Iron uptake and transport (Bos taurus)

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6, 51, 9553, 126, 139111, 12315, 25, 118725441, 52, 66, 76, 90...1170, 105, 1226310443, 45145446888, 14724, 131, 14150, 11069, 10135, 58, 6727, 31, 37, 1385, 18, 23, 56, 60...1244, 119, 135, 14026, 331, 10, 13, 19, 30...22, 117, 142137, 14634, 49, 55, 79, 9432117, 12920, 109, 112113, 62, 103, 106, 13229, 39, 8357, 801159, 72, 989328, 48, 75, 14469, 101, 13614, 38, 47111, 12312, 21, 64, 82, 87...7743, 451258, 16, 17, 71, 84...81, 9236, 42134462ATP6V1G [cytosol]endosome lumenASIC trimer:H+[plasma membrane]sarcoplasmic reticulum lumenSGK1/2/3 [cytosol]ATP1B [plasmamembrane]RYR1 tetramer[sarcoplasmicreticulum membrane]MTP1:CP:6Cu2+[plasma membrane]GLRA:GLRB:Gly[plasma membrane]ASIC5 trimer:H+[plasma membrane]holoTF:TFRC [plasmamembrane]holoTF[extracellularregion]ATP6V0D [endosomemembrane]mitochondrial matrixRYR tetramer:CASQpolymer:TRDN:junctin[sarcoplasmicreticulum membrane]CLCNKB:BSND [plasmamembrane]NALCN:UNC79:UNC80[plasma membrane]GABRR pentamer:GABA[plasma membrane]GABRAs [plasmamembrane]CYBRD1:Heme[extracellularregion]HTR3 receptors[plasma membrane]ABCG2 dimer [plasmamembrane]ATP6V0C hexamer[endosome membrane]ATP6V1A trimer[cytosol]sperm flagellumTFRC dimer [plasmamembrane]late endosome lumenTF:TFRC [plasmamembrane]holoTF:TFRC dimer[endosome membrane]GABRBs [plasmamembrane]ATP6V1G dimer[cytosol]platelet dense tubular network lumenASIC2 trimer:H+[plasma membrane]TF:TFRC dimer[endosome membrane]holoTF[extracellularregion]holoTF [endosomemembrane]V-ATPase [endosomemembrane]ATP6V1E [cytosol]RAF1:SGK:TSC22D3:WPP[cytosol]lysosomal lumenGolgi lumenATP6V1B trimer[cytosol]Ub-SCNN channels[plasma membrane]CASQ polymer[sarcoplasmicreticulum lumen]GABRR1-3 [plasmamembrane]ATP4A/12A:ATP4B[plasma membrane]TFRC dimer [plasmamembrane]SCNN channels[plasma membrane]ATP2C1/2:Mg2+ [Golgimembrane]TFRC dimer [endosomemembrane]cytosolUb-SCNN1A/SCNN1D[plasma membrane]ATP6V1 [cytosol]CLCN1/2/KA/KB[plasma membrane]ATP1A:ATP1B:FXYD[plasma membrane]CLCN7:OSTM1[lysosomal membrane]ATP6V0E [endosomemembrane]endoplasmic reticulum lumenMTP1:HEPH:6Cu2+[plasma membrane]HTR3:5HT [plasmamembrane]SCNN1A/1D [plasmamembrane]ATP6V1C [cytosol]FXYDs [plasmamembrane]TFRC dimer [plasmamembrane]ATP6V1B [cytosol]ASIC1 trimer:H+[plasma membrane]TFRC dimer [endosomemembrane]2GABRA:2GABRB:GABRG:GABA[plasma membrane]CLCNKA:BSND [plasmamembrane]ATP6V0A [endosomemembrane]FTH1:FTL [cytosol]Ferritin Complex[cytosol]RYR tetramers[sarcoplasmicreticulum membrane]ATP6V0 [endosomemembrane]RYR2 tetramer[sarcoplasmicreticulum membrane]mitochondrial intermembrane spaceRYR3 tetramer[sarcoplasmicreticulum membrane]ATP4A/12A [plasmamembrane]ATP1A [plasmamembrane]GABRGs [plasmamembrane]GABRA2:ARHGEF9[plasma membrane]WPP1/NEDD4L[cytosol]ATP2C1/2 [Golgimembrane]ASIC3 trimer:H+[plasma membrane]K+Fe3+TFATP1B3Urate5HT [extracellularregion]Fe3+V-ATPaseATP6V1HSGK1Mg2+ [Golgimembrane]H+heme [plasmamembrane]CLIC2AMPH2OSLC9B2Gly [extracellularregion]Cl-OSTM1Ca2+ATP1A3ATPHTR3DTFNa+H+TFPiRYR tetramer:CASQpolymer:TRDN:junctinPiSCNN1AATP6V0E1H2OHTR3BMTP1:CP:6Cu2+NALCNH+TFRCASIC4O2H+ATP2C2GABRG2H+GABRB2H+SCNN1DATP6V0BADPATP6V0A1H+ATP2A1-3ATP6V0D2GABRR1ATP1A4PiGABRB1SLC9B1/C2GABRA5Cu2+ [extracellularregion]GABRR pentamer:GABAFXYD7FXYD4 [plasmamembrane]Na+ATPATP1A2RAF1Cl-P-type ATPases typeIVGABRR2FXYD1TFRCK+ATP2C1H+Ca2+HTR3:5HTH2ONa+Fe2+RYR3TPCN1/2Cu2+ATP6V1G3ATPNAADPH+GABA [extracellularregion]GLRBASIC5H2OCPTFRC dimerATP6V1B1SCNN1BADPSTEAP3Fe3+Fe2+Cl-Ferritin ComplexADPATPATP6V1ACl-COH+ATP7BNa+Ub-SCNN channelsCLCN4/5/6ATPCl-H2OATPANOsH+Cl-ASIC trimer:H+ATP1B1ATP4AADPH2OHTR3C [plasmamembrane]Na+holoTFCa2+ATPATP2C1/2:Mg2+ARHGEF9ADPCLCN2Na+H+Ca2+CLCN7:OSTM1SCNN1DhemeH+SCNN1AFe3+ [extracellularregion]TFRCGABRA2HEPH2GABRA:2GABRB:GABRG:GABACLCN1Cl-HMOX1/2K+Cu2+BESTsFLVCR1ATP6V0A2ATP12ACu2+GABA [extracellularregion]Na+ASIC2 [plasmamembrane]Na+PiABCG2 dimerASIC1Cu2+ [plasmamembrane]HTR3Ae-Na+GABRA1SCNN channelsFeHMATPFe3+SLC17A3FTL [cytosol]PPiSGK2Ca2+BVFXYD2ATP2A1-3UbCLCN7ATP6V1C2Ca2+ATP7ATSC22D3Cl-Ca2+H+Cl-hemeTFTFRCholoTF:TFRCTFCLCN1/2/KA/KBATP6V1E1H+ [extracellularregion]TFRCGABRA6APLsATP6V1DCa2+FeHMCLCNKB [plasmamembrane]RYR1Ca2+Cl-SLC40A1H+ATP1A1NADP+SCNN1GNa+ATP6V1C1SGK3 [cytosol]ADPATP6V1G1GABRA4TF:TFRC dimerCa2+ACCN3ATP1B2ATP6V0D1ATPCYBRD1:HemeBSNDSCNN1BPiCa2+UNC80PiCa2+GABRB3RYR2Fe3+ [endosomemembrane]H2OH2OATP6V0E2Fe3+ [extracellularregion]ATP1A:ATP1B:FXYDFXYD6SLC40A1PiNa+HCO3-HCO3-ATP6V1G2NADPHFe2+TRDNH+TFTCIRG1GABRG3 [plasmamembrane]PiPiATP4A/12A:ATP4BATP6V1E2GLRA:GLRB:GlyFXYD3RAF1:SGK:TSC22D3:WPPH+ATP4Be-H2ONEDD4LNSAIDFe3+H+Na+SCNN1GMCOLN1ATP6V0CUrateCa2+H+O2amilorideH+O2Na+NALCN:UNC79:UNC80FTH1(2-183)[cytosol]APLsWWP1holoTF:TFRC dimerCa2+H2OADPH+TF:TFRCCLCNKA [plasmamembrane]SLC9C1ATP6V0A4CYBRD1SLC46A1ABCG2Fe2+Na+ATP6V1B2H+CLCN3MTP1:HEPH:6Cu2+ATP6V1F [cytosol]WNKsGABRR3 [plasmamembrane]UNC79Na+Ca2+TTYH2/3Na+GABRA3HTR3EATP2B1-4H+K+SLC11A2TTYH1-3SLC17A3102mitochondrial intermembrane spaceH+H+SLC9B2Li+Li+36, 42mitochondrial matrix


Description

The transport of iron between cells is mediated by transferrin. However, iron can also enter and leave cells not only by itself, but also in the form of heme and siderophores. When entering the cell via the main path (by transferrin endocytosis), its goal is not the (still elusive) chelated iron pool in the cytosol nor the lysosomes but the mitochondria, where heme is synthesized and iron-sulfur clusters are assembled (Kurz et al,2008, Hower et al 2009, Richardson et al 2010).Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=917937

Comments

HomologyConvert 
This pathway was inferred from Homo sapiens pathway WP2670(76854) with a 88.0% conversion rate.

