Gamma carboxylation, hypusine formation and arylsulfatase activation (Homo sapiens)

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25, 26, 43, 495425, 26, 43, 492, 19, 21-23, 39...4, 25, 26, 43, 491, 6, 725, 26, 43, 493, 16, 5225, 26, 43, 4933, 44, 483, 15, 5025, 26, 43, 4911, 1225, 26, 43, 491, 8, 10, 13, 28...36, 3845, 56cytosolGolgi lumenendoplasmic reticulum lumenO2ARSD factor X light chainpropeptidepro-factor X,uncarboxylatedUptake and functionof diphtheria toxinPROC(33-42)OxA-ARSI VKOARSE aminocarboxypropylEEF2NAD+ARSJ DPH1 CO2OxA-STS DPH6pro-protein C,uncarboxylatedOxA-ARSH 3D-PROC(33-197) DPH5pro-factor VIIPROC(200-461) ARSDHPS Ca2+ 11xCbxE-GAS6(31-691)VKOVKODhp-EIF5A2 DOHH GGCXARSA(448-507) VKHQprotein CSUMF2factor X heavy chain ARSA(19-444) pro-factor XO2SUMF1factor X heavy chain pro-prothrombin(factor II)8xCbxE-3D-PROC(33-197) active ARSOxA-ARSJ EIF5A2 11xCbxE-PROS1STS CO211xCbxE-PROS1(25-676)SUMF1:SUMF2ARSH OxA-ARSG 3D-F9(29-461)H2OMe-diphthine EEF23D-F10(32-179) H+DPH2 FURIN13xCbxE-PROZVKHQGAS6(31-38)OxA-ARSK Fe2+ AdoMetDPH1:DPH2:DPH3pro-protein C12xCbxE-3D-F9(47-461)OxA-ARSF PROZ(24-40)11xCbxE-3D-F10(41-179) 10xCbxE-F2(25-622)10xCbxE-F2(44-622)12xCbxE-3D-F9(29-461)EIF5A(Hyp)H+diphthine EEF2prothrombin (factorII) propeptideAMPfactor X heavy chain NADHDPH711xCbxE-3D-F10(32-179) CO2CO2Dhp-EIF5A 1,3-diaminopropane13xCbxE-PROZ(24-400)H2OCO2PROS1(25-676)VKONAD+11xCbxE-GAS6(39-691)H2SO2ATPPROC(200-461) ARSK factor X heavy chain pro-protein CAdoHcyVKOGAS6(31-691)OxA-ARSE PROC(200-461) factor IX propeptideH2OEIF5Apro-factor X10xCbxE-F2(25-622)ARSI 13xCbxE-PROZ(24-400)CO211xCbxE-GAS6(31-691)factor XO2factor VIISUMF1 NH4+EIF5A(Dhp)SPMPPiDPH3 8xCbxE-3D-PROC(33-197) 12xCbxE-3D-F9(29-461)Hypu-EIF5A2 MTAD10xCbxE-F7(21-466)VKORC1nascent EEF2NADHCO2factor VIIpropeptideVKHQO2ARSA(448-507) SUMF2 ARSF DOHH:Fe++8xCbxE-3D-PROC(43-197) DNAJC24EEF2deoxyhypusinesynthase tetramer11xCbxE-PROS1(25-676)OxA-ARSA(19-444) OxA-ARSB PROZ(24-400)ARSG pro-factor VIIH2OVKHQCO2OxA-ARSD VKHQHypu-EIF5A 11xCbxE-3D-F10(32-179) PROC(200-461) EIF5A PROS1(25-41)ARSB H2O20, 325, 9, 351, 105, 9, 3542, 51, 5330, 4242, 51, 5320, 322430, 4230, 425, 9, 351220, 324020, 32242417, 2730, 4251, 535, 9, 3518, 3117, 2742, 51, 534634, 3720, 32124651, 5317, 2751, 534642, 51, 532417, 271, 13, 2942, 51, 5351, 534630, 425, 9, 3514, 47, 5517, 2724


Description

After translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the body. These modifications include the vitamin K-dependent attachment of carboxyl groups to glutamate residues and the conversion of a lysine residue in eIF5A to hypusine, and the conversion of a histidine residue in EEF to diphthamide. View original pathway at:Reactome.

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Bibliography

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  1. Abdel-Fattah W, Scheidt V, Uthman S, Stark MJ, Schaffrath R.; ''Insights into diphthamide, key diphtheria toxin effector.''; PubMed Europe PMC Scholia
  2. Clement PM, Henderson CA, Jenkins ZA, Smit-McBride Z, Wolff EC, Hershey JW, Park MH, Johansson HE.; ''Identification and characterization of eukaryotic initiation factor 5A-2.''; PubMed Europe PMC Scholia
  3. Brenner B, Sánchez-Vega B, Wu SM, Lanir N, Stafford DW, Solera J.; ''A missense mutation in gamma-glutamyl carboxylase gene causes combined deficiency of all vitamin K-dependent blood coagulation factors.''; PubMed Europe PMC Scholia
  4. Foster D, Davie EW.; ''Characterization of a cDNA coding for human protein C.''; PubMed Europe PMC Scholia
  5. Wasley LC, Rehemtulla A, Bristol JA, Kaufman RJ.; ''PACE/furin can process the vitamin K-dependent pro-factor IX precursor within the secretory pathway.''; PubMed Europe PMC Scholia
  6. Uthman S, Bär C, Scheidt V, Liu S, ten Have S, Giorgini F, Stark MJ, Schaffrath R.; ''The amidation step of diphthamide biosynthesis in yeast requires DPH6, a gene identified through mining the DPH1-DPH5 interaction network.''; PubMed Europe PMC Scholia
  7. Leduc R, Molloy SS, Thorne BA, Thomas G.; ''Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage.''; PubMed Europe PMC Scholia
  8. Roeser D, Preusser-Kunze A, Schmidt B, Gasow K, Wittmann JG, Dierks T, von Figura K, Rudolph MG.; ''A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme.''; PubMed Europe PMC Scholia
  9. Wolff EC, Folk JE, Park MH.; ''Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase.''; PubMed Europe PMC Scholia
  10. Su X, Lin Z, Lin H.; ''The biosynthesis and biological function of diphthamide.''; PubMed Europe PMC Scholia
  11. Lau HY, Ramanujulu PM, Guo D, Yang T, Wirawan M, Casey PJ, Go ML, Wang M.; ''An improved isoprenylcysteine carboxylmethyltransferase inhibitor induces cancer cell death and attenuates tumor growth in vivo.''; PubMed Europe PMC Scholia
  12. Morris DP, Stevens RD, Wright DJ, Stafford DW.; ''Processive post-translational modification. Vitamin K-dependent carboxylation of a peptide substrate.''; PubMed Europe PMC Scholia
  13. Van Ness BG, Howard JB, Bodley JW.; ''ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products.''; PubMed Europe PMC Scholia
  14. Stenina O, Pudota BN, McNally BA, Hommema EL, Berkner KL.; ''Tethered processivity of the vitamin K-dependent carboxylase: factor IX is efficiently modified in a mechanism which distinguishes Gla's from Glu's and which accounts for comprehensive carboxylation in vivo.''; PubMed Europe PMC Scholia
  15. Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K.; ''Nucleotide sequence of the gene for human factor IX (antihemophilic factor B).''; PubMed Europe PMC Scholia
  16. Manfioletti G, Brancolini C, Avanzi G, Schneider C.; ''The protein encoded by a growth arrest-specific gene (gas6) is a new member of the vitamin K-dependent proteins related to protein S, a negative coregulator in the blood coagulation cascade.''; PubMed Europe PMC Scholia
  17. Lin Z, Su X, Chen W, Ci B, Zhang S, Lin H.; ''Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis.''; PubMed Europe PMC Scholia
  18. Michnick DA, Pittman DD, Wise RJ, Kaufman RJ.; ''Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage.''; PubMed Europe PMC Scholia
  19. Pittman DD, Wang JH, Kaufman RJ.; ''Identification and functional importance of tyrosine sulfate residues within recombinant factor VIII.''; PubMed Europe PMC Scholia
  20. Di Scipio RG, Hermodson MA, Yates SG, Davie EW.; ''A comparison of human prothrombin, factor IX (Christmas factor), factor X (Stuart factor), and protein S.''; PubMed Europe PMC Scholia
  21. Mariappan M, Preusser-Kunze A, Balleininger M, Eiselt N, Schmidt B, Gande SL, Wenzel D, Dierks T, von Figura K.; ''Expression, localization, structural, and functional characterization of pFGE, the paralog of the Calpha-formylglycine-generating enzyme.''; PubMed Europe PMC Scholia
  22. Kirchhausen T.; ''Three ways to make a vesicle.''; PubMed Europe PMC Scholia
  23. Poser JW, Esch FS, Ling NC, Price PA.; ''Isolation and sequence of the vitamin K-dependent protein from human bone. Undercarboxylation of the first glutamic acid residue.''; PubMed Europe PMC Scholia
  24. Ferron M, Lacombe J, Germain A, Oury F, Karsenty G.; ''GGCX and VKORC1 inhibit osteocalcin endocrine functions.''; PubMed Europe PMC Scholia
  25. Wei H, Bera TK, Wayne AS, Xiang L, Colantonio S, Chertov O, Pastan I.; ''A modified form of diphthamide causes immunotoxin resistance in a lymphoma cell line with a deletion of the WDR85 gene.''; PubMed Europe PMC Scholia
  26. Collier RJ.; ''Diphtheria toxin: mode of action and structure.''; PubMed Europe PMC Scholia
  27. Pappenheimer AM.; ''Diphtheria toxin.''; PubMed Europe PMC Scholia
  28. Yang J, Kulkarni K, Manolaridis I, Zhang Z, Dodd RB, Mas-Droux C, Barford D.; ''Mechanism of isoprenylcysteine carboxyl methylation from the crystal structure of the integral membrane methyltransferase ICMT.''; PubMed Europe PMC Scholia
  29. Ware J, Diuguid DL, Liebman HA, Rabiet MJ, Kasper CK, Furie BC, Furie B, Stafford DW.; ''Factor IX San Dimas. Substitution of glutamine for Arg-4 in the propeptide leads to incomplete gamma-carboxylation and altered phospholipid binding properties.''; PubMed Europe PMC Scholia
  30. Hauschka PV, Lian JB, Cole DE, Gundberg CM.; ''Osteocalcin and matrix Gla protein: vitamin K-dependent proteins in bone.''; PubMed Europe PMC Scholia
  31. Landgrebe J, Dierks T, Schmidt B, von Figura K.; ''The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes.''; PubMed Europe PMC Scholia
  32. Zhang Y, Zhu X, Torelli AT, Lee M, Dzikovski B, Koralewski RM, Wang E, Freed J, Krebs C, Ealick SE, Lin H.; ''Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme.''; PubMed Europe PMC Scholia
  33. Ouyang Yb, Lane WS, Moore KL.; ''Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins.''; PubMed Europe PMC Scholia
  34. DiScipio RG, Davie EW.; ''Characterization of protein S, a gamma-carboxyglutamic acid containing protein from bovine and human plasma.''; PubMed Europe PMC Scholia
  35. Dierks T, Schmidt B, Borissenko LV, Peng J, Preusser A, Mariappan M, von Figura K.; ''Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme.''; PubMed Europe PMC Scholia
  36. Diver MM, Long SB.; ''Mutational analysis of the integral membrane methyltransferase isoprenylcysteine carboxyl methyltransferase (ICMT) reveals potential substrate binding sites.''; PubMed Europe PMC Scholia
  37. Kang KR, Kim YS, Wolff EC, Park MH.; ''Specificity of the deoxyhypusine hydroxylase-eukaryotic translation initiation factor (eIF5A) interaction: identification of amino acid residues of the enzyme required for binding of its substrate, deoxyhypusine-containing eIF5A.''; PubMed Europe PMC Scholia
  38. Cosma MP, Pepe S, Annunziata I, Newbold RF, Grompe M, Parenti G, Ballabio A.; ''The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases.''; PubMed Europe PMC Scholia
  39. Dong M, Su X, Dzikovski B, Dando EE, Zhu X, Du J, Freed JH, Lin H.; ''Dph3 is an electron donor for Dph1-Dph2 in the first step of eukaryotic diphthamide biosynthesis.''; PubMed Europe PMC Scholia
  40. Su X, Lin Z, Chen W, Jiang H, Zhang S, Lin H.; ''Chemogenomic approach identified yeast YLR143W as diphthamide synthetase.''; PubMed Europe PMC Scholia
  41. Delpierrre G, Vertommen D, Communi D, Rider MH, Van Schaftingen E.; ''Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin.''; PubMed Europe PMC Scholia
  42. Foster DC, Sprecher CA, Holly RD, Gambee JE, Walker KM, Kumar AA.; ''Endoproteolytic processing of the dibasic cleavage site in the human protein C precursor in transfected mammalian cells: effects of sequence alterations on efficiency of cleavage.''; PubMed Europe PMC Scholia
  43. Moehring JM, Moehring TJ.; ''The post-translational trimethylation of diphthamide studied in vitro.''; PubMed Europe PMC Scholia
  44. Murphy JR.; ''Mechanism of diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process.''; PubMed Europe PMC Scholia
  45. Wright LP, Court H, Mor A, Ahearn IM, Casey PJ, Philips MR.; ''Topology of mammalian isoprenylcysteine carboxyl methyltransferase determined in live cells with a fluorescent probe.''; PubMed Europe PMC Scholia
  46. Shearer MJ, Fu X, Booth SL.; ''Vitamin K nutrition, metabolism, and requirements: current concepts and future research.''; PubMed Europe PMC Scholia
  47. Thim L, Bjoern S, Christensen M, Nicolaisen EM, Lund-Hansen T, Pedersen AH, Hedner U.; ''Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells.''; PubMed Europe PMC Scholia
  48. Collard F, Delpierre G, Stroobant V, Matthijs G, Van Schaftingen E.; ''A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines.''; PubMed Europe PMC Scholia
  49. Degen SJ, Davie EW.; ''Nucleotide sequence of the gene for human prothrombin.''; PubMed Europe PMC Scholia
  50. von Figura K, Schmidt B, Selmer T, Dierks T.; ''A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease.''; PubMed Europe PMC Scholia
  51. Sjölinder M, Uhlmann J, Ponstingl H.; ''Characterisation of an evolutionary conserved protein interacting with the putative guanine nucleotide exchange factor DelGEF and modulating secretion.''; PubMed Europe PMC Scholia
  52. McMullen BA, Fujikawa K, Kisiel W.; ''The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens.''; PubMed Europe PMC Scholia
  53. Kim YS, Kang KR, Wolff EC, Bell JK, McPhie P, Park MH.; ''Deoxyhypusine hydroxylase is a Fe(II)-dependent, HEAT-repeat enzyme. Identification of amino acid residues critical for Fe(II) binding and catalysis [corrected].''; PubMed Europe PMC Scholia
  54. Danan LM, Yu Z, Hoffhines AJ, Moore KL, Leary JA.; ''Mass spectrometric kinetic analysis of human tyrosylprotein sulfotransferase-1 and -2.''; PubMed Europe PMC Scholia
  55. Van Ness BG, Howard JB, Bodley JW.; ''ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products.''; PubMed Europe PMC Scholia
  56. Berkner KL.; ''The vitamin K-dependent carboxylase.''; PubMed Europe PMC Scholia
  57. Joe YA, Wolff EC, Park MH.; ''Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins.''; PubMed Europe PMC Scholia
  58. Shearer MJ, Newman P.; ''Recent trends in the metabolism and cell biology of vitamin K with special reference to vitamin K cycling and MK-4 biosynthesis.''; PubMed Europe PMC Scholia
  59. Walz DA, Hewett-Emmett D, Seegers WH.; ''Amino acid sequence of human prothrombin fragments 1 and 2.''; PubMed Europe PMC Scholia
  60. Leytus SP, Chung DW, Kisiel W, Kurachi K, Davie EW.; ''Characterization of a cDNA coding for human factor X.''; PubMed Europe PMC Scholia
  61. Mattheakis LC, Shen WH, Collier RJ.; ''DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae.''; PubMed Europe PMC Scholia
  62. Teramoto T, Fujikawa Y, Kawaguchi Y, Kurogi K, Soejima M, Adachi R, Nakanishi Y, Mishiro-Sato E, Liu MC, Sakakibara Y, Suiko M, Kimura M, Kakuta Y.; ''Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction.''; PubMed Europe PMC Scholia
  63. Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH.; ''Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2.''; PubMed Europe PMC Scholia
  64. Hammed A, Matagrin B, Spohn G, Prouillac C, Benoit E, Lattard V.; ''VKORC1L1, an enzyme rescuing the vitamin K 2,3-epoxide reductase activity in some extrahepatic tissues during anticoagulation therapy.''; PubMed Europe PMC Scholia
  65. Furie B, Bouchard BA, Furie BC.; ''Vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid.''; PubMed Europe PMC Scholia
  66. Park MH.; ''The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A).''; PubMed Europe PMC Scholia
  67. Hagen FS, Gray CL, O'Hara P, Grant FJ, Saari GC, Woodbury RG, Hart CE, Insley M, Kisiel W, Kurachi K.; ''Characterization of a cDNA coding for human factor VII.''; PubMed Europe PMC Scholia
  68. Liu S, Leppla SH.; ''Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins.''; PubMed Europe PMC Scholia
  69. Preusser-Kunze A, Mariappan M, Schmidt B, Gande SL, Mutenda K, Wenzel D, von Figura K, Dierks T.; ''Molecular characterization of the human Calpha-formylglycine-generating enzyme.''; PubMed Europe PMC Scholia
  70. Bär C, Zabel R, Liu S, Stark MJ, Schaffrath R.; ''A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3.''; PubMed Europe PMC Scholia
  71. Park JH, Wolff EC, Folk JE, Park MH.; ''Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase.''; PubMed Europe PMC Scholia
  72. Delpierre G, Rider MH, Collard F, Stroobant V, Vanstapel F, Santos H, Van Schaftingen E.; ''Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase.''; PubMed Europe PMC Scholia
  73. Butkowski RJ, Elion J, Downing MR, Mann KG.; ''Primary structure of human prethrombin 2 and alpha-thrombin.''; PubMed Europe PMC Scholia
  74. Zito E, Fraldi A, Pepe S, Annunziata I, Kobinger G, Di Natale P, Ballabio A, Cosma MP.; ''Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2.''; PubMed Europe PMC Scholia
  75. Tie JK, Jin DY, Stafford DW.; ''Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regeneration.''; PubMed Europe PMC Scholia
  76. McMullen BA, Fujikawa K, Kisiel W, Sasagawa T, Howald WN, Kwa EY, Weinstein B.; ''Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid.''; PubMed Europe PMC Scholia
  77. Selmer T, Hallmann A, Schmidt B, Sumper M, von Figura K.; ''The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri.''; PubMed Europe PMC Scholia
  78. Collard F, Wiame E, Bergans N, Fortpied J, Vertommen D, Vanstapel F, Delpierre G, Van Schaftingen E.; ''Fructosamine 3-kinase-related protein and deglycation in human erythrocytes.''; PubMed Europe PMC Scholia
  79. Schaffrath R, Abdel-Fattah W, Klassen R, Stark MJ.; ''The diphthamide modification pathway from Saccharomyces cerevisiae--revisited.''; PubMed Europe PMC Scholia
  80. Hirota Y, Tsugawa N, Nakagawa K, Suhara Y, Tanaka K, Uchino Y, Takeuchi A, Sawada N, Kamao M, Wada A, Okitsu T, Okano T.; ''Menadione (vitamin K3) is a catabolic product of oral phylloquinone (vitamin K1) in the intestine and a circulating precursor of tissue menaquinone-4 (vitamin K2) in rats.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
114840view16:34, 25 January 2021ReactomeTeamReactome version 75
113286view11:35, 2 November 2020ReactomeTeamReactome version 74
112497view15:45, 9 October 2020ReactomeTeamReactome version 73
101409view11:29, 1 November 2018ReactomeTeamreactome version 66
100947view21:05, 31 October 2018ReactomeTeamreactome version 65
100484view19:39, 31 October 2018ReactomeTeamreactome version 64
100029view16:23, 31 October 2018ReactomeTeamreactome version 63
99582view14:55, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99204view12:43, 31 October 2018ReactomeTeamreactome version 62
94013view13:51, 16 August 2017ReactomeTeamreactome version 61
93632view11:29, 9 August 2017ReactomeTeamreactome version 61
87451view13:58, 22 July 2016MkutmonOntology Term : 'peptide and protein metabolic process' added !
86744view09:25, 11 July 2016ReactomeTeamreactome version 56
83388view11:04, 18 November 2015ReactomeTeamVersion54
81771view10:19, 26 August 2015ReactomeTeamVersion53
77021view08:31, 17 July 2014ReactomeTeamFixed remaining interactions
76726view12:09, 16 July 2014ReactomeTeamFixed remaining interactions
76052view10:11, 11 June 2014ReactomeTeamRe-fixing comment source
75761view11:26, 10 June 2014ReactomeTeamReactome 48 Update
75111view14:06, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74861view18:44, 2 May 2014KhanspersChanged comment source for description
74758view08:50, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
1,3-diaminopropaneMetaboliteCHEBI:15725 (ChEBI)
10xCbxE-F2(25-622)ProteinP00734 (Uniprot-TrEMBL)
10xCbxE-F2(44-622)ProteinP00734 (Uniprot-TrEMBL)
10xCbxE-F7(21-466)ProteinP08709 (Uniprot-TrEMBL)
11xCbxE-3D-F10(32-179) ProteinP00742 (Uniprot-TrEMBL)
11xCbxE-3D-F10(41-179) ProteinP00742 (Uniprot-TrEMBL)
11xCbxE-GAS6(31-691)ProteinQ14393 (Uniprot-TrEMBL)
11xCbxE-GAS6(39-691)ProteinQ14393 (Uniprot-TrEMBL)
11xCbxE-PROS1(25-676)ProteinP07225 (Uniprot-TrEMBL)
11xCbxE-PROS1ProteinP07225 (Uniprot-TrEMBL)
12xCbxE-3D-F9(29-461)ProteinP00740 (Uniprot-TrEMBL)
12xCbxE-3D-F9(47-461)ProteinP00740 (Uniprot-TrEMBL)
13xCbxE-PROZ(24-400)ProteinP22891 (Uniprot-TrEMBL)
13xCbxE-PROZProteinP22891 (Uniprot-TrEMBL)
3D-F10(32-179) ProteinP00742 (Uniprot-TrEMBL)
3D-F9(29-461)ProteinP00740 (Uniprot-TrEMBL)
3D-PROC(33-197) ProteinP04070 (Uniprot-TrEMBL)
8xCbxE-3D-PROC(33-197) ProteinP04070 (Uniprot-TrEMBL)
8xCbxE-3D-PROC(43-197) ProteinP04070 (Uniprot-TrEMBL)
AMPMetaboliteCHEBI:16027 (ChEBI)
ARSA(19-444) ProteinP15289 (Uniprot-TrEMBL)
ARSA(448-507) ProteinP15289 (Uniprot-TrEMBL)
ARSB ProteinP15848 (Uniprot-TrEMBL)
ARSD ProteinP51689 (Uniprot-TrEMBL)
ARSE ProteinP51690 (Uniprot-TrEMBL)
ARSF ProteinP54793 (Uniprot-TrEMBL)
ARSG ProteinQ96EG1 (Uniprot-TrEMBL)
ARSH ProteinQ5FYA8 (Uniprot-TrEMBL)
ARSI ProteinQ5FYB1 (Uniprot-TrEMBL)
ARSJ ProteinQ5FYB0 (Uniprot-TrEMBL)
ARSK ProteinQ6UWY0 (Uniprot-TrEMBL)
ARSComplexR-HSA-1614312 (Reactome)
ATPMetaboliteCHEBI:15422 (ChEBI)
AdoHcyMetaboliteCHEBI:16680 (ChEBI)
AdoMetMetaboliteCHEBI:15414 (ChEBI)
CO2MetaboliteCHEBI:16526 (ChEBI)
Ca2+ MetaboliteCHEBI:29108 (ChEBI)
DHPS ProteinP49366 (Uniprot-TrEMBL)
DNAJC24ProteinQ6P3W2 (Uniprot-TrEMBL)
DOHH ProteinQ9BU89 (Uniprot-TrEMBL)
DOHH:Fe++ComplexR-HSA-204627 (Reactome)
DPH1 ProteinQ9BZG8 (Uniprot-TrEMBL)
DPH1:DPH2:DPH3ComplexR-HSA-5358365 (Reactome)
DPH2 ProteinQ9BQC3 (Uniprot-TrEMBL)
DPH3 ProteinQ96FX2 (Uniprot-TrEMBL)
DPH5ProteinQ9H2P9 (Uniprot-TrEMBL)
DPH6ProteinQ7L8W6 (Uniprot-TrEMBL)
DPH7ProteinQ9BTV6 (Uniprot-TrEMBL)
Dhp-EIF5A ProteinP63241 (Uniprot-TrEMBL)
Dhp-EIF5A2 ProteinQ9GZV4 (Uniprot-TrEMBL)
EEF2ProteinP13639 (Uniprot-TrEMBL)
EIF5A ProteinP63241 (Uniprot-TrEMBL)
EIF5A(Dhp)ComplexR-HSA-3149583 (Reactome)
EIF5A(Hyp)ComplexR-HSA-204658 (Reactome)
EIF5A2 ProteinQ9GZV4 (Uniprot-TrEMBL)
EIF5AComplexR-HSA-3149585 (Reactome)
FURINProteinP09958 (Uniprot-TrEMBL)
Fe2+ MetaboliteCHEBI:18248 (ChEBI)
GAS6(31-38)ProteinQ14393 (Uniprot-TrEMBL)
GAS6(31-691)ProteinQ14393 (Uniprot-TrEMBL)
GGCXProteinP38435 (Uniprot-TrEMBL)
H+MetaboliteCHEBI:15378 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
H2SMetaboliteCHEBI:16136 (ChEBI)
Hypu-EIF5A ProteinP63241 (Uniprot-TrEMBL)
Hypu-EIF5A2 ProteinQ9GZV4 (Uniprot-TrEMBL)
MTADMetaboliteCHEBI:17509 (ChEBI)
Me-diphthine EEF2ProteinP13639 (Uniprot-TrEMBL)
NAD+MetaboliteCHEBI:15846 (ChEBI)
NADHMetaboliteCHEBI:16908 (ChEBI)
NH4+MetaboliteCHEBI:28938 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
OxA-ARSA(19-444) ProteinP15289 (Uniprot-TrEMBL)
OxA-ARSB ProteinP15848 (Uniprot-TrEMBL)
OxA-ARSD ProteinP51689 (Uniprot-TrEMBL)
OxA-ARSE ProteinP51690 (Uniprot-TrEMBL)
OxA-ARSF ProteinP54793 (Uniprot-TrEMBL)
OxA-ARSG ProteinQ96EG1 (Uniprot-TrEMBL)
OxA-ARSH ProteinQ5FYA8 (Uniprot-TrEMBL)
OxA-ARSI ProteinQ5FYB1 (Uniprot-TrEMBL)
OxA-ARSJ ProteinQ5FYB0 (Uniprot-TrEMBL)
OxA-ARSK ProteinQ6UWY0 (Uniprot-TrEMBL)
OxA-STS ProteinP08842 (Uniprot-TrEMBL)
PPiMetaboliteCHEBI:29888 (ChEBI)
PROC(200-461) ProteinP04070 (Uniprot-TrEMBL)
PROC(33-42)ProteinP04070 (Uniprot-TrEMBL)
PROS1(25-41)ProteinP07225 (Uniprot-TrEMBL)
PROS1(25-676)ProteinP07225 (Uniprot-TrEMBL)
PROZ(24-40)ProteinP22891 (Uniprot-TrEMBL)
PROZ(24-400)ProteinP22891 (Uniprot-TrEMBL)
SPMMetaboliteCHEBI:16610 (ChEBI)
STS ProteinP08842 (Uniprot-TrEMBL)
SUMF1 ProteinQ8NBK3 (Uniprot-TrEMBL)
SUMF1:SUMF2ComplexR-HSA-1614330 (Reactome)
SUMF1ProteinQ8NBK3 (Uniprot-TrEMBL)
SUMF2 ProteinQ8NBJ7 (Uniprot-TrEMBL)
SUMF2ProteinQ8NBJ7 (Uniprot-TrEMBL)
Uptake and function of diphtheria toxinPathwayR-HSA-5336415 (Reactome) Diphtheria is a serious, often fatal human disease associated with damage to many tissues. Bacteria in infected individuals, however, are typically confined to the lining of the throat or to a skin lesion; systemic effects are due to the secretion of an exotoxin encoded by a lysogenic bacteriophage. The toxin is encoded as a single polypeptide but is cleaved by host furin-like proteases to yield an aminoterminal fragment A and a carboxyterminal fragment B, linked by a disulfide bond. Toxin cleavage can occur when it first contacts the target cell surface, as annotated here, or as late as the point at which fragment A is released into the cytosol. Fragment B mediates toxin uptake into target cell endocytic vesicles, where acidification promotes a conformational change enabling fragment B to form a channel in the vesicle membrane through which fragment A is extruded into the target cell cytosol. Cleavage of the inter-fragment disulfide bond frees DT fragment A, which catalyzes ADP ribosylation of the translation elongation factor 2 (EEF2) in a target cell, thereby blocking protein synthesis. Neither fragment is toxic to human cells by itself (Collier 1975; Pappenheim 1977; Murphy 2011).
VKHQMetaboliteCHEBI:28433 (ChEBI)
VKOMetaboliteCHEBI:28371 (ChEBI)
VKORC1ProteinQ9BQB6 (Uniprot-TrEMBL)
active ARSComplexR-HSA-1614309 (Reactome)
aminocarboxypropyl EEF2ProteinP13639 (Uniprot-TrEMBL)
deoxyhypusine synthase tetramerComplexR-HSA-204644 (Reactome)
diphthine EEF2ProteinP13639 (Uniprot-TrEMBL)
factor IX propeptideProteinP00740 (Uniprot-TrEMBL)
factor VII propeptideProteinP08709 (Uniprot-TrEMBL)
factor VIIProteinP08709 (Uniprot-TrEMBL)
factor X heavy chain ProteinP00742 (Uniprot-TrEMBL)
factor X light chain propeptideProteinP00742 (Uniprot-TrEMBL)
factor XComplexR-HSA-159785 (Reactome)
nascent EEF2ProteinP13639 (Uniprot-TrEMBL)
pro-factor VIIProteinP08709 (Uniprot-TrEMBL)
pro-factor X, uncarboxylatedComplexR-HSA-159754 (Reactome)
pro-factor XComplexR-HSA-159734 (Reactome)
pro-factor XComplexR-HSA-159744 (Reactome)
pro-protein C, uncarboxylatedComplexR-HSA-159852 (Reactome)
pro-protein CComplexR-HSA-159731 (Reactome)
pro-protein CComplexR-HSA-159772 (Reactome)
pro-prothrombin (factor II)ProteinP00734 (Uniprot-TrEMBL)
protein CComplexR-HSA-159830 (Reactome)
prothrombin (factor II) propeptideProteinP00734 (Uniprot-TrEMBL)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
1,3-diaminopropaneArrowR-HSA-204647 (Reactome)
1,3-diaminopropaneR-HSA-204617 (Reactome)
10xCbxE-F2(25-622)ArrowR-HSA-159826 (Reactome)
10xCbxE-F2(25-622)ArrowR-HSA-159843 (Reactome)
10xCbxE-F2(25-622)R-HSA-159728 (Reactome)
10xCbxE-F2(25-622)R-HSA-159843 (Reactome)
10xCbxE-F2(44-622)ArrowR-HSA-159728 (Reactome)
10xCbxE-F7(21-466)ArrowR-HSA-159761 (Reactome)
10xCbxE-F7(21-466)R-HSA-159783 (Reactome)
11xCbxE-GAS6(31-691)ArrowR-HSA-163809 (Reactome)
11xCbxE-GAS6(31-691)ArrowR-HSA-163810 (Reactome)
11xCbxE-GAS6(31-691)R-HSA-163809 (Reactome)
11xCbxE-GAS6(31-691)R-HSA-163843 (Reactome)
11xCbxE-GAS6(39-691)ArrowR-HSA-163843 (Reactome)
11xCbxE-PROS1(25-676)ArrowR-HSA-159729 (Reactome)
11xCbxE-PROS1(25-676)ArrowR-HSA-159752 (Reactome)
11xCbxE-PROS1(25-676)R-HSA-159729 (Reactome)
11xCbxE-PROS1(25-676)R-HSA-159773 (Reactome)
11xCbxE-PROS1ArrowR-HSA-159773 (Reactome)
12xCbxE-3D-F9(29-461)ArrowR-HSA-159803 (Reactome)
12xCbxE-3D-F9(29-461)ArrowR-HSA-159836 (Reactome)
12xCbxE-3D-F9(29-461)R-HSA-159796 (Reactome)
12xCbxE-3D-F9(29-461)R-HSA-159836 (Reactome)
12xCbxE-3D-F9(47-461)ArrowR-HSA-159796 (Reactome)
13xCbxE-PROZ(24-400)ArrowR-HSA-163820 (Reactome)
13xCbxE-PROZ(24-400)ArrowR-HSA-163825 (Reactome)
13xCbxE-PROZ(24-400)R-HSA-163798 (Reactome)
13xCbxE-PROZ(24-400)R-HSA-163825 (Reactome)
13xCbxE-PROZArrowR-HSA-163798 (Reactome)
3D-F9(29-461)R-HSA-159803 (Reactome)
AMPArrowR-HSA-5358475 (Reactome)
ARSR-HSA-1614362 (Reactome)
ATPR-HSA-5358475 (Reactome)
AdoHcyArrowR-HSA-5358484 (Reactome)
AdoMetR-HSA-5358484 (Reactome)
AdoMetR-HSA-5358494 (Reactome)
CO2R-HSA-159752 (Reactome)
CO2R-HSA-159761 (Reactome)
CO2R-HSA-159795 (Reactome)
CO2R-HSA-159803 (Reactome)
CO2R-HSA-159819 (Reactome)
CO2R-HSA-159826 (Reactome)
CO2R-HSA-163810 (Reactome)
CO2R-HSA-163820 (Reactome)
DNAJC24ArrowR-HSA-5358494 (Reactome)
DOHH:Fe++mim-catalysisR-HSA-204662 (Reactome)
DPH1:DPH2:DPH3mim-catalysisR-HSA-5358494 (Reactome)
DPH5mim-catalysisR-HSA-5358484 (Reactome)
DPH6mim-catalysisR-HSA-5358475 (Reactome)
DPH7mim-catalysisR-HSA-5367022 (Reactome)
EEF2ArrowR-HSA-5358475 (Reactome)
EIF5A(Dhp)ArrowR-HSA-204647 (Reactome)
EIF5A(Dhp)R-HSA-204617 (Reactome)
EIF5A(Dhp)R-HSA-204662 (Reactome)
EIF5A(Hyp)ArrowR-HSA-204662 (Reactome)
EIF5AArrowR-HSA-204617 (Reactome)
EIF5AR-HSA-204647 (Reactome)
FURINmim-catalysisR-HSA-159728 (Reactome)
FURINmim-catalysisR-HSA-159733 (Reactome)
FURINmim-catalysisR-HSA-159771 (Reactome)
FURINmim-catalysisR-HSA-159773 (Reactome)
FURINmim-catalysisR-HSA-159796 (Reactome)
FURINmim-catalysisR-HSA-159868 (Reactome)
FURINmim-catalysisR-HSA-163798 (Reactome)
FURINmim-catalysisR-HSA-163843 (Reactome)
GAS6(31-38)ArrowR-HSA-163843 (Reactome)
GAS6(31-691)R-HSA-163810 (Reactome)
GGCXmim-catalysisR-HSA-159752 (Reactome)
GGCXmim-catalysisR-HSA-159761 (Reactome)
GGCXmim-catalysisR-HSA-159795 (Reactome)
GGCXmim-catalysisR-HSA-159803 (Reactome)
GGCXmim-catalysisR-HSA-159819 (Reactome)
GGCXmim-catalysisR-HSA-159826 (Reactome)
GGCXmim-catalysisR-HSA-163810 (Reactome)
GGCXmim-catalysisR-HSA-163820 (Reactome)
H+ArrowR-HSA-204647 (Reactome)
H+R-HSA-159790 (Reactome)
H+R-HSA-204617 (Reactome)
H2OArrowR-HSA-159752 (Reactome)
H2OArrowR-HSA-159761 (Reactome)
H2OArrowR-HSA-159795 (Reactome)
H2OArrowR-HSA-159803 (Reactome)
H2OArrowR-HSA-159819 (Reactome)
H2OArrowR-HSA-159826 (Reactome)
H2OArrowR-HSA-163810 (Reactome)
H2OArrowR-HSA-163820 (Reactome)
H2SArrowR-HSA-1614362 (Reactome)
MTADArrowR-HSA-5358494 (Reactome)
Me-diphthine EEF2ArrowR-HSA-5358484 (Reactome)
Me-diphthine EEF2R-HSA-5367022 (Reactome)
NAD+ArrowR-HSA-204617 (Reactome)
NAD+R-HSA-1614362 (Reactome)
NAD+R-HSA-204647 (Reactome)
NADHArrowR-HSA-1614362 (Reactome)
NADHArrowR-HSA-204647 (Reactome)
NH4+R-HSA-5358475 (Reactome)
O2R-HSA-159752 (Reactome)
O2R-HSA-159761 (Reactome)
O2R-HSA-159795 (Reactome)
O2R-HSA-159803 (Reactome)
O2R-HSA-159819 (Reactome)
O2R-HSA-159826 (Reactome)
O2R-HSA-163810 (Reactome)
O2R-HSA-163820 (Reactome)
O2R-HSA-204662 (Reactome)
PPiArrowR-HSA-5358475 (Reactome)
PROC(33-42)ArrowR-HSA-159771 (Reactome)
PROS1(25-41)ArrowR-HSA-159773 (Reactome)
PROS1(25-676)R-HSA-159752 (Reactome)
PROZ(24-40)ArrowR-HSA-163798 (Reactome)
PROZ(24-400)R-HSA-163820 (Reactome)
R-HSA-159728 (Reactome) At the beginning of this reaction, 1 molecule of 'pro-prothrombin (factor II)' is present. At the end of this reaction, 1 molecule of 'prothrombin (factor II) propeptide', and 1 molecule of 'prothrombin (factor II)' are present.

This reaction takes place in the 'Golgi membrane' and is mediated by the 'furin activity' of 'furin'.

R-HSA-159729 (Reactome) In this reaction, 1 molecule of 'pro-protein S' is translocated from endoplasmic reticulum membrane to Golgi membrane.

This reaction takes place in the 'ER to Golgi transport vesicle'.

R-HSA-159733 (Reactome) At the beginning of this reaction, 1 molecule of 'pro-factor X' is present. At the end of this reaction, 1 molecule of 'factor X light chain propeptide', and 1 molecule of 'factor X' are present.

This reaction takes place in the 'Golgi membrane' and is mediated by the 'furin activity' of 'furin'.

R-HSA-159752 (Reactome) At the beginning of this reaction, 11 molecules of 'Oxygen', 11 molecules of 'vitamin K hydroquinone', 11 molecules of 'CO2', and 1 molecule of 'pro-protein S, uncarboxylated' are present. At the end of this reaction, 1 molecule of 'pro-protein S', 11 molecules of 'H2O', and 11 molecules of 'vitamin K epoxide' are present.

This reaction takes place in the 'endoplasmic reticulum membrane' and is mediated by the 'gamma-glutamyl carboxylase activity' of 'vitamin K-dependent gamma-carboxylase'.

R-HSA-159757 (Reactome) In this reaction, 1 molecule of 'pro-factor X' is translocated from endoplasmic reticulum lumen to Golgi lumen.

This reaction takes place in the 'ER to Golgi transport vesicle'.

R-HSA-159761 (Reactome) At the beginning of this reaction, 10 molecules of 'Oxygen', 10 molecules of 'vitamin K hydroquinone', 10 molecules of 'CO2', and 1 molecule of 'pro-factor VII, uncarboxylated' are present. At the end of this reaction, 1 molecule of 'pro-factor VII', 10 molecules of 'H2O', and 10 molecules of 'vitamin K epoxide' are present.

This reaction takes place in the 'endoplasmic reticulum membrane' and is mediated by the 'gamma-glutamyl carboxylase activity' of 'vitamin K-dependent gamma-carboxylase'.

R-HSA-159762 (Reactome) In this reaction, 1 molecule of 'pro-protein C' is translocated from endoplasmic reticulum lumen to Golgi lumen.

This reaction takes place in the 'ER to Golgi transport vesicle'.

R-HSA-159771 (Reactome) At the beginning of this reaction, 1 molecule of 'pro-protein C' is present. At the end of this reaction, 1 molecule of 'protein C', and 1 molecule of 'protein C light chain propeptide' are present.

This reaction takes place in the 'Golgi lumen' and is mediated by the 'furin activity' of 'furin'.

R-HSA-159773 (Reactome) At the beginning of this reaction, 1 molecule of 'pro-protein S' is present. At the end of this reaction, 1 molecule of 'protein S propeptide', and 1 molecule of 'protein S' are present.

This reaction takes place in the 'Golgi lumen' and is mediated by the 'furin activity' of 'furin'.

R-HSA-159783 (Reactome) In this reaction, 1 molecule of 'pro-factor VII' is translocated from endoplasmic reticulum lumen to Golgi lumen.

This reaction takes place in the 'ER to Golgi transport vesicle'.

R-HSA-159790 (Reactome) The regeneration of reduced vitamin K (vitamin K hydroquinone) from vitamin K epoxide is catalyzed by vitamin K epoxide reductase (VKORC1) (Sadler 2004). This enzyme is the target of the anticoagulant drug warfarin. Two important features of this reaction remain unclear. First, dithiothreitol functions efficiently as a reductant in vitro (Wallin and Martin 1985), but the in vivo reductant remains unknown. Second, while people homozygous for mutations in VKORC1 protein lack epoxide reductase activity (Rost et al. 2004) and cultured insect cells transfected with the cloned human VKORC1 gene express vitamin K epoxide reductase activity (Li et al. 2004), the possibility that the active form of the enzyme is a complex with other proteins cannot be formally excluded.
R-HSA-159795 (Reactome) At the beginning of this reaction, 8 molecules of 'Oxygen', 8 molecules of 'vitamin K hydroquinone', 8 molecules of 'CO2', and 1 molecule of 'pro-protein C, uncarboxylated' are present. At the end of this reaction, 8 molecules of 'H2O', 8 molecules of 'vitamin K epoxide', and 1 molecule of 'pro-protein C' are present.

This reaction takes place in the 'endoplasmic reticulum membrane' and is mediated by the 'gamma-glutamyl carboxylase activity' of 'vitamin K-dependent gamma-carboxylase'.

R-HSA-159796 (Reactome) At the beginning of this reaction, 1 molecule of 'pro-factor IX' is present. At the end of this reaction, 1 molecule of 'factor IX', and 1 molecule of 'factor IX propeptide' are present.

This reaction takes place in the 'Golgi membrane' and is mediated by the 'furin activity' of 'furin'.

R-HSA-159803 (Reactome) At the beginning of this reaction, 12 molecules of 'Oxygen', 12 molecules of 'vitamin K hydroquinone', 12 molecules of 'CO2', and 1 molecule of 'pro-factor IX, uncarboxylated' are present. At the end of this reaction, 12 molecules of 'H2O', 12 molecules of 'vitamin K epoxide', and 1 molecule of 'pro-factor IX' are present.

This reaction takes place in the 'endoplasmic reticulum membrane' and is mediated by the 'gamma-glutamyl carboxylase activity' of 'vitamin K-dependent gamma-carboxylase'.

R-HSA-159819 (Reactome) At the beginning of this reaction, 11 molecules of 'Oxygen', 1 molecule of 'pro-factor X, uncarboxylated', 11 molecules of 'vitamin K hydroquinone', and 11 molecules of 'CO2' are present. At the end of this reaction, 1 molecule of 'pro-factor X', 11 molecules of 'H2O', and 11 molecules of 'vitamin K epoxide' are present.

This reaction takes place in the 'endoplasmic reticulum membrane' and is mediated by the 'gamma-glutamyl carboxylase activity' of 'vitamin K-dependent gamma-carboxylase'.

R-HSA-159826 (Reactome) At the beginning of this reaction, 10 molecules of 'Oxygen', 10 molecules of 'vitamin K hydroquinone', 10 molecules of 'CO2', and 1 molecule of 'pro-prothrombin (factor II), uncarboxylated' are present. At the end of this reaction, 1 molecule of 'pro-prothrombin (factor II)', 10 molecules of 'H2O', and 10 molecules of 'vitamin K epoxide' are present.

This reaction takes place in the 'endoplasmic reticulum membrane' and is mediated by the 'gamma-glutamyl carboxylase activity' of 'vitamin K-dependent gamma-carboxylase'.

R-HSA-159836 (Reactome) In this reaction, 1 molecule of 'pro-factor IX' is translocated from endoplasmic reticulum lumen to Golgi lumen.

This reaction takes place in the 'ER to Golgi transport vesicle'.

R-HSA-159843 (Reactome) In this reaction, 1 molecule of 'pro-prothrombin (factor II)' is translocated from endoplasmic reticulum lumen to Golgi lumen.

This reaction takes place in the 'ER to Golgi transport vesicle'.

R-HSA-159868 (Reactome) At the beginning of this reaction, 1 molecule of 'pro-factor VII' is present. At the end of this reaction, 1 molecule of 'factor VII', and 1 molecule of 'factor VII propeptide' are present.

This reaction takes place in the 'Golgi membrane' and is mediated by the 'furin activity' of 'furin'.

R-HSA-1614336 (Reactome) Sulfatase-modifying factor 2 (SUMF2, also called C-alpha-formylglycine-generating enzyme 2, pFGE) is the paralogue of SUMF1. While SUMF1 can modify a critical residue on arylsulfatases to confer activity to them, SUMF2 lacks this ability (Mariappan et al. 2005) and instead, SUMF2 can inhibit the action of SUMF1 by dimerising with it (Zito et al. 2005). SUMF2 can interact with sulfatases with and without SUMF1 (Zito et al. 2005).
R-HSA-1614362 (Reactome) The sulfatase-modifying factor 1 (SUMF1, also called C-alpha-formylglycine-generating enzyme, FGE) (Preusser-Kunze et al. 2005, Cosma et al. 2003, Landgrebe et al. 2003) oxidises the critical cysteine residue in arylsulfatases to an active site 3-oxoalanine residue thus confering sulfatase activity (Roeser et al. 2006). Defects in SUMF1 cause multiple sulfatase deficiency (MSD) (MIM:272200), an impairment of arylsulfatase activity due to defective post-translational modification of the cysteine residue (Cosma et al. 2003, Dierks et al, 2003). This post-translational modification is thought to be highly conserved in eukaryotes (Selmer et al. 1996, von Figura et al. 1998). SUMF1 is active as either a monomer or a homodimer. A monomer is described in this reaction.
R-HSA-163798 (Reactome) At the beginning of this reaction, 1 molecule of 'pro-protein Z' is present. At the end of this reaction, 1 molecule of 'protein Z propeptide', and 1 molecule of 'protein Z' are present.

This reaction takes place in the 'Golgi lumen' and is mediated by the 'furin activity' of 'furin'.

R-HSA-163809 (Reactome) In this reaction, 1 molecule of 'pro-GAS6' is translocated from endoplasmic reticulum lumen to Golgi lumen.

This reaction takes place in the 'ER to Golgi transport vesicle'.

R-HSA-163810 (Reactome) The details of the gamma-carboxylation of GAS6 have not been determined directly, but are inferred from those worked out for protein S (Manfioletti et al. 1993).
R-HSA-163820 (Reactome) At the beginning of this reaction, 1 molecule of 'pro-protein Z, uncarboxylated', 13 molecules of 'Oxygen', 13 molecules of 'vitamin K hydroquinone', and 13 molecules of 'CO2' are present. At the end of this reaction, 1 molecule of 'pro-protein Z', 13 molecules of 'H2O', and 13 molecules of 'vitamin K epoxide' are present.

This reaction takes place in the 'endoplasmic reticulum membrane' and is mediated by the 'gamma-glutamyl carboxylase activity' of 'vitamin K-dependent gamma-carboxylase'.

R-HSA-163825 (Reactome) In this reaction, 1 molecule of 'pro-protein Z' is translocated from endoplasmic reticulum lumen to Golgi lumen.

This reaction takes place in the 'ER to Golgi transport vesicle'.

R-HSA-163843 (Reactome) The details of the gamma-carboxylation of GAS6 have not been determined directly, but are inferred from those worked out for protein S (Manfioletti et al. 1993).
R-HSA-204617 (Reactome) The reaction of EIF5A, spermidine, and NAD+ to form EIF5A(Dhp), 1,3-diaminopropane, and NADH + H+ is reversible in vitro. Under physiological conditions, the reverse reaction is probably minimized by the rapid, irreversible conversion of FIF5A(Dhp) to EIF5A(Hyp).
R-HSA-204647 (Reactome) Cytosolic deoxyhypusine synthase catalyzes the reaction of EIF5A protein, spermidine, and NAD+ to convert lysine-50 of EIF5A to deoxyhypusine, generating 1,3-diaminopropane and NADH + H+ in the process (Park 2006). Although the reaction is reversible, the reverse reaction is probably minimized under physiological conditions by the rapid, irreversible conversion of EIF5A(Dhp) to EIF5A(Hyp).
R-HSA-204662 (Reactome) Cytosolic deoxyhypusine hydroxylase catalyzes the irreversible conversion of peptidyl-deoxyhypusine to peptidyl-hypusine. The only known substrate for this enzyme is the modified lysine at residue 50 of eIF5A (Kang et al. 2007; Kim et al. 2006).
R-HSA-5358475 (Reactome) Cytosolic diphthamide biosynthesis protein 6 (DPH6) ligates an ammonium ion to diphthine-EEF2 to generate diphthamide-EEF2 in a reaction coupled to the hydrolysis of ATP to yield AMP and PPi (Su et al. 2012; Uthman et al. 2013; Wei et al. 2013).
R-HSA-5358484 (Reactome) Cytosolic diphthamide biosynthesis protein 5 (DPH5) transfers four methyl groups from S-adenosylmethionine (AdoMet) to elongation factor 2 (EEF2) whose histidine residue at position 715 has been conjugated with a 3-amino 3-carboxypropyl group, forming methylated diphthine EEF2 and S-adenosylhomocysteine (AdoHcy). DPH5 activity has been identified in cells of diverse eukaryotic species including humans and has been characterized in detail in budding yeast (Liu et al. 2004; Matteakis et al. 1992; Moehring & Moehring 1988).
R-HSA-5358494 (Reactome) The diphthamide biosynthesis protein 2 (DPH2) subunit of the cytosolic DPH1:DPH2:DPH3 complex catalyzes the transfer of a 3-amino-3-carboxypropyl group from S-adenosylmethionine (AdoMet) to residue 715 of nascent elongation factor 2 (EEF2), forming aminocarboxypropyl EEF2 and S-methylthioadenosine (MTAD). The association of DPH1, 2, and 3 to form a complex is inferred from studies of the homologous yeast proteins (Abdel-Fattah et al. 2013; Bar et al. 2008) and more limited studies of interactions among mouse and human ones (Liu et al. 2004). The identification of DPH2 as the catalytically active subunit of the DPH1:DPH2:DPH3 complex is inferred from the properties of the homologous Pyrococcus horikoshii protein (Zhang et al. 2010). DPH4 (DNAJC24) is needed for the reaction to occur but its exact role is unknown (Liu et al. 2004; Su et al. 2013). DPH3 is an electron donor for DPH1-DPH2 in the first step of diphthamide biosynthesis (Dong et al. 2014).
R-HSA-5367022 (Reactome) By analogy to the activity of its experimentally characterized budding yeast homolog (Lin et al. 2014; Schaffrath et al. 2014), cytosolic DPH7 is inferred to catalyze the removal of a methyl group of Me-diphthine EEF2, yielding diphthine EEF2.
SPMArrowR-HSA-204617 (Reactome)
SPMR-HSA-204647 (Reactome)
SUMF1:SUMF2ArrowR-HSA-1614336 (Reactome)
SUMF1R-HSA-1614336 (Reactome)
SUMF1mim-catalysisR-HSA-1614362 (Reactome)
SUMF2R-HSA-1614336 (Reactome)
SUMF2TBarR-HSA-1614362 (Reactome)
VKHQArrowR-HSA-159790 (Reactome)
VKHQR-HSA-159752 (Reactome)
VKHQR-HSA-159761 (Reactome)
VKHQR-HSA-159795 (Reactome)
VKHQR-HSA-159803 (Reactome)
VKHQR-HSA-159819 (Reactome)
VKHQR-HSA-159826 (Reactome)
VKHQR-HSA-163810 (Reactome)
VKHQR-HSA-163820 (Reactome)
VKOArrowR-HSA-159752 (Reactome)
VKOArrowR-HSA-159761 (Reactome)
VKOArrowR-HSA-159795 (Reactome)
VKOArrowR-HSA-159803 (Reactome)
VKOArrowR-HSA-159819 (Reactome)
VKOArrowR-HSA-159826 (Reactome)
VKOArrowR-HSA-163810 (Reactome)
VKOArrowR-HSA-163820 (Reactome)
VKOR-HSA-159790 (Reactome)
VKORC1mim-catalysisR-HSA-159790 (Reactome)
active ARSArrowR-HSA-1614362 (Reactome)
aminocarboxypropyl EEF2ArrowR-HSA-5358494 (Reactome)
aminocarboxypropyl EEF2R-HSA-5358484 (Reactome)
deoxyhypusine synthase tetramermim-catalysisR-HSA-204617 (Reactome)
deoxyhypusine synthase tetramermim-catalysisR-HSA-204647 (Reactome)
diphthine EEF2ArrowR-HSA-5367022 (Reactome)
diphthine EEF2R-HSA-5358475 (Reactome)
factor IX propeptideArrowR-HSA-159796 (Reactome)
factor VII propeptideArrowR-HSA-159868 (Reactome)
factor VIIArrowR-HSA-159868 (Reactome)
factor X light chain propeptideArrowR-HSA-159733 (Reactome)
factor XArrowR-HSA-159733 (Reactome)
nascent EEF2R-HSA-5358494 (Reactome)
pro-factor VIIArrowR-HSA-159783 (Reactome)
pro-factor VIIR-HSA-159761 (Reactome)
pro-factor VIIR-HSA-159868 (Reactome)
pro-factor X, uncarboxylatedR-HSA-159819 (Reactome)
pro-factor XArrowR-HSA-159757 (Reactome)
pro-factor XArrowR-HSA-159819 (Reactome)
pro-factor XR-HSA-159733 (Reactome)
pro-factor XR-HSA-159757 (Reactome)
pro-protein C, uncarboxylatedR-HSA-159795 (Reactome)
pro-protein CArrowR-HSA-159762 (Reactome)
pro-protein CArrowR-HSA-159795 (Reactome)
pro-protein CR-HSA-159762 (Reactome)
pro-protein CR-HSA-159771 (Reactome)
pro-prothrombin (factor II)R-HSA-159826 (Reactome)
protein CArrowR-HSA-159771 (Reactome)
prothrombin (factor II) propeptideArrowR-HSA-159728 (Reactome)
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