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Human Metabolome Database Version 2.5

 

Showing metabocard for Niacinamide (HMDB01406)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:48
Accession Number HMDB01406
Secondary Accession Numbers Not Available
Common Name Niacinamide
Description Niacinamide or vitamin B3 is an important compound functioning as a component of the coenzyme NAD. Its primary significance is in the prevention and/or cure of blacktongue and pellagra. Most animals cannot manufacture this compound in amounts sufficient to prevent nutritional deficiency and it therefore must be supplemented through dietary intake. Niacinamide is used to increase the effect of radiation therapy on tumor cells. Niacin (nicotinic acid) and niacinamide, while both labeled as vitamin B3 also have different applications. Niacinamide is useful in arthritis and early-onset type I diabetes while niacin is an effective reducer of high cholesterol levels.
Synonyms
  1. 3-Carbamoylpyridine
  2. 3-Pyridinecarboxamide
  3. 3-Pyridinecarboxylic acid amide
  4. Amid kyseliny nikotinove
  5. Amide PP
  6. Aminicotin
  7. Amixicotyn
  8. Amnicotin
  9. Austrovit PP
  10. Benicot
  11. Delonin Amide
  12. Dipegyl
  13. Dipigyl
  14. Endobion
  15. Factor pp
  16. Hansamid
  17. Inovitan PP
  18. Mediatric
  19. NAM
  20. Nandervit-N
  21. Niacevit
  22. Niacinamide
  23. Niamide
  24. Niavit PP
  25. Nicamide
  26. Nicamina
  27. Nicamindon
  28. Nicasir
  29. Nicobion
  30. Nicofort
  31. Nicogen
  32. Nicomidol
  33. Nicosan 2
  34. Nicosylamide
  35. Nicota
  36. Nicotamide
  37. Nicotilamide
  38. Nicotililamido
  39. Nicotinamida
  40. Nicotinamide
  41. Nicotinamidum
  42. Nicotine acid amide
  43. Nicotine amide
  44. Nicotinic acid amide
  45. Nicotinic amide
  46. Nicotinsaureamid
  47. Nicotol
  48. Nicotylamide
  49. Nicotylamidum
  50. Nicovel
  51. Nicovit
  52. Nicovitina
  53. Nicovitol
  54. Nicozymin
  55. Nictoamide
  56. Niko-tamin
  57. Nikotinamid
  58. Nikotinsaeureamid
  59. Niocinamide
  60. Niozymin
  61. PP-Faktor
  62. Papulex
  63. Pelmin
  64. Pelmine
  65. Pelonin amide
  66. Propamine A
  67. Pyridine-3-carboxylic acid amide
  68. Savacotyl
  69. Vi-Nicotyl
  70. Vi-noctyl
  71. Vitamin B3
  72. Vitamin PP
  73. Witamina PP
  74. acid amide
  75. b-Pyridinecarboxamide
  76. beta-Pyridinecarboxamide
  77. m-(Aminocarbonyl)pyridine
Chemical IUPAC Name pyridine-3-carboxamide
Chemical Formula C6H6N2O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amines
Class
  • Cyclic Amines
Sub Class
  • Heterocyclic amines
Family
  • Mammalian Metabolite
Species
  • primary carboxylic acid amide
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Nicotinate and nicotinamide metabolism
Application
Source
  • Endogenous
Average Molecular Weight 122.125
Monoisotopic Molecular Weight 122.048012
Isomeric SMILES NC(=O)C1=CN=CC=C1
Canonical SMILES NC(=O)C1=CN=CC=C1
KEGG Compound ID C00153 Link Image
BioCyc ID NIACINAMIDE Link Image
BiGG ID 34058 Link Image
Wikipedia Link Niacinamide Link Image
NuGOwiki Link HMDB01406 Link Image
Metagene Link HMDB01406 Link Image
METLIN ID 1497 Link Image
PubChem Compound 936 Link Image
PubChem Substance 866551 Link Image
ChEBI ID 17154 Link Image
CAS Registry Number 98-92-0
InChI Identifier InChI=1/C6H6N2O/c7-6(9)5-2-1-3-8-4-5/h1-4H,(H2,7,9)
Synthesis Reference Galat, Alexander. Nicotinamide from nicotinonitrile by catalytic hydration. Journal of the American Chemical Society (1948), 70 3945.
Melting Point (Experimental) 130 oC
Experimental Water Solubility 500 mg/mL at 25 oC [MERCK INDEX (1996)] Source: PhysProp
Predicted Water Solubility 50.100002 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -0.37 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -0.45 [Predicted by ALOGPS]; -0.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID 1DMA Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Bladder
Fibroblasts
Neuron
Pancreas
Placenta
Skin
Spleen
Stratum Corneum
Concentrations (Normal)
Biofluid Blood
Value 0.44 +/- 0.0054 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Stratford MR, Dennis MF: High-performance liquid chromatographic determination of nicotinamide and its metabolites in human and murine plasma and urine. J Chromatogr. 1992 Nov 6;582(1-2):145-51. [PubMed Link Image]
Biofluid Urine
Value 0.30 +/- 0.51 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Nicotinate and Nicotinamide Metabolism SMP00048 Link Image map00760 Link Image
General References
  1. Draelos ZD, Ertel K, Berge C: Niacinamide-containing facial moisturizer improves skin barrier and benefits subjects with rosacea. Cutis. 2005 Aug;76(2):135-41. [PubMed Link Image]
  2. Soma Y, Kashima M, Imaizumi A, Takahama H, Kawakami T, Mizoguchi M: Moisturizing effects of topical nicotinamide on atopic dry skin. Int J Dermatol. 2005 Mar;44(3):197-202. [PubMed Link Image]
  3. Final report of the safety assessment of niacinamide and niacin. Int J Toxicol. 2005;24 Suppl 5:1-31. [PubMed Link Image]
  4. Draelos ZD, Matsubara A, Smiles K: The effect of 2% niacinamide on facial sebum production. J Cosmet Laser Ther. 2006 Jun;8(2):96-101. [PubMed Link Image]
  5. Schulpis K, Spiropoulos A, Gavrili S, Karikas G, Grigori C, Vlachos G, Papassotiriou I: Maternal - neonatal folate and vitamin B12 serum concentrations in Greeks and in Albanian immigrants. J Hum Nutr Diet. 2004 Oct;17(5):443-8. [PubMed Link Image]
  6. Yang L, Yao Y, Shi Y, Wang X, Shi J: [Expression of nicotinamide edenine dinucleotide dehydrogenase gene in placenta of patients with pregnancy induced hypertension] Zhonghua Fu Chan Ke Za Zhi. 2002 Nov;37(11):660-2. [PubMed Link Image]
  7. Sonee M, Martens JR, Mukherjee SK: Nicotinamide protects HCN2 cells from the free radical generating toxin, tertiary butylhydroperoxide (t-BuOOH). Neurotox Res. 2002 Nov;4(7-8):595-599. [PubMed Link Image]
  8. Bayraktar F, Dereli D, Ozgen AG, Yilmaz C: Plasma homocysteine levels in polycystic ovary syndrome and congenital adrenal hyperplasia. Endocr J. 2004 Dec;51(6):601-8. [PubMed Link Image]
  9. Sonee M, Martens JR, Evers MR, Mukherjee SK: The effect of tertiary butylhydroperoxide and nicotinamide on human cortical neurons. Neurotoxicology. 2003 Jun;24(3):443-8. [PubMed Link Image]
  10. Anisimov AG, Bolotnikov IA: [Nicotinamide decreases DNA destabilization in K562 cells treated with AlF(-4)] Tsitologiia. 1997;39(9):822-8. [PubMed Link Image]
  11. Matuoka K, Chen KY, Takenawa T: Rapid reversion of aging phenotypes by nicotinamide through possible modulation of histone acetylation. Cell Mol Life Sci. 2001 Dec;58(14):2108-16. [PubMed Link Image]
  12. Bartalena L, Tanda ML, Piantanida E, Lai A: Oxidative stress and Graves' ophthalmopathy: in vitro studies and therapeutic implications. Biofactors. 2003;19(3-4):155-63. [PubMed Link Image]
  13. Bissett DL, Oblong JE, Berge CA: Niacinamide: A B vitamin that improves aging facial skin appearance. Dermatol Surg. 2005 Jul;31(7 Pt 2):860-5; discussion 865. [PubMed Link Image]
  14. Baeza N, Moriscot C, Figarella C, Guy-Crotte O, Vialettes B: Reg protein: a potential beta-cell-specific growth factor? Diabetes Metab. 1996 Jul;22(4):229-34. [PubMed Link Image]
  15. Hoskin PJ, Rojas AM, Phillips H, Saunders MI: Acute and late morbidity in the treatment of advanced bladder carcinoma with accelerated radiotherapy, carbogen, and nicotinamide. Cancer. 2005 Jun 1;103(11):2287-97. [PubMed Link Image]
  16. Rembold CM: Combination therapy of dyslipidemia in non-insulin-dependent diabetes mellitus and the metabolic syndrome. Curr Diab Rep. 2004 Oct;4(5):330-4. [PubMed Link Image]
  17. Kawasaki E, Abiru N, Eguchi K: Prevention of type 1 diabetes: from the view point of beta cell damage. Diabetes Res Clin Pract. 2004 Dec;66 Suppl 1:S27-32. [PubMed Link Image]
  18. Rybak ME, Pfeiffer CM: Clinical analysis of vitamin B(6): determination of pyridoxal 5'-phosphate and 4-pyridoxic acid in human serum by reversed-phase high-performance liquid chromatography with chlorite postcolumn derivatization. Anal Biochem. 2004 Oct 15;333(2):336-44. [PubMed Link Image]
  19. Wikipedia Link Image
Metabolic Enzymes
  1. Nicotinamide N-methyltransferase
  2. Purine nucleoside phosphorylase
  3. Tankyrase-2
  4. NAD-dependent deacetylase sirtuin-6
  5. Poly [ADP-ribose] polymerase 3
  6. Ecto-ADP-ribosyltransferase 3
  7. GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1
  8. Tankyrase-1
  9. Poly [ADP-ribose] polymerase 1
  10. ADP-ribosyl cyclase 2
  11. Poly [ADP-ribose] polymerase 2
  12. ADP-ribosyl cyclase 1
  13. Ecto-ADP-ribosyltransferase 4
  14. Pre-B-cell colony enhancing factor 1
  15. Nicotinamide phosphoribosyltransferase
  16. ART5 protein precursor (ADP-ribosyltransferase 5, isoform CRA_b)
  17. Poly (ADP-ribose) polymerase family, member 4
  18. cDNA, FLJ92858, highly similar to Homo sapiens bone marrow stromal cell antigen 1 (BST1), mRNA (Bone marrow stromal cell antigen 1)
  19. Poly (ADP-ribose) polymerase family, member 1 (Poly (ADP-ribose) polymerase family, member 1, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5660
Enzyme 1 Name Nicotinamide N-methyltransferase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name NNMT
Enzyme 1 Protein Sequence >Nicotinamide N-methyltransferase
MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLI
DIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGN
RVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRAL
RNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQ
SYSSTMANNEGLFSLVARKLSRPL
Enzyme 1 Number of Residues 264
Enzyme 1 Molecular Weight 29573.7
Enzyme 1 Theoretical pI 5.45
Enzyme 1 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 1 General Function Involved in methyltransferase activity
Enzyme 1 Specific Function Catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds
Enzyme 1 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 1 Reactions
  • S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide [RN:R01269]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 494989 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P40261 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name NNMT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >795 bp
ATGGAATCAGGCTTCACCTCCAAGGACACCTATCTAAGCCATTTTAACCCTCGGGATTAC
CTAGAAAAATATTACAAGTTTGGTTCTAGGCACTCTGCAGAAAGCCAGATTCTTAAGCAC
CTTCTGAAAAATCTTTTCAAGATATTCTGCCTAGACGGTGTGAAGGGAGACCTGCTGATT
GACATCGGCTCTGGCCCCACTATCTATCAGCTCCTCTCTGCTTGTGAATCCTTTAAGGAG
ATCGTCGTCACTGACTACTCAGACCAGAACCTGCAGGAGCTGGAGAAGTGGCTGAAGAAA
GAGCCAGAGGCCTTTGACTGGTCCCCAGTGGTGACCTATGTGTGTGATCTTGAAGGGAAC
AGAGTCAAGGGTCCAGAGAAGGAGGAGAAGTTGAGACAGGCGGTCAAGCAGGTGCTGAAG
TGTGATGTGACTCAGAGCCAGCCACTGGGGGCCGTCCCCTTACCCCCGGCTGACTGCGTG
CTCAGCACACTGTGTCTGGATGCCGCCTGCCCAGACCTCCCCACCTACTGCAGGGCGCTC
AGGAACCTCGGCAGCCTACTGAAGCCAGGGGGCTTCCTGGTGATCATGGATGCGCTCAAG
AGCAGCTACTACATGATTGGTGAGCAGAAGTTCTCCAGCCTCCCCCTGGGCCGGGAGGCA
GTAGAGGCTGCTGTGAAAGAGGCTGGCTACACAATCGAATGGTTTGAGGTGATCTCGCAA
AGTTATTCTTCCACCATGGCCAACAACGAAGGACTTTTCTCCCTGGTGGCGAGGAAGCTG
AGCAGACCCCTGTGA
Enzyme 1 GenBank Gene ID U08021 Link Image
Enzyme 1 GeneCard ID NNMT Link Image
Enzyme 1 GenAtlas ID NNMT Link Image
Enzyme 1 HGNC ID HGNC:7861 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 11q23.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Aksoy S, Szumlanski CL, Weinshilboum RM: Human liver nicotinamide N-methyltransferase. cDNA cloning, expression, and biochemical characterization. J Biol Chem. 1994 May 20;269(20):14835-40. [PubMed Link Image]
  2. Aksoy S, Brandriff BF, Ward A, Little PF, Weinshilboum RM: Human nicotinamide N-methyltransferase gene: molecular cloning, structural characterization and chromosomal localization. Genomics. 1995 Oct 10;29(3):555-61. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5805
Enzyme 2 Name Purine nucleoside phosphorylase
Enzyme 2 Synonyms
  1. PNP
  2. Inosine phosphorylase
Enzyme 2 Gene Name PNP
Enzyme 2 Protein Sequence >Purine nucleoside phosphorylase
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Enzyme 2 Number of Residues 289
Enzyme 2 Molecular Weight 32117.7
Enzyme 2 Theoretical pI 6.95
Enzyme 2 GO Classification
Function
  • catalytic activity
  • purine-nucleoside phosphorylase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside metabolic process
Component
Enzyme 2 General Function Involved in purine-nucleoside phosphorylase activity
Enzyme 2 Specific Function Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate [RN:R08368]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 35565 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P00491 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PNPH_HUMAN Link Image
Enzyme 2 PDB ID 1RT9 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >870 bp
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
Enzyme 2 GenBank Gene ID X00737 Link Image
Enzyme 2 GeneCard ID PNP Link Image
Enzyme 2 GenAtlas ID PNP Link Image
Enzyme 2 HGNC ID HGNC:7892 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 14q13.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. [PubMed Link Image]
  2. Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. [PubMed Link Image]
  3. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [PubMed Link Image]
  9. Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [PubMed Link Image]
  10. Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6189
Enzyme 3 Name Tankyrase-2
Enzyme 3 Synonyms
  1. TANK2
  2. Poly [ADP-ribose] polymerase 5B
  3. TNKS-2
  4. TRF1-interacting ankyrin-related ADP-ribose polymerase 2
  5. Tankyrase II
  6. Tankyrase-like protein
  7. Tankyrase-related protein
Enzyme 3 Gene Name TNKS2
Enzyme 3 Protein Sequence >Tankyrase-2
MSGRRCAGGGAACASAAAEAVEPAARELFEACRNGDVERVKRLVTPEKVNSRDTAGRKST
PLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNAR
DNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSAKAVLTGEYKKDE
LLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAK
DKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYG
ADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREADVTRIKKHLSLEMVNFKH
PQTHETALHCAAASPYPKRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVV
KHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQMGNENVQQL
LQEGISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVS
VVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAA
AKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAALLDAAKKGCLAR
VKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAA
SYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQT
PLDLVSADDVSALLTAAMPPSALPSCYKPQVLNGVRSPGATADALSSGPSSPSSLSAASS
LDNLSGSFSELSSVVSSSGTEGASSLEKKEVPGVDFSITQFVRNLGLEHLMDIFEREQIT
LDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISGQQGLNPYLTLNTSGSGTILIDLSP
DDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEEN
HNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTG
CPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYV
IYRGEQAYPEYLITYQIMRPEGMVDG
Enzyme 3 Number of Residues 1166
Enzyme 3 Molecular Weight 126916.9
Enzyme 3 Theoretical pI 7.20
Enzyme 3 GO Classification
Function
  • NAD+ ADP-ribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
Component
Enzyme 3 General Function Involved in NAD+ ADP-ribosyltransferase activity
Enzyme 3 Specific Function May regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Has PARP activity and can modify TRF1, and thereby contribute to the regulation of telomere length
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ [RN:R04176]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 12005976 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9H2K2 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name TNKS2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >3501 bp
ATGTCGGGTCGCCGCTGCGCCGGCGGGGGAGCGGCCTGCGCGAGCGCCGCGGCCGAGGCC
GTGGAGCCGGCCGCCCGAGAGCTGTTCGAGGCGTGCCGCAACGGGGACGTGGAACGAGTC
AAGAGGCTGGTGACGCCTGAGAAGGTGAACAGCCGCGACACGGCGGGCAGGAAATCCACC
CCGCTGCACTTCGCCGCAGGTTTTGGGCGGAAAGACGTAGTTGAATATTTGCTTCAGAAT
GGTGCAAATGTCCAAGCACGTGATGATGGGGGCCTTATTCCTCTTCATAATGCATGCTCT
TTTGGTCATGCTGAAGTAGTCAATCTCCTTTTGCGACATGGTGCAGACCCCAATGCTCGA
GATAATTGGAATTATACTCCTCTCCATGAAGCTGCAATTAAAGGAAAGATTGATGTTTGC
ATTGTGCTGTTACAGCATGGAGCTGAGCCAACCATCCGAAATACAGATGGAAGGACAGCA
TTGGATTTAGCAGATCCATCTGCCAAAGCAGTGCTTACTGGTGAATATAAGAAAGATGAA
CTCTTAGAAAGTGCCAGGAGTGGCAATGAAGAAAAAATGATGGCTCTACTCACACCATTA
AATGTCAACTGCCACGCAAGTGATGGCAGAAAGTCAACTCCATTACATTTGGCAGCAGGA
TATAACAGAGTAAAGATTGTACAGCTGTTACTGCAACATGGAGCTGATGTCCATGCTAAA
GATAAAGGTGATCTGGTACCATTACACAATGCCTGTTCTTATGGTCATTATGAAGTAACT
GAACTTTTGGTCAAGCATGGTGCCTGTGTAAATGCAATGGACTTGTGGCAATTCACTCCT
CTTCATGAGGCAGCTTCTAAGAACAGGGTTGAAGTATGTTCTCTTCTCTTAAGTTATGGT
GCAGACCCAACACTGCTCAATTGTCACAATAAAAGTGCTATAGACTTGGCTCCCACACCA
CAGTTAAAAGAAAGATTAGCATATGAATTTAAAGGCCACTCGTTGCTGCAAGCTGCACGA
GAAGCTGATGTTACTCGAATCAAAAAACATCTCTCTCTGGAAATGGTGAATTTCAAGCAT
CCTCAAACACATGAAACAGCATTGCATTGTGCTGCTGCATCTCCATATCCCAAAAGAAAG
CAAATATGTGAACTGTTGCTAAGAAAAGGAGCAAACATCAATGAAAAGACTAAAGAATTC
TTGACTCCTCTGCACGTGGCATCTGAGAAAGCTCATAATGATGTTGTTGAAGTAGTGGTG
AAACATGAAGCAAAGGTTAATGCTCTGGATAATCTTGGTCAGACTTCTCTACACAGAGCT
GCATATTGTGGTCATCTACAAACCTGCCGCCTACTCCTGAGCTATGGGTGTGATCCTAAC
ATTATATCCCTTCAGGGCTTTACTGCTTTACAGATGGGAAATGAAAATGTACAGCAACTC
CTCCAAGAGGGTATCTCATTAGGTAATTCAGAGGCAGACAGACAATTGCTGGAAGCTGCA
AAGGCTGGAGATGTCGAAACTGTAAAAAAACTGTGTACTGTTCAGAGTGTCAACTGCAGA
GACATTGAAGGGCGTCAGTCTACACCACTTCATTTTGCAGCTGGGTATAACAGAGTGTCC
GTGGTGGAATATCTGCTACAGCATGGAGCTGATGTGCATGCTAAAGATAAAGGAGGCCTT
GTACCTTTGCACAATGCATGTTCTTATGGACATTATGAAGTTGCAGAACTTCTTGTTAAA
CATGGAGCAGTAGTTAATGTAGCTGATTTATGGAAATTTACACCTTTACATGAAGCAGCA
GCAAAAGGAAAATATGAAATTTGCAAACTTCTGCTCCAGCATGGTGCAGACCCTACAAAA
AAAAACAGGGATGGAAATACTCCTTTGGATCTTGTTAAAGATGGAGATACAGATATTCAA
GATCTGCTTAGGGGAGATGCAGCTTTGCTAGATGCTGCCAAGAAGGGTTGTTTAGCCAGA
GTGAAGAAGTTGTCTTCTCCTGATAATGTAAATTGCCGCGATACCCAAGGCAGACATTCA
ACACCTTTACATTTAGCAGCTGGTTATAATAATTTAGAAGTTGCAGAGTATTTGTTACAA
CACGGAGCTGATGTGAATGCCCAAGACAAAGGAGGACTTATTCCTTTACATAATGCAGCA
TCTTACGGGCATGTAGATGTAGCAGCTCTACTAATAAAGTATAATGCATGTGTCAATGCC
ACGGACAAATGGGCTTTCACACCTTTGCACGAAGCAGCCCAAAAGGGACGAACACAGCTT
TGTGCTTTGTTGCTAGCCCATGGAGCTGACCCGACTCTTAAAAATCAGGAAGGACAAACA
CCTTTAGATTTAGTTTCAGCAGATGATGTCAGCGCTCTTCTGACAGCAGCCATGCCCCCA
TCTGCTCTGCCCTCTTGTTACAAGCCTCAAGTGCTCAATGGTGTGAGAAGCCCAGGAGCC
ACTGCAGATGCTCTCTCTTCAGGTCCATCTAGCCCATCAAGCCTTTCTGCAGCCAGCAGT
CTTGACAACTTATCTGGGAGTTTTTCAGAACTGTCTTCAGTAGTTAGTTCAAGTGGAACA
GAGGGTGCTTCCAGTTTGGAGAAAAAGGAGGTTCCAGGAGTAGATTTTAGCATAACTCAA
TTCGTAAGGAATCTTGGACTTGAGCACCTAATGGATATATTTGAGAGAGAACAGATCACT
TTGGATGTATTAGTTGAGATGGGGCACAAGGAGCTGAAGGAGATTGGAATCAATGCTTAT
GGACATAGGCACAAACTAATTAAAGGAGTCGAGAGACTTATCTCCGGACAACAAGGTCTT
AACCCATATTTAACTTTGAACACCTCTGGTAGTGGAACAATTCTTATAGATCTGTCTCCT
GATGATAAAGAGTTTCAGTCTGTGGAGGAAGAGATGCAAAGTACAGTTCGAGAGCACAGA
GATGGAGGTCATGCAGGTGGAATCTTCAACAGATACAATATTCTCAAGATTCAGAAGGTT
TGTAACAAGAAACTATGGGAAAGATACACTCACCGGAGAAAAGAAGTTTCTGAAGAAAAC
CACAACCATGCCAATGAACGAATGCTATTTCATGGGTCTCCTTTTGTGAATGCAATTATC
CACAAAGGCTTTGATGAAAGGCATGCGTACATAGGTGGTATGTTTGGAGCTGGCATTTAT
TTTGCTGAAAACTCTTCCAAAAGCAATCAATATGTATATGGAATTGGAGGAGGTACTGGG
TGTCCAGTTCACAAAGACAGATCTTGTTACATTTGCCACAGGCAGCTGCTCTTTTGCCGG
GTAACCTTGGGAAAGTCTTTCCTGCAGTTCAGTGCAATGAAAATGGCACATTCTCCTCCA
GGTCATCACTCAGTCACTGGTAGGCCCAGTGTAAATGGCCTAGCATTAGCTGAATATGTT
ATTTACAGAGGAGAACAGGCTTATCCTGAGTATTTAATTACTTACCAGATTATGAGGCCT
GAAGGTATGGTCGATGGATAA
Enzyme 3 GenBank Gene ID AF264912 Link Image
Enzyme 3 GeneCard ID TNKS2 Link Image
Enzyme 3 GenAtlas ID TNKS2 Link Image
Enzyme 3 HGNC ID HGNC:15677 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 10q23.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Monz D, Munnia A, Comtesse N, Fischer U, Steudel WI, Feiden W, Glass B, Meese EU: Novel tankyrase-related gene detected with meningioma-specific sera. Clin Cancer Res. 2001 Jan;7(1):113-9. [PubMed Link Image]
  2. Kuimov AN, Kuprash DV, Petrov VN, Vdovichenko KK, Scanlan MJ, Jongeneel CV, Lagarkova MA, Nedospasov SA: Cloning and characterization of TNKL, a member of tankyrase gene family. Genes Immun. 2001 Feb;2(1):52-5. [PubMed Link Image]
  3. Lyons RJ, Deane R, Lynch DK, Ye ZS, Sanderson GM, Eyre HJ, Sutherland GR, Daly RJ: Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14. J Biol Chem. 2001 May 18;276(20):17172-80. Epub 2001 Feb 22. [PubMed Link Image]
  4. Kaminker PG, Kim SH, Taylor RD, Zebarjadian Y, Funk WD, Morin GB, Yaswen P, Campisi J: TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression. J Biol Chem. 2001 Sep 21;276(38):35891-9. Epub 2001 Jul 13. [PubMed Link Image]
  5. Sbodio JI, Lodish HF, Chi NW: Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase). Biochem J. 2002 Feb 1;361(Pt 3):451-9. [PubMed Link Image]
  6. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  7. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  8. Cook BD, Dynek JN, Chang W, Shostak G, Smith S: Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres. Mol Cell Biol. 2002 Jan;22(1):332-42. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6191
Enzyme 4 Name NAD-dependent deacetylase sirtuin-6
Enzyme 4 Synonyms
  1. SIR2-like protein 6
Enzyme 4 Gene Name SIRT6
Enzyme 4 Protein Sequence >NAD-dependent deacetylase sirtuin-6
MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVWQSSSVVFHTGAGISTASG
IPDFRGPHGVWTMEERGLAPKFDTTFESARPTQTHMALVQLERVGLLRFLVSQNVDGLHV
RSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKATGRLCTVAKARGLRACRGE
LRDTILDWEDSLPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVN
LQPTKHDRHADLRIHGYVDEVMTRLMKHLGLEIPAWDGPRVLERALPPLPRPPTPKLEPK
EESPTRINGSIPAGPKQEPCAQHNGSEPASPKRERPTSPAPHRPPKRVKAKAVPS
Enzyme 4 Number of Residues 355
Enzyme 4 Molecular Weight 39118.5
Enzyme 4 Theoretical pI 9.67
Enzyme 4 GO Classification
Function
  • NAD binding
  • NAD or NADH binding
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
  • ion binding
  • metal ion binding
  • nucleotide binding
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • cellular process
  • chromatin silencing
  • gene silencing
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid deacetylation
  • protein modification process
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
Component
Enzyme 4 General Function Involved in zinc ion binding
Enzyme 4 Specific Function NAD-dependent protein deacetylase. Has deacetylase activity towards 'Lys-9' and 'Lys-56' of histone H3. Modulates acetylation of histone H3 in telomeric chromatin during the S- phase of the cell cycle. Deacetylates 'Lys-9' of histone H3 at NF- kappa-B target promoters and may down-regulate the expression of a subset of NF-kappa-B target genes. Deacetylation of nucleosomes interferes with RELA binding to target DNA. May be required for the association of WRN with telomeres during S-phase and for normal telomere maintenance. Required for genomic stability. Required for normal IGF1 serum levels and normal glucose homeostasis. Modulates cellular senescence and apoptosis. Regulates the production of TNF protein
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 7243749 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q8N6T7 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SIRT6_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1068 bp
ATGTCGGTGAATTACGCGGCGGGGCTGTCGCCGTACGCGGACAAGGGCAAGTGCGGCCTC
CCGGAGATCTTCGACCCCCCGGAGGAGCTGGAGCGGAAGGTGTGGGAACTGGCGAGGCTG
GTCTGGCAGTCTTCCAGTGTGGTGTTCCACACGGGTGCCGGCATCAGCACTGCCTCTGGC
ATCCCCGACTTCAGGGGTCCCCACGGAGTCTGGACCATGGAGGAGCGAGGTCTGGCCCCC
AAGTTCGACACCACCTTTGAGAGCGCGCGGCCCACGCAGACCCACATGGCGCTGGTGCAG
CTGGAGCGCGTGGGCCTCCTCCGCTTCCTGGTCAGCCAGAACGTGGACGGGCTCCATGTG
CGCTCAGGCTTCCCCAGGGACAAACTGGCAGAGCTCCACGGGAACATGTTTGTGGAAGAA
TGTGCCAAGTGTAAGACGCAGTACGTCCGAGACACAGTCGTGGGCACCATGGGCCTGAAG
GCCACGGGCCGGCTCTGCACCGTGGCTAAGGCAAGGGGGCTGCGAGCCTGCAGGGGAGAG
CTGAGGGACACCATCCTAGACTGGGAGGACTCCCTGCCCGACCGGGACCTGGCACTCGCC
GATGAGGCCAGCAGGAACGCCGACCTGTCCATCACGCTGGGTACATCGCTGCAGATCCGG
CCCAGCGGGAACCTGCCGCTGGCTACCAAGCGCCGGGGAGGCCGCCTGGTCATCGTCAAC
CTGCAGCCCACCAAGCACGACCGCCATGCTGACCTCCGCATCCATGGCTACGTTGACGAG
GTCATGACCCGGCTCATGGAGCACCTGGGGCTGGAGATCCCCGCCTGGGACGGCCCCCGT
GTGCTGGAGAGGGCGCTGCCACCCCTGCCCCGCCCGCCCACCCCCAAGCTGGAGCCCAAG
GAGGAATCTCCCACCCGGATCAACGGCTCTATCCCCGCCGGCCCCAAGCAGGAGCCCTGC
GCCCAGCACAACGGCTCAGAGCCCGCCAGCCCCAAACGGGAGCGGCCCACCAGCCCTGCC
CCCCACAGACCCCCCAAAAGGGTGAAGGCCAAGGCGGTCCCCAGCTGA
Enzyme 4 GenBank Gene ID AF233396 Link Image
Enzyme 4 GeneCard ID SIRT6 Link Image
Enzyme 4 GenAtlas ID SIRT6 Link Image
Enzyme 4 HGNC ID HGNC:14934 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 19p13.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Frye RA: Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun. 2000 Jul 5;273(2):793-8. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Michishita E, Park JY, Burneskis JM, Barrett JC, Horikawa I: Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell. 2005 Oct;16(10):4623-35. Epub 2005 Aug 3. [PubMed Link Image]
  6. Michishita E, McCord RA, Berber E, Kioi M, Padilla-Nash H, Damian M, Cheung P, Kusumoto R, Kawahara TL, Barrett JC, Chang HY, Bohr VA, Ried T, Gozani O, Chua KF: SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature. 2008 Mar 27;452(7186):492-6. Epub 2008 Mar 12. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Kawahara TL, Michishita E, Adler AS, Damian M, Berber E, Lin M, McCord RA, Ongaigui KC, Boxer LD, Chang HY, Chua KF: SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span. Cell. 2009 Jan 9;136(1):62-74. [PubMed Link Image]
  10. Michishita E, McCord RA, Boxer LD, Barber MF, Hong T, Gozani O, Chua KF: Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6. Cell Cycle. 2009 Aug 15;8(16):2664-6. Epub 2009 Aug 26. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6193
Enzyme 5 Name Poly [ADP-ribose] polymerase 3
Enzyme 5 Synonyms
  1. PARP-3
  2. hPARP-3
  3. IRT1
  4. NAD(+) ADP-ribosyltransferase 3
  5. ADPRT-3
  6. Poly[ADP-ribose] synthase 3
  7. pADPRT-3
Enzyme 5 Gene Name PARP3
Enzyme 5 Protein Sequence >Poly [ADP-ribose] polymerase 3
MAPKPKPWVQTEGPEKKKGRQAGREEDPFRSTAEALKAIPAEKRIIRVDPTCPLSSNPGT
QVYEDYNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNHWGRVGEVGQSKINHFTRLED
AKKDFEKKFREKTKNNWAERDHFVSHPGKYTLIEVQAEDEAQEAVVKVDRGPVRTVTKRV
QPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEAL
KGPTDGGQSLEELSSHFYTVIPHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQA
VSEQEKTVEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQTGSNHRCPTLQHIWK
VNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHSGGRVGKGIYFASENS
KSAGYVIGMKCGAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPT
QDTELELDGQQVVVPQGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVHL
Enzyme 5 Number of Residues 533
Enzyme 5 Molecular Weight 60069.7
Enzyme 5 Theoretical pI 6.73
Enzyme 5 GO Classification
Function
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
Component
Enzyme 5 General Function Involved in NAD+ ADP-ribosyltransferase activity
Enzyme 5 Specific Function Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ [RN:R04176]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 158634482 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9Y6F1 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PARP3_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1602 bp
ATGGCTCCAAAGCCGAAGCCCTGGGTACAGACTGAGGGCCCTGAGAAGAAGAAGGGCCGG
CAGGCAGGAAGGGAGGAGGACCCCTTCCGCTCCACCGCTGAGGCCCTCAAGGCCATACCC
GCAGAGAAGCGCATAATCCGCGTGGATCCAACATGTCCACTCAGCAGCAACCCCGGGACC
CAGGTGTATGAGGACTACAACTGCACCCTGAACCAGACCAACATCGAGAACAACAACAAC
AAGTTCTACATCATCCAGCTGCTCCAAGACAGCAACCGCTTCTTCACCTGCTGGAACCAC
TGGGGCCGTGTGGGAGAGGTCGGCCAGTCAAAGATCAACCACTTCACAAGGCTAGAAGAT
GCAAAGAAGGACTTTGAGAAGAAATTTCGGGAAAAGACCAAGAACAACTGGGCAGAGCGG
GACCACTTTGTGTCTCACCCGGGCAAGTACACACTTATCGAAGTACAGGCAGAGGATGAG
GCCCAGGAAGCTGTGGTGAAGGTGGACAGAGGCCCAGTGAGGACTGTGACTAAGCGGGTG
CAGCCCTGCTCCCTGGACCCAGCCACGCAGAAGCTCATCACTAACATCTTCAGCAAGGAG
ATGTTCAAGAACACCATGGCCCTCATGGACCTGGATGTGAAGAAGATGCCCCTGGGAAAG
CTGAGCAAGCAACAGATTGCACGGGGTTTCGAGGCCTTGGAGGCGCTGGAGGAGGCCCTG
AAAGGCCCCACGGATGGTGGCCAAAGCCTGGAGGAGCTGTCCTCACACTTTTACACCGTC
ATCCCGCACAACTTCGGCCACAGCCAGCCCCCGCCCATCAATTCCCCTGAGCTTCTGCAG
GCCAAGAAGGACATGCTGCTGGTGCTGGCGGACATCGAGCTGGCCCAGGCCCTGCAGGCA
GTCTCTGAGCAGGAGAAGACGGTGGAGGAGGTGCCACACCCCCTGGACCGAGACTACCAG
CTTCTCAAGTGCCAGCTGCAGCTGCTAGACTCTGGAGCACCTGAGTACAAGGTGATACAG
ACCTACTTAGAACAGACTGGCAGCAACCACAGGTGCCCTACACTTCAACACATCTGGAAA
GTAAACCAAGAAGGGGAGGAAGACAGATTCCAGGCCCACTCCAAACTGGGTAATCGGAAG
CTGCTGTGGCATGGCACCAACATGGCCGTGGTGGCCGCCATCCTCACTAGTGGGCTCCGC
ATCATGCCACATTCTGGTGGGCGTGTTGGCAAGGGCATCTACTTTGCCTCAGAGAACAGC
AAGTCAGCTGGATATGTTATTGGCATGAAGTGTGGGGCCCACCATGTCGGCTACATGTTC
CTGGGTGAGGTGGCCCTGGGCAGAGAGCACCATATCAACACGGACAACCCCAGCTTGAAG
AGCCCACCTCCTGGCTTCGACAGTGTCATTGCCCGAGGCCACACCGAGCCTGATCCGACC
CAGGACACTGAGTTGGAGCTGGATGGCCAGCAAGTGGTGGTGCCCCAGGGCCAGCCTGTG
CCCTGCCCAGAGTTCAGCAGCTCCACATTCTCCCAGAGCGAGTACCTCATCTACCAGGAG
AGCCAGTGTCGCCTGCGCTACCTGCTGGAGGTCCACCTCTGA
Enzyme 5 GenBank Gene ID NM_005485.4 Link Image
Enzyme 5 GeneCard ID PARP3 Link Image
Enzyme 5 GenAtlas ID PARP3 Link Image
Enzyme 5 HGNC ID HGNC:273 Link Image
Enzyme 5 Chromosome Location 3
Enzyme 5 Locus 3p21.31-p21.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Johansson M: A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues. Genomics. 1999 May 1;57(3):442-5. [PubMed Link Image]
  2. Augustin A, Spenlehauer C, Dumond H, Menissier-De Murcia J, Piel M, Schmit AC, Apiou F, Vonesch JL, Kock M, Bornens M, De Murcia G: PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression. J Cell Sci. 2003 Apr 15;116(Pt 8):1551-62. [PubMed Link Image]
  3. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Rouleau M, McDonald D, Gagne P, Ouellet ME, Droit A, Hunter JM, Dutertre S, Prigent C, Hendzel MJ, Poirier GG: PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery. J Cell Biochem. 2007 Feb 1;100(2):385-401. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6194
Enzyme 6 Name Ecto-ADP-ribosyltransferase 3
Enzyme 6 Synonyms
  1. Mono(ADP-ribosyl)transferase 3
  2. NAD(P)(+)--arginine ADP-ribosyltransferase 3
Enzyme 6 Gene Name ART3
Enzyme 6 Protein Sequence >Ecto-ADP-ribosyltransferase 3
MKTGHFEIVTMLLATMILVDIFQVKAEVLDMADNAFDDEYLKCTDRMEIKYVPQLLKEEK
ASHQQLDTVWENAKAKWAARKTQIFLPMNFKDNHGIALMAYISEAQEQTPFYHLFSEAVK
MAGQSREDYIYGFQFKAFHFYLTRALQLLRKPCEASSKTVVYRTSQGTSFTFGGLNQARF
GHFTLAYSAKPQAANDQLTVLSIYTCLGVDIENFLDKESERITLIPLNEVFQVSQEGAGN
NLILQSINKTCSHYECAFLGGLKTENCIENLEYFQPIYVYNPGEKNQKLEDHSEKNWKLE
DHGEKNQKLEDHGVKILEPTQIPGMKIPEPFPLPEDKSQGNINNPTPGPVPVPGPKSHPS
ASSGKLLLPQFGMVIILISVSAINLFVAL
Enzyme 6 Number of Residues 389
Enzyme 6 Molecular Weight 43923.0
Enzyme 6 Theoretical pI 5.97
Enzyme 6 GO Classification
Function
  • NAD(P)+-protein-arginine ADP-ribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
Component
Enzyme 6 General Function Involved in NAD(P)+-protein-arginine ADP-ribosyltransferase activity
Enzyme 6 Specific Function NAD(+) + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • NAD+ + protein L-arginine = nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine [RN:R00555]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-26
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 14250010 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q13508 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NAR3_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1170 bp
ATGAAGACGGGACATTTTGAAATAGTCACCATGCTGCTGGCAACCATGATTCTAGTGGAC
ATTTTCCAGGTGAAGGCTGAAGTGTTAGACATGGCAGATAATGCATTTGATGATGAATAC
CTGAAATGTACGGACAGGATGGAAATTAAATACGTTCCCCAACTGCTAAAGGAGGAAAAA
GCAAGCCACCAGCAATTAGATACTGTGTGGGAAAATGCAAAAGCCAAATGGGCAGCCCGA
AAGACTCAAATCTTTCTCCCTATGAATTTTAAGGATAACCATGGAATAGCCCTGATGGCA
TATATTTCCGAAGCTCAAGAGCAAACTCCCTTTTACCATCTGTTCAGTGAAGCTGTGAAG
ATGGCTGGCCAATCTCGAGAAGATTATATCTATGGCTTCCAGTTCAAAGCTTTCCACTTT
TACCTCACAAGAGCCCTGCAGTTGCTGAGAAAACCTTGTGAGGCCAGTTCCAAAACTGTG
GTATATAGAACAAGCCAGGGCACTTCATTTACATTTGGAGGGCTAAACCAAGCCAGGTTT
GGCCATTTTACCTTGGCATATTCAGCCAAACCTCAGGCTGCTAATGACCAGCTCACTGTG
TTATCCATCTACACATGCCTTGGAGTTGACATTGAAAATTTTCTTGATAAAGAAAGTGAA
AGAATTACTTTAATACCTCTGAATGAGGTTTTTCAAGTGTCACAGGAGGGGGCTGGCAAT
AACCTTATCCTTCAAAGCATAAACAAGACCTGCAGCCATTATGAGTGTGCATTTCTAGGT
GGACTAAAAACCGAAAACTGTATTGAGAACCTAGAATATTTTCAACCCATCTATGTCTAC
AACCCTGGTGAGAAAAACCAGAAGCTTGAAGACCATAGTGAGAAAAACTGGAAGCTTGAA
GACCATGGTGAGAAAAACCAGAAGCTTGAAGACCATGGTGTGAAAATCCTTGAACCCACC
CAAATACCTGGAATGAAAATTCCAGAACCTTTTCCACTACCTGAAGATAAAAGTCAAGGA
AATATCAACAATCCTACTCCAGGTCCAGTTCCTGTTCCAGGTCCCAAAAGCCATCCTTCT
GCATCCTTGGGCAAACTGCTGCTTCCACAGTTTGGGATGGTCATCATTTTAATCAGTGTT
TCTGCTATAAATCTCTTTGTTGCTCTGTAG
Enzyme 6 GenBank Gene ID BC008397 Link Image
Enzyme 6 GeneCard ID ART3 Link Image
Enzyme 6 GenAtlas ID ART3 Link Image
Enzyme 6 HGNC ID HGNC:725 Link Image
Enzyme 6 Chromosome Location 4
Enzyme 6 Locus 4p15.1-p14|4p15.1-p14|4p15.1-p14
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Levy I, Wu YQ, Roeckel N, Bulle F, Pawlak A, Siegrist S, Mattei MG, Guellaen G: Human testis specifically expresses a homologue of the rodent T lymphocytes RT6 mRNA. FEBS Lett. 1996 Mar 18;382(3):276-80. [PubMed Link Image]
  2. Koch-Nolte F, Haag F, Braren R, Kuhl M, Hoovers J, Balasubramanian S, Bazan F, Thiele HG: Two novel human members of an emerging mammalian gene family related to mono-ADP-ribosylating bacterial toxins. Genomics. 1997 Feb 1;39(3):370-6. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6197
Enzyme 7 Name GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1
Enzyme 7 Synonyms
  1. Mono(ADP-ribosyl)transferase 1
  2. CD296 antigen
Enzyme 7 Gene Name ART1
Enzyme 7 Protein Sequence >GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1
MQMPAMMSLLLVSVGLMEALQAQSHPITRRDLFSQEIQLDMALASFDDQYAGCAAAMTAA
LPDLNHTEFQANQVYADSWTLASSQWQERQARWPEWSLSPTRPSPPPLGFRDEHGVALLA
YTANSPLHKEFNAAVREAGRSRAHYLHHFSFKTLHFLLTEALQLLGSGQRPPRCHQVFRG
VHGLRFRPAGPRATVRLGGFASASLKHVAAQQFGEDTFFGIWTCLGAPIKGYSFFPGEEE
VLIPPFETFQVINASRLAQGPARIYLRALGKHSTYNCEYIKDKKCKSGPCHLDNSAMGQS
PLSAVWSLLLLLWFLVVRAFPDGPGLL
Enzyme 7 Number of Residues 327
Enzyme 7 Molecular Weight 36334.3
Enzyme 7 Theoretical pI 8.38
Enzyme 7 GO Classification
Function
  • NAD(P)+-protein-arginine ADP-ribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
Component
Enzyme 7 General Function Involved in NAD(P)+-protein-arginine ADP-ribosyltransferase activity
Enzyme 7 Specific Function NAD(+) + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • NAD+ + protein L-arginine = nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine [RN:R00555]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-22
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 158634472 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P52961 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NAR1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >984 bp
ATGCAGATGCCTGCTATGATGTCTCTGCTTCTTGTGTCTGTGGGCCTCATGGAAGCACTT
CAGGCCCAGAGCCACCCCATCACACGACGAGACCTCTTCTCTCAAGAGATTCAGCTGGAC
ATGGCCCTGGCCTCCTTTGATGACCAGTACGCTGGCTGTGCTGCTGCCATGACAGCTGCT
CTCCCGGATCTCAACCACACGGAGTTCCAGGCCAACCAGGTGTATGCAGACAGCTGGACA
CTGGCAAGCAGCCAATGGCAGGAGCGTCAGGCCAGGTGGCCAGAGTGGAGTCTCAGCCCC
ACCCGTCCATCCCCGCCACCCCTGGGCTTCCGCGATGAGCATGGGGTGGCCCTCCTGGCC
TACACAGCCAACAGCCCCCTGCACAAGGAGTTCAATGCAGCCGTGCGTGAGGCGGGCCGC
TCCCGGGCCCACTACCTCCACCACTTCTCCTTCAAGACACTCCATTTCCTGCTGACTGAG
GCCCTGCAGCTCCTGGGCAGCGGCCAGCGTCCACCCCGGTGCCACCAGGTGTTCCGAGGT
GTGCACGