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Literature summary extracted from

  • Letourneau, I.J.; Nakajima, A.; Deeley, R.G.; Cole, S.P.
    Role of proline 1150 in functional interactions between the membrane spanning domains and nucleotide binding domains of the MRP1 (ABCC1) transporter (2008), Biochem. Pharmacol., 75, 1659-1669.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.6.2.2 expression of wild-type and mutant enzymes in HEK-293 cell membranes Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
7.6.2.2 P1150A mutant MRP1 exhibits selectively increased estradiol glucuronide and methotrexate transport as well as altered interactions with ATP, the mutant displays very a low level of substrate-independent vanadate-induced trapping of [alphalpha32P]8N3ADP due to enhanced ADP release following ATP hydrolysis rather than a reduction in ATP hydrolysis itself. [alpha32P]8N3ADP trapping by MRP1-P1150A can be increased by using Ni2+ instead of Mg2+, and by decreasing temperature; however, the transport properties of the mutant remain unchanged Homo sapiens
7.6.2.2 P1150G mutant MRP1 exhibits selectively increased estradiol glucuronide and methotrexate transport as well as altered interactions with ATP, the mutant displays very a low level of substrate-independent vanadate-induced trapping of [alpha32P]8N3ADP due to enhanced ADP release following ATP hydrolysis rather than a reduction in ATP hydrolysis itself Homo sapiens
7.6.2.2 P1150I mutant MRP1 exhibits selectively increased estradiol glucuronide and methotrexate transport as well as altered interactions with ATP, the mutant displays very a low level of substrate-independent vanadate-induced trapping of [alpha32P]8N3ADP due to enhanced ADP release following ATP hydrolysis rather than a reduction in ATP hydrolysis itself Homo sapiens
7.6.2.2 P1150L mutant MRP1 exhibits selectively increased estradiol glucuronide and methotrexate transport as well as altered interactions with ATP, the mutant displays very a low level of substrate-independent vanadate-induced trapping of [alpha32P]8N3ADP due to enhanced ADP release following ATP hydrolysis rather than a reduction in ATP hydrolysis itself Homo sapiens
7.6.2.2 P1150V mutant MRP1 exhibits selectively increased estradiol glucuronide and methotrexate transport as well as altered interactions with ATP, the mutant displays very a low level of substrate-independent vanadate-induced trapping of [alpha32P]8N3ADP due to enhanced ADP release following ATP hydrolysis rather than a reduction in ATP hydrolysis itself Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.6.2.2 membrane
-
Homo sapiens 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.6.2.2 Mg2+
-
Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.6.2.2 ATP + H2O + xenobiotic/in Homo sapiens the ATP-binding cassette multidrug resistance protein 1 mediates ATP-dependent cellular efflux of drugs and organic anions ADP + phosphate + xenobiotic/out
-
?

Organism

EC Number Organism UniProt Comment Textmining
7.6.2.2 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.6.2.2 recombinant wild-type and mutant enzymes from HEK-293 cells partially by membrane preparation Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.6.2.2 ATP + H2O + xenobiotic/in the ATP-binding cassette multidrug resistance protein 1 mediates ATP-dependent cellular efflux of drugs and organic anions Homo sapiens ADP + phosphate + xenobiotic/out
-
?
7.6.2.2 ATP + H2O + xenobiotic/in functional importance of MRP1-Pro1150 at the interface of transmembrane helix 15 and cytoplasmic loop 7 Homo sapiens ADP + phosphate + xenobiotic/out
-
?

Synonyms

EC Number Synonyms Comment Organism
7.6.2.2 MRP1
-
Homo sapiens
7.6.2.2 multidrug resistance protein 1
-
Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
7.6.2.2 ATP
-
Homo sapiens