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Bibliography

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  1. Nozu K, Inagaki T, Fu XJ, Nozu Y, Kaito H, Kanda K, Sekine T, Igarashi T, Nakanishi K, Yoshikawa N, Iijima K, Matsuo M.; ''Molecular analysis of digenic inheritance in Bartter syndrome with sensorineural deafness.''; PubMed Europe PMC Scholia
  2. Paulusma CC, Oude Elferink RP.; ''The type 4 subfamily of P-type ATPases, putative aminophospholipid translocases with a role in human disease.''; PubMed Europe PMC Scholia
  3. Vulpe C, Levinson B, Whitney S, Packman S, Gitschier J.; ''Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase.''; PubMed Europe PMC Scholia
  4. Cutting GR, Lu L, O'Hara BF, Kasch LM, Montrose-Rafizadeh C, Donovan DM, Shimada S, Antonarakis SE, Guggino WB, Uhl GR.; ''Cloning of the gamma-aminobutyric acid (GABA) rho 1 cDNA: a GABA receptor subunit highly expressed in the retina.''; PubMed Europe PMC Scholia
  5. Tunwell RE, Wickenden C, Bertrand BM, Shevchenko VI, Walsh MB, Allen PD, Lai FA.; ''The human cardiac muscle ryanodine receptor-calcium release channel: identification, primary structure and topological analysis.''; PubMed Europe PMC Scholia
  6. Kurz T, Terman A, Gustafsson B, Brunk UT.; ''Lysosomes in iron metabolism, ageing and apoptosis.''; PubMed Europe PMC Scholia
  7. Horisberger JD.; ''Amiloride-sensitive Na channels.''; PubMed Europe PMC Scholia
  8. Hadingham KL, Wafford KA, Thompson SA, Palmer KJ, Whiting PJ.; ''Expression and pharmacology of human GABAA receptors containing gamma 3 subunits.''; PubMed Europe PMC Scholia
  9. Yang XL, Miura N, Kawarada Y, Terada K, Petrukhin K, Gilliam T, Sugiyama T.; ''Two forms of Wilson disease protein produced by alternative splicing are localized in distinct cellular compartments.''; PubMed Europe PMC Scholia
  10. Waldegger S, Jentsch TJ.; ''Functional and structural analysis of ClC-K chloride channels involved in renal disease.''; PubMed Europe PMC Scholia
  11. Hémadi M, Ha-Duong NT, El Hage Chahine JM.; ''The mechanism of iron release from the transferrin-receptor 1 adduct.''; PubMed Europe PMC Scholia
  12. Choudhury K, McQuillin A, Puri V, Pimm J, Datta S, Thirumalai S, Krasucki R, Lawrence J, Bass NJ, Quested D, Crombie C, Fraser G, Walker N, Nadeem H, Johnson S, Curtis D, St Clair D, Gurling HM.; ''A genetic association study of chromosome 11q22-24 in two different samples implicates the FXYD6 gene, encoding phosphohippolin, in susceptibility to schizophrenia.''; PubMed Europe PMC Scholia
  13. Estévez R, Boettger T, Stein V, Birkenhäger R, Otto E, Hildebrandt F, Jentsch TJ.; ''Barttin is a Cl- channel beta-subunit crucial for renal Cl- reabsorption and inner ear K+ secretion.''; PubMed Europe PMC Scholia
  14. Tian Y, Schreiber R, Kunzelmann K.; ''Anoctamins are a family of Ca2+-activated Cl- channels.''; PubMed Europe PMC Scholia
  15. Stobrawa SM, Breiderhoff T, Takamori S, Engel D, Schweizer M, Zdebik AA, Bösl MR, Ruether K, Jahn H, Draguhn A, Jahn R, Jentsch TJ.; ''Disruption of ClC-3, a chloride channel expressed on synaptic vesicles, leads to a loss of the hippocampus.''; PubMed Europe PMC Scholia
  16. Edenberg HJ, Dick DM, Xuei X, Tian H, Almasy L, Bauer LO, Crowe RR, Goate A, Hesselbrock V, Jones K, Kwon J, Li TK, Nurnberger JI Jr, O'Connor SJ, Reich T, Rice J, Schuckit MA, Porjesz B, Foroud T, Begleiter H.; ''Variations in GABRA2, encoding the alpha 2 subunit of the GABA(A) receptor, are associated with alcohol dependence and with brain oscillations.''; PubMed Europe PMC Scholia
  17. Khan ZU, Fernando LP, Escribá P, Busquets X, Mallet J, Miralles CP, Filla M, De Blas AL.; ''Antibodies to the human gamma 2 subunit of the gamma-aminobutyric acidA/benzodiazepine receptor.''; PubMed Europe PMC Scholia
  18. Board PG, Coggan M, Watson S, Gage PW, Dulhunty AF.; ''CLIC-2 modulates cardiac ryanodine receptor Ca2+ release channels.''; PubMed Europe PMC Scholia
  19. Koch MC, Steinmeyer K, Lorenz C, Ricker K, Wolf F, Otto M, Zoll B, Lehmann-Horn F, Grzeschik KH, Jentsch TJ.; ''The skeletal muscle chloride channel in dominant and recessive human myotonia.''; PubMed Europe PMC Scholia
  20. Davies PA, Pistis M, Hanna MC, Peters JA, Lambert JJ, Hales TG, Kirkness EF.; ''The 5-HT3B subunit is a major determinant of serotonin-receptor function.''; PubMed Europe PMC Scholia
  21. Ruiz A, Bhat SP, Bok D.; ''Expression and synthesis of the Na,K-ATPase beta 2 subunit in human retinal pigment epithelium.''; PubMed Europe PMC Scholia
  22. Chen H, Attieh ZK, Dang T, Huang G, van der Hee RM, Vulpe C.; ''Decreased hephaestin expression and activity leads to decreased iron efflux from differentiated Caco2 cells.''; PubMed Europe PMC Scholia
  23. Zorzato F, Fujii J, Otsu K, Phillips M, Green NM, Lai FA, Meissner G, MacLennan DH.; ''Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+ release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum.''; PubMed Europe PMC Scholia
  24. Maeda M, Oshiman K, Tamura S, Futai M.; ''Human gastric (H+ + K+)-ATPase gene. Similarity to (Na+ + K+)-ATPase genes in exon/intron organization but difference in control region.''; PubMed Europe PMC Scholia
  25. Borsani G, Rugarli EI, Taglialatela M, Wong C, Ballabio A.; ''Characterization of a human and murine gene (CLCN3) sharing similarities to voltage-gated chloride channels and to a yeast integral membrane protein.''; PubMed Europe PMC Scholia
  26. Lu B, Zhang Q, Wang H, Wang Y, Nakayama M, Ren D.; ''Extracellular calcium controls background current and neuronal excitability via an UNC79-UNC80-NALCN cation channel complex.''; PubMed Europe PMC Scholia
  27. Farr TJ, Coddington-Lawson SJ, Snyder PM, McDonald FJ.; ''Human Nedd4 interacts with the human epithelial Na+ channel: WW3 but not WW1 binds to Na+-channel subunits.''; PubMed Europe PMC Scholia
  28. Sun H, Tsunenari T, Yau KW, Nathans J.; ''The vitelliform macular dystrophy protein defines a new family of chloride channels.''; PubMed Europe PMC Scholia
  29. Zdebik AA, Zifarelli G, Bergsdorf EY, Soliani P, Scheel O, Jentsch TJ, Pusch M.; ''Determinants of anion-proton coupling in mammalian endosomal CLC proteins.''; PubMed Europe PMC Scholia
  30. Niemeyer MI, Cid LP, Yusef YR, Briones R, Sepúlveda FV.; ''Voltage-dependent and -independent titration of specific residues accounts for complex gating of a ClC chloride channel by extracellular protons.''; PubMed Europe PMC Scholia
  31. Staub O, Abriel H, Plant P, Ishikawa T, Kanelis V, Saleki R, Horisberger JD, Schild L, Rotin D.; ''Regulation of the epithelial Na+ channel by Nedd4 and ubiquitination.''; PubMed Europe PMC Scholia
  32. Griffiths TA, Mauk AG, MacGillivray RT.; ''Recombinant expression and functional characterization of human hephaestin: a multicopper oxidase with ferroxidase activity.''; PubMed Europe PMC Scholia
  33. Lu B, Su Y, Das S, Liu J, Xia J, Ren D.; ''The neuronal channel NALCN contributes resting sodium permeability and is required for normal respiratory rhythm.''; PubMed Europe PMC Scholia
  34. Pangrazio A, Pusch M, Caldana E, Frattini A, Lanino E, Tamhankar PM, Phadke S, Lopez AG, Orchard P, Mihci E, Abinun M, Wright M, Vettenranta K, Bariae I, Melis D, Tezcan I, Baumann C, Locatelli F, Zecca M, Horwitz E, Mansour LS, Van Roij M, Vezzoni P, Villa A, Sobacchi C.; ''Molecular and clinical heterogeneity in CLCN7-dependent osteopetrosis: report of 20 novel mutations.''; PubMed Europe PMC Scholia
  35. Grenningloh G, Schmieden V, Schofield PR, Seeburg PH, Siddique T, Mohandas TK, Becker CM, Betz H.; ''Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes.''; PubMed Europe PMC Scholia
  36. Taglicht D, Padan E, Schuldiner S.; ''Proton-sodium stoichiometry of NhaA, an electrogenic antiporter from Escherichia coli.''; PubMed Europe PMC Scholia
  37. Soundararajan R, Melters D, Shih IC, Wang J, Pearce D.; ''Epithelial sodium channel regulated by differential composition of a signaling complex.''; PubMed Europe PMC Scholia
  38. Yang YD, Cho H, Koo JY, Tak MH, Cho Y, Shim WS, Park SP, Lee J, Lee B, Kim BM, Raouf R, Shin YK, Oh U.; ''TMEM16A confers receptor-activated calcium-dependent chloride conductance.''; PubMed Europe PMC Scholia
  39. Kawasaki M, Fukuma T, Yamauchi K, Sakamoto H, Marumo F, Sasaki S.; ''Identification of an acid-activated Cl(-) channel from human skeletal muscles.''; PubMed Europe PMC Scholia
  40. Takeuchi Y, Uchida S, Marumo F, Sasaki S.; ''Cloning, tissue distribution, and intrarenal localization of ClC chloride channels in human kidney.''; PubMed Europe PMC Scholia
  41. Voilley N, de Weille J, Mamet J, Lazdunski M.; ''Nonsteroid anti-inflammatory drugs inhibit both the activity and the inflammation-induced expression of acid-sensing ion channels in nociceptors.''; PubMed Europe PMC Scholia
  42. Xiang M, Feng M, Muend S, Rao R.; ''A human Na+/H+ antiporter sharing evolutionary origins with bacterial NhaA may be a candidate gene for essential hypertension.''; PubMed Europe PMC Scholia
  43. Spamer C, Heilmann C, Gerok W.; ''Ca2+-activated ATPase in microsomes from human liver.''; PubMed Europe PMC Scholia
  44. West AP Jr, Giannetti AM, Herr AB, Bennett MJ, Nangiana JS, Pierce JR, Weiner LP, Snow PM, Bjorkman PJ.; ''Mutational analysis of the transferrin receptor reveals overlapping HFE and transferrin binding sites.''; PubMed Europe PMC Scholia
  45. Bokkala S, el-Daher SS, Kakkar VV, Wuytack F, Authi KS.; ''Localization and identification of Ca2+ATPases in highly purified human platelet plasma and intracellular membranes. Evidence that the monoclonal antibody PL/IM 430 recognizes the SERCA 3 Ca2+ATPase in human platelets.''; PubMed Europe PMC Scholia
  46. Harrison PM, Arosio P.; ''The ferritins: molecular properties, iron storage function and cellular regulation.''; PubMed Europe PMC Scholia
  47. Scudieri P, Sondo E, Ferrera L, Galietta LJ.; ''The anoctamin family: TMEM16A and TMEM16B as calcium-activated chloride channels.''; PubMed Europe PMC Scholia
  48. Petrukhin K, Koisti MJ, Bakall B, Li W, Xie G, Marknell T, Sandgren O, Forsman K, Holmgren G, Andreasson S, Vujic M, Bergen AA, McGarty-Dugan V, Figueroa D, Austin CP, Metzker ML, Caskey CT, Wadelius C.; ''Identification of the gene responsible for Best macular dystrophy.''; PubMed Europe PMC Scholia
  49. Graves AR, Curran PK, Smith CL, Mindell JA.; ''The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes.''; PubMed Europe PMC Scholia
  50. Brailoiu E, Churamani D, Cai X, Schrlau MG, Brailoiu GC, Gao X, Hooper R, Boulware MJ, Dun NJ, Marchant JS, Patel S.; ''Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling.''; PubMed Europe PMC Scholia
  51. Hower V, Mendes P, Torti FM, Laubenbacher R, Akman S, Shulaev V, Torti SV.; ''A general map of iron metabolism and tissue-specific subnetworks.''; PubMed Europe PMC Scholia
  52. Ishibashi K, Marumo F.; ''Molecular cloning of a DEG/ENaC sodium channel cDNA from human testis.''; PubMed Europe PMC Scholia
  53. Zhang W, Mojsilovic-Petrovic J, Andrade MF, Zhang H, Ball M, Stanimirovic DB.; ''The expression and functional characterization of ABCG2 in brain endothelial cells and vessels.''; PubMed Europe PMC Scholia
  54. Jutabha P, Anzai N, Kitamura K, Taniguchi A, Kaneko S, Yan K, Yamada H, Shimada H, Kimura T, Katada T, Fukutomi T, Tomita K, Urano W, Yamanaka H, Seki G, Fujita T, Moriyama Y, Yamada A, Uchida S, Wempe MF, Endou H, Sakurai H.; ''Human sodium phosphate transporter 4 (hNPT4/SLC17A3) as a common renal secretory pathway for drugs and urate.''; PubMed Europe PMC Scholia
  55. Pangrazio A, Poliani PL, Megarbane A, Lefranc G, Lanino E, Di Rocco M, Rucci F, Lucchini F, Ravanini M, Facchetti F, Abinun M, Vezzoni P, Villa A, Frattini A.; ''Mutations in OSTM1 (grey lethal) define a particularly severe form of autosomal recessive osteopetrosis with neural involvement.''; PubMed Europe PMC Scholia
  56. Fujii J, Willard HF, MacLennan DH.; ''Characterization and localization to human chromosome 1 of human fast-twitch skeletal muscle calsequestrin gene.''; PubMed Europe PMC Scholia
  57. Verma AK, Filoteo AG, Stanford DR, Wieben ED, Penniston JT, Strehler EE, Fischer R, Heim R, Vogel G, Mathews S.; ''Complete primary structure of a human plasma membrane Ca2+ pump.''; PubMed Europe PMC Scholia
  58. Handford CA, Lynch JW, Baker E, Webb GC, Ford JH, Sutherland GR, Schofield PR.; ''The human glycine receptor beta subunit: primary structure, functional characterisation and chromosomal localisation of the human and murine genes.''; PubMed Europe PMC Scholia
  59. Steinmeyer K, Lorenz C, Pusch M, Koch MC, Jentsch TJ.; ''Multimeric structure of ClC-1 chloride channel revealed by mutations in dominant myotonia congenita (Thomsen).''; PubMed Europe PMC Scholia
  60. Taske NL, Eyre HJ, O'Brien RO, Sutherland GR, Denborough MA, Foster PS.; ''Molecular cloning of the cDNA encoding human skeletal muscle triadin and its localisation to chromosome 6q22-6q23.''; PubMed Europe PMC Scholia
  61. Fischer M, Janssen AG, Fahlke C.; ''Barttin activates ClC-K channel function by modulating gating.''; PubMed Europe PMC Scholia
  62. Ambrosini L, Mercer JF.; ''Defective copper-induced trafficking and localization of the Menkes protein in patients with mild and copper-treated classical Menkes disease.''; PubMed Europe PMC Scholia
  63. Adachi K, Oiwa K, Nishizaka T, Furuike S, Noji H, Itoh H, Yoshida M, Kinosita K Jr.; ''Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation.''; PubMed Europe PMC Scholia
  64. Lane LK, Shull MM, Whitmer KR, Lingrel JB.; ''Characterization of two genes for the human Na,K-ATPase beta subunit.''; PubMed Europe PMC Scholia
  65. Meyer-Kleine C, Steinmeyer K, Ricker K, Jentsch TJ, Koch MC.; ''Spectrum of mutations in the major human skeletal muscle chloride channel gene (CLCN1) leading to myotonia.''; PubMed Europe PMC Scholia
  66. Schaefer L, Sakai H, Mattei M, Lazdunski M, Lingueglia E.; ''Molecular cloning, functional expression and chromosomal localization of an amiloride-sensitive Na(+) channel from human small intestine.''; PubMed Europe PMC Scholia
  67. Nikolic Z, Laube B, Weber RG, Lichter P, Kioschis P, Poustka A, Mülhardt C, Becker CM.; ''The human glycine receptor subunit alpha3. Glra3 gene structure, chromosomal localization, and functional characterization of alternative transcripts.''; PubMed Europe PMC Scholia
  68. Wally J, Halbrooks PJ, Vonrhein C, Rould MA, Everse SJ, Mason AB, Buchanan SK.; ''The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding.''; PubMed Europe PMC Scholia
  69. Suzuki M.; ''The Drosophila tweety family: molecular candidates for large-conductance Ca2+-activated Cl- channels.''; PubMed Europe PMC Scholia
  70. Sudbrak R, Brown J, Dobson-Stone C, Carter S, Ramser J, White J, Healy E, Dissanayake M, Larrègue M, Perrussel M, Lehrach H, Munro CS, Strachan T, Burge S, Hovnanian A, Monaco AP.; ''Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump.''; PubMed Europe PMC Scholia
  71. Garrett KM, Duman RS, Saito N, Blume AJ, Vitek MP, Tallman JF.; ''Isolation of a cDNA clone for the alpha subunit of the human GABA-A receptor.''; PubMed Europe PMC Scholia
  72. Thomas GR, Forbes JR, Roberts EA, Walshe JM, Cox DW.; ''The Wilson disease gene: spectrum of mutations and their consequences.''; PubMed Europe PMC Scholia
  73. Nakashima Y, Nishimura S, Maeda A, Barsoumian EL, Hakamata Y, Nakai J, Allen PD, Imoto K, Kita T.; ''Molecular cloning and characterization of a human brain ryanodine receptor.''; PubMed Europe PMC Scholia
  74. Kim E, Youn B, Kemper L, Campbell C, Milting H, Varsanyi M, Kang C.; ''Characterization of human cardiac calsequestrin and its deleterious mutants.''; PubMed Europe PMC Scholia
  75. Marquardt A, Stöhr H, Passmore LA, Krämer F, Rivera A, Weber BH.; ''Mutations in a novel gene, VMD2, encoding a protein of unknown properties cause juvenile-onset vitelliform macular dystrophy (Best's disease).''; PubMed Europe PMC Scholia
  76. García-Añoveros J, Derfler B, Neville-Golden J, Hyman BT, Corey DP.; ''BNaC1 and BNaC2 constitute a new family of human neuronal sodium channels related to degenerins and epithelial sodium channels.''; PubMed Europe PMC Scholia
  77. Ye G, Chen C, Han D, Xiong X, Kong Y, Wan B, Yu L.; ''Cloning of a novel human NHEDC1 (Na+/H+ exchanger like domain containing 1) gene expressed specifically in testis.''; PubMed Europe PMC Scholia
  78. Dulhunty AF, Pouliquin P, Coggan M, Gage PW, Board PG.; ''A recently identified member of the glutathione transferase structural family modifies cardiac RyR2 substate activity, coupled gating and activation by Ca2+ and ATP.''; PubMed Europe PMC Scholia
  79. Frattini A, Pangrazio A, Susani L, Sobacchi C, Mirolo M, Abinun M, Andolina M, Flanagan A, Horwitz EM, Mihci E, Notarangelo LD, Ramenghi U, Teti A, Van Hove J, Vujic D, Young T, Albertini A, Orchard PJ, Vezzoni P, Villa A.; ''Chloride channel ClCN7 mutations are responsible for severe recessive, dominant, and intermediate osteopetrosis.''; PubMed Europe PMC Scholia
  80. Schatzmann HJ.; ''ATP-dependent Ca++-extrusion from human red cells.''; PubMed Europe PMC Scholia
  81. Turi JL, Wang X, McKie AT, Nozik-Grayck E, Mamo LB, Crissman K, Piantadosi CA, Ghio AJ.; ''Duodenal cytochrome b: a novel ferrireductase in airway epithelial cells.''; PubMed Europe PMC Scholia
  82. Swoboda KJ, Kanavakis E, Xaidara A, Johnson JE, Leppert MF, Schlesinger-Massart MB, Ptacek LJ, Silver K, Youroukos S.; ''Alternating hemiplegia of childhood or familial hemiplegic migraine? A novel ATP1A2 mutation.''; PubMed Europe PMC Scholia
  83. Neagoe I, Stauber T, Fidzinski P, Bergsdorf EY, Jentsch TJ.; ''The late endosomal ClC-6 mediates proton/chloride countertransport in heterologous plasma membrane expression.''; PubMed Europe PMC Scholia
  84. Yang W, Drewe JA, Lan NC.; ''Cloning and characterization of the human GABAA receptor alpha 4 subunit: identification of a unique diazepam-insensitive binding site.''; PubMed Europe PMC Scholia
  85. Kieferle S, Fong P, Bens M, Vandewalle A, Jentsch TJ.; ''Two highly homologous members of the ClC chloride channel family in both rat and human kidney.''; PubMed Europe PMC Scholia
  86. Cid LP, Montrose-Rafizadeh C, Smith DI, Guggino WB, Cutting GR.; ''Cloning of a putative human voltage-gated chloride channel (CIC-2) cDNA widely expressed in human tissues.''; PubMed Europe PMC Scholia
  87. de Carvalho Aguiar P, Sweadner KJ, Penniston JT, Zaremba J, Liu L, Caton M, Linazasoro G, Borg M, Tijssen MA, Bressman SB, Dobyns WB, Brashear A, Ozelius LJ.; ''Mutations in the Na+/K+ -ATPase alpha3 gene ATP1A3 are associated with rapid-onset dystonia parkinsonism.''; PubMed Europe PMC Scholia
  88. Quigley JG, Yang Z, Worthington MT, Phillips JD, Sabo KM, Sabath DE, Berg CL, Sassa S, Wood BL, Abkowitz JL.; ''Identification of a human heme exporter that is essential for erythropoiesis.''; PubMed Europe PMC Scholia
  89. Scholl U, Hebeisen S, Janssen AG, Müller-Newen G, Alekov A, Fahlke C.; ''Barttin modulates trafficking and function of ClC-K channels.''; PubMed Europe PMC Scholia
  90. Donier E, Rugiero F, Jacob C, Wood JN.; ''Regulation of ASIC activity by ASIC4--new insights into ASIC channel function revealed by a yeast two-hybrid assay.''; PubMed Europe PMC Scholia
  91. Schofield PR, Pritchett DB, Sontheimer H, Kettenmann H, Seeburg PH.; ''Sequence and expression of human GABAA receptor alpha 1 and beta 1 subunits.''; PubMed Europe PMC Scholia
  92. Oakhill JS, Marritt SJ, Gareta EG, Cammack R, McKie AT.; ''Functional characterization of human duodenal cytochrome b (Cybrd1): Redox properties in relation to iron and ascorbate metabolism.''; PubMed Europe PMC Scholia
  93. Qu Z, Hartzell HC.; ''Bestrophin Cl- channels are highly permeable to HCO3-.''; PubMed Europe PMC Scholia
  94. Leisle L, Ludwig CF, Wagner FA, Jentsch TJ, Stauber T.; ''ClC-7 is a slowly voltage-gated 2Cl(-)/1H(+)-exchanger and requires Ostm1 for transport activity.''; PubMed Europe PMC Scholia
  95. Richardson DR, Lane DJ, Becker EM, Huang ML, Whitnall M, Suryo Rahmanto Y, Sheftel AD, Ponka P.; ''Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol.''; PubMed Europe PMC Scholia
  96. Hadingham KL, Garrett EM, Wafford KA, Bain C, Heavens RP, Sirinathsinghji DJ, Whiting PJ.; ''Cloning of cDNAs encoding the human gamma-aminobutyric acid type A receptor alpha 6 subunit and characterization of the pharmacology of alpha 6-containing receptors.''; PubMed Europe PMC Scholia
  97. Keryanov S, Gardner KL.; ''Physical mapping and characterization of the human Na,K-ATPase isoform, ATP1A4.''; PubMed Europe PMC Scholia
  98. Bull PC, Thomas GR, Rommens JM, Forbes JR, Cox DW.; ''The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene.''; PubMed Europe PMC Scholia
  99. Vanmolkot KR, Kors EE, Hottenga JJ, Terwindt GM, Haan J, Hoefnagels WA, Black DF, Sandkuijl LA, Frants RR, Ferrari MD, van den Maagdenberg AM.; ''Novel mutations in the Na+, K+-ATPase pump gene ATP1A2 associated with familial hemiplegic migraine and benign familial infantile convulsions.''; PubMed Europe PMC Scholia
  100. Wagstaff J, Chaillet JR, Lalande M.; ''The GABAA receptor beta 3 subunit gene: characterization of a human cDNA from chromosome 15q11q13 and mapping to a region of conserved synteny on mouse chromosome 7.''; PubMed Europe PMC Scholia
  101. Suzuki M, Mizuno A.; ''A novel human Cl(-) channel family related to Drosophila flightless locus.''; PubMed Europe PMC Scholia
  102. 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.''; PubMed Europe PMC Scholia
  103. Petris MJ, Mercer JF.; ''The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal.''; PubMed Europe PMC Scholia
  104. Tandy S, Williams M, Leggett A, Lopez-Jimenez M, Dedes M, Ramesh B, Srai SK, Sharp P.; ''Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells.''; PubMed Europe PMC Scholia
  105. Vanoevelen J, Dode L, Van Baelen K, Fairclough RJ, Missiaen L, Raeymaekers L, Wuytack F.; ''The secretory pathway Ca2+/Mn2+-ATPase 2 is a Golgi-localized pump with high affinity for Ca2+ ions.''; PubMed Europe PMC Scholia
  106. Chelly J, Tümer Z, Tønnesen T, Petterson A, Ishikawa-Brush Y, Tommerup N, Horn N, Monaco AP.; ''Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein.''; PubMed Europe PMC Scholia
  107. Hadingham KL, Wingrove P, Le Bourdelles B, Palmer KJ, Ragan CI, Whiting PJ.; ''Cloning of cDNA sequences encoding human alpha 2 and alpha 3 gamma-aminobutyric acidA receptor subunits and characterization of the benzodiazepine pharmacology of recombinant alpha 1-, alpha 2-, alpha 3-, and alpha 5-containing human gamma-aminobutyric acidA receptors.''; PubMed Europe PMC Scholia
  108. de Weille JR, Bassilana F, Lazdunski M, Waldmann R.; ''Identification, functional expression and chromosomal localisation of a sustained human proton-gated cation channel.''; PubMed Europe PMC Scholia
  109. Niesler B, Walstab J, Combrink S, Möller D, Kapeller J, Rietdorf J, Bönisch H, Göthert M, Rappold G, Brüss M.; ''Characterization of the novel human serotonin receptor subunits 5-HT3C,5-HT3D, and 5-HT3E.''; PubMed Europe PMC Scholia
  110. Calcraft PJ, Ruas M, Pan Z, Cheng X, Arredouani A, Hao X, Tang J, Rietdorf K, Teboul L, Chuang KT, Lin P, Xiao R, Wang C, Zhu Y, Lin Y, Wyatt CN, Parrington J, Ma J, Evans AM, Galione A, Zhu MX.; ''NAADP mobilizes calcium from acidic organelles through two-pore channels.''; PubMed Europe PMC Scholia
  111. Willingham MC, Hanover JA, Dickson RB, Pastan I.; ''Morphologic characterization of the pathway of transferrin endocytosis and recycling in human KB cells.''; PubMed Europe PMC Scholia
  112. Miyake A, Mochizuki S, Takemoto Y, Akuzawa S.; ''Molecular cloning of human 5-hydroxytryptamine3 receptor: heterogeneity in distribution and function among species.''; PubMed Europe PMC Scholia
  113. Shull MM, Pugh DG, Lingrel JB.; ''Characterization of the human Na,K-ATPase alpha 2 gene and identification of intragenic restriction fragment length polymorphisms.''; PubMed Europe PMC Scholia
  114. Meij IC, Koenderink JB, van Bokhoven H, Assink KF, Groenestege WT, de Pont JJ, Bindels RJ, Monnens LA, van den Heuvel LP, Knoers NV.; ''Dominant isolated renal magnesium loss is caused by misrouting of the Na(+),K(+)-ATPase gamma-subunit.''; PubMed Europe PMC Scholia
  115. Wang D, King SM, Quill TA, Doolittle LK, Garbers DL.; ''A new sperm-specific Na+/H+ exchanger required for sperm motility and fertility.''; PubMed Europe PMC Scholia
  116. Wingrove P, Hadingham K, Wafford K, Kemp JA, Ragan CI, Whiting P.; ''Cloning and expression of a cDNA encoding the human GABA-A receptor alpha 5 subunit.''; PubMed Europe PMC Scholia
  117. Schimanski LM, Drakesmith H, Merryweather-Clarke AT, Viprakasit V, Edwards JP, Sweetland E, Bastin JM, Cowley D, Chinthammitr Y, Robson KJ, Townsend AR.; ''In vitro functional analysis of human ferroportin (FPN) and hemochromatosis-associated FPN mutations.''; PubMed Europe PMC Scholia
  118. Hara-Chikuma M, Yang B, Sonawane ND, Sasaki S, Uchida S, Verkman AS.; ''ClC-3 chloride channels facilitate endosomal acidification and chloride accumulation.''; PubMed Europe PMC Scholia
  119. Cutting GR, Curristin S, Zoghbi H, O'Hara B, Seldin MF, Uhl GR.; ''Identification of a putative gamma-aminobutyric acid (GABA) receptor subunit rho2 cDNA and colocalization of the genes encoding rho2 (GABRR2) and rho1 (GABRR1) to human chromosome 6q14-q21 and mouse chromosome 4.''; PubMed Europe PMC Scholia
  120. Malik N, Canfield VA, Beckers MC, Gros P, Levenson R.; ''Identification of the mammalian Na,K-ATPase 3 subunit.''; PubMed Europe PMC Scholia
  121. Kawakami K, Ohta T, Nojima H, Nagano K.; ''Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence.''; PubMed Europe PMC Scholia
  122. Hu Z, Bonifas JM, Beech J, Bench G, Shigihara T, Ogawa H, Ikeda S, Mauro T, Epstein EH Jr.; ''Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease.''; PubMed Europe PMC Scholia
  123. Harding C, Heuser J, Stahl P.; ''Receptor-mediated endocytosis of transferrin and recycling of the transferrin receptor in rat reticulocytes.''; PubMed Europe PMC Scholia
  124. Sato M, Schilsky ML, Stockert RJ, Morell AG, Sternlieb I.; ''Detection of multiple forms of human ceruloplasmin. A novel Mr 200,000 form.''; PubMed Europe PMC Scholia
  125. Dong XP, Cheng X, Mills E, Delling M, Wang F, Kurz T, Xu H.; ''The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel.''; PubMed Europe PMC Scholia
  126. Krishnamurthy P, Ross DD, Nakanishi T, Bailey-Dell K, Zhou S, Mercer KE, Sarkadi B, Sorrentino BP, Schuetz JD.; ''The stem cell marker Bcrp/ABCG2 enhances hypoxic cell survival through interactions with heme.''; PubMed Europe PMC Scholia
  127. Birkenhäger R, Otto E, Schürmann MJ, Vollmer M, Ruf EM, Maier-Lutz I, Beekmann F, Fekete A, Omran H, Feldmann D, Milford DV, Jeck N, Konrad M, Landau D, Knoers NV, Antignac C, Sudbrak R, Kispert A, Hildebrandt F.; ''Mutation of BSND causes Bartter syndrome with sensorineural deafness and kidney failure.''; PubMed Europe PMC Scholia
  128. Ovchinnikov YuA, Monastyrskaya GS, Broude NE, Ushkaryov YuA, Melkov AM, Smirnov YuV, Malyshev IV, Allikmets RL, Kostina MB, Dulubova IE.; ''Family of human Na+, K+-ATPase genes. Structure of the gene for the catalytic subunit (alpha III-form) and its relationship with structural features of the protein.''; PubMed Europe PMC Scholia
  129. Texel SJ, Xu X, Harris ZL.; ''Ceruloplasmin in neurodegenerative diseases.''; PubMed Europe PMC Scholia
  130. Price MP, Snyder PM, Welsh MJ.; ''Cloning and expression of a novel human brain Na+ channel.''; PubMed Europe PMC Scholia
  131. Ma JY, Song YH, Sjöstrand SE, Rask L, Mårdh S.; ''cDNA cloning of the beta-subunit of the human gastric H,K-ATPase.''; PubMed Europe PMC Scholia
  132. Dierick HA, Adam AN, Escara-Wilke JF, Glover TW.; ''Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network.''; PubMed Europe PMC Scholia
  133. Schlingmann KP, Konrad M, Jeck N, Waldegger P, Reinalter SC, Holder M, Seyberth HW, Waldegger S.; ''Salt wasting and deafness resulting from mutations in two chloride channels.''; PubMed Europe PMC Scholia
  134. Melis D, Havelaar AC, Verbeek E, Smit GP, Benedetti A, Mancini GM, Verheijen F.; ''NPT4, a new microsomal phosphate transporter: mutation analysis in glycogen storage disease type Ic.''; PubMed Europe PMC Scholia
  135. Bailey ME, Albrecht BE, Johnson KJ, Darlison MG.; ''Genetic linkage and radiation hybrid mapping of the three human GABA(C) receptor rho subunit genes: GABRR1, GABRR2 and GABRR3.''; PubMed Europe PMC Scholia
  136. Campbell HD, Kamei M, Claudianos C, Woollatt E, Sutherland GR, Suzuki Y, Hida M, Sugano S, Young IG.; ''Human and mouse homologues of the Drosophila melanogaster tweety (tty) gene: a novel gene family encoding predicted transmembrane proteins.''; PubMed Europe PMC Scholia
  137. Ohgami RS, Campagna DR, Greer EL, Antiochos B, McDonald A, Chen J, Sharp JJ, Fujiwara Y, Barker JE, Fleming MD.; ''Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells.''; PubMed Europe PMC Scholia
  138. Heise CJ, Xu BE, Deaton SL, Cha SK, Cheng CJ, Earnest S, Sengupta S, Juang YC, Stippec S, Xu Y, Zhao Y, Huang CL, Cobb MH.; ''Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial sodium channel are regulated by multiple with no lysine (WNK) family members.''; PubMed Europe PMC Scholia
  139. Doyle L, Ross DD.; ''Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2).''; PubMed Europe PMC Scholia
  140. Zhu Y, Ripps H, Qian H.; ''A single amino acid in the second transmembrane domain of GABA rho receptors regulates channel conductance.''; PubMed Europe PMC Scholia
  141. Grishin AV, Sverdlov VE, Kostina MB, Modyanov NN.; ''Cloning and characterization of the entire cDNA encoded by ATP1AL1--a member of the human Na,K/H,K-ATPase gene family.''; PubMed Europe PMC Scholia
  142. Han O, Kim EY.; ''Colocalization of ferroportin-1 with hephaestin on the basolateral membrane of human intestinal absorptive cells.''; PubMed Europe PMC Scholia
  143. Hadingham KL, Wingrove PB, Wafford KA, Bain C, Kemp JA, Palmer KJ, Wilson AW, Wilcox AS, Sikela JM, Ragan CI.; ''Role of the beta subunit in determining the pharmacology of human gamma-aminobutyric acid type A receptors.''; PubMed Europe PMC Scholia
  144. Tsunenari T, Sun H, Williams J, Cahill H, Smallwood P, Yau KW, Nathans J.; ''Structure-function analysis of the bestrophin family of anion channels.''; PubMed Europe PMC Scholia
  145. Shayeghi M, Latunde-Dada GO, Oakhill JS, Laftah AH, Takeuchi K, Halliday N, Khan Y, Warley A, McCann FE, Hider RC, Frazer DM, Anderson GJ, Vulpe CD, Simpson RJ, McKie AT.; ''Identification of an intestinal heme transporter.''; PubMed Europe PMC Scholia
  146. Ohgami RS, Campagna DR, McDonald A, Fleming MD.; ''The Steap proteins are metalloreductases.''; PubMed Europe PMC Scholia
  147. Rey MA, Duffy SP, Brown JK, Kennedy JA, Dick JE, Dror Y, Tailor CS.; ''Enhanced alternative splicing of the FLVCR1 gene in Diamond Blackfan anemia disrupts FLVCR1 expression and function that are critical for erythropoiesis.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
102616view07:54, 13 January 2019EgonwCorrect Cu2+ ChEBI ID.
96436view07:52, 15 March 2018EgonwReplaced a secondary ChEBI identifier with a primary identifier.
93185view14:17, 2 August 2017DeSlSplit up the Na+/Li+ transport in separate metabolite nodes.
86959view13:27, 15 July 2016MkutmonOntology Term : 'iron transport pathway' added !
80817view15:27, 30 June 2015MkutmonNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
2GABRA:2GABRB:GABRG:GABAComplexREACT_26202 (Reactome)
5HT [extracellular region]MetaboliteCHEBI:28790 (ChEBI)
ABCG2 dimerComplexREACT_26835 (Reactome)
ABCG2ProteinENSBTAG00000017704 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9UNQ0
ACCN3ProteinENSBTAG00000007762 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9UHC3
ADPMetaboliteCHEBI:16761 (ChEBI)
AMPMetaboliteCHEBI:16027 (ChEBI)
ANOsProtein
APLsMetaboliteREACT_26259 (Reactome)
APLsMetaboliteREACT_26709 (Reactome)
ARHGEF9ProteinENSBTAG00000012729 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O43307
ASIC trimer:H+ComplexREACT_160877 (Reactome)
ASIC1ProteinENSBTAG00000000970 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P78348
ASIC2 [plasma membrane]Protein
ASIC4ProteinENSBTAG00000020537 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q96FT7
ASIC5ProteinENSBTAG00000044109 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9NY37
ATP12AProteinENSBTAG00000014486 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P54707
ATP1A1ProteinENSBTAG00000001246 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P05023
ATP1A2ProteinENSBTAG00000010551 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P50993
ATP1A3ProteinENSBTAG00000018635 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P13637
ATP1A4ProteinENSBTAG00000038523 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q13733
ATP1A:ATP1B:FXYDComplexREACT_26819 (Reactome)
ATP1B1ProteinENSBTAG00000002688 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P05026
ATP1B2ProteinENSBTAG00000013680 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P14415
ATP1B3ProteinENSBTAG00000014140 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P54709
ATP2A1-3REACT_24286 (Reactome)
ATP2A1-3REACT_26227 (Reactome)
ATP2B1-4REACT_24662 (Reactome)
ATP2C1/2:Mg2+ComplexREACT_27002 (Reactome)
ATP2C1ProteinENSBTAG00000011626 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P98194
ATP2C2ProteinENSBTAG00000000945 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O75185
ATP4A/12A:ATP4BComplexREACT_26485 (Reactome)
ATP4AProteinENSBTAG00000045598 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P20648
ATP4BProteinENSBTAG00000019961 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51164
ATP6V0A1ProteinENSBTAG00000019218 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q93050
ATP6V0A2ProteinENSBTAG00000007272 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9Y487
ATP6V0A4ProteinENSBTAG00000004263 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9HBG4
ATP6V0BProteinENSBTAG00000018889 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q99437
ATP6V0CProteinENSBTAG00000026428 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P27449
ATP6V0D1ProteinENSBTAG00000014553 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P61421
ATP6V0D2ProteinENSBTAG00000021092 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8N8Y2
ATP6V0E1ProteinENSBTAG00000015100 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O15342
ATP6V0E2ProteinENSBTAG00000006022 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8NHE4
ATP6V1AProteinENSBTAG00000002703 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P38606
ATP6V1B1ProteinENSBTAG00000010620 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P15313
ATP6V1B2ProteinENSBTAG00000018646 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P21281
ATP6V1C1ProteinENSBTAG00000013513 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P21283
ATP6V1C2ProteinENSBTAG00000001927 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8NEY4
ATP6V1DProteinENSBTAG00000016309 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9Y5K8
ATP6V1E1ProteinENSBTAG00000014238 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P36543
ATP6V1E2ProteinENSBTAG00000013734 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q96A05
ATP6V1F [cytosol]ProteinENSBTAG00000045497 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q16864
ATP6V1G1ProteinENSBTAG00000000203 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O75348
ATP6V1G2ProteinENSBTAG00000014491 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O95670
ATP6V1G3ProteinENSBTAG00000019890 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q96LB4
ATP6V1HProteinENSBTAG00000003450 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9UI12
ATP7AProteinENSBTAG00000010018 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q04656
ATP7BProteinENSBTAG00000010353 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P35670
ATPMetaboliteCHEBI:15422 (ChEBI)
BESTsProtein
BSNDProteinENSBTAG00000013241 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8WZ55
BVMetaboliteCHEBI:17033 (ChEBI)
CLCN1/2/KA/KBComplexREACT_161219 (Reactome)
CLCN1ProteinENSBTAG00000009182 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P35523
CLCN2ProteinENSBTAG00000012284 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51788
CLCN3ProteinENSBTAG00000020130 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51790
CLCN4/5/6Protein
CLCN7:OSTM1ComplexREACT_160803 (Reactome)
CLCN7ProteinENSBTAG00000015889 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51798
CLCNKA [plasma membrane]ProteinENSBTAG00000034674 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51800
CLCNKB [plasma membrane]ProteinENSBTAG00000034674 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51801
CLIC2ProteinENSBTAG00000010948 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O15247
COMetaboliteCHEBI:17245 (ChEBI)
CPProteinENSBTAG00000012164 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P00450
CYBRD1:HemeComplexREACT_25782 (Reactome)
CYBRD1ProteinENSBTAG00000007898 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q53TN4
Ca2+MetaboliteCHEBI:29108 (ChEBI)
Cl-MetaboliteCHEBI:17996 (ChEBI)
Cu2+ [extracellular region]MetaboliteCHEBI:29036 (ChEBI)
Cu2+ [plasma membrane]MetaboliteCHEBI:29036 (ChEBI)
Cu2+MetaboliteCHEBI:29036 (ChEBI)
FLVCR1ProteinENSBTAG00000015974 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9Y5Y0
FTH1(2-183) [cytosol]Protein
FTL [cytosol]ProteinENSBTAG00000019709 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02792
FXYD1ProteinENSBTAG00000017816 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O00168
FXYD2ProteinENSBTAG00000009828 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P54710
FXYD3ProteinENSBTAG00000040005 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q14802
FXYD4 [plasma membrane]Protein
FXYD6ProteinENSBTAG00000014354 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9H0Q3
FXYD7ProteinENSBTAG00000018326 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P58549
Fe2+MetaboliteCHEBI:18248 (ChEBI)
Fe3+ [endosome membrane]MetaboliteCHEBI:29034 (ChEBI)
Fe3+ [extracellular region]MetaboliteCHEBI:29034 (ChEBI)
Fe3+MetaboliteCHEBI:29034 (ChEBI)
FeHMMetaboliteCHEBI:36144 (ChEBI)
Ferritin ComplexComplexREACT_19855 (Reactome) The ferritin complex is an oligomer of 24 subunits with light and heavy chains. The major chain can be light or heavy, depending on the tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited. Iron metabolism provides a useful example of gene expression translational control. Increased iron levels stimulate the synthesis of the iron-binding protein, ferritin, without any corresponding increase in the amount of ferritin mRNA. The 5?-UTR of both ferritin heavy chain mRNA and light chain mRNA contain a single iron-response element (IRE), a specific cis-acting regulatory sequence which forms a hairpin structure.
GABA [extracellular region]MetaboliteCHEBI:16865 (ChEBI)
GABRA1ProteinENSBTAG00000030286 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P14867
GABRA2ProteinENSBTAG00000011817 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P47869
GABRA3ProteinENSBTAG00000006691 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P34903
GABRA4ProteinENSBTAG00000016645 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P48169
GABRA5ProteinENSBTAG00000003392 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P31644
GABRA6ProteinENSBTAG00000013262 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q16445
GABRB1ProteinENSBTAG00000017837 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P18505
GABRB2ProteinENSBTAG00000018585 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P47870
GABRB3ProteinENSBTAG00000013422 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P28472
GABRG2ProteinENSBTAG00000010251 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P18507
GABRG3 [plasma membrane]Protein
GABRR pentamer:GABAComplexREACT_26162 (Reactome)
GABRR1ProteinENSBTAG00000011672 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P24046
GABRR2ProteinENSBTAG00000018435 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P28476
GABRR3 [plasma membrane]Protein
GLRA:GLRB:GlyComplexREACT_26060 (Reactome)
GLRBProteinENSBTAG00000021764 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P48167
Gly [extracellular region]MetaboliteCHEBI:15428 (ChEBI)
H+ [extracellular region]MetaboliteCHEBI:15378 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HCO3-MetaboliteCHEBI:17544 (ChEBI)
HEPHProteinENSBTAG00000047416 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9BQS7
HMOX1/2REACT_22577 (Reactome)
HTR3:5HTComplexREACT_25951 (Reactome)
HTR3AProteinENSBTAG00000010791 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P46098
HTR3BProteinENSBTAG00000031330 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O95264
HTR3C [plasma membrane]Protein
HTR3DProteinENSBTAG00000039011 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q70Z44
HTR3EProteinENSBTAG00000040304 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:A5X5Y0
K+MetaboliteCHEBI:29103 (ChEBI)
Li+Metabolite28486 (PubChem-compound)
MCOLN1ProteinENSBTAG00000005592 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9GZU1
MTP1:CP:6Cu2+ComplexREACT_24142 (Reactome)
MTP1:HEPH:6Cu2+ComplexREACT_24553 (Reactome)
Mg2+ [Golgi membrane]MetaboliteCHEBI:18420 (ChEBI)
NAADPMetaboliteCHEBI:76072 (ChEBI)
NADP+MetaboliteCHEBI:18009 (ChEBI)
NADPHMetaboliteCHEBI:16474 (ChEBI)
NALCN:UNC79:UNC80ComplexREACT_161143 (Reactome)
NALCNProteinENSBTAG00000037786 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8IZF0
NEDD4LProteinENSBTAG00000005412 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q96PU5
NSAIDMetaboliteCHEBI:35475 (ChEBI)
Na+Metabolite923 (PubChem-compound)
Na+MetaboliteCHEBI:29101 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
OSTM1ProteinENSBTAG00000010134 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q86WC4
P-type ATPases type IVREACT_26376 (Reactome)
PPiMetaboliteCHEBI:29888 (ChEBI)
PiMetaboliteCHEBI:18367 (ChEBI)
RAF1:SGK:TSC22D3:WPPComplexREACT_160466 (Reactome)
RAF1ProteinENSBTAG00000045748 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P04049
RYR tetramer:CASQ polymer:TRDN:junctinComplexREACT_161358 (Reactome)
RYR1ProteinENSBTAG00000006999 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P21817
RYR2ProteinENSBTAG00000022886 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q92736
RYR3ProteinENSBTAG00000025642 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q15413
SCNN channelsComplexREACT_160382 (Reactome)
SCNN1AProteinENSBTAG00000002631 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P37088
SCNN1BProteinENSBTAG00000012290 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51168
SCNN1DProteinENSBTAG00000017674 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51172
SCNN1GProteinENSBTAG00000010163 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51170
SGK1ProteinENSBTAG00000004269 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O00141
SGK2ProteinENSBTAG00000021033 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9HBY8
SGK3 [cytosol]ProteinHomologyConvert: Multiple homologues found: En:ENSBTAG00000013284;En:ENSBTAG00000013284;
SLC11A2ProteinENSBTAG00000002355 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P49281
SLC17A3ProteinENSBTAG00000003797 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O00476
SLC40A1ProteinENSBTAG00000010498 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9NP59
SLC46A1ProteinENSBTAG00000002817 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q96NT5
SLC9B1/C2Protein
SLC9B2ProteinENSBTAG00000040088 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q86UD5
SLC9C1ProteinENSBTAG00000019332 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q4G0N8
STEAP3ProteinENSBTAG00000007111 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q658P3
TCIRG1ProteinENSBTAG00000000292 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q13488
TF:TFRC dimerComplexREACT_26824 (Reactome)
TF:TFRCComplexREACT_25753 (Reactome)
TFProteinENSBTAG00000007273 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02787
TFRC dimerComplexREACT_26822 (Reactome)
TFRCProteinENSBTAG00000032719 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02786
TPCN1/2Protein
TRDNProteinENSBTAG00000038849 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q13061
TSC22D3ProteinENSBTAG00000045877 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q99576
TTYH1-3Protein
TTYH2/3Protein
UNC79ProteinENSBTAG00000008017 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9P2D8
UNC80ProteinENSBTAG00000015415 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8N2C7
UbProtein
Ub-SCNN channelsComplexREACT_161185 (Reactome)
UrateMetaboliteCHEBI:17775 (ChEBI)
V-ATPaseComplexREACT_24332 (Reactome)
WNKsProtein
WWP1ProteinENSBTAG00000015720 (Ensembl) HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9H0M0
amilorideMetaboliteCHEBI:2639 (ChEBI)
e-MetaboliteCHEBI:10545 (ChEBI)
heme [plasma membrane]MetaboliteCHEBI:17627 (ChEBI)
hemeMetaboliteCHEBI:17627 (ChEBI)
holoTF:TFRC dimerComplexREACT_26531 (Reactome)
holoTF:TFRCComplexREACT_26372 (Reactome)
holoTFComplexREACT_26297 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
2GABRA:2GABRB:GABRG:GABAmim-catalysisREACT_25130 (Reactome)
ABCG2 dimermim-catalysisREACT_25155 (Reactome)
ADPArrowREACT_115892 (Reactome)
ADPArrowREACT_24963 (Reactome)
ADPArrowREACT_24989 (Reactome)
ADPArrowREACT_25071 (Reactome)
ADPArrowREACT_25155 (Reactome)
ADPArrowREACT_25173 (Reactome)
ADPArrowREACT_25268 (Reactome)
ADPArrowREACT_25287 (Reactome)
ADPArrowREACT_25301 (Reactome)
AMPArrowREACT_160256 (Reactome)
ANOsmim-catalysisREACT_160277 (Reactome)
APLsArrowREACT_115892 (Reactome)
APLsArrowREACT_24989 (Reactome)
APLsREACT_115892 (Reactome)
APLsREACT_24989 (Reactome)
ASIC trimer:H+mim-catalysisREACT_160227 (Reactome)
ASIC4TBarREACT_160227 (Reactome)
ATP1A:ATP1B:FXYDmim-catalysisREACT_25287 (Reactome)
ATP2A1-3mim-catalysisREACT_23784 (Reactome)
ATP2A1-3mim-catalysisREACT_25316 (Reactome)
ATP2B1-4mim-catalysisREACT_23956 (Reactome)
ATP2C1/2:Mg2+mim-catalysisREACT_25301 (Reactome)
ATP4A/12A:ATP4Bmim-catalysisREACT_25173 (Reactome)
ATP7Amim-catalysisREACT_25071 (Reactome)
ATP7Bmim-catalysisREACT_24963 (Reactome)
ATPArrowREACT_160216 (Reactome)
ATPREACT_115892 (Reactome)
ATPREACT_160256 (Reactome)
ATPREACT_24963 (Reactome)
ATPREACT_24989 (Reactome)
ATPREACT_25071 (Reactome)
ATPREACT_25155 (Reactome)
ATPREACT_25173 (Reactome)
ATPREACT_25268 (Reactome)
ATPREACT_25287 (Reactome)
ATPREACT_25301 (Reactome)
BESTsmim-catalysisREACT_160081 (Reactome)
BESTsmim-catalysisREACT_160220 (Reactome)
BVArrowREACT_22100 (Reactome)
CLCN1/2/KA/KBmim-catalysisREACT_160109 (Reactome)
CLCN3mim-catalysisREACT_160116 (Reactome)
CLCN4/5/6mim-catalysisREACT_160268 (Reactome)
CLCN7:OSTM1mim-catalysisREACT_160230 (Reactome)
CLIC2TBarREACT_160216 (Reactome)
COArrowREACT_22100 (Reactome)
CYBRD1:Hememim-catalysisREACT_25114 (Reactome)
Ca2+ArrowREACT_160216 (Reactome)
Ca2+ArrowREACT_160220 (Reactome)
Ca2+ArrowREACT_160263 (Reactome)
Ca2+ArrowREACT_160271 (Reactome)
Ca2+ArrowREACT_160277 (Reactome)
Ca2+ArrowREACT_23784 (Reactome)
Ca2+ArrowREACT_23956 (Reactome)
Ca2+ArrowREACT_25246 (Reactome)
Ca2+ArrowREACT_25301 (Reactome)
Ca2+ArrowREACT_25316 (Reactome)
Ca2+REACT_160216 (Reactome)
Ca2+REACT_160271 (Reactome)
Ca2+REACT_23784 (Reactome)
Ca2+REACT_23956 (Reactome)
Ca2+REACT_25246 (Reactome)
Ca2+REACT_25301 (Reactome)
Ca2+REACT_25316 (Reactome)
Ca2+TBarREACT_160155 (Reactome)
Cl-ArrowREACT_160109 (Reactome)
Cl-ArrowREACT_160116 (Reactome)
Cl-ArrowREACT_160181 (Reactome)
Cl-ArrowREACT_160220 (Reactome)
Cl-ArrowREACT_160230 (Reactome)
Cl-ArrowREACT_160263 (Reactome)
Cl-ArrowREACT_160268 (Reactome)
Cl-ArrowREACT_160277 (Reactome)
Cl-ArrowREACT_25130 (Reactome)
Cl-ArrowREACT_25304 (Reactome)
Cl-ArrowREACT_25391 (Reactome)
Cl-REACT_160109 (Reactome)
Cl-REACT_160116 (Reactome)
Cl-REACT_160181 (Reactome)
Cl-REACT_160220 (Reactome)
Cl-REACT_160230 (Reactome)
Cl-REACT_160263 (Reactome)
Cl-REACT_160268 (Reactome)
Cl-REACT_160277 (Reactome)
Cl-REACT_25130 (Reactome)
Cl-REACT_25304 (Reactome)
Cl-REACT_25391 (Reactome)
Cu2+ArrowREACT_24963 (Reactome)
Cu2+ArrowREACT_25071 (Reactome)
Cu2+REACT_24963 (Reactome)
Cu2+REACT_25071 (Reactome)
FLVCR1mim-catalysisREACT_25203 (Reactome)
Fe2+ArrowREACT_20526 (Reactome)
Fe2+ArrowREACT_22100 (Reactome)
Fe2+ArrowREACT_23996 (Reactome)
Fe2+ArrowREACT_24919 (Reactome)
Fe2+ArrowREACT_25069 (Reactome)
Fe2+ArrowREACT_25114 (Reactome)
Fe2+REACT_115629 (Reactome)
Fe2+REACT_20526 (Reactome)
Fe2+REACT_23996 (Reactome)
Fe2+REACT_25069 (Reactome)
Fe2+REACT_25098 (Reactome)
Fe2+REACT_25198 (Reactome)
Fe3+ArrowREACT_115629 (Reactome)
Fe3+ArrowREACT_20531 (Reactome)
Fe3+ArrowREACT_25098 (Reactome)
Fe3+ArrowREACT_25198 (Reactome)
Fe3+ArrowREACT_25277 (Reactome)
Fe3+REACT_20531 (Reactome)
Fe3+REACT_24919 (Reactome)
Fe3+REACT_25114 (Reactome)
Fe3+REACT_25385 (Reactome)
FeHMArrowREACT_25025 (Reactome)
FeHMREACT_25025 (Reactome)
Ferritin Complexmim-catalysisREACT_115629 (Reactome)
GABRR pentamer:GABAmim-catalysisREACT_25391 (Reactome)
GLRA:GLRB:Glymim-catalysisREACT_25304 (Reactome)
H+ArrowREACT_160116 (Reactome)
H+ArrowREACT_160226 (Reactome)
H+ArrowREACT_160230 (Reactome)
H+ArrowREACT_160252 (Reactome)
H+ArrowREACT_160268 (Reactome)
H+ArrowREACT_160312 (Reactome)
H+ArrowREACT_20526 (Reactome)
H+ArrowREACT_23784 (Reactome)
H+ArrowREACT_25173 (Reactome)
H+ArrowREACT_25268 (Reactome)
H+ArrowREACT_25316 (Reactome)
H+REACT_115629 (Reactome)
H+REACT_160116 (Reactome)
H+REACT_160226 (Reactome)
H+REACT_160230 (Reactome)
H+REACT_160252 (Reactome)
H+REACT_160268 (Reactome)
H+REACT_160312 (Reactome)
H+REACT_20526 (Reactome)
H+REACT_23784 (Reactome)
H+REACT_25098 (Reactome)
H+REACT_25173 (Reactome)
H+REACT_25198 (Reactome)
H+REACT_25268 (Reactome)
H+REACT_25316 (Reactome)
H2OArrowREACT_115629 (Reactome)
H2OArrowREACT_22100 (Reactome)
H2OArrowREACT_25098 (Reactome)
H2OArrowREACT_25198 (Reactome)
H2OREACT_115892 (Reactome)
H2OREACT_24963 (Reactome)
H2OREACT_24989 (Reactome)
H2OREACT_25071 (Reactome)
H2OREACT_25155 (Reactome)
H2OREACT_25173 (Reactome)
H2OREACT_25268 (Reactome)
H2OREACT_25287 (Reactome)
H2OREACT_25301 (Reactome)
HCO3-ArrowREACT_160081 (Reactome)
HCO3-REACT_160081 (Reactome)
HMOX1/2mim-catalysisREACT_22100 (Reactome)
HTR3:5HTmim-catalysisREACT_25246 (Reactome)
K+ArrowREACT_25173 (Reactome)
K+ArrowREACT_25246 (Reactome)
K+ArrowREACT_25287 (Reactome)
K+REACT_25173 (Reactome)
K+REACT_25246 (Reactome)
K+REACT_25287 (Reactome)
Li+ArrowREACT_160252 (Reactome)
Li+REACT_160252 (Reactome)
MCOLN1mim-catalysisREACT_25069 (Reactome)
MTP1:CP:6Cu2+mim-catalysisREACT_23996 (Reactome)
MTP1:CP:6Cu2+mim-catalysisREACT_25098 (Reactome)
MTP1:HEPH:6Cu2+mim-catalysisREACT_20531 (Reactome)
MTP1:HEPH:6Cu2+mim-catalysisREACT_25198 (Reactome)
NAADPArrowREACT_160271 (Reactome)
NADP+ArrowREACT_22100 (Reactome)
NADPHREACT_22100 (Reactome)
NALCN:UNC79:UNC80mim-catalysisREACT_160155 (Reactome)
NSAIDTBarREACT_160227 (Reactome)
Na+ArrowREACT_160084 (Reactome)
Na+ArrowREACT_160095 (Reactome)
Na+ArrowREACT_160155 (Reactome)
Na+ArrowREACT_160226 (Reactome)
Na+ArrowREACT_160227 (Reactome)
Na+ArrowREACT_160252 (Reactome)
Na+ArrowREACT_160312 (Reactome)
Na+ArrowREACT_25246 (Reactome)
Na+ArrowREACT_25287 (Reactome)
Na+REACT_160084 (Reactome)
Na+REACT_160095 (Reactome)
Na+REACT_160155 (Reactome)
Na+REACT_160226 (Reactome)
Na+REACT_160227 (Reactome)
Na+REACT_160252 (Reactome)
Na+REACT_160312 (Reactome)
Na+REACT_25246 (Reactome)
Na+REACT_25287 (Reactome)
O2REACT_115629 (Reactome)
O2REACT_22100 (Reactome)
O2REACT_25098 (Reactome)
O2REACT_25198 (Reactome)
P-type ATPases type IVmim-catalysisREACT_115892 (Reactome)
P-type ATPases type IVmim-catalysisREACT_24989 (Reactome)
PPiArrowREACT_160256 (Reactome)
PiArrowREACT_115892 (Reactome)
PiArrowREACT_160084 (Reactome)
PiArrowREACT_24963 (Reactome)
PiArrowREACT_24989 (Reactome)
PiArrowREACT_25071 (Reactome)
PiArrowREACT_25155 (Reactome)
PiArrowREACT_25173 (Reactome)
PiArrowREACT_25268 (Reactome)
PiArrowREACT_25287 (Reactome)
PiArrowREACT_25301 (Reactome)
PiREACT_160084 (Reactome)
RAF1:SGK:TSC22D3:WPPmim-catalysisREACT_160256 (Reactome)
REACT_115629 (Reactome) Ferritin oxidises Fe(II) ions to Fe(III), migrates them to its centre, and collects thousands of them as FeO(OH) in the central mineral core from which they can be later remobilised (Harrison & Arrosio 1996).
REACT_115892 (Reactome) The plasma membrane contains a broad range of lipids making up the bilayer. Aminophospholipids (APLs) such as phosphatidylserine (PS) and phosphatidylethanolamine (PE) are distributed in this bilayer and their arrangement is mediated by the P-type ATPases type IV family (Paulusma and Oude Elferink, 2005).
REACT_160081 (Reactome) Many Cl- channels such as CFTR, ClC, CaCC, and ligand-gated anion channels are permeable to bicarbonate (HCO3-) which is an important anion in the regulation of pH. Many tissues, including retinal pigment epithelium (RPE), utilize HCO3- transporters to mediate transport of HCO3-. Bestrophns 1-4 (BEST1-4, aka vitelliform macular dystrophy proteins) have high permeability to HCO3- (Hu & Hartzell 2008). Defective BEST1 may play a role in macular degeneration in the eye due to impaired HCO3- and Cl- conductance (Hu & Hartzell 2008).
REACT_160084 (Reactome) The microsomal Na+/(PO4)3- transporter isoform 1 (SLC17A3, NPT4 isoform 1) is a member of the anion-cation symporter family. It is expressed in liver, kidney and intestine and may function as a cotransporter of sodium (Na+) and phosphate ((PO4)3- or Pi) across the ER membrane (Melis et al. 2004).
REACT_160095 (Reactome) Amiloride-sensitive sodium channels (SCNNs, aka ENaCs, epithelial Na+ channels, non voltage-gated sodium channels) belong to the epithelial Na+ channel/degenerin (ENaC/DEG) protein family and mediate the transport of Na+ (and associated water) through the apical membrane of epithelial cells in kidney, colon and lungs. This makes SCNNs important determinants of systemic blood pressure. The physiological activator for SCNNs is unknown but as they belong in the same family as acid-sensitive ion channels (ASICs, which are mediated by protons), these may also be the activating ligands for SCNNs. SCNNs are probable heterotrimers comprising an alpha (or interchangeable delta subunit), beta and gamma subunit (Horisberger 1998).
REACT_160104 (Reactome) Human serum urate levels are largely maintained by its reabsorption and secretion in the kidney. Loss of this maintenance can elevate urate levels leading to gout, hypertension, and various cardiovascular diseases. Renal urate reabsorption is controlled via two proximal tubular urate transporters; apical SLC22A12 (URAT1) and basolateral SLC2A9 (URATv1, GLUT9). On the other hand, urate secretion is mediated by the orphan sodium phosphate transporter 4 isoform 2 (SLC17A3, NPT4 isoform 2). It is mainly expressed at the apical side of renal tubules and functions as a voltage-driven urate transporter (Jutabha et al. 2010).

Genetic variations in SLC17A3 influence the variance in serum uric acid concentrations and define the serum uric acid concentration quantitative trait locus 4 (UAQTL4; MIM:612671). Excess serum urate (hyperuricemia) can lead to the development of gout, characterized by tissue deposition of monosodium urate crystals.
REACT_160109 (Reactome) Chloride channel proteins 1, 2, Ka and Kb (CLCN1, 2, KA, KB) can mediate Cl- influx across the plasma membrane of almost all cells. CLCN1 is expressed mainly on skeletal muscle where it is involved in the electrical stability of the muscle. CLCN1 is thought to function in a homotetrameric form (Steimeyer et al. 1994). CLCN2 is ubiquitously expressed, playing a role in the regulation of cell volume (Cid et al. 1995, Niemeyer et al. 2009). Defects in CLCN1 cause myotonia congenita, an autosomal dominant disease (MCD aka Thomsen disease, MIM:160800). It is characterized by muscle stiffness due to delayed relaxation, resulting from membrane hyperexcitability (Meyer-Kleine et al. 1995, Steimeyer et al. 1994). Defects in CLCN1 also cause autosomal recessive myotonia congenita (MCR aka Becker disease, MIM:255700) (Koch et al. 1992, Meyer-Kleine et al. 1995), a nondystrophic skeletal muscle disorder characterized by muscle stiffness and an inability of the muscle to relax after voluntary contraction. Becker disease is more common and more severe than Thomsen disease.

CLCNKA and B (Kieferle et al. 1994) are predominantly expressed in distal nephron segments of the kidney (Takeuchi et al. 1995) and the inner ear (Estevez et al. 2001, Schlingmann et al. 2004). They are tightly associated with their essential beta subunit barttin (BSND), requiring it to be fully functional channels (Fischer et al. 2010, Scholl et al. 2006). These channels bound to BSND are essential for renal Cl- reabsorption (Waldegger & Jentsch 2000) and K+ recycling in the inner ear (Estevez et al. 2001). Defects in CLCNKA and B cause Bartter syndrome type 4B (BS4B; MIM:613090) characterized by impaired salt reabsorption and sensorineural deafness (Schlingmann et al. 2004, Nozu et al. 2008). Defects in BSND cause Bartter syndrome type 4A (BS4A aka infantile Bartter syndrome with sensorineural deafness; MIM:602522) characterized by impaired salt reabsorption in the thick ascending loop of Henle and sensorineural deafness (Birkenhager et al. 2001, Nozu et al. 2008).
REACT_160116 (Reactome) The H+/Cl- exchange transporter CLCN3 (Borsani et al. 1995) mediates the exchange of endosomal Cl- for cytosolic H+ across late endosomal membranes, contributing to the acidification of endosomes. The activity of CLCN3 is inferred from experiments in mice (Stobrawa et al. 2001, Hara-Chikuma et al. 2005).
REACT_160155 (Reactome) The sodium leak channel non-selective protein NALCN, a nonselective cation channel, forms the background Na+ leak conductance and controls neuronal excitability (Lu et al. 2007). Mice with mutant NALCN have a severely disrupted respiratory rhythm and die within 24 hours of birth. Calcium (Ca2+) influences neuronal excitability via the NALCN:UNC79:UNC80 complex, with high Ca2+ concentrations inhibiting transport of Na+ (Lu et al. 2010).
REACT_160181 (Reactome) Protein tweety homolog 1 (TTYH1) has 5 isoforms. Isoform 3 (Campbell et al. 2000) mediates the Ca+-independent efflux of Cl- across plasma membranes (Suzuki & Mizuno 2004, Suzuki 2006).
REACT_160216 (Reactome) Ryanodine receptors (RYRs) are located in the sarcoplasmic reticulum (SR) membrane and mediate the release of Ca2+ from intracellular stores during excitation-contraction (EC) coupling in both cardiac and skeletal muscle. RYRs are the largest known ion channels (>2MDa) and are functional in their homotetrameric forms. There are three mammalian isoforms (RYR1-3); RYR1 is prominent in skeletal muscle (Zorzato et al. 1990), RYR2 in cardiac muscle (Tunwell et al. 1996) and RYR3 is found in the brain (Nakashima et al. 1997). For review see Lanner et al. 2010. The function of RYRs are controlled by intracellular Ca2+-binding proteins calsequestrin 1 and 2 (CASQ1 and 2) and the anchoring proteins triadin (TRDN) and junctin. Together, they make up the Ca2+-release complex. CASQ1 and 2 buffer intra-SR Ca2+ stores in skeletal muscle and cardiac muscle respectively (Fujii et al. 1990, Kim et al. 2007). When Ca2+ concentrations reach 1mM, CASQs polymerize (Kim et al. 2007) and can attach to one end of RYRs, mediated by anchoring proteins TRDN and junctin (Taske et al. 1995). By sequestering Ca2+ ions, CASQs can inhibit RYRs function. For reviews see Beard et al. 2004, Beard et al. 2009a, Beard et al. 2009b.

A member of the intracellular Cl- channel protein family, CLIC2, has also been determined to inhibit RYR-mediated Ca2+ transport (Board et al. 2004), potentially playing a role in the homeostasis of Ca2+ release from intracellular stores. Inhibition is thought to be via reducing activation of the channels by their primary endogenous cytoplasmic ligands, ATP and Ca2+ (Dulhunty et al. 2005).
REACT_160220 (Reactome) Bestrophins 1-4 (BEST1-4, aka vitelliform macular dystrophy proteins) mediate cytosolic Cl- efflux across plasma membranes. This transport is sensitive to intracellular Ca2+ concentrations (Sun et al. 2002, Tsunenari et al. 2003). Mutations in bestrophins that impair their function are implicated in macular degeneration in the eye. Defects in BEST1 cause vitelliform macular dystrophy (BVMD, Best's disease, MIM:153700), an autosomal dominant form of macular degeneration that usually begins in childhood and is characterized lesions due to abnormal accumulation of lipofuscin within and beneath retinal pigment epithelium (RPE) cells (Marquardt et al. 1998, Petrukhin et al. 1998).
REACT_160226 (Reactome) The sperm-specific Na+/H+ exchanger SLC9C1 (aka sodium/hydrogen exchanger 10, NHE10) is localized to the flagellar membrane and is involved in pH regulation of spermatozoa required for sperm motility and fertility. The activity of human SLC9C1 is inferred from experiments using mouse Slc9c1 (Wang et al. 2003).
REACT_160227 (Reactome) Acid-sensing ion channels 1, 2, 3 and 5 (ASIC1, 2, 3 and 5, aka amiloride-sensitive cation channels) are homotrimeric, multi-pass membrane proteins which can transport sodium (Na+) when activated by extracellular protons. Members of the ASIC family are sensitive to amiloride and function in neurotransmission. The encoded proteins function in learning, pain transduction, touch sensation, and development of memory and fear. Many neuronal diseases cause acidosis, accompanied by pain and neuronal damage; ASICs can mediate the pathophysiological effects seen in acidiosis (Wang & Xu 2011, Qadri et al. 2012). The diuretic drug amiloride inhibits these channels, resulting in analgesic effects. NSAIDs (Nonsteroidal anti-inflammatory drugs) can also inhibit ASICs to produce analgesia (Voilley et al. 2001). ASICs are also partially permeable to Ca2+, Li+ and K+ (not shown here). ASIC1 and 2 are expressed mostly in brain (Garcia-Anoveros et al. 1997, Price et al. 1996), ASIC3 is strongly expressed in testis (de Weille et al. 1998, Ishibashi & Marumo 1998) and ASIC5 is found mainly in intestine (Schaefer et al. 2000). ASIC4 subunits do not form functional channels and it's activity is unknown. It could play a part in regulating other ASIC activity (Donier et al. 2008).
REACT_160230 (Reactome) Chloride channel 7 comprises H+/Cl- exchange transporter 7 (CLCN7) and osteopetrosis-associated transmembrane protein 1 (OSTM1) (Leisle et al. 2011). This complex localises to the lysosomal membrane where it mediates the exchange of Cl- and H+ ions, perhaps playing a role in the acidification of the lysosome (Graves et al. 2008).

Defects in CLCN7 cause osteopetrosis autosomal recessive types 2 and 4 (OPTB2, MIM:166600 and OPTB4, MIM:611490) (Frattini et al. 2003, Pangrazio et al. 2010). Defects in OSTM1 cause osteopetrosis autosomal recessive type 5 (OPTB5, MIM:259720) (Pangrazio et al. 2006).
REACT_160252 (Reactome) Mitochondrial sodium/hydrogen exchanger 9B2 (SLC9B2, aka NHA2) is ubiquitously expressed and mediates the electrogenic exchange of 1 Na+ (or 1 Li+) for 2 H+ across the inner mitochondrial membrane (Xiang et al. 2007, Taglicht et al. 1993). This transport is thought to play a role in salt homeostasis and pH regulation in humans.
REACT_160256 (Reactome) Amiloride-sensitive sodium channels (SCNNs, aka ENaCs, epithelial Na+ channels, non voltage-gated sodium channels) comprises three subunits (alpha, beta and gamma) and plays an essential role in Na+ and fluid absorption in the kidney, colon and lung. The number of channels at the cell's surface (consequently its function) can be regulated. This is achieved by ubiquitination of SCNN via E3 ubiquitin-protein ligases (NED4L and WPP1) (Staub et al. 2000, Farr et al. 2000). NED4L/WPP1 is found in a signaling complex including Raf1 (RAF proto-oncogene serine/threonine-protein kinase), SGK (serum/glucocorticoid-regulated kinase) and GILZ (glucocorticoid-induced leucine zipper protein, TSC22D3) (Soundararajan et al. 2009). Ubiquitinated SCNN (Ub-SCNN) is targeted for degradation so a lesser number of channels are present at the cell surface, reducing the amount of Na+ absorption. Proline-rich sequences at the C-terminus of SCNNs include the PY motif containing a PPxY sequence. PY motifs bind WW domains of NED4L/WPP1. Protein kinases with no lysine K (WNKs) can activate SCNN activity by interacting non-enzymatically with the signaling complex, specifically SGK although the mechanism is unknown (Heise et al. 2010).
REACT_160263 (Reactome) Human homologues 2 and 3 (TTYH2 and 3) mediate the efflux of Cl- from cells in response to the increase in intracellular Ca2+ levels (Suzuki & Mizuno 2004, Suzuki 2006).
REACT_160268 (Reactome) The H+/Cl- exchange transporters CLCN4 (Kawasaki et al. 1999, Zdebik et al. 2008), CLCN5 (Zdebik et al. 2008) and CLCN6 (Neagoe et al. 2010) mediate the exchange of endosomal Cl- for cytosolic H+ across endosomal membranes, contributing to the acidification of endosomes.
REACT_160271 (Reactome) Calcium (Ca2+) can be mobilised from intracellular stores by the presence of nicotinic acid adenine dinucleotide phosphate (NAADP). Two pore calcium channel proteins 1 and 2 (TPCN1 and 2) are expressed on endosomal (not shown here) and lysosomal membranes and mediate the mobilization of Ca2+ from these organelles when activated by NAADP (Brailoiu et al. 2009, Calcraft et al. 2009).
REACT_160277 (Reactome) Calcium-activated chloride channels (CaCCs) are ubiquitously expressed and implicated in physiological processes such as sensory transduction, fertilization, epithelial secretion, and smooth muscle contraction. The anoctamin family of transmembrane proteins (ANO, TMEM16) belong to CaCCs and have been shown to transport Cl- ions when activated by intracellular Ca2+ (Galietta 2009, Huang et al. 2012). There are currently 10 members, ANO1-10, all having a similar structure, with eight putative transmembrane domains and cytosolic amino- and carboxy-termini. ANO1 and 2 possess Ca2+ activated Cl- transport activity (Yang et al. 2008, Scudieri et al. 2012) while the remaining members also show some demonstrable activity (Tian et al. 2012).
REACT_160312 (Reactome) The sodium/hydrogen exchanger 9B1 (SLC9B1 aka Na+/H+ exchanger like domain containing 1, NHEDC1) is specifically expressed on the plasma membrane of the testis and may be implicated in infertility (Ye et al. 2006). Sodium/hydrogen exchanger 9C2 (SLC9C2), also localized to the plasma membrane, may be involved in pH regulation although this protein has not been fully characterized.
REACT_20526 (Reactome) The primary site for absorption of dietary iron is the duodenum. Ferrous iron (Fe2+) is taken up from the gut lumen across the apical membranes of enterocytes and released into the portal vein circulation across basolateral membranes.
The human gene SLC11A2 encodes the divalent cation transporter DCT1 (NRAMP2, Natural resistance-associated macrophage protein 2). NRAMP2 resides on the apical membrane of enterocytes and mediates the uptake of ferrous iron into these cells (Tandy S et al, 2000). DCT1 can also accept a broad range of transition metal ions.
REACT_20531 (Reactome) The primary site for absorption of dietary iron is the duodenum. Ferrous iron (Fe2+) is taken up from the gut lumen across the apical membranes of enterocytes and released into the portal vein circulation across basolateral membranes.
The human gene SLC40A1 encodes a metal transporter protein MTP1 (also called ferroportin or IREG1). This protein resides on the basolateral membrane of enterocytes and mediates ferrous iron efflux into the portal vein (Schimanski LM et al, 2005). MTP1 colocalizes with hephaestin (HEPH) which stablizes MTP1 and is necessary for the efflux reaction to occur (Han O and Kim EY, 2007; Chen H et al, 2009). As well as the dudenum, MTP1 is also highly expressed on macrophages (where it mediates iron efflux from the breakdown of haem) and the placenta (where it may mediate the transport of iron from maternal to foetal circulation). It is also expressed in muscle and spleen.
REACT_22100 (Reactome) Heme oxygenase (HO) cleaves the heme ring at the alpha-methene bridge to form bilverdin. This reaction forms the only endogenous source of carbon monoxide. HO-1 is inducible and is thought to have an antioxidant role as it's activated in virtually all cell types and by many types of "oxidative stress" (Poss and Tonegawa, 1997). HO-2 is non-inducible.
REACT_23784 (Reactome) Intracellular pools of Ca2+ serve as the source for inositol 1,4,5-trisphosphate (IP3) -induced alterations in cytoplasmic free Ca2+. In most human cells Ca2+ is stored in the lumen of the sarco/endoplastic reticulum by ATPases known as SERCAs (ATP2As). In platelets, ATP2As transport Ca2+ into the platelet dense tubular network. ATP2As are P-type ATPases, similar to the plasma membrane Na+ and Ca+-ATPases. Humans have three genes for SERCA pumps; ATP2A1-3. Studies on ATP2A1 suggest that it binds two Ca2+ ions from the cytoplasm and is subsequently phosphorylated at Asp351 before translocating Ca2+ into the SR lumen. There is a counter transport of two or possibly three protons ensuring partial charge balancing.
REACT_23956 (Reactome) The plasma membrane Ca-ATPases 1-4 (ATP2B1-4, PMCAs) are P-type Ca2+-ATPases regulated by calmodulin. The PMCA also counter-transports a proton. PMCA is important for Ca2+ homeostasis and function.
REACT_23996 (Reactome) MTP1 is also highly expressed on macrophages where it mediates iron efflux from the breakdown of haem.
The human gene SLC40A1 encodes a metal transporter protein MTP1 (also called ferroportin or IREG1) (Schimanski LM et al, 2005). MTP1 colocalizes with ceruloplasmin (CP) which stablizes MTP1 and is necessary for the efflux reaction to occur (Texel SJ et al, 2008). Ceruloplasmin also catalyzes the conversion of iron from ferrous (Fe2+) to ferric form (Fe3+), therefore assisting in its transport in the plasma in association with transferrin, which can only carry iron in the ferric state. As well as on macrophages, MTP1 is also highly expressed in the duodenum, placenta (where it may mediate the transport of iron from maternal to foetal circulation), in muscle and the spleen.
REACT_24919 (Reactome) The iron ions that are no longer bound to transferrin are reduced by the metalloreductase STEAP3, an endosomal membrane protein. The electron donor partner of the enzyme is unknown (Ohgami et al, 2005; Ohgami et al, 2006).
REACT_24927 (Reactome) After about 15 minutes on the cell surface, the equilibrium favors dissociation of transferrin, and the transferrin receptor 1 dimer is available again for binding (Hemadi et al., 2006).
REACT_24945 (Reactome) Transferrin receptor 1 molecules can be found on the outside of any cell. Transferrin transports two iron ions through the blood and two transferrins bind to a TfR1 dimer (West et al, 2001).
REACT_24963 (Reactome) The human gene ATP7B encodes the copper-transporting ATPase 2 (ATP7B, ATPase2, Wilson's protein) which is expressed mainly in the liver, brain and kidneys (Bull et al, 1993). ATP7B resides on the trans-Golgi membrane where it it thought to sequester copper from the cytosol into the golgi (Yang et al, 1997). Defects in ATP7B are the cause of Wilson disease (WD), an autosomal recessive disorder of copper metabolism characterized by the toxic accumulation of copper in a number of organs, particularly the liver and brain (Thomas et al, 1995).
REACT_24977 (Reactome) The transferrin/receptor complex is internalized as a clathrin-coated vesicle (Willingham et al, 1984; Harding et al, 1983).
REACT_24989 (Reactome) The plasma membrane contains a broad range of lipids making up the bilayer. Aminophospholipids such as phosphatidylserine (PS) and phosphatidylethanolamine (PE) are distributed in this bilayer and their arrangement is mediated by the P-type ATPases type IV family (Paulusma and Oude Elferink, 2005).
REACT_25025 (Reactome) Uptake of iron from meat happens in the form of ferriheme, and via the same transporter that is used for folate. The process is more effective than taking up iron ions (Shayeghi M et al, 2005).
REACT_25069 (Reactome) Mucolipin-1 is an iron ion channel specifically expressed in endosome and lysosome membranes. It catalyzes the diffusion of Fe2+ ions into the cytosol (Dong et al, 2008).
REACT_25071 (Reactome) The human gene ATP7A (MNK) encodes the copper-transporting ATPase 1 (ATP7A, ATPase1, Menkes protein) which is expressed in most tissues except the liver (Vulpe et al, 1993; Chelly et al, 1993). Normally, ATP7A resides on the trans-Golgi membrane (Dierick et al, 1997). When cells are exposed to excessive copper levels, it is rapidly relocalized to the plasma membrane where it functions in copper efflux (Petris and Mercer, 1999). Defects in ATP7A are the cause of Menkes disease (MNKD), an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency (Ambrosini and Mercer, 1999).
REACT_25098 (Reactome) In tissues other than the duodenum, ceruloplasmin oxidizes ferrous iron after it is exported from the cell (Sato et al, 1990).
REACT_25114 (Reactome) Cytochrome b reductase 1 not only reduces ferrous iron in the brush-border membrane but also in the airways. It is upregulated on iron starvation. However, its electron donor molecule is still unknown (Oakhill et al, 2007; Turi et al, 2006).
REACT_25130 (Reactome) The GABA(A) receptor (GABR) family belongs to the ligand-gated ion channel superfamily (LGIC). Its endogenous ligand is gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the central nervous system. There are six alpha subunits (GABRA) (Garrett et al. 1988, Schofield et al. 1989, Hadingham et al. 1993, Edenberg et al. 2004, Hadingham et al. 1993, Yang et al. 1995, Wingrove et al. 1992, Hadingham et al. 1996), three beta subunits (GABRB) (Schofield et al. 1989, Hadingham et al. 1993, Wagstaff et al. 1991) and 2 gamma subunits (GABRG) (Khan et al. 1993, Hadingham et al. 1995) characterized. GABA(A) functions as a heteropentamer, the most common structure being 2 alpha subunits, 2 beta subunits and a gamma subunit (2GABRA:2GABRB:GABRG). Upon binding of GABA, this complex conducts chloride ions through its pore, resulting in hyperpolarization of the neuron. This causes an inhibitory effect on neurotransmission by reducing the chances of a successful action potential occurring.
REACT_25155 (Reactome) The efflux pump ABCG2 can relieve cells from toxic heme concentrations even against a concentration gradient. It is expressed in placenta, liver, and small intestine (Krishnamurthy et al, 2004; Doyle & Ross, 2003; Zhang et al, 2003).
REACT_25173 (Reactome) The potassium-transporting ATPase heterodimer (ATP4A/12A:ATP4B) catalyzes the hydrolysis of ATP coupled with the exchange of H+ and K+ ions across the plasma membrane. It is composed of alpha and beta chains. Two human genes encode the catalytic alpha subunit, ATP4A and ATP12A (Maeda et al, 1990; Grishin et al, 1994). ATP4A is responsible for acid production in the stomach. ATP12A is responsible for potassium absorption in various tissues. One human gene encodes the beta subunit, ATP4B (Ma et al, 1991).
REACT_25198 (Reactome) Hephaestin oxidizes ferrous iron after export from duodenal cells to enable its transport via transferrin (Griffiths et al, 2005).
REACT_25203 (Reactome) The heme transporter FLVCR is expressed in intestine and liver tissue, but also in developing erythroid cells where it is required to protect them from heme toxicity (Quigley et al, 2004; Rey et al, 2008).
REACT_25246 (Reactome) The 5-hydroxytryptamine receptor (HTR3) family are members of the superfamily of ligand-gated ion channels (LGICs). Five receptors (HTR3A-E) form a heteropentamer. Binding of the neurotransmitter 5-hydroxytryptamine (5HT, serotonin) to the HTR3 complex opens the channel, which in turn, leads to an excitatory response in neurons and is permeable to sodium, potassium, and calcium ions (Miyake et al. 1995, Davies et al. 1999, Niesler et al. 2007).
REACT_25268 (Reactome) The function of V-type proton pumping ATPases is basically the same as that of F-type ATPases, except that V-ATPases cannot synthesize ATP from the proton motive force, the reverse reaction of pumping. When pumping, ATP hydrolysis drives a 120 degree rotation of the rotor which leads to movement of three protons into the phagosome (Adachi et al. 2007).
REACT_25277 (Reactome) When endosomal pH reaches 6,0, protons replace the iron ions in the transferrin/receptor complex (Hemadi et al, 2006).
REACT_25287 (Reactome) The sodium/potassium-transporting ATPase (ATP1A:ATP1B:FXYD) is composed of three subunits - alpha (catalytic part), beta and gamma. The trimer catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane, creating the electrochemical gradient which provides energy for the active transport of various nutrients.
Four human genes encode the catalytic alpha subunits, ATP1A1-4 (Kawakami et al, 1986; Shull et al, 1989; Ovchinnikov et al, 1988; Keryanov and Gardner, 2002). Defects in ATP1A2 cause alternating hemiplegia of childhood (AHC) (Swoboda et al, 2004). Another defect in ATP1A2 causes familial hemiplegic migraine type 2 (FHM2) (Vanmolkot et al, 2003). Defects in ATP1A3 are the cause of dystonia type 12 (DYT12) (de Carvalho Aguiar et al, 2004).

Three human genes encode the non-catalytic beta subunits, ATP1B1-3. The beta subunits are thought to mediate the number of sodium pumps transported to the plasma membrane (Lane et al, 1989; Ruiz et al, 1996; Malik et al, 1996). FXYD proteins belong to a family of small membrane proteins that are auxiliary gamma subunits of Na-K-ATPase. At least six members of this family, FYD1-4, 6 and 7, have been shown to regulate Na-K-ATPase activity (Geering 2006, Choudhury et al. 2007). Defects in FXYD2 are the cause of hypomagnesemia type 2 (HOMG2) (Meij et al, 2000).
REACT_25301 (Reactome) Accumulation of calcium into the Golgi apparatus is mediated by sarco(endo)plasmic reticulum calcium-ATPases (SERCAs) and by secretory pathway calcium-ATPases (SPCAs). There are two human genes which encode SPCAs; ATP2C1 and ATP2C2 which encode magnesium-dependent calcium-transporting ATPase type 2C members 1 and 2 (ATP2C1 and 2) respectively (Sudbrak et al, 2000; Vanoevelen et al, 2005). Defects in ATP2C1 are the cause of Hailey-Hailey disease (HHD), an autosomal dominant disease characterized by persistent blisters and erosions of the skin (Hu et al, 2000).
REACT_25304 (Reactome) The glycine receptor (GLR) is a ligand-gated ion channel. It is functional as a heteropentamer, consisting of alpha (GLRA) and beta (GLRB) subunits. With no ligand bound, the receptor complex is closed to chloride ions. Binding of the inhibitory neurotransmitter glycine (Gly) to this receptor complex increases chloride conductance into neurons and thus produces hyperpolarization (inhibition of neuronal firing) (Grenningloh et al. 1990, Nikolic et al. 1998, Handford et al. 1996).
REACT_25316 (Reactome) Intracellular pools of Ca2+ serve as the source for inositol 1,4,5-trisphosphate (IP3) -induced alterations in cytoplasmic free Ca2+. In most human cells Ca2+ is stored in the lumen of the sarco/endoplastic reticulum by ATPases known as SERCAs (ATP2As). In platelets, ATP2As transport Ca2+ into the platelet dense tubular network. ATP2As are P-type ATPases, similar to the plasma membrane Na+ and Ca+-ATPases. Humans have three genes for SERCA pumps; ATP2A1-3. Studies on ATP2A1 suggest that it binds two Ca2+ ions from the cytoplasm and is subsequently phosphorylated at Asp351 before translocating Ca2+ into the SR lumen. There is a counter transport of two or possibly three protons ensuring partial charge balancing.
REACT_25385 (Reactome) Transferrin is the main transporter of iron in the blood. It can take up two ferric iron ions (Wally et al, 2006).
REACT_25389 (Reactome) Acidification of the endosome does not continue further, and the endosome fuses again with the plasma membrane (Willingham et al, 1984; Harding et al, 1983).
REACT_25391 (Reactome) The GABA(A)-rho receptor (GABRR) is expressed in many areas of the brain, but in contrast to other GABA(A) receptors, has especially high expression in the retina. It is functional as a homopentamer and is permeable to chloride ions when GABA binds to it (Cutting et al. 1991, Cutting et al. 1992, Bailey et al. 1990).
RYR tetramer:CASQ polymer:TRDN:junctinmim-catalysisREACT_160216 (Reactome)
SCNN channelsREACT_160256 (Reactome)
SCNN channelsmim-catalysisREACT_160095 (Reactome)
SLC11A2mim-catalysisREACT_20526 (Reactome)
SLC17A3mim-catalysisREACT_160084 (Reactome)
SLC17A3mim-catalysisREACT_160104 (Reactome)
SLC46A1mim-catalysisREACT_25025 (Reactome)
SLC9B1/C2mim-catalysisREACT_160312 (Reactome)
SLC9B2mim-catalysisREACT_160252 (Reactome)
SLC9C1mim-catalysisREACT_160226 (Reactome)
STEAP3mim-catalysisREACT_24919 (Reactome)
TF:TFRC dimerArrowREACT_25277 (Reactome)
TF:TFRC dimerREACT_25389 (Reactome)
TF:TFRCArrowREACT_25389 (Reactome)
TF:TFRCREACT_24927 (Reactome)
TFArrowREACT_24927 (Reactome)
TFRC dimerArrowREACT_24927 (Reactome)
TFRC dimerREACT_24945 (Reactome)
TFREACT_25385 (Reactome)
TPCN1/2mim-catalysisREACT_160271 (Reactome)
TTYH1-3mim-catalysisREACT_160181 (Reactome)
TTYH2/3mim-catalysisREACT_160263 (Reactome)
Ub-SCNN channelsArrowREACT_160256 (Reactome)
UbREACT_160256 (Reactome)
UrateArrowREACT_160104 (Reactome)
UrateREACT_160104 (Reactome)
V-ATPasemim-catalysisREACT_25268 (Reactome)
WNKsArrowREACT_160256 (Reactome)
amilorideTBarREACT_160095 (Reactome)
amilorideTBarREACT_160227 (Reactome)
e-REACT_24919 (Reactome)
e-REACT_25114 (Reactome)
hemeArrowREACT_25155 (Reactome)
hemeArrowREACT_25203 (Reactome)
hemeREACT_22100 (Reactome)
hemeREACT_25155 (Reactome)
hemeREACT_25203 (Reactome)
holoTF:TFRC dimerArrowREACT_24977 (Reactome)
holoTF:TFRC dimerREACT_25277 (Reactome)
holoTF:TFRCArrowREACT_24945 (Reactome)
holoTF:TFRCREACT_24977 (Reactome)
holoTFArrowREACT_25385 (Reactome)
holoTFREACT_24945 (Reactome)
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