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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.
13-FEB-2019, entry version 191.
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:
Self; NbExp=5; IntAct=EBI-1569435, EBI-1569435;
P11309-2:PIM1; NbExp=5; IntAct=EBI-1569435, EBI-1018633;
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";
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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.
PDB; 6ETI; EM; 3.10 A; A/B=1-655.
PDB; 6FEQ; EM; 3.60 A; A/B=1-655.
PDB; 6FFC; EM; 3.56 A; A/B=2-655.
PDB; 6HBU; EM; 3.09 A; A/B=1-655.
PDB; 6HCO; EM; 3.58 A; A/B=2-655.
PDB; 6HIJ; EM; 3.56 A; A/B=1-655.
PDB; 6HZM; EM; 3.09 A; A/B=1-655.
PDBsum; 5NJ3; -.
PDBsum; 5NJG; -.
PDBsum; 6ETI; -.
PDBsum; 6FEQ; -.
PDBsum; 6FFC; -.
PDBsum; 6HBU; -.
PDBsum; 6HCO; -.
PDBsum; 6HIJ; -.
PDBsum; 6HZM; -.
ProteinModelPortal; Q9UNQ0; -.
SMR; Q9UNQ0; -.
BioGrid; 114821; 19.
DIP; DIP-29162N; -.
IntAct; Q9UNQ0; 19.
MINT; Q9UNQ0; -.
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; -.
EPD; Q9UNQ0; -.
jPOST; Q9UNQ0; -.
PaxDb; Q9UNQ0; -.
PeptideAtlas; Q9UNQ0; -.
PRIDE; Q9UNQ0; -.
ProteomicsDB; 85323; -.
ProteomicsDB; 85324; -. [Q9UNQ0-2]
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; -.
EuPathDB; HostDB:ENSG00000118777.10; -.
GeneCards; ABCG2; -.
HGNC; HGNC:74; ABCG2.
HPA; CAB037299; -.
HPA; HPA054719; -.
MalaCards; ABCG2; -.
MIM; 138900; phenotype.
MIM; 603756; gene.
MIM; 614490; phenotype.
neXtProt; NX_Q9UNQ0; -.
OpenTargets; ENSG00000118777; -.
PharmGKB; PA390; -.
eggNOG; ENOG410IN8P; Eukaryota.
eggNOG; COG0842; LUCA.
GeneTree; ENSGT00940000162658; -.
HOVERGEN; HBG050441; -.
InParanoid; Q9UNQ0; -.
KO; K05681; -.
OMA; AICTGEE; -.
OrthoDB; 51918at2759; -.
PhylomeDB; Q9UNQ0; -.
TreeFam; TF105211; -.
Reactome; R-HSA-2161517; Abacavir transmembrane transport.
Reactome; R-HSA-917937; Iron uptake and transport.
SABIO-RK; Q9UNQ0; -.
SIGNOR; Q9UNQ0; -.
ChiTaRS; ABCG2; human.
GeneWiki; ABCG2; -.
GenomeRNAi; 9429; -.
PRO; PR:Q9UNQ0; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000118777; Expressed in 188 organ(s), highest expression level in jejunal mucosa.
ExpressionAtlas; Q9UNQ0; baseline and differential.
Genevisible; Q9UNQ0; HS.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
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:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0015232; F:heme transporter activity; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0008559; F:xenobiotic transmembrane transporting ATPase activity; TAS:ProtInc.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0042493; P:response to drug; TAS:ProtInc.
GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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:SF452; PTHR19241:SF452; 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 (in dbSNP:rs1319203095).
{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 (in dbSNP:rs1354553769).
{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}.
STRAND 37 42 {ECO:0000244|PDB:6HBU}.
STRAND 66 71 {ECO:0000244|PDB:6HBU}.
STRAND 73 79 {ECO:0000244|PDB:6HBU}.
HELIX 86 93 {ECO:0000244|PDB:6HBU}.
TURN 99 101 {ECO:0000244|PDB:6ETI}.
STRAND 104 108 {ECO:0000244|PDB:6HBU}.
TURN 116 120 {ECO:0000244|PDB:6HBU}.
STRAND 121 124 {ECO:0000244|PDB:6HBU}.
HELIX 136 147 {ECO:0000244|PDB:6HBU}.
HELIX 154 168 {ECO:0000244|PDB:6HBU}.
TURN 172 175 {ECO:0000244|PDB:6HBU}.
STRAND 181 183 {ECO:0000244|PDB:6HBU}.
HELIX 188 198 {ECO:0000244|PDB:6HBU}.
TURN 199 202 {ECO:0000244|PDB:6HBU}.
STRAND 205 211 {ECO:0000244|PDB:6HBU}.
TURN 212 215 {ECO:0000244|PDB:6HBU}.
HELIX 218 232 {ECO:0000244|PDB:6HBU}.
TURN 233 235 {ECO:0000244|PDB:6HBU}.
STRAND 237 241 {ECO:0000244|PDB:6HBU}.
HELIX 247 250 {ECO:0000244|PDB:6HBU}.
STRAND 254 260 {ECO:0000244|PDB:6HBU}.
STRAND 263 268 {ECO:0000244|PDB:6HBU}.
HELIX 274 277 {ECO:0000244|PDB:6HBU}.
TURN 278 281 {ECO:0000244|PDB:6HBU}.
HELIX 290 297 {ECO:0000244|PDB:6HBU}.
TURN 298 301 {ECO:0000244|PDB:6HBU}.
HELIX 303 307 {ECO:0000244|PDB:6HBU}.
HELIX 328 337 {ECO:0000244|PDB:6HBU}.
HELIX 340 352 {ECO:0000244|PDB:6HBU}.
HELIX 373 390 {ECO:0000244|PDB:6HBU}.
HELIX 393 412 {ECO:0000244|PDB:6HBU}.
HELIX 423 439 {ECO:0000244|PDB:6HBU}.
HELIX 440 447 {ECO:0000244|PDB:6HBU}.
TURN 448 451 {ECO:0000244|PDB:6HBU}.
HELIX 452 460 {ECO:0000244|PDB:6HBU}.
HELIX 466 478 {ECO:0000244|PDB:6HBU}.
HELIX 479 483 {ECO:0000244|PDB:6HBU}.
HELIX 484 492 {ECO:0000244|PDB:6HBU}.
TURN 493 497 {ECO:0000244|PDB:6HBU}.
HELIX 504 528 {ECO:0000244|PDB:6HBU}.
HELIX 535 550 {ECO:0000244|PDB:6HBU}.
STRAND 553 556 {ECO:0000244|PDB:6HBU}.
TURN 558 560 {ECO:0000244|PDB:6HBU}.
TURN 563 567 {ECO:0000244|PDB:6HBU}.
HELIX 568 570 {ECO:0000244|PDB:6HBU}.
HELIX 573 585 {ECO:0000244|PDB:6HBU}.
STRAND 586 588 {ECO:0000244|PDB:6HBU}.
STRAND 597 599 {ECO:0000244|PDB:6HBU}.
STRAND 602 605 {ECO:0000244|PDB:6ETI}.
HELIX 610 617 {ECO:0000244|PDB:6HBU}.
HELIX 624 649 {ECO:0000244|PDB:6HBU}.
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


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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

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1616: ABC transporters
WP1531: Vitamin D synthesis
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
WP1493: Carbon assimilation C4 pathway
WP1689: Porphyrin and chlorophyll metabolism
WP1713: Two-component system
WP1909: Signal regulatory protein (SIRP) family interactions
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination

Related Genes :
[ABCG2 ABCP BCRP BCRP1 MXR] 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 Abcp Bcrp1] ATP-binding cassette sub-family G member 2 (Breast cancer resistance protein 1 homolog) (Urate exporter) (CD antigen CD338)
[ABCB1 MDR1 PGY1] Multidrug resistance protein 1 (EC 7.6.2.2) (ATP-binding cassette sub-family B member 1) (P-glycoprotein 1) (CD antigen CD243)
[ABCC6 ARA MRP6] Multidrug resistance-associated protein 6 (ATP-binding cassette sub-family C member 6) (Anthracycline resistance-associated protein) (Multi-specific organic anion transporter E) (MOAT-E)
[ABCC11 MRP8] ATP-binding cassette sub-family C member 11 (Multidrug resistance-associated protein 8)
[ABCA1 ABC1 CERP] ATP-binding cassette sub-family A member 1 (ATP-binding cassette transporter 1) (ABC-1) (ATP-binding cassette 1) (Cholesterol efflux regulatory protein)
[ABCA4 ABCR] Retinal-specific ATP-binding cassette transporter (ATP-binding cassette sub-family A member 4) (RIM ABC transporter) (RIM protein) (RmP) (Stargardt disease protein)
[ABCB9 KIAA1520] ATP-binding cassette sub-family B member 9 (ATP-binding cassette transporter 9) (ABC transporter 9 protein) (hABCB9) (TAP-like protein) (TAPL)
[ABCB10] ATP-binding cassette sub-family B member 10, mitochondrial (ATP-binding cassette transporter 10) (ABC transporter 10 protein) (Mitochondrial ATP-binding cassette 2) (M-ABC2)
[TAP1 ABCB2 PSF1 RING4 Y3] Antigen peptide transporter 1 (APT1) (ATP-binding cassette sub-family B member 2) (Peptide supply factor 1) (Peptide transporter PSF1) (PSF-1) (Peptide transporter TAP1) (Peptide transporter involved in antigen processing 1) (Really interesting new gene 4 protein)
[Abcb4 Mdr2 Pgy-2 Pgy2] Phosphatidylcholine translocator ABCB4 (ATP-binding cassette sub-family B member 4) (Multidrug resistance protein 2) (Multidrug resistance protein 3) (EC 7.6.2.2) (P-glycoprotein 2) (P-glycoprotein 3)
[TAP2 ABCB3 PSF2 RING11 Y1] Antigen peptide transporter 2 (APT2) (ATP-binding cassette sub-family B member 3) (Peptide supply factor 2) (Peptide transporter PSF2) (PSF-2) (Peptide transporter TAP2) (Peptide transporter involved in antigen processing 2) (Really interesting new gene 11 protein)
[ABCA12 ABC12] ATP-binding cassette sub-family A member 12 (ATP-binding cassette transporter 12) (ATP-binding cassette 12)
[Abcg1 Abc8 Wht1] ATP-binding cassette sub-family G member 1 (ATP-binding cassette transporter 8) (White protein homolog)
[ABCB4 MDR3 PGY3] Phosphatidylcholine translocator ABCB4 (ATP-binding cassette sub-family B member 4) (Multidrug resistance protein 3) (EC 7.6.2.2) (P-glycoprotein 3)
[Abca1 Abc1] ATP-binding cassette sub-family A member 1 (ATP-binding cassette transporter 1) (ABC-1) (ATP-binding cassette 1)
[ABCB6 MTABC3 PRP UMAT] ATP-binding cassette sub-family B member 6, mitochondrial (Mitochondrial ABC transporter 3) (Mt-ABC transporter 3) (P-glycoprotein-related protein) (Ubiquitously-expressed mammalian ABC half transporter)
[ABCB7 ABC7] ATP-binding cassette sub-family B member 7, mitochondrial (ATP-binding cassette transporter 7) (ABC transporter 7 protein)
[ABCG1 ABC8 WHT1] ATP-binding cassette sub-family G member 1 (ATP-binding cassette transporter 8) (White protein homolog)
[Abcb1a Abcb4 Mdr1a Mdr3 Pgy-3 Pgy3] Multidrug resistance protein 1A (EC 7.6.2.2) (ATP-binding cassette sub-family B member 1A) (MDR1A) (Multidrug resistance protein 3) (P-glycoprotein 3)
[Abcb1b Abcb1 Mdr1 Mdr1b Pgy1 Pgy1-1] Multidrug resistance protein 1B (EC 7.6.2.2) (ATP-binding cassette sub-family B member 1B) (P-glycoprotein 1) (CD antigen CD243)
[Abcb10] ATP-binding cassette sub-family B member 10, mitochondrial (ABC-mitochondrial erythroid protein) (ABC-me protein) (ATP-binding cassette transporter 10) (ABC transporter 10 protein)
[Abcb4 Mdr2 Pgp3 Pgy2] Phosphatidylcholine translocator ABCB4 (ATP-binding cassette sub-family B member 4) (Multidrug resistance protein 2) (Multidrug resistance protein 3) (EC 7.6.2.2) (P-glycoprotein 2) (P-glycoprotein 3)
[Abca2 Abc2] ATP-binding cassette sub-family A member 2 (ATP-binding cassette transporter 2) (ATP-binding cassette 2)
[Abca4 Abcr] Retinal-specific ATP-binding cassette transporter (ATP-binding cassette sub-family A member 4) (RIM ABC transporter) (RIM protein) (RmP)
[Abca7] ATP-binding cassette sub-family A member 7
[ABCA7] ATP-binding cassette sub-family A member 7 (ABCA-SSN) (Autoantigen SS-N) (Macrophage ABC transporter)
[ABCB4 PGP3 PGY3] Phosphatidylcholine translocator ABCB4 (ATP-binding cassette sub-family B member 4) (Multidrug resistance protein 3) (EC 7.6.2.2) (P-glycoprotein 3)
[Abcg8] ATP-binding cassette sub-family G member 8 (Sterolin-2)
[Abcg5] ATP-binding cassette sub-family G member 5 (Sterolin-1)

Bibliography :