ABCC3 p.Val765Leu
| Predicted by SNAP2: | A: N (93%), C: N (93%), D: D (53%), E: N (57%), F: N (82%), G: N (61%), H: N (57%), I: N (93%), K: N (57%), L: N (93%), M: N (82%), N: N (66%), P: N (53%), Q: N (66%), R: N (57%), S: N (72%), T: N (78%), W: N (57%), Y: N (66%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: N, K: D, L: N, M: D, N: D, P: D, Q: D, R: D, S: D, T: D, W: D, Y: D, |
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[hide] Pharmacogenetics of drug transporters in the enter... Pharmacogenomics. 2011 May;12(5):611-31. Stieger B, Meier PJ
Pharmacogenetics of drug transporters in the enterohepatic circulation.
Pharmacogenomics. 2011 May;12(5):611-31., [PMID:21619426]
Abstract [show]
This article summarizes the impact of the pharmacogenetics of drug transporters expressed in the enterohepatic circulation on the pharmacokinetics and pharmacodynamics of drugs. The role of pharmacogenetics in the function of drug transporter proteins in vitro is now well established and evidence is rapidly accumulating from in vivo pharmacokinetic studies, which suggests that genetic variants of drug transporter proteins can translate into clinically relevant phenotypes. However, a large amount of conflicting information on the clinical relevance of drug transporter proteins has so far precluded the emergence of a clear picture regarding the role of drug transporter pharmacogenetics in medical practice. This is very well exemplified by the case of P-glycoprotein (MDR1, ABCB1). The challenge is now to develop pharmacogenetic models with sufficient predictive power to allow for translation into drug therapy. This will require a combination of pharmacogenetics of drug transporters, drug metabolism and pharmacodynamics of the respective drugs.
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No. Sentence Comment
97 Gene name Transporter SNP Protein Population size (n) In vitro function Ref. Intestinal efflux transporters (cont.) ABCC2 MRP2 c.1249G>A p.V417I N/A Unchanged [221] c.1249G>A p.S789F N/A Reduced transport protein expression, no change in transport activity [221] c.1249G>A p.A1450T N/A Reduced transport protein expression, no change in transport activity [221] ABCC3 MRP3 c.32G>A p.G11D N/A Unchanged [222] c.1037C>T p.S346F N/A Reduced transport activity [222] c.1820G>A p.S607N N/A Reduced transport activity [222] c.2293G>C p.V765L N/A Unchanged [222] c.2758C>T p.P920S N/A Unchanged [222] c.2768G>A p.R923Q N/A Increased transport activity [222] c.3856G>C p.R1286G N/A Unchanged [222] c.3890G>A p.R1297H 52 Unchanged [131] c.4042C>T p.R1348C N/A Increased transport activity [222] c.4094A>G p.Q1365R N/A Unchanged [222] c.4141C>A p.R1381S N/A Unchanged [222] Liver uptake transporters SLCO1B1 OATP1B1 c.218T>C p.F73L N/A Increased Km , reduced protein synthesis and membrane expression [143] c.245T>C p.V82A N/A [143] c.388A>G p.N130D N/A Increased Km [143] c.455G>A p.R152K N/A [143] c.463C>A p.P155T N/A Unchanged [143] c.467A>G p.E156G N/A [143] c.521T>C p.V174A N/A Decreased Vmax , reduced transport protein expression [143] c.721G>A p.D241N N/A [143] c.1058T>C p.I353T N/A Increased Km , reduced transport protein expression [143] c.1294A>G p.N432D N/A Decreased Vmax [143] c.1385A>G p.D462G N/A Decreased Vmax [143] c.1463G>C p.G488A N/A Reduced intrinsic clearance, reduced transport protein expression [143] c.1964A>G p.D655G N/A Increased Km [143] c.2000A>G p.E667G N/A Unchanged [143] SLCO1B3 OATP1B3 c.334T>G p.S112A N/A Unchanged [223,224] c.439A>G p.T147A N/A Unchanged [223] c.699G>A p.M233I N/A Reduced transport activity, substrate-dependent alteration of Km [223,224] c.767G>C p.G256A N/A Unchanged [223] c.1559A>G p.H520P N/A Reduced transport activity [223] c.1564G>T p.G522C N/A Reduced transport activity [224] c.1679T>C p.V560A N/A Reduced transport activity [223] SLCO2B1 OATP2B1 c.43C>T p.P15S N/A Reduced transport activity [149] c.601G>A p.V201M N/A Reduced transport activity [149] c.1175C>T p.T392I N/A Reduced Vmax [148] For more information on members of the SLC superfamily of transporters please consult [301] and for more information of ABC transporters please consult [302].
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ABCC3 p.Val765Leu 21619426:97:530
status: NEW[hide] Xenobiotic, bile acid, and cholesterol transporter... Pharmacol Rev. 2010 Mar;62(1):1-96. Epub 2010 Jan 26. Klaassen CD, Aleksunes LM
Xenobiotic, bile acid, and cholesterol transporters: function and regulation.
Pharmacol Rev. 2010 Mar;62(1):1-96. Epub 2010 Jan 26., [PMID:20103563]
Abstract [show]
Transporters influence the disposition of chemicals within the body by participating in absorption, distribution, and elimination. Transporters of the solute carrier family (SLC) comprise a variety of proteins, including organic cation transporters (OCT) 1 to 3, organic cation/carnitine transporters (OCTN) 1 to 3, organic anion transporters (OAT) 1 to 7, various organic anion transporting polypeptide isoforms, sodium taurocholate cotransporting polypeptide, apical sodium-dependent bile acid transporter, peptide transporters (PEPT) 1 and 2, concentrative nucleoside transporters (CNT) 1 to 3, equilibrative nucleoside transporter (ENT) 1 to 3, and multidrug and toxin extrusion transporters (MATE) 1 and 2, which mediate the uptake (except MATEs) of organic anions and cations as well as peptides and nucleosides. Efflux transporters of the ATP-binding cassette superfamily, such as ATP-binding cassette transporter A1 (ABCA1), multidrug resistance proteins (MDR) 1 and 2, bile salt export pump, multidrug resistance-associated proteins (MRP) 1 to 9, breast cancer resistance protein, and ATP-binding cassette subfamily G members 5 and 8, are responsible for the unidirectional export of endogenous and exogenous substances. Other efflux transporters [ATPase copper-transporting beta polypeptide (ATP7B) and ATPase class I type 8B member 1 (ATP8B1) as well as organic solute transporters (OST) alpha and beta] also play major roles in the transport of some endogenous chemicals across biological membranes. This review article provides a comprehensive overview of these transporters (both rodent and human) with regard to tissue distribution, subcellular localization, and substrate preferences. Because uptake and efflux transporters are expressed in multiple cell types, the roles of transporters in a variety of tissues, including the liver, kidneys, intestine, brain, heart, placenta, mammary glands, immune cells, and testes are discussed. Attention is also placed upon a variety of regulatory factors that influence transporter expression and function, including transcriptional activation and post-translational modifications as well as subcellular trafficking. Sex differences, ontogeny, and pharmacological and toxicological regulation of transporters are also addressed. Transporters are important transmembrane proteins that mediate the cellular entry and exit of a wide range of substrates throughout the body and thereby play important roles in human physiology, pharmacology, pathology, and toxicology.
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7118 Nucleotide Change Amino Acid Change In Vitro Function Protein Expression/Localization ABCC1 MRP1 G128C C43S 1↔ Intracellular C218T T73I 1↔ Normal C257T S92F 2↔ Normal C350T T117M 2↔ Normal G689A R230Q ↔ Normal G1057A V353M N.D. N.D. G1299T R433S 2↔ Normal G1898A R633Q 2↔ Normal G2012T G671V ↔ Normal G2168A R723Q 2 Normal G2965A A989T 2↔ Normal G3140C C1047S 1↔ Normal G3173A R1058Q ↔ Normal C4535T S1512L ↔ Normal ABCC2 MRP2 C-24T N.D. N.D. G1058A R353H N.D. N.D. G1249A V417I ↔ Normal C2366T S789F 12 Intracellular T2780G L927R N.D. N.D. C3298T R1100C N.D. N.D. G3299A R1100H N.D. N.D. T3563A V1188E N.D. N.D. G4348A A1450T ↔ Normal/Intracellular G4544A C1515Y N.D. N.D. ABCC3 MRP3 G32A G11D ↔ Normal C202T H68Y N.D. N.D. G296A R99Q N.D. Normal C1037T S346F 2 Normal C1537A Q513K N.D. N.D. T1643A L548Q N.D. N.D. G1820A S607N 2 Normal C2221T Gln741STOP N.D. N.D. G2293C V765L ↔ Normal G2395A V799M N.D. N.D. C2758T P920S 1 Normal G2768A R923Q 1 Normal C3657A S1219R N.D. N.D. C3856G R1286G ↔ Normal G3890A R1297H N.D. N.D. C4042T R1348C 1 Normal A4094G Q1365R ↔ Normal C4141A R1381S ↔ Intracellular C4217T T1406M N.D. N.D. G4267A G1423R N.D. N.D. ABCC4 MRP4 C52A L18I N.D. N.D. C232G P78A 2↔ Normal T551C M184T N.D. N.D. G559T G187W 2 Reduced A877G K293E ↔ Normal G912T K304N ↔ Normal C1067T T356M N.D. N.D. C1208T P403L 2↔ Normal G1460A G487E 2 Normal A1492G K498E ↔ Normal A1875G I625M N.D. N.D. C2000T P667L N.D. N.D. A2230G M744V ↔ Normal G2269A E757K N.D. Intracellular G2459T R820I N.D. N.D. G2560T V854F N.D. N.D. G2698T V900L N.D. N.D. G2867C C956S 1↔ Normal G3211A V1071I ↔ Normal C3425T T1142M N.D. N.D. G3659A R1220Q N.D. N.D. A3941G Q1314R N.D. N.D. 2, reduced function; 1, increased function; ↔, no change in function; N.D. not determined.
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ABCC3 p.Val765Leu 20103563:7118:978
status: NEW7115 Nucleotide Change Amino Acid Change In Vitro Function Protein Expression/Localization ABCC1 MRP1 G128C C43S 1 Intracellular C218T T73I 1 Normal C257T S92F 2 Normal C350T T117M 2 Normal G689A R230Q Normal G1057A V353M N.D. N.D. G1299T R433S 2 Normal G1898A R633Q 2 Normal G2012T G671V Normal G2168A R723Q 2 Normal G2965A A989T 2 Normal G3140C C1047S 1 Normal G3173A R1058Q Normal C4535T S1512L Normal ABCC2 MRP2 C-24T N.D. N.D. G1058A R353H N.D. N.D. G1249A V417I Normal C2366T S789F 12 Intracellular T2780G L927R N.D. N.D. C3298T R1100C N.D. N.D. G3299A R1100H N.D. N.D. T3563A V1188E N.D. N.D. G4348A A1450T Normal/Intracellular G4544A C1515Y N.D. N.D. ABCC3 MRP3 G32A G11D Normal C202T H68Y N.D. N.D. G296A R99Q N.D. Normal C1037T S346F 2 Normal C1537A Q513K N.D. N.D. T1643A L548Q N.D. N.D. G1820A S607N 2 Normal C2221T Gln741STOP N.D. N.D. G2293C V765L Normal G2395A V799M N.D. N.D. C2758T P920S 1 Normal G2768A R923Q 1 Normal C3657A S1219R N.D. N.D. C3856G R1286G Normal G3890A R1297H N.D. N.D. C4042T R1348C 1 Normal A4094G Q1365R Normal C4141A R1381S Intracellular C4217T T1406M N.D. N.D. G4267A G1423R N.D. N.D. ABCC4 MRP4 C52A L18I N.D. N.D. C232G P78A 2 Normal T551C M184T N.D. N.D. G559T G187W 2 Reduced A877G K293E Normal G912T K304N Normal C1067T T356M N.D. N.D. C1208T P403L 2 Normal G1460A G487E 2 Normal A1492G K498E Normal A1875G I625M N.D. N.D. C2000T P667L N.D. N.D. A2230G M744V Normal G2269A E757K N.D. Intracellular G2459T R820I N.D. N.D. G2560T V854F N.D. N.D. G2698T V900L N.D. N.D. G2867C C956S 1 Normal G3211A V1071I Normal C3425T T1142M N.D. N.D. G3659A R1220Q N.D. N.D. A3941G Q1314R N.D. N.D. 2, reduced function; 1, increased function; , no change in function; N.D. not determined.
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ABCC3 p.Val765Leu 20103563:7115:963
status: NEW[hide] Functional analysis of nonsynonymous single nucleo... Pharmacogenet Genomics. 2008 Sep;18(9):823-33. Kobayashi K, Ito K, Takada T, Sugiyama Y, Suzuki H
Functional analysis of nonsynonymous single nucleotide polymorphism type ATP-binding cassette transmembrane transporter subfamily C member 3.
Pharmacogenet Genomics. 2008 Sep;18(9):823-33., [PMID:18698235]
Abstract [show]
OBJECTIVES: The multidrug resistance-associated protein 3/ATP-binding cassette transmembrane transporter subfamily C member 3 (MRP3/ABCC3) plays an important role in exporting endogenous and xenobiotic anionic substrates, including glucuronide conjugates of xenobiotics, from hepatocytes into the blood circulation. This excretory function of ABCC3 becomes very apparent particularly under cholestatic conditions, since ABCC3 is induced when the biliary excretion pathway is impaired. In this study, we analyzed the functional properties of 11 nonsynonymous single nucleotide polymorphisms (SNPs) in the ABCC3 gene found in the public SNP database. METHODS: HeLa and Sf9 insect cells were used to analyze the protein expression and transport function, respectively. RESULTS: After transient transfection of cDNA into HeLa cells, it was found that R1381S ABCC3 exhibits intracellular accumulation of immature protein, the localization of which was mostly merged with a marker for the endoplasmic reticulum. Two kinds of SNPs type ABCC3 (S346F and S607N) lost their transport activity for [H]estradiol-17beta-D-glucuronide in membrane vesicles from Sf9 cells infected with the recombinant baculoviruses, although the band length and the amount of protein expression remained normal. In contrast, the cellular localization, protein expression and function of other eight kinds of SNPs type ABCC3 (G11D, R99Q, V765L, P920S, R923Q, R1286G, R1348C, and Q1365R ABCC3) remained normal. CONCLUSION: The results of this study suggest that the possession of R1381S, S346F, and S607N types of ABCC3 sequences may be a possible risk factor for the acquisition of hepatotoxicity, due to their poor ability to transport toxic compounds across the sinusoidal membrane.
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6 In contrast, the cellular localization, protein expression and function of other eight kinds of SNPs type ABCC3 (G11D, R99Q, V765L, P920S, R923Q, R1286G, R1348C, and Q1365R ABCC3) remained normal.
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ABCC3 p.Val765Leu 18698235:6:125
status: NEW40 Using site-directed mutagenesis, SNP-type ABCC3 (G11D, R99Q, S346F, S607N, V765L, P920S, R923Q, R1286G, R1348C, Q1365R, and R1381S ABCC3) was constructed on a pBluescript SK ( - ) vector.
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ABCC3 p.Val765Leu 18698235:40:75
status: NEW93 Protein expression of ATP-binding cassette transmembrane transporter subfamily C member 3 in HeLa cells The protein expression and modification of ABCC3 in HeLa cells were determined by Western blot analysis Fig. 1 G11D 0.18% R99Q 0.54% S346F 0.91% S607N 0.99% V765L 1.09% P920S 3.88% R923Q 0.55% R1286G 0.18% R1348C 1.65% R1381S 0.22% Q1365R 0.33% Outside Inside NBD2 NBD1 Predicted secondary structure of ATP-binding cassette transmembrane transporter subfamily C member 3 showing the position of the eleven nonsynonymous variants.
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ABCC3 p.Val765Leu 18698235:93:261
status: NEW118 Transport activities of the ATP-binding cassette transmembrane transporter subfamily C member 3 variants The transport function of wild-type and SNP-type ABCC3 was studied by examining the ATP-dependent uptake of [3 H]E217bG into membrane vesicles isolated from Sf9 cells infected with recombinant baculoviruses Table 1 Allele frequency of ABCC3 SNPs examined in this study Ethnic population SNP sequence Asian (%) African-American (%) Pacific islander (%) Mexican (%) Caucasian (%) SubSaharan- African (%) Total (%) Reference G11D 0.83 (120) 0 (160) 0 (12) 0 (100) 0 (160) 0.18 (552) PharmGKB 0.6 (178)a Fukushima-Uesaka et al. 0.5 (206) Lang et al. R99Q 0 (120) 1.88 (160) 0 (12) 0 (100) 0 (160) 0.54 (552) PharmGKB S346F 0 (120) 0.62 (160) 0 (12) 0 (100) 2.5 (160) 0.91 (552) PharmGKB 0.5 (206) Lang et al. S607N 0 (296) 2.76 (290) 0 (10) 1 (100) 0 (210) 0.99 (906) PharmGKB 11.7 (120) dbSNP V765L 0 (120) 3.12 (160) 0 (12) 1 (100) 0 (160) 1.09 (552) PharmGKB P920S 0 (292) 10.3 (290) 0 (12) 0 (100) 2.4 (280) 3.88 (902) PharmGKB R923Q 0 (108) 0.62 (160) 0 (12) 0 (100) 1.25 (160) 0.55 (550) PharmGKB R1286G 0 (120) 0.62 (160) 0 (12) 0 (100) 0 (160) 0.18 (552) PharmGKB R1348C 0 (298) 5.17 (290) 0 (12) 0 (100) 0 (210) 1.65 (910) PharmGKB 7.5 (120) dbSNP Q1365R 0 (298) 1.05 (286) 0 (12) 0 (100) 0 (208) 0.33 (904) PharmGKB R1381S 0 (298) 0 (290) 0 (12) 2 (100) 0 (210) 0.22 (910) PharmGKB Allele frequencies (%) in individual ethnic population are shown.
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ABCC3 p.Val765Leu 18698235:118:895
status: NEW124 ABCC3 SNP analysis Kobayashi et al. 827 Fig. WT R1381S G11D R99Q S346F S607N V765L P920S R923Q R1286G WT ABCC3 Calnexin Calnexin merge R1381S merge ABCC3 R1348C Q1365R (a) (b) Subcellular localization of ATP-binding cassette transmembrane transporter subfamily C member 3 (ABCC3) in HeLa cells.
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ABCC3 p.Val765Leu 18698235:124:79
status: NEW140 Discussion On account of its inducible nature under cholestatic conditions, ABCC3/Abcc3 is considered to provide a compensatory efflux pathway for endogenous and exo- Table 2 Corresponding amino acid residues in other ABCC family proteins Protein Species G11D R99Q S346F S607N V765L P920S R923Q R1286G R1348C Q1365R R1381S ABCC3 Human G R S S V P R R R Q R Abcc3 Mouse G S T N V T K R V Q R Abcc3 Rat G S T N V P K S F Q R ABCC1 Human S I D S V R N V I K R ABCC2 Human - A L G T K R K I K R ABCC4 Human - - L L V Q R E W K R ABCC5 Human - - L L L - D E K K R Amino acid residues in other ABCC family proteins at the corresponding positions to 11 amino acid residues in human ABCC3 examined in this study.
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ABCC3 p.Val765Leu 18698235:140:277
status: NEW142 Fig. 3 (a) (b) Treatment WT R1381S Endo HPNGaseEndo HPNGase 190 kDa 180 kDa 170 kDa 160 kDa 190 kDa 170 kDa 160 kDa WT G11D S346F R99Q S607N V765L P920S R923Q R1286G R1348C Q1365R R1381S pcDNA3.1(+) Western blot analysis of wild-type and single nucleotide polymorphism-type ATP-binding cassette transmembrane transporter subfamily C member 3 (ABCC3) proteins expressed in HeLa cells.
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ABCC3 p.Val765Leu 18698235:142:141
status: NEW160 Fig. 5 WT 170 kDa Band density 1.00 1.01 0.77 1.21 1.16 0.95 1.00 1.01 0.91 1.29 1.10 G11D S346F S607N V765L P920S R923Q R1286G R1348C Q1365R R1381S GFP Western blot analysis of wild-type or single nucleotide polymorphisms-type ATP-binding cassette transmembrane transporter subfamily C member 3 (ABCC3) proteins in membrane vesicles isolated from Sf9 cells.
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ABCC3 p.Val765Leu 18698235:160:103
status: NEW190 These are Q741Stop and Fig. 7 10 8 ATP-dependentuptakenormalizedbyrelative ABCC3expressionlevel(pmol/mgprotein/2min) 6 * * ** ** ** ** ** ** ** 4 2 WT G11D S346F S607N V765L P920S R923Q R1286G R1348C Q1365R R1381S GFP 0 Uptake of [3 H]estradiol-17b-D-glucuronide (E217bG) by ATP-binding cassette transmembrane transporter subfamily C member 3 (ABCC3) variants.
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ABCC3 p.Val765Leu 18698235:190:168
status: NEW[hide] Functional hot spots in human ATP-binding cassette... Protein Sci. 2010 Nov;19(11):2110-21. Kelly L, Fukushima H, Karchin R, Gow JM, Chinn LW, Pieper U, Segal MR, Kroetz DL, Sali A
Functional hot spots in human ATP-binding cassette transporter nucleotide binding domains.
Protein Sci. 2010 Nov;19(11):2110-21., [PMID:20799350]
Abstract [show]
The human ATP-binding cassette (ABC) transporter superfamily consists of 48 integral membrane proteins that couple the action of ATP binding and hydrolysis to the transport of diverse substrates across cellular membranes. Defects in 18 transporters have been implicated in human disease. In hundreds of cases, disease phenotypes and defects in function can be traced to nonsynonymous single nucleotide polymorphisms (nsSNPs). The functional impact of the majority of ABC transporter nsSNPs has yet to be experimentally characterized. Here, we combine experimental mutational studies with sequence and structural analysis to describe the impact of nsSNPs in human ABC transporters. First, the disease associations of 39 nsSNPs in 10 transporters were rationalized by identifying two conserved loops and a small alpha-helical region that may be involved in interdomain communication necessary for transport of substrates. Second, an approach to discriminate between disease-associated and neutral nsSNPs was developed and tailored to this superfamily. Finally, the functional impact of 40 unannotated nsSNPs in seven ABC transporters identified in 247 ethnically diverse individuals studied by the Pharmacogenetics of Membrane Transporters consortium was predicted. Three predictions were experimentally tested using human embryonic kidney epithelial (HEK) 293 cells stably transfected with the reference multidrug resistance transporter 4 and its variants to examine functional differences in transport of the antiviral drug, tenofovir. The experimental results confirmed two predictions. Our analysis provides a structural and evolutionary framework for rationalizing and predicting the functional effects of nsSNPs in this clinically important membrane transporter superfamily.
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72 Predictions of the Functional Effects of 40 nsSNPs in ABC Transporters Comon name HUGO name Mutation NBD Prediction BSEP ABCB11 E592Q NBD1 Neutral BSEP ABCB11 N591S NBD1 Neutral BSEP ABCB11 Q558H NBD1 Neutral BSEP ABCB11 V444A NBD1 Neutral BSEP ABCB11 E1186K NBD2 Disease MDR1 ABCB1 P1051A NBD2 Neutral MDR1 ABCB1 S1141T NBD2 Neutral MDR1 ABCB1 T1256K NBD2 Disease MDR1 ABCB1 V1251I NBD2 Neutral MDR1 ABCB1 W1108R NBD2 Disease MRP2 ABCC2 I670T NBD1 Disease MRP2 ABCC2 L849R NBD1 Disease MRP2 ABCC2 C1515Y NBD2 Disease MRP3 ABCC3 D770N NBD1 Neutral MRP3 ABCC3 K718M NBD1 Neutral MRP3 ABCC3 T809M NBD1 Disease MRP3 ABCC3 V765L NBD1 Disease MRP3 ABCC3 Q1365R NBD2 Disease MRP3 ABCC3 R1297H NBD2 Disease MRP3 ABCC3 R1348C NBD2 Disease MRP3 ABCC3 R1381S NBD2 Disease MRP4 ABCC4 G487E NBD1 Disease MRP4 ABCC4 K498E NBD1 Neutral MRP4 ABCC4 R1220Q NBD2 Neutral MRP4 ABCC4 T1142M NBD2 Neutral MRP4 ABCC4 V1071I NBD2 Neutral MRP6 ABCC6 I1330L NBD1 Neutral MRP6 ABCC6 I742V NBD1 Neutral MRP6 ABCC6 P664S NBD1 Neutral MRP6 ABCC6 R724K NBD1 Neutral MRP6 ABCC6 R769K NBD1 Neutral MRP6 ABCC6 A1291T NBD2 Neutral MRP6 ABCC6 E1369K NBD2 Neutral MRP6 ABCC6 G1327E NBD2 Disease MRP6 ABCC6 L1416R NBD2 Disease MRP6 ABCC6 R1268Q NBD2 Disease MRP6 ABCC6 R1461H NBD2 Disease MXR ABCG2 I206L NBD1 Neutral MXR ABCG2 P269S NBD1 Disease MXR ABCG2 Q141K NBD1 Neutral nsSNPs.
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ABCC3 p.Val765Leu 20799350:72:619
status: NEW