ABC-family proteins mediated transport (Homo sapiens)

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23, 30, 469, 13, 3352, 63471, 5122, 38, 6185, 6, 28, 48, 5725, 39, 56, 62, 6912, 16, 42, 67187, 15, 17, 41, 44...20, 31, 34, 36, 50...32, 43, 535, 6, 28, 48, 57255, 654, 2711, 14, 21, 29, 5626, 64, 7019, 356045, 49, 58, 6810, 373, 24, 4045, 49, 58, 68mitochondrial matrixlysosomal lumentransport vesiclelamellar bodyperoxisomal matrixendoplasmic reticulum lumencytosolPG PiCHOLADPKCNJ11 H2OABCG4 dimerABCB10 PEX19 lipidsADPSPHM RNASEL ABCD2 porphyrinABCG5 H2OPiABCE1sterolsADPorganic aniona xenobioticK+H2OABCD3 PiADPH2OLCFAH2O23mer peptideH2OABCD1 PEX19:ABCD1/2/3EIF2S3 CFTR ABCG1 dimerATPATPATPABCD3 ADPABCA2 ABCC2CHOL hemeATPCFTR G551D IvacaftorEIF2S3 ADPABCC9 ABCB1 ABCG4 ABCE1 ABCCsKCNJ11:ABCC9ADPMTABC3 dimerPiH2ORNASEL dimerCl-ABCA4SPHM atRALABCG5:ABCG8ABCA10 23mer peptidePC PEX3BMG,BDGBMG,BDGABCC11 PiADPEIF2S1 ATPBMG phytosterols H2OABCA8 H2OATPCl-PiABCC4 ABCC1 Ivacaftor:CFTR G551DPiABCB7(23-752) Cl-PC BDG ABCD1 atRALCHOL ABCG1 ABCC10 PCATPATPABCB9 dimerATPlipidsABCC2 ABCF1:EIF2S1:EIF2S2:EIF2S3ABCA8/B1/B5ABCA cholesteroltransportersH2OCHOLPCABCA7-1:ApoA1complexABCD2 ABCA9 ADPporphyrinPiPiPiABCA7-dependentphospholipidsABCA12a xenobioticPiH2OADPABCF1 organic anionABCA6 ABCG8 CFTRADPADPEIF2S2 PiCHOLEIF2S2 ADPEIF2S1 ADPK+ABCC3 ABCF1PC, PGPiEIF2S1:EIF2S2:EIF2S3PiABCC5 ATPABCB6 H2OH2OATPATPHeme transportersPC ABCC6 ABCA7 sterolsPEX19ABCD1-3 dimersBMG HCO3-ABCC9 BDG H2OATPPC, PGHCO3-CHOLPiRNASEL PiABCB9 PG ATPABCB4CFTR G551DPC ADPADPABCB5 H2OABCB8 ADPABCC8 CHOLhemephytosterols LCFAAPOA1(25-266) CHOLATPH2OABCA3PiIvacaftor ABCA7-dependentphospholipidsABCE1:RNASEL dimerATP


The ATP-binding cassette (ABC) superfamily of active transporters involves a large number of functionally diverse transmembrane proteins. They transport a variety of compounds through membranes against steep concentration gradients at the cost of ATP hydrolysis. These substrates include amino acids, lipids, inorganic ions, peptides, saccharides, peptides for antigen presentation, metals, drugs, and proteins. The ABC transporters not only move a variety of substrates into and out of the cell, but are also involved in intracellular compartmental transport. Energy derived from the hydrolysis of ATP is used to transport the substrate across the membrane against a concentration gradient. Human genome contains 48 ABC genes; 16 of these have a known function and 14 are associated with a defined human disease (Dean et al. 2001, Borst and Elferink 2002, Rees et al. 2009). View original pathway at:Reactome.


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  1. Park M, Ko SB, Choi JY, Muallem G, Thomas PJ, Pushkin A, Lee MS, Kim JY, Lee MG, Muallem S, Kurtz I.; ''The cystic fibrosis transmembrane conductance regulator interacts with and regulates the activity of the HCO3- salvage transporter human Na+-HCO3- cotransport isoform 3.''; PubMed Europe PMC
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  9. Frank NY, Margaryan A, Huang Y, Schatton T, Waaga-Gasser AM, Gasser M, Sayegh MH, Sadee W, Frank MH.; ''ABCB5-mediated doxorubicin transport and chemoresistance in human malignant melanoma.''; PubMed Europe PMC
  10. Wei SJ, Williams JG, Dang H, Darden TA, Betz BL, Humble MM, Chang FM, Trempus CS, Johnson K, Cannon RE, Tennant RW.; ''Identification of a specific motif of the DSS1 protein required for proteasome interaction and p53 protein degradation.''; PubMed Europe PMC
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  16. Picciotto MR, Cohn JA, Bertuzzi G, Greengard P, Nairn AC.; ''Phosphorylation of the cystic fibrosis transmembrane conductance regulator.''; PubMed Europe PMC
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  18. Shen DW, Fojo A, Chin JE, Roninson IB, Richert N, Pastan I, Gottesman MM.; ''Human multidrug-resistant cell lines: increased mdr1 expression can precede gene amplification.''; PubMed Europe PMC
  19. Morita SY, Terada T.; ''Molecular mechanisms for biliary phospholipid and drug efflux mediated by ABCB4 and bile salts.''; PubMed Europe PMC
  20. Ramjeesingh M, Ugwu F, Li C, Dhani S, Huan LJ, Wang Y, Bear CE.; ''Stable dimeric assembly of the second membrane-spanning domain of CFTR (cystic fibrosis transmembrane conductance regulator) reconstitutes a chloride-selective pore.''; PubMed Europe PMC
  21. Wenzel JJ, Kaminski WE, Piehler A, Heimerl S, Langmann T, Schmitz G.; ''ABCA10, a novel cholesterol-regulated ABCA6-like ABC transporter.''; PubMed Europe PMC
  22. Small DM.; ''Role of ABC transporters in secretion of cholesterol from liver into bile.''; PubMed Europe PMC
  23. Ledford H.; ''Drug bests cystic-fibrosis mutation.''; PubMed Europe PMC
  24. Gloeckner CJ, Mayerhofer PU, Landgraf P, Muntau AC, Holzinger A, Gerber JK, Kammerer S, Adamski J, Roscher AA.; ''Human adrenoleukodystrophy protein and related peroxisomal ABC transporters interact with the peroxisomal assembly protein PEX19p.''; PubMed Europe PMC
  25. Kaminski WE, Orsó E, Diederich W, Klucken J, Drobnik W, Schmitz G.; ''Identification of a novel human sterol-sensitive ATP-binding cassette transporter (ABCA7).''; PubMed Europe PMC
  26. Oldfield S, Lowry C, Ruddick J, Lightman S.; ''ABCG4: a novel human white family ABC-transporter expressed in the brain and eye.''; PubMed Europe PMC
  27. Nasonkin I, Illing M, Koehler MR, Schmid M, Molday RS, Weber BH.; ''Mapping of the rod photoreceptor ABC transporter (ABCR) to 1p21-p22.1 and identification of novel mutations in Stargardt's disease.''; PubMed Europe PMC
  28. Sun H, Molday RS, Nathans J.; ''Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specific ATP-binding cassette transporter responsible for Stargardt disease.''; PubMed Europe PMC
  29. Zhao C, Haase W, Tampé R, Abele R.; ''Peptide specificity and lipid activation of the lysosomal transport complex ABCB9 (TAPL).''; PubMed Europe PMC
  30. Aubourg P, Mosser J, Douar AM, Sarde CO, Lopez J, Mandel JL.; ''Adrenoleukodystrophy gene: unexpected homology to a protein involved in peroxisome biogenesis.''; PubMed Europe PMC
  31. Abe-Dohmae S, Ikeda Y, Matsuo M, Hayashi M, Okuhira K, Ueda K, Yokoyama S.; ''Human ABCA7 supports apolipoprotein-mediated release of cellular cholesterol and phospholipid to generate high density lipoprotein.''; PubMed Europe PMC
  32. Yamano G, Funahashi H, Kawanami O, Zhao LX, Ban N, Uchida Y, Morohoshi T, Ogawa J, Shioda S, Inagaki N.; ''ABCA3 is a lamellar body membrane protein in human lung alveolar type II cells.''; PubMed Europe PMC
  33. Csere P, Lill R, Kispal G.; ''Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p.''; PubMed Europe PMC
  34. Dean M, Rzhetsky A, Allikmets R.; ''The human ATP-binding cassette (ABC) transporter superfamily.''; PubMed Europe PMC
  35. Petry F, Kotthaus A, Hirsch-Ernst KI.; ''Cloning of human and rat ABCA5/Abca5 and detection of a human splice variant.''; PubMed Europe PMC
  36. Sacksteder KA, Jones JM, South ST, Li X, Liu Y, Gould SJ.; ''PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis.''; PubMed Europe PMC
  37. Osborne L, Knight R, Santis G, Hodson M.; ''A mutation in the second nucleotide binding fold of the cystic fibrosis gene.''; PubMed Europe PMC
  38. Kamijo K, Osumi T, Hashimoto T.; ''[PMP70, the 70-kDa peroxisomal membrane protein: a member of the ATP-binding cassette transporters].''; PubMed Europe PMC
  39. Holzinger A, Kammerer S, Berger J, Roscher AA.; ''cDNA cloning and mRNA expression of the human adrenoleukodystrophy related protein (ALDRP), a peroxisomal ABC transporter.''; PubMed Europe PMC
  40. Paytubi S, Wang X, Lam YW, Izquierdo L, Hunter MJ, Jan E, Hundal HS, Proud CG.; ''ABC50 promotes translation initiation in mammalian cells.''; PubMed Europe PMC
  41. Biswas EE, Biswas SB.; ''The C-terminal nucleotide binding domain of the human retinal ABCR protein is an adenosine triphosphatase.''; PubMed Europe PMC
  42. Vembar SS, Brodsky JL.; ''One step at a time: endoplasmic reticulum-associated degradation.''; PubMed Europe PMC
  43. Akiyama M, Sugiyama-Nakagiri Y, Sakai K, McMillan JR, Goto M, Arita K, Tsuji-Abe Y, Tabata N, Matsuoka K, Sasaki R, Sawamura D, Shimizu H.; ''Mutations in lipid transporter ABCA12 in harlequin ichthyosis and functional recovery by corrective gene transfer.''; PubMed Europe PMC
  44. Babenko AP, Gonzalez G, Aguilar-Bryan L, Bryan J.; ''Reconstituted human cardiac KATP channels: functional identity with the native channels from the sarcolemma of human ventricular cells.''; PubMed Europe PMC
  45. Fang Y, Morrell JC, Jones JM, Gould SJ.; ''PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins.''; PubMed Europe PMC
  46. Wolters JC, Abele R, Tampé R.; ''Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9).''; PubMed Europe PMC
  47. Chloupková M, Reaves SK, LeBard LM, Koeller DM.; ''The mitochondrial ABC transporter Atm1p functions as a homodimer.''; PubMed Europe PMC
  48. Morita SY, Kobayashi A, Takanezawa Y, Kioka N, Handa T, Arai H, Matsuo M, Ueda K.; ''Bile salt-dependent efflux of cellular phospholipids mediated by ATP binding cassette protein B4.''; PubMed Europe PMC
  49. Piehler A, Kaminski WE, Wenzel JJ, Langmann T, Schmitz G.; ''Molecular structure of a novel cholesterol-responsive A subclass ABC transporter, ABCA9.''; PubMed Europe PMC
  50. Kapoor H, Koolwal A, Singh A.; ''Ivacaftor: a novel mutation modulating drug.''; PubMed Europe PMC
  51. Klugbauer N, Hofmann F.; ''Primary structure of a novel ABC transporter with a chromosomal localization on the band encoding the multidrug resistance-associated protein.''; PubMed Europe PMC
  52. Voges D, Zwickl P, Baumeister W.; ''The 26S proteasome: a molecular machine designed for controlled proteolysis.''; PubMed Europe PMC
  53. Rees DC, Johnson E, Lewinson O.; ''ABC transporters: the power to change.''; PubMed Europe PMC
  54. Tsuruoka S, Ishibashi K, Yamamoto H, Wakaumi M, Suzuki M, Schwartz GJ, Imai M, Fujimura A.; ''Functional analysis of ABCA8, a new drug transporter.''; PubMed Europe PMC
  55. Allikmets R, Raskind WH, Hutchinson A, Schueck ND, Dean M, Koeller DM.; ''Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A).''; PubMed Europe PMC
  56. Paytubi S, Morrice NA, Boudeau J, Proud CG.; ''The N-terminal region of ABC50 interacts with eukaryotic initiation factor eIF2 and is a target for regulatory phosphorylation by CK2.''; PubMed Europe PMC
  57. Tammaro P, Ashcroft FM.; ''A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit.''; PubMed Europe PMC
  58. Engel T, Lorkowski S, Lueken A, Rust S, Schlüter B, Berger G, Cullen P, Assmann G.; ''The human ABCG4 gene is regulated by oxysterols and retinoids in monocyte-derived macrophages.''; PubMed Europe PMC
  59. Kaminski WE, Piehler A, Schmitz G.; ''Genomic organization of the human cholesterol-responsive ABC transporter ABCA7: tandem linkage with the minor histocompatibility antigen HA-1 gene.''; PubMed Europe PMC
  60. Jensen TJ, Loo MA, Pind S, Williams DB, Goldberg AL, Riordan JR.; ''Multiple proteolytic systems, including the proteasome, contribute to CFTR processing.''; PubMed Europe PMC
  61. Vaughan AM, Oram JF.; ''ABCG1 redistributes cell cholesterol to domains removable by high density lipoprotein but not by lipid-depleted apolipoproteins.''; PubMed Europe PMC
  62. Gelman MS, Kannegaard ES, Kopito RR.; ''A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator.''; PubMed Europe PMC
  63. Liu LX, Janvier K, Berteaux-Lecellier V, Cartier N, Benarous R, Aubourg P.; ''Homo- and heterodimerization of peroxisomal ATP-binding cassette half-transporters.''; PubMed Europe PMC
  64. Kamisako T, Leier I, Cui Y, König J, Buchholz U, Hummel-Eisenbeiss J, Keppler D.; ''Transport of monoglucuronosyl and bisglucuronosyl bilirubin by recombinant human and rat multidrug resistance protein 2.''; PubMed Europe PMC
  65. Demirel O, Waibler Z, Kalinke U, Grünebach F, Appel S, Brossart P, Hasilik A, Tampé R, Abele R.; ''Identification of a lysosomal peptide transport system induced during dendritic cell development.''; PubMed Europe PMC
  66. Zhang F, Zhang W, Liu L, Fisher CL, Hui D, Childs S, Dorovini-Zis K, Ling V.; ''Characterization of ABCB9, an ATP binding cassette protein associated with lysosomes.''; PubMed Europe PMC
  67. Younger JM, Chen L, Ren HY, Rosser MF, Turnbull EL, Fan CY, Patterson C, Cyr DM.; ''Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator.''; PubMed Europe PMC
  68. Graf SA, Haigh SE, Corson ED, Shirihai OS.; ''Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me).''; PubMed Europe PMC
  69. Berge KE, Tian H, Graf GA, Yu L, Grishin NV, Schultz J, Kwiterovich P, Shan B, Barnes R, Hobbs HH.; ''Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters.''; PubMed Europe PMC
  70. Ousingsawat J, Kongsuphol P, Schreiber R, Kunzelmann K.; ''CFTR and TMEM16A are separate but functionally related Cl- channels.''; PubMed Europe PMC
  71. Ikeda Y, Abe-Dohmae S, Munehira Y, Aoki R, Kawamoto S, Furuya A, Shitara K, Amachi T, Kioka N, Matsuo M, Yokoyama S, Ueda K.; ''Posttranscriptional regulation of human ABCA7 and its function for the apoA-I-dependent lipid release.''; PubMed Europe PMC
  72. Zhang F, Hogue DL, Liu L, Fisher CL, Hui D, Childs S, Ling V.; ''M-ABC2, a new human mitochondrial ATP-binding cassette membrane protein.''; PubMed Europe PMC
  73. Stefková J, Poledne R, Hubácek JA.; ''ATP-binding cassette (ABC) transporters in human metabolism and diseases.''; PubMed Europe PMC
  74. Mitsuhashi N, Miki T, Senbongi H, Yokoi N, Yano H, Miyazaki M, Nakajima N, Iwanaga T, Yokoyama Y, Shibata T, Seino S.; ''MTABC3, a novel mitochondrial ATP-binding cassette protein involved in iron homeostasis.''; PubMed Europe PMC
  75. Vulevic B, Chen Z, Boyd JT, Davis W, Walsh ES, Belinsky MG, Tew KD.; ''Cloning and characterization of human adenosine 5'-triphosphate-binding cassette, sub-family A, transporter 2 (ABCA2).''; PubMed Europe PMC
  76. Deeley RG, Westlake C, Cole SP.; ''Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.''; PubMed Europe PMC
  77. Shulenin S, Nogee LM, Annilo T, Wert SE, Whitsett JA, Dean M.; ''ABCA3 gene mutations in newborns with fatal surfactant deficiency.''; PubMed Europe PMC
  78. Accurso FJ, Rowe SM, Clancy JP, Boyle MP, Dunitz JM, Durie PR, Sagel SD, Hornick DB, Konstan MW, Donaldson SH, Moss RB, Pilewski JM, Rubenstein RC, Uluer AZ, Aitken ML, Freedman SD, Rose LM, Mayer-Hamblett N, Dong Q, Zha J, Stone AJ, Olson ER, Ordoñez CL, Campbell PW, Ashlock MA, Ramsey BW.; ''Effect of VX-770 in persons with cystic fibrosis and the G551D-CFTR mutation.''; PubMed Europe PMC
  79. Ward CL, Kopito RR.; ''Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins.''; PubMed Europe PMC
  80. Kaminski WE, Wenzel JJ, Piehler A, Langmann T, Schmitz G.; ''ABCA6, a novel a subclass ABC transporter.''; PubMed Europe PMC
  81. Roerig P, Mayerhofer P, Holzinger A, Gärtner J.; ''Characterization and functional analysis of the nucleotide binding fold in human peroxisomal ATP binding cassette transporters.''; PubMed Europe PMC


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101456view11:32, 1 November 2018ReactomeTeamreactome version 66
100994view21:11, 31 October 2018ReactomeTeamreactome version 65
100530view19:45, 31 October 2018ReactomeTeamreactome version 64
100077view16:29, 31 October 2018ReactomeTeamreactome version 63
99628view15:01, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99234view12:44, 31 October 2018ReactomeTeamreactome version 62
93773view13:35, 16 August 2017ReactomeTeamreactome version 61
93299view11:19, 9 August 2017ReactomeTeamreactome version 61
86383view09:16, 11 July 2016ReactomeTeamreactome version 56
83823view13:07, 13 December 2015EgonwTypo: LFCA -> LCFA
83165view10:15, 18 November 2015ReactomeTeamVersion54
82708view09:11, 23 October 2015EgonwTypo: LFCA -> LCFA
81529view13:04, 21 August 2015ReactomeTeamVersion53
76998view08:29, 17 July 2014ReactomeTeamFixed remaining interactions
76703view12:07, 16 July 2014ReactomeTeamFixed remaining interactions
76516view11:41, 16 July 2014ReactomeTeamFixed remaining interactions
76029view10:09, 11 June 2014ReactomeTeamRe-fixing comment source
75738view11:22, 10 June 2014ReactomeTeamReactome 48 Update
75088view14:04, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74735view08:49, 30 April 2014ReactomeTeamReactome46
44936view12:20, 6 October 2011MartijnVanIerselOntology Term : 'transport pathway' added !
42004view21:49, 4 March 2011MaintBotAutomatic update
39806view05:50, 21 January 2011MaintBotNew pathway

External references


View all...
NameTypeDatabase referenceComment
23mer peptideR-NUL-5223341 (Reactome)
23mer peptideR-NUL-5223344 (Reactome)
ABCA cholesterol transportersComplexR-HSA-383207 (Reactome)
ABCA10 ProteinQ8WWZ4 (Uniprot-TrEMBL)
ABCA12ProteinQ86UK0 (Uniprot-TrEMBL)
ABCA2 ProteinQ9BZC7 (Uniprot-TrEMBL)
ABCA3ProteinQ99758 (Uniprot-TrEMBL)
ABCA4ProteinP78363 (Uniprot-TrEMBL)
ABCA6 ProteinQ8N139 (Uniprot-TrEMBL)
ABCA7 ProteinQ8IZY2 (Uniprot-TrEMBL)
ABCA7-1:ApoA1 complexComplexR-HSA-382558 (Reactome)
ABCA7-dependent phospholipidsComplexR-ALL-382526 (Reactome)
ABCA7-dependent phospholipidsComplexR-ALL-382530 (Reactome)
ABCA8 ProteinO94911 (Uniprot-TrEMBL)
ABCA8/B1/B5ComplexR-HSA-1467470 (Reactome)
ABCA9 ProteinQ8IUA7 (Uniprot-TrEMBL)
ABCB1 ProteinP08183 (Uniprot-TrEMBL)
ABCB10 ProteinQ9NRK6 (Uniprot-TrEMBL)
ABCB4ProteinP21439 (Uniprot-TrEMBL)
ABCB5 ProteinQ2M3G0 (Uniprot-TrEMBL)
ABCB6 ProteinQ9NP58 (Uniprot-TrEMBL)
ABCB7(23-752) ProteinO75027 (Uniprot-TrEMBL)
ABCB8 ProteinQ9NUT2 (Uniprot-TrEMBL)
ABCB9 ProteinQ9NP78 (Uniprot-TrEMBL)
ABCB9 dimerComplexR-HSA-5223347 (Reactome)
ABCC1 ProteinP33527 (Uniprot-TrEMBL)
ABCC10 ProteinQ5T3U5 (Uniprot-TrEMBL)
ABCC11 ProteinQ96J66 (Uniprot-TrEMBL)
ABCC2 ProteinQ92887 (Uniprot-TrEMBL)
ABCC2ProteinQ92887 (Uniprot-TrEMBL)
ABCC3 ProteinO15438 (Uniprot-TrEMBL)
ABCC4 ProteinO15439 (Uniprot-TrEMBL)
ABCC5 ProteinO15440 (Uniprot-TrEMBL)
ABCC6 ProteinO95255 (Uniprot-TrEMBL)
ABCC8 ProteinQ09428 (Uniprot-TrEMBL)
ABCC9 ProteinO60706 (Uniprot-TrEMBL)
ABCCsComplexR-HSA-1454912 (Reactome)
ABCD1 ProteinP33897 (Uniprot-TrEMBL)
ABCD1-3 dimersComplexR-HSA-1456465 (Reactome)
ABCD2 ProteinQ9UBJ2 (Uniprot-TrEMBL)
ABCD3 ProteinP28288 (Uniprot-TrEMBL)
ABCE1 ProteinP61221 (Uniprot-TrEMBL)
ABCE1:RNASEL dimerComplexR-HSA-5223322 (Reactome)
ABCE1ProteinP61221 (Uniprot-TrEMBL)
ABCF1 ProteinQ8NE71 (Uniprot-TrEMBL)
ABCF1:EIF2S1:EIF2S2:EIF2S3ComplexR-HSA-5226905 (Reactome)
ABCF1ProteinQ8NE71 (Uniprot-TrEMBL)
ABCG1 ProteinP45844 (Uniprot-TrEMBL)
ABCG1 dimerComplexR-HSA-194222 (Reactome)
ABCG4 ProteinQ9H172 (Uniprot-TrEMBL)
ABCG4 dimerComplexR-HSA-1454940 (Reactome)
ABCG5 ProteinQ9H222 (Uniprot-TrEMBL)
ABCG5:ABCG8ComplexR-HSA-265452 (Reactome)
ABCG8 ProteinQ9H221 (Uniprot-TrEMBL)
ADPMetaboliteCHEBI:16761 (ChEBI)
APOA1(25-266) ProteinP02647 (Uniprot-TrEMBL)
ATPMetaboliteCHEBI:15422 (ChEBI)
BDG MetaboliteCHEBI:18392 (ChEBI)
BMG MetaboliteCHEBI:16427 (ChEBI)
BMG,BDGComplexR-ALL-5679042 (Reactome)
BMG,BDGComplexR-HSA-5679034 (Reactome)
CFTR G551D ProteinP13569 (Uniprot-TrEMBL)
CFTR G551DProteinP13569 (Uniprot-TrEMBL)
CFTR ProteinP13569 (Uniprot-TrEMBL)
CFTRProteinP13569 (Uniprot-TrEMBL)
CHOL MetaboliteCHEBI:16113 (ChEBI)
CHOLMetaboliteCHEBI:16113 (ChEBI)
Cl-MetaboliteCHEBI:17996 (ChEBI)
EIF2S1 ProteinP05198 (Uniprot-TrEMBL)
EIF2S1:EIF2S2:EIF2S3ComplexR-HSA-72515 (Reactome)
EIF2S2 ProteinP20042 (Uniprot-TrEMBL)
EIF2S3 ProteinP41091 (Uniprot-TrEMBL)
H2OMetaboliteCHEBI:15377 (ChEBI)
HCO3-MetaboliteCHEBI:17544 (ChEBI)
Heme transportersComplexR-HSA-1369030 (Reactome)
Ivacaftor MetaboliteCHEBI:66901 (ChEBI)
Ivacaftor:CFTR G551DComplexR-HSA-5678990 (Reactome)
IvacaftorMetaboliteCHEBI:66901 (ChEBI)
K+MetaboliteCHEBI:29103 (ChEBI)
KCNJ11 ProteinQ14654 (Uniprot-TrEMBL)
KCNJ11:ABCC9ComplexR-HSA-5678267 (Reactome)
LCFAMetaboliteCHEBI:15904 (ChEBI)
MTABC3 dimerComplexR-HSA-1368982 (Reactome)
PC MetaboliteCHEBI:16110 (ChEBI)
PC, PGComplexR-ALL-5684863 (Reactome)
PC, PGComplexR-ALL-5684869 (Reactome)
PCMetaboliteCHEBI:16110 (ChEBI)
PEX19 ProteinP40855 (Uniprot-TrEMBL)
PEX19:ABCD1/2/3ComplexR-HSA-382586 (Reactome)
PEX19ProteinP40855 (Uniprot-TrEMBL)
PEX3ProteinP56589 (Uniprot-TrEMBL)
PG MetaboliteCHEBI:17517 (ChEBI)
PiMetaboliteCHEBI:18367 (ChEBI)
RNASEL ProteinQ05823 (Uniprot-TrEMBL)
RNASEL dimerComplexR-HSA-5357403 (Reactome)
SPHM MetaboliteCHEBI:17636 (ChEBI)
a xenobioticMetaboliteCHEBI:35703 (ChEBI)
atRALMetaboliteCHEBI:17898 (ChEBI)
hemeMetaboliteCHEBI:17627 (ChEBI)
lipidsMetaboliteCHEBI:18059 (ChEBI)
organic anionMetaboliteCHEBI:25696 (ChEBI)
phytosterols MetaboliteCHEBI:26125 (ChEBI)
porphyrinMetaboliteCHEBI:8337 (ChEBI)
sterolsComplexR-ALL-265781 (Reactome)
sterolsComplexR-ALL-265784 (Reactome)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
23mer peptideArrowR-HSA-5223317 (Reactome)
23mer peptideR-HSA-5223317 (Reactome)
ABCA cholesterol transportersmim-catalysisR-HSA-1369028 (Reactome)
ABCA cholesterol transportersmim-catalysisR-HSA-1369052 (Reactome)
ABCA12mim-catalysisR-HSA-5682285 (Reactome)
ABCA3mim-catalysisR-HSA-5683714 (Reactome)
ABCA4mim-catalysisR-HSA-1467466 (Reactome)
ABCA7-1:ApoA1 complexmim-catalysisR-HSA-382553 (Reactome)
ABCA7-dependent phospholipidsArrowR-HSA-382553 (Reactome)
ABCA7-dependent phospholipidsR-HSA-382553 (Reactome)
ABCA8/B1/B5mim-catalysisR-HSA-1467457 (Reactome)
ABCB4mim-catalysisR-HSA-5678706 (Reactome)
ABCB9 dimermim-catalysisR-HSA-5223317 (Reactome)
ABCC2mim-catalysisR-HSA-5679041 (Reactome)
ABCCsmim-catalysisR-HSA-1454916 (Reactome)
ABCD1-3 dimersArrowR-HSA-382613 (Reactome)
ABCD1-3 dimersmim-catalysisR-HSA-382575 (Reactome)
ABCE1:RNASEL dimerArrowR-HSA-5223305 (Reactome)
ABCE1R-HSA-5223305 (Reactome)
ABCF1:EIF2S1:EIF2S2:EIF2S3ArrowR-HSA-5227009 (Reactome)
ABCF1R-HSA-5227009 (Reactome)
ABCG1 dimermim-catalysisR-HSA-266082 (Reactome)
ABCG4 dimermim-catalysisR-HSA-1454928 (Reactome)
ABCG5:ABCG8mim-catalysisR-HSA-265783 (Reactome)
ADPArrowR-HSA-1369028 (Reactome)
ADPArrowR-HSA-1369052 (Reactome)
ADPArrowR-HSA-1369065 (Reactome)
ADPArrowR-HSA-1454916 (Reactome)
ADPArrowR-HSA-1454928 (Reactome)
ADPArrowR-HSA-1467457 (Reactome)
ADPArrowR-HSA-1467466 (Reactome)
ADPArrowR-HSA-265783 (Reactome)
ADPArrowR-HSA-266082 (Reactome)
ADPArrowR-HSA-382553 (Reactome)
ADPArrowR-HSA-382560 (Reactome)
ADPArrowR-HSA-382575 (Reactome)
ADPArrowR-HSA-383190 (Reactome)
ADPArrowR-HSA-5223317 (Reactome)
ADPArrowR-HSA-5678706 (Reactome)
ADPArrowR-HSA-5678863 (Reactome)
ADPArrowR-HSA-5678992 (Reactome)
ADPArrowR-HSA-5679041 (Reactome)
ADPArrowR-HSA-5682285 (Reactome)
ADPArrowR-HSA-5683714 (Reactome)
ATPR-HSA-1369028 (Reactome)
ATPR-HSA-1369052 (Reactome)
ATPR-HSA-1369065 (Reactome)
ATPR-HSA-1454916 (Reactome)
ATPR-HSA-1454928 (Reactome)
ATPR-HSA-1467457 (Reactome)
ATPR-HSA-1467466 (Reactome)
ATPR-HSA-265783 (Reactome)
ATPR-HSA-266082 (Reactome)
ATPR-HSA-382553 (Reactome)
ATPR-HSA-382560 (Reactome)
ATPR-HSA-382575 (Reactome)
ATPR-HSA-383190 (Reactome)
ATPR-HSA-5223317 (Reactome)
ATPR-HSA-5678706 (Reactome)
ATPR-HSA-5678863 (Reactome)
ATPR-HSA-5678992 (Reactome)
ATPR-HSA-5679041 (Reactome)
ATPR-HSA-5682285 (Reactome)
ATPR-HSA-5683714 (Reactome)
BMG,BDGArrowR-HSA-5679041 (Reactome)
BMG,BDGR-HSA-5679041 (Reactome)
CFTR G551DR-HSA-5679000 (Reactome)
CFTRmim-catalysisR-HSA-383190 (Reactome)
CFTRmim-catalysisR-HSA-5678863 (Reactome)
CHOLArrowR-HSA-1369028 (Reactome)
CHOLArrowR-HSA-1369052 (Reactome)
CHOLArrowR-HSA-1454928 (Reactome)
CHOLArrowR-HSA-266082 (Reactome)
CHOLR-HSA-1369028 (Reactome)
CHOLR-HSA-1369052 (Reactome)
CHOLR-HSA-1454928 (Reactome)
CHOLR-HSA-266082 (Reactome)
Cl-ArrowR-HSA-5678863 (Reactome)
Cl-ArrowR-HSA-5678992 (Reactome)
Cl-R-HSA-5678863 (Reactome)
Cl-R-HSA-5678992 (Reactome)
EIF2S1:EIF2S2:EIF2S3R-HSA-5227009 (Reactome)
H2OR-HSA-1369028 (Reactome)
H2OR-HSA-1369052 (Reactome)
H2OR-HSA-1369065 (Reactome)
H2OR-HSA-1454916 (Reactome)
H2OR-HSA-1454928 (Reactome)
H2OR-HSA-1467457 (Reactome)
H2OR-HSA-1467466 (Reactome)
H2OR-HSA-265783 (Reactome)
H2OR-HSA-266082 (Reactome)
H2OR-HSA-382553 (Reactome)
H2OR-HSA-382560 (Reactome)
H2OR-HSA-382575 (Reactome)
H2OR-HSA-383190 (Reactome)
H2OR-HSA-5223317 (Reactome)
H2OR-HSA-5678706 (Reactome)
H2OR-HSA-5678863 (Reactome)
H2OR-HSA-5678992 (Reactome)
H2OR-HSA-5679041 (Reactome)
H2OR-HSA-5682285 (Reactome)
H2OR-HSA-5683714 (Reactome)
HCO3-ArrowR-HSA-383190 (Reactome)
HCO3-R-HSA-383190 (Reactome)
Heme transportersmim-catalysisR-HSA-382560 (Reactome)
Ivacaftor:CFTR G551DArrowR-HSA-5679000 (Reactome)
Ivacaftor:CFTR G551Dmim-catalysisR-HSA-5678992 (Reactome)
IvacaftorR-HSA-5679000 (Reactome)
K+ArrowR-HSA-5678261 (Reactome)
K+R-HSA-5678261 (Reactome)
KCNJ11:ABCC9mim-catalysisR-HSA-5678261 (Reactome)
LCFAArrowR-HSA-382575 (Reactome)
LCFAR-HSA-382575 (Reactome)
MTABC3 dimermim-catalysisR-HSA-1369065 (Reactome)
PC, PGArrowR-HSA-5683714 (Reactome)
PC, PGR-HSA-5683714 (Reactome)
PCArrowR-HSA-5678706 (Reactome)
PCR-HSA-5678706 (Reactome)
PEX19:ABCD1/2/3R-HSA-382613 (Reactome)
PEX19ArrowR-HSA-382613 (Reactome)
PEX3ArrowR-HSA-382613 (Reactome)
PEX3R-HSA-382613 (Reactome)
PiArrowR-HSA-1369028 (Reactome)
PiArrowR-HSA-1369052 (Reactome)
PiArrowR-HSA-1369065 (Reactome)
PiArrowR-HSA-1454916 (Reactome)
PiArrowR-HSA-1454928 (Reactome)
PiArrowR-HSA-1467457 (Reactome)
PiArrowR-HSA-1467466 (Reactome)
PiArrowR-HSA-265783 (Reactome)
PiArrowR-HSA-266082 (Reactome)
PiArrowR-HSA-382553 (Reactome)
PiArrowR-HSA-382560 (Reactome)
PiArrowR-HSA-382575 (Reactome)
PiArrowR-HSA-383190 (Reactome)
PiArrowR-HSA-5223317 (Reactome)
PiArrowR-HSA-5678706 (Reactome)
PiArrowR-HSA-5678863 (Reactome)
PiArrowR-HSA-5678992 (Reactome)
PiArrowR-HSA-5679041 (Reactome)
PiArrowR-HSA-5682285 (Reactome)
PiArrowR-HSA-5683714 (Reactome)
R-HSA-1369028 (Reactome) The exact roles of ABCA2 (Vulevic et al. 2001, Kaminski et al. 2001), ABCA6 (Kaminski & Wenzel et al. 2001), ABCA9 (Piehler et al. 2002) and ABCA10 (Wenzel et al. 2003), candidates for ABC lipid transporter-related activities, need to be elucidated. Even thought cholesterol-responsiveness has been noted in experimental systems, contribution of these proteins in regulation or in active transport is not yet clear.
R-HSA-1369052 (Reactome) The exact roles of ABCA2 (Vulevic et al. 2001, Kaminski et al. 2001), ABCA6 (Kaminski & Wenzel et al. 2001), ABCA9 (Piehler et al. 2002) and ABCA10 (Wenzel et al. 2003), candidates for ABC lipid transporter-related activities, need to be elucidated. Even thought cholesterol-responsiveness has been noted in experimental systems, contribution of these proteins in regulation or in active transport is not yet clear.
R-HSA-1369065 (Reactome) The human gene ABCB6 encodes a mitochondrial half-type ATP-binding cassette (ABC) protein MTABC3 which is uniquely located on the outer mitochondrial membrane and is functional as a homodimer (Krishnamurthy et al. 2006). It plays a crucial role in heme synthesis by mediating porphyrin uptake into mitochondria (Mitsuhashi et al. 2000, Krishnamurthy et al. 2006).
R-HSA-1454916 (Reactome) The multidrug resistance associated protein (MRPs) subfamily of the ABC transporter family can transport a wide and diverse range of organic anions that can be endogenous compounds and xenobiotics and their metabolites. All human MRPs (except MRP9) can mediate these transport reactions (Deeley et al. 2006). Separately, specific reactions have also been annotated to describe the roles of ABCC4 in platelet dense granule assembly, of ABCC1 in LTC4 export (an aspect of leukotriene synthesis), and of ABCC3 in bile salt efflux.
R-HSA-1454928 (Reactome) Human ABCG4 shows sequence homology to the Drosophila white gene, the product of which must dimerise to become functionally active. ABCG4 is closely related to ABCG1 with 74% identity and is thus thought to play a role in the efflux of excess cholesterol (Engel et al. 2001). Northern Blot analysis shows that ABCG4 is expressed specifically in brain and the eye (Oldfield et al. 2002).
R-HSA-1467457 (Reactome) Some members of the ABC transporter superfamily are able to mediate the efflux of a broad range of cytotoxic drugs from cells, leading to the name multidrug resistance (MDR) proteins (Seeger and van Veen 2009). The ABCB1 (P-glycoprotein 1[PGP], multidrug resistance protein 1 [MRP1]) is the most characterised MDR (Shen et al. 1986, Gottesman & Pastan 1988). ABCB5 (Frank et al. 2005) and ABCA8 (Tsuruoka et al. 2002) are newer members of MDRs.
R-HSA-1467466 (Reactome) Rhodopsin (RHO) is localised to both the disc membrane and the plasma membrane of rod outer segments (ROS). All-trans-retinal (atRAL) released from rhodopsin during the bleaching process, needs to translocate to the cytosol for reduction to all-trans-retinol (atROL) via all-trans-retinol dehydrogenases. Although atRAL can diffuse through membranes unaided, there exists an ABC transporter on disc membranes which may facilitate the transport of excess atRAL. Retinal-specific ATP-binding cassette transporter (ABCA4, ABCR) is the only ABC transporter which mediates the transport of retinoids (Biswas & Biswas 2000). Studies using bovine ABCA4 demonstrates atRAL transport (Sun et al. 1999). Human ABCR was found to be identical to the ABC transporter linked to Stargardt's disease type 1 (STGD1, MIM:248200), a cause of macular degeneration in childhood (Nasonkin et al. 1998).
R-HSA-265783 (Reactome) The complex of ATP-binding cassette sub-family G members 5 and 8 (ABCG5:ABCG8) in the plasma membrane mediates the ATP-dependent export of cytosolic sterols (cholesterol and phytosterols). Mutations affecting the ABCG5/8 proteins are associated with the accumulation of high levels of cholesterol and phytosterols in the body, demonstrating the specificity and physiological importance of this process (Berge et al. 2000). Human ABCG5/8 has not been studied in detail, but the homologous mouse protein complex mediate ATP-dependent sterol export (Wang et al. 2006). The mouse proteins localize to the apical plasma membranes of enterocytes and hepatocytes, consistent with the hypothesis that in vivo ABCG5/8 mediates sterol export into the gut lumen and from hepatocytes into the bile (Graf et al. 2003).
R-HSA-266082 (Reactome) In an ATP-dependent reaction, ABCG1 mediates the movement of intracellular cholesterol to the extracellular face of the plasma membrane. In a tissue culture model system, the active form of ABCG1 is predominantly a tetramer (Vuaghan and Oram 2005). The number of lipid molecules transported per ATP consumed is not known.
R-HSA-382553 (Reactome) ABCA7 has the ability to bind apolipoproteins and promote efflux of cellular phospholipids and may have a possible role in cellular phospholipid metabolism in peripheral tissues. Like many other ABC-transporters, the exact role of ABCA7 is waiting to be elucidated.
R-HSA-382560 (Reactome) Mitochondrial ABC transporters are thought to play a key role in iron metabolism and heme biosynthesis. All mitochondrial ABC transporters described to date are of the half-transporter type and would probably function as dimers (Ramjeesingh et al. 2003) but their dimerization partners have not yet been identified. ABC7 is the functional human orthologue of yeast Atm1p (Csere et al. 1998), is predicted to dimerize in the same way as Atm1p (Chloupková et al. 2004) and is probably involved in iron homeostasis. Defects in ABCB7 are the cause of X-linked sideroblastic anemia with ataxia (ASAT) [MIM:301310] (Allikmets et al. 1999). Human genes ABCB8 and ABCB10 encode mABC1 and mABC2 respectively (Hogue et al. 1999, Zhang et al 2000 respectively). They would be expected to dimerize, as demonstrated for mABC2 (Graf et al. 2004). Both are believed to have similar functionality to ABC7 although this has not been demonstrated yet.
R-HSA-382575 (Reactome) The 70-kDa peroxisomal membrane protein (PMP70) and the adrenoleukodystrophy protein (ALDP aka ABCD1) are half ATP binding cassette (ABC) transporters in the peroxisome membrane. They are involved in metabolic transport of long and very long chain fatty acids into peroxisomes. Mutations in the ALD gene result in the X-linked neurodegenerative disorder adrenoleukodystrophy (ALD; MIM:300100). ABCD1 deficiency impairs the peroxisomal beta-oxidation of very long-chain fatty acids (VLCFA) and facilitates their further chain elongation by ELOVL1 resulting in accumulation of VLCFA in plasma and tissues. While all patients with ALD have mutations in the ABCD1 gene, there is no general genotype-phenotype correlation. In addition to ABCD1, other genes and environmental factors determine clinical features of ALD (Kemp et al. 2012, Berger et al. 2014).
R-HSA-382613 (Reactome) PEX19 is a chaperone protein that binds a broad spectrum of peroxisomal membrane proteins (PMPs), and interacts with regions of PMPs required for their targeting to peroxisomes. PEX3 is required for PEX19 to dock at peroxisomes, interacts specifically with the docking domain of PEX19, and is required for recruitment of the PEX19 docking domain to peroxisomes. The ABC transporters D1, D2 and D3 must first form dimers to become fully functional (Liu et al.1999) which then can bind with PEX19.
R-HSA-383190 (Reactome) Regulation of epithelial chloride flux, which is defective in patients with cystic fibrosis, may be mediated by phosphorylation of the cystic fibrosis transmembrane conductance regulator (CFTR) by cyclic AMP-dependent protein kinase (PKA) or protein kinase C (PKC). CFTR regulates both HCO(3)(-) secretion and HCO(3)(-) salvage in secretory epithelia.
R-HSA-5223305 (Reactome) 2-5A-dependent ribonuclease (RNASEL) is an endoribonuclease that is activated in the interferon (IFN) antiviral response. Its anti-viral effects are probably a combination of induction of apoptosis, cleavage of viral mRNA and induction of other anti-viral genes. ATP-binding cassette sub-family E member 1 (ABCE1, aka RNase L inhibitor, RLI) directly interacts with RNASEL and inhibits its endoribonuclease activity, thus antagonising the anti-viral effect of the IFN-regulated 2-5A/RNase L pathway (Martinand et al. 1998, Martinand et al. 1999, Le Roy et al. 2001).
R-HSA-5223317 (Reactome) ATP-binding cassette sub-family B member 9 (ABCB9, aka lysosomal ABC transporter associated with antigen processing-like, TAPL) is a homodimeric ATP-dependent low affinity peptide transporter (Wolters et al. 2005), localised on the lysosomal membrane (Zhang et al. 2000). It is able to transport a broad spectrum of peptides (from 6mer up to at least 59mer peptides, optimum of 23mers) from the cytosol to the lysosomal lumen. ABCB9 favours positively charged, aromatic or hydrophobic residues in the N- and C-terminal positions whereas negatively charged residues and asparagine and methionine residues are not favoured (Wolters et al. 2005, Demirel et al. 2007, Zhao et al. 2008). The reaction described here shows the transport of the optimum 23mer peptide.
R-HSA-5227009 (Reactome) ATP-binding cassette sub-family F member 1 (ABCF1 aka ABC50) is unlike most ABC proteins in that it does not possess membrane-spanning domains. ABCF1 interacts with eukaryotic initiation factor 2 complex (EIF2S1:EIF2S2:EIF2S3), a key player in translation initiation and control and in ribosome regulation. ABCF1 is predominantly located in the cytosol, whereas a smaller amount is also found in the nucleoplasm but not in the nucleolus. Knockout of ABCF1 impaired translation of both cap-dependent and cap-independent reporters, consistent with a positive role for ABCF1 in the function of the EIF2 complex (Paytubi et al. 2008, Paytubi et al. 2009).
R-HSA-5678261 (Reactome) ATP-sensitive inward rectifier potassium channel 11 (KCNJ11) is an inward rectifier potassium channel, favouring potassium flow into the cell rather than out of it. KCNJ11 can complex with ATP-binding cassette sub-family member 9 (ABCC9) to form cardiac and smooth muscle-type K+(ATP) channels. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation (Babenko et al. 1998, Tammaro & Ashcroft 2007).
R-HSA-5678706 (Reactome) Multidrug resistance protein 3 (ATP-binding cassette sub-family B member 4, ABCB4 aka MDR3) mediates the ATP-dependent export of organic anions and drugs from hepatocytes into the canalicular lumen in the presence of bile salts. ABCB4 is especially important for the export of phospholipids such as phosphatidylcholine (PC) from the plasma membrane of hepatocytes (Morita et al. 2007). Biliary phospholipids associate with bile salts and cholesterol in mixed micelles, thereby reducing the detergent activity and cytotoxicity of bile salts and preventing cholesterol crystallisation. Thus, ABCB4 plays a crucial role in bile formation and lipid homeostasis (Morita & Terada 2014).
R-HSA-5678863 (Reactome) Cystic fibrosis transmembrane conductance regulator (CFTR) is a low conductance chloride-selective channel that mediates the transport of chloride ions in human airway epithelial cells which plays a key role in maintaining homoeostasis of epithelial secretions in the lungs. Defects in CFTR can cause cystic fibrosis (CF; MIM:602421), a common generalised disorder in Caucasians affecting the exocrine glands. CF results in an ionic imbalance that impairs clearance of secretions, not only in the lung, but also in the pancreas, gastrointestinal tract and liver (Riordan et al. 1999, Ousingsawat et al. 2011).
R-HSA-5678992 (Reactome) Cystic fibrosis transmembrane conductance regulator (CFTR) is a low conductance chloride-selective channel that mediates the transport of chloride ions in human airway epithelial cells which plays a key role in maintaining homoeostasis of epithelial secretions in the lungs. Defects in CFTR can cause cystic fibrosis (CF; MIM:602421), a common generalised disorder in Caucasians affecting the exocrine glands. CF results in an ionic imbalance that impairs clearance of secretions, not only in the lung, but also in the pancreas, gastrointestinal tract and liver. Wide-ranging manifestations of the disease include chronic lung disease, exocrine pancreatic insufficiency, blockage of the terminal ileum, male infertility and salty sweat.

The class 3 mutations of CFTR such as G551D strongly decrease the time spent by CFTR in the open state (a gating defect). Results from 2-phase clinical trials using VX-770 (aka Ivacaftor), a CFTR potentiator, showed an increased CFTR channel open probability in G551D patients. Ivacaftor use showed improvements in CFTR and lung function of patients with at least one G551D allele (Accurso et al. 2010, Ramsey et al. 2011, Kapoor et al. 2014). In 2012, the FDA approved Ivacaftor (under the trade name Kalydeco) for use in cystic fibrosis patients with the G551D mutation (Ledford 2012).
R-HSA-5679000 (Reactome) Defects in cystic fibrosis transmembrane conductance regulator (CFTR) can cause cystic fibrosis (CF; MIM:602421), a common generalised disorder in Caucasians affecting the exocrine glands. CF results in an ionic imbalance that impairs clearance of secretions, not only in the lung, but also in the pancreas, gastrointestinal tract and liver. Wide-ranging manifestations of the disease include chronic lung disease, exocrine pancreatic insufficiency, blockage of the terminal ileum, male infertility and salty sweat. The class 3 mutations of CFTR such as G551D strongly decrease the time spent by CFTR in the open state (a gating defect). Results from 2-phase clinical trials using VX-770 (aka Ivacaftor), a CFTR potentiator, showed an increased CFTR channel open probability in G551D patients. Ivacaftor use showed improvements in CFTR and lung function of patients with at least one G551D allele (Accurso et al. 2010, Ramsey et al. 2011, Kapoor et al. 2014). In 2012, the FDA approved Ivacaftor (under the trade name Kalydeco) for use in cystic fibrosis patients with the G551D mutation (Ledford 2012).
R-HSA-5679041 (Reactome) Canalicular multispecific organic anion transporter 1 (ABCC2 aka multidrug resistance-associated protein 2, MRP2), in addition to transporting many organic anions, mediates the ATP-dependent transport of glutathione and glucuronate conjugates from hepatocytes into bile. In the reaction annotated here, ABCC2 specifically transports, with high affinity and efficiency, mono- and di-glucuronated bilirubin into bile (Kamisako et al. 1999). Bilirubin, the end product of heme breakdown, is an important constituent of bile and is responsible for its characteristic colour.
R-HSA-5682285 (Reactome) ATP-binding cassette sub-family A member 12 (ABCA12) is thought to function as an epidermal keratinocyte lipid transporter. Lipids such as glucosylceramides and gangliosides form extracellular lipid layers in the stratum corneum of the epidermis, essential for skin barrier function (Akiyama et al. 2005). Mutations in ABCA12 can cause autosomal recessive congenital ichthyoses (ARCI).
R-HSA-5683714 (Reactome) ATP-binding cassette sub-family A member 3 (ABCA3) plays an important role in the formation of pulmonary surfactant, probably by transporting phospholipids such as phosphatidylcholine (PC) and phosphatidylglycerol (PG) from the ER membrane to lamellar bodies (LBs). PC and PG are the major phospholipid constituents of pulmonary surfactant. LBs are the surfactant storage organelles of type II epithelial cells from where phospholipids can be secreted together with surfactant proteins (SFTPs) into the alveolar airspace (Klugbauer & Hofmann 1996, Yamano et al. 2001). Defects in ABCA3 are the cause of pulmonary surfactant metabolism dysfunction type 3 (SMDP3; MIM:610921) (Shulenin et al. 2004).
RNASEL dimerR-HSA-5223305 (Reactome)
a xenobioticArrowR-HSA-1467457 (Reactome)
a xenobioticR-HSA-1467457 (Reactome)
atRALArrowR-HSA-1467466 (Reactome)
atRALR-HSA-1467466 (Reactome)
hemeArrowR-HSA-382560 (Reactome)
hemeR-HSA-382560 (Reactome)
lipidsArrowR-HSA-5682285 (Reactome)
lipidsR-HSA-5682285 (Reactome)
organic anionArrowR-HSA-1454916 (Reactome)
organic anionR-HSA-1454916 (Reactome)
porphyrinArrowR-HSA-1369065 (Reactome)
porphyrinR-HSA-1369065 (Reactome)
sterolsArrowR-HSA-265783 (Reactome)
sterolsR-HSA-265783 (Reactome)
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