGEN 482 482 R->T,Y: Decreases transport activity.
{ECO:0000269|PubMed:15670731}.
MUTAGEN 557 557 N->Q: No effect.
{ECO:0000269|PubMed:15807535}.
MUTAGEN 583 583 H->A: Strongly reduced binding to hemin
but not to PPIX.
{ECO:0000269|PubMed:20705604}.
MUTAGEN 596 596 N->Q: Loss of glycosylation.
{ECO:0000269|PubMed:15807535}.
MUTAGEN 603 603 C->A: Strongly reduced binding to hemin
but not to PPIX.
{ECO:0000269|PubMed:20705604}.
MUTAGEN 605 605 Y->A: No effect on hemin binding.
{ECO:0000269|PubMed:20705604}.
CONFLICT 24 24 A -> V (in Ref. 1; AAD09188 and 7;
AAP44087). {ECO:0000305}.
CONFLICT 315 316 Missing (in Ref. 10; BAA92050).
{ECO:0000305}.
CONFLICT 390 390 G -> V (in Ref. 13; AAH92408).
{ECO:0000305}.
CONFLICT 482 482 R -> G (in Ref. 14; AF093771/AF093772).
{ECO:0000305}.
CONFLICT 482 482 R -> T (in Ref. 2; AAC97367).
{ECO:0000305}.
CONFLICT 484 485 LP -> FT (in Ref. 14; AF093772).
{ECO:0000305}.
CONFLICT 501 501 P -> A (in Ref. 6; AAG52982).
{ECO:0000305}.
SEQUENCE 655 AA; 72314 MW; A8AF66B96034C5A8 CRC64;
MSSSNVEVFI PVSQGNTNGF PATASNDLKA FTEGAVLSFH NICYRVKLKS GFLPCRKPVE
KEILSNINGI MKPGLNAILG PTGGGKSSLL DVLAARKDPS GLSGDVLING APRPANFKCN
SGYVVQDDVV MGTLTVRENL QFSAALRLAT TMTNHEKNER INRVIQELGL DKVADSKVGT
QFIRGVSGGE RKRTSIGMEL ITDPSILFLD EPTTGLDSST ANAVLLLLKR MSKQGRTIIF
SIHQPRYSIF KLFDSLTLLA SGRLMFHGPA QEALGYFESA GYHCEAYNNP ADFFLDIING
DSTAVALNRE EDFKATEIIE PSKQDKPLIE KLAEIYVNSS FYKETKAELH QLSGGEKKKK
ITVFKEISYT TSFCHQLRWV SKRSFKNLLG NPQASIAQII VTVVLGLVIG AIYFGLKNDS
TGIQNRAGVL FFLTTNQCFS SVSAVELFVV EKKLFIHEYI SGYYRVSSYF LGKLLSDLLP
MRMLPSIIFT CIVYFMLGLK PKADAFFVMM FTLMMVAYSA SSMALAIAAG QSVVSVATLL
MTICFVFMMI FSGLLVNLTT IASWLSWLQY FSIPRYGFTA LQHNEFLGQN FCPGLNATGN
NPCNYATCTG EEYLVKQGID LSPWGLWKNH VALACMIVIF LTIAYLKLLF LKKYS


Related products :

Catalog number Product name Quantity
20-783-74648 MOUSE ANTI HUMAN BREAST CANCER RESISTANCE PROTEIN - Placenta-specific ATP-binding cassette transporter; Breast cancer resistance protein; Mitoxantrone resistance-associated protein; CD338 antigen; CDw 1 ml
U0960h CLIA ABCG2,ABCP,ATP-binding cassette sub-family G member 2,BCRP,BCRP1,Breast cancer resistance protein,CDw338,Homo sapiens,Human,Mitoxantrone resistance-associated protein,MXR,Placenta-specific ATP-bi 96T
E0960h ELISA ABCG2,ABCP,ATP-binding cassette sub-family G member 2,BCRP,BCRP1,Breast cancer resistance protein,CDw338,Homo sapiens,Human,Mitoxantrone resistance-associated protein,MXR,Placenta-specific ATP-b 96T
E0960h ELISA kit ABCG2,ABCP,ATP-binding cassette sub-family G member 2,BCRP,BCRP1,Breast cancer resistance protein,CDw338,Homo sapiens,Human,Mitoxantrone resistance-associated protein,MXR,Placenta-specific 96T
E0960r ELISA Abcg2,ATP-binding cassette sub-family G member 2,Bcrp1,Breast cancer resistance protein 1 homolog,Rat,Rattus norvegicus 96T
U0960r CLIA Abcg2,ATP-binding cassette sub-family G member 2,Bcrp1,Breast cancer resistance protein 1 homolog,Rat,Rattus norvegicus 96T
E0960r ELISA kit Abcg2,ATP-binding cassette sub-family G member 2,Bcrp1,Breast cancer resistance protein 1 homolog,Rat,Rattus norvegicus 96T
U0960m CLIA Abcg2,Abcp,ATP-binding cassette sub-family G member 2,Bcrp1,Breast cancer resistance protein 1 homolog,Mouse,Mus musculus 96T
E0960m ELISA Abcg2,Abcp,ATP-binding cassette sub-family G member 2,Bcrp1,Breast cancer resistance protein 1 homolog,Mouse,Mus musculus 96T
E0960m ELISA kit Abcg2,Abcp,ATP-binding cassette sub-family G member 2,Bcrp1,Breast cancer resistance protein 1 homolog,Mouse,Mus musculus 96T
EIAAB25437 ABCC6,Anthracycline resistance-associated protein,ARA,ATP-binding cassette sub-family C member 6,Homo sapiens,Human,MOAT-E,MRP6,Multidrug resistance-associated protein 6,Multi-specific organic anion t
EIAAB25433 ABCC4,ATP-binding cassette sub-family C member 4,Homo sapiens,Human,MOAT-B,MRP_cMOAT-related ABC transporter,MRP4,Multidrug resistance-associated protein 4,Multi-specific organic anion transporter B
EIAAB25426 Abcc2,ATP-binding cassette sub-family C member 2,Canalicular multidrug resistance protein,Canalicular multispecific organic anion transporter 1,Cmoat,Cmrp,Mrp2,Multidrug resistance-associated protein
EIAAB25434 Abcc5,Abcc5a,ATP-binding cassette sub-family C member 5,MOAT-C,Mouse,Mrp5,Multidrug resistance-associated protein 5,Multi-specific organic anion transporter C,Mus musculus,SMRP
EIAAB25435 ABCC5,ATP-binding cassette sub-family C member 5,Homo sapiens,Human,MOAT-C,MRP5,Multidrug resistance-associated protein 5,Multi-specific organic anion transporter C,pABC11,SMRP
E1068r ELISA kit Abcc1,ATP-binding cassette sub-family C member 1,Leukotriene C(4) transporter,LTC4 transporter,Mrp1,Multidrug resistance-associated protein 1,Rat,Rattus norvegicus 96T
E1068r ELISA Abcc1,ATP-binding cassette sub-family C member 1,Leukotriene C(4) transporter,LTC4 transporter,Mrp1,Multidrug resistance-associated protein 1,Rat,Rattus norvegicus 96T
U1068r CLIA Abcc1,ATP-binding cassette sub-family C member 1,Leukotriene C(4) transporter,LTC4 transporter,Mrp1,Multidrug resistance-associated protein 1,Rat,Rattus norvegicus 96T
U1068b CLIA ABCC1,ATP-binding cassette sub-family C member 1,Bos taurus,Bovine,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
E1068b ELISA kit ABCC1,ATP-binding cassette sub-family C member 1,Bos taurus,Bovine,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
E1068b ELISA ABCC1,ATP-binding cassette sub-family C member 1,Bos taurus,Bovine,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
E1068h ELISA kit ABCC1,ATP-binding cassette sub-family C member 1,Homo sapiens,Human,Leukotriene C(4) transporter,LTC4 transporter,MRP,MRP1,Multidrug resistance-associated protein 1 96T
E1068h ELISA ABCC1,ATP-binding cassette sub-family C member 1,Homo sapiens,Human,Leukotriene C(4) transporter,LTC4 transporter,MRP,MRP1,Multidrug resistance-associated protein 1 96T
U1068h CLIA ABCC1,ATP-binding cassette sub-family C member 1,Homo sapiens,Human,Leukotriene C(4) transporter,LTC4 transporter,MRP,MRP1,Multidrug resistance-associated protein 1 96T
U1242h CLIA ABC1,ABC-1,ABCA1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,CERP,Cholesterol efflux regulatory protein,Homo sapiens,Human 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur