ABCG2
entrez
9429
canonical
uniprot
Q9UNQ0
canonical
ensembl
ENSG00000118777
resolver
ensp
ENSP00000237612
resolver
ensp
ENSP00000426917
resolver
ensp
ENSP00000498246
resolver
ensp
ENSP00000559138
resolver
ensp
ENSP00000559143
resolver
ensp
ENSP00000559144
resolver
ensp
ENSP00000559146
resolver
ensp
ENSP00000559149
resolver
ensp
ENSP00000559151
resolver
ensp
ENSP00000559154
resolver
ensp
ENSP00000559157
resolver
ensp
ENSP00000632272
resolver
genesymbol
ABCG2
resolver
genesymbol_syn
ABCP
resolver
genesymbol_syn
BCRP
resolver
genesymbol_syn
BCRP1
resolver
genesymbol_syn
MXR
resolver
hgnc
HGNC:74
resolver
uniprot
A0A1W3
resolver
uniprot
A8K1T5
resolver
uniprot
O95374
resolver
uniprot
Q4W5I3
resolver
uniprot
Q53ZQ1
resolver
uniprot
Q569L4
resolver
uniprot
Q5YLG4
resolver
uniprot
Q86V64
resolver
uniprot
Q8IX16
resolver
uniprot
Q96LD6
resolver
uniprot
Q96TA8
resolver
uniprot
Q9BY73
resolver
uniprot
Q9NUS0
resolver
uniprot_entry
ABCG2_HUMAN
resolver
uniprot_sec
A0A1W3
resolver
uniprot_sec
A8K1T5
resolver
uniprot_sec
O95374
resolver
uniprot_sec
Q4W5I3
resolver
uniprot_sec
Q53ZQ1
resolver
uniprot_sec
Q569L4
resolver
uniprot_sec
Q5YLG4
resolver
uniprot_sec
Q86V64
resolver
uniprot_sec
Q8IX16
resolver
uniprot_sec
Q96LD6
resolver
uniprot_sec
Q96TA8
resolver
uniprot_sec
Q9BY73
resolver
uniprot_sec
Q9NUS0
resolver
activity_regulation
ACTIVITY REGULATION: Specifically inhibited by the fungal toxin fumitremorgin C and Ko143. {ECO:0000269|PubMed:12477054}.
uniprot
proteins
amino_acid_sequence
MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS
uniprot
proteins
ec_number
7.6.2.-
uniprot
proteins
ec_number
7.6.2.2
uniprot
proteins
function
FUNCTION: Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells (PubMed:11306452, PubMed:12958161, PubMed:19506252, PubMed:20705604, PubMed:28554189, PubMed:30405239, PubMed:31003562). Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme (PubMed:20705604, PubMed:23189181). Also mediates the efflux of sphingosine-1-P from cells (PubMed:20110355). Acts as a urate exporter functioning in both renal and extrarenal urate excretion (PubMed:19506252, PubMed:20368174, PubMed:22132962, PubMed:31003562, PubMed:36749388). In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates (PubMed:12682043, PubMed:28554189, PubMed:30405239). Mediates the secretion of the vitamins riboflavin and biotin into milk (By similarity). Involved in the excretion of the riboflavin-derived compound lumichrome into the intestinal lumen and in its secretion into milk (PubMed:39337371). Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity). Plays an important role in the exclusion of xenobiotics from the brain (Probable). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux (PubMed:11306452, PubMed:12477054, PubMed:15670731, PubMed:18056989, PubMed:31254042). In placenta, it limits the penetration of drugs from the maternal plasma into the fetus (By similarity). May play a role in early stem cell self-renewal by blocking differentiation (By similarity). In inflammatory macrophages, exports itaconate from the cytosol to the extracellular compartment and limits the activation of TFEB-dependent lysosome biogenesis involved in antibacterial innate immune response (PubMed:38181789). Operates at apical membranes of polarized cells such as hepatocytes and intestinal epithelial cells, where it may contribute to the efflux of conjugated substrates from intestine and liver into the intestinal lumen as well as their enterohepatic recycling. Can transport estrogen and androgen substrates conjugated with glucuronate or sulfate at C-3, C-16 and C-17 positions. Among androgen glucuronates, appears to selectively transport dihydrotestosterone-17-glucuronate while displaying no transporter activity toward testosterone, androsterone and etiocholanolone glucuronates (PubMed:29175180, PubMed:30959153, PubMed:39993711). {ECO:0000250|UniProtKB:Q7TMS5, ECO:0000269|PubMed:11306452, ECO:0000269|PubMed:12477054, ECO:0000269|PubMed:12682043, ECO:0000269|PubMed:12958161, ECO:0000269|PubMed:15670731, ECO:0000269|PubMed:18056989, ECO:0000269|PubMed:19506252, ECO:0000269|PubMed:20110355, ECO:0000269|PubMed:20368174, ECO:0000269|PubMed:20705604, ECO:0000269|PubMed:22132962, ECO:0000269|PubMed:23189181, ECO:0000269|PubMed:28554189, ECO:0000269|PubMed:29175180, ECO:0000269|PubMed:30405239, ECO:0000269|PubMed:30959153, ECO:0000269|PubMed:31003562, ECO:0000269|PubMed:31254042, ECO:0000269|PubMed:36749388, ECO:0000269|PubMed:38181789, ECO:0000269|PubMed:39337371, ECO:0000269|PubMed:39993711, ECO:0000305|PubMed:12958161}.
uniprot
proteins
mass_dalton
72314
uniprot
proteins
mutagenesis
MUTAGEN 71; /note="M->V: Decreased protein abundance. No effect on substrate transmembrane transport."; /evidence="ECO:0000269|PubMed:31254042"; MUTAGEN 86; /note="K->M: Decreased protein abundance. Decreased localization to the plasma membrane and retained intracellularly. Loss of ATPase-coupled transmembrane transporter activity."; /evidence="ECO:0000269|PubMed:15769853, ECO:0000269|PubMed:31254042"; MUTAGEN 211; /note="E->Q: Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Loss of ATP-dependent itaconate export resulting in itaconate cytosolic accumulation."; /evidence="ECO:0000269|PubMed:28554189, ECO:0000269|PubMed:30405239, ECO:0000269|PubMed:38181789"; MUTAGEN 362; /note="T->A: Loss of phosphorylation by PIM1. Decreased localization to the plasma membrane. Decreased homooligomerization. Loss of function in resistance to drug treatment."; /evidence="ECO:0000269|PubMed:18056989"; MUTAGEN 362; /note="T->D: Loss of phosphorylation by PIM1. Constitutive drug resistance independent of PIM1."; /evidence="ECO:0000269|PubMed:18056989"; MUTAGEN 383; /note="R->C: Loss of protein expression."; /evidence="ECO:0000269|PubMed:31254042"; MUTAGEN 418; /note="N->Q: No effect."; /evidence="ECO:0000269|PubMed:15807535"; MUTAGEN 435; /note="T->A: No effect on stability. Increased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased substrate-induced ATP hydrolysis. Increased substrate transport."; /evidence="ECO:0000269|PubMed:30405239"; MUTAGEN 435; /note="T->F: No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport."; /evidence="ECO:0000269|PubMed:30405239"; MUTAGEN 436; /note="N->A: No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport."; /evidence="ECO:0000269|PubMed:30405239"; MUTAGEN 439; /note="F->A: No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport."; /evidence="ECO:0000269|PubMed:30405239"; MUTAGEN 482; /note="R->D: Decreases ATPase activity."; /evidence="ECO:0000269|PubMed:15670731"; MUTAGEN 482; /note="R->G,N,S,T: Increases ATPase activity."; /evidence="ECO:0000269|PubMed:15670731"; MUTAGEN 482; /note="R->K,I,M,Y: No change in ATPase activity."; /evidence="ECO:0000269|PubMed:15670731"; MUTAGEN 482; /note="R->T,Y: Decreases transport activity."; /evidence="ECO:0000269|PubMed:15670731"; MUTAGEN 546; /note="V->A: No effect on stability. No effect on estrone-3 sulfate ATPase-coupled transmembrane transporter activity. No effect on substrate-induced ATP hydrolysis. No effect on substrate transport."; /evidence="ECO:0000269|PubMed:30405239"; MUTAGEN 546; /note="V->F: No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased basal and substrate-induced ATP hydrolysis. Decreased substrate transport."; /evidence="ECO:0000269|PubMed:30405239"; MUTAGEN 549; /note="M->A: No effect on stability. No effect on estrone-3 sulfate ATPase-coupled transmembrane transporter activity. No effect on substrate-induced ATP hydrolysis. No effect on substrate transport."; /evidence="ECO:0000269|PubMed:30405239"; MUTAGEN 554; /note="L->A: No effect on stability. Increased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased basal and substrate-induced ATP hydrolysis. Increased substrate transport."; /evidence="ECO:0000269|PubMed:30405239"; MUTAGEN 555; /note="L->A: Loss of protein expression."; /evidence="ECO:0000269|PubMed:30405239"; MUTAGEN 557; /note="N->Q: No effect."; /evidence="ECO:0000269|PubMed:15807535"; MUTAGEN 583; /note="H->A: Strongly reduced binding to hemin but not to PPIX."; /evidence="ECO:0000269|PubMed:20705604"; MUTAGEN 596; /note="N->Q: Loss of glycosylation."; /evidence="ECO:0000269|PubMed:15807535"; MUTAGEN 603; /note="C->A: Strongly reduced binding to hemin but not to PPIX."; /evidence="ECO:0000269|PubMed:20705604"; MUTAGEN 605; /note="Y->A: No effect on hemin binding."; /evidence="ECO:0000269|PubMed:20705604
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:15807535, PubMed:23189181). Glycosylation-deficient ABCG2 is normally expressed and functional. {ECO:0000269|PubMed:15807535, ECO:0000269|PubMed:23189181}.; PTM: Phosphorylated. Phosphorylation at Thr-362 by PIM1 is induced by drugs like mitoxantrone and is associated with cells increased drug resistance. It regulates the localization to the plasma membrane, the homooligomerization and therefore, the activity of the transporter. {ECO:0000269|PubMed:18056989}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCG family
uniprot
proteins
protein_family
Eye pigment precursor importer (TC 3.A.1.204) subfamily
uniprot
proteins
pubmed
11306452
uniprot
proteins
pubmed
11533706
uniprot
proteins
pubmed
12111378
uniprot
proteins
pubmed
12477054
uniprot
proteins
pubmed
12544509
uniprot
proteins
pubmed
12682043
uniprot
proteins
pubmed
12958161
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15001581
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15618737
uniprot
proteins
pubmed
15670731
uniprot
proteins
pubmed
15769853
uniprot
proteins
pubmed
15807535
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15838659
uniprot
proteins
pubmed
16702730
uniprot
proteins
pubmed
17686774
uniprot
proteins
pubmed
18056989
uniprot
proteins
pubmed
18834626
uniprot
proteins
pubmed
19506252
uniprot
proteins
pubmed
20110355
uniprot
proteins
pubmed
20332504
uniprot
proteins
pubmed
20368174
uniprot
proteins
pubmed
20705604
uniprot
proteins
pubmed
22132962
uniprot
proteins
pubmed
22246505
uniprot
proteins
pubmed
22246507
uniprot
proteins
pubmed
23189181
uniprot
proteins
pubmed
24312054
uniprot
proteins
pubmed
28554189
uniprot
proteins
pubmed
28623970
uniprot
proteins
pubmed
29175180
uniprot
proteins
pubmed
29610494
uniprot
proteins
pubmed
30405239
uniprot
proteins
pubmed
30959153
uniprot
proteins
pubmed
31003562
uniprot
proteins
pubmed
31254042
uniprot
proteins
pubmed
36749388
uniprot
proteins
pubmed
38181789
uniprot
proteins
pubmed
39337371
uniprot
proteins
pubmed
39993711
uniprot
proteins
pubmed
9850061
uniprot
proteins
pubmed
9861027
uniprot
proteins
pubmed
9892175
uniprot
proteins
sequence_length
655
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15001581, ECO:0000269|PubMed:15769853, ECO:0000269|PubMed:15807535, ECO:0000269|PubMed:18056989, ECO:0000269|PubMed:31003562, ECO:0000269|PubMed:31254042}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:19506252}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:23189181}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched in membrane lipid rafts. {ECO:0000269|PubMed:28623970}.
uniprot
proteins
transmembrane_region
TRANSMEM 396..416; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 429..449; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 478..498; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 507..527; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 536..556; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 631..651; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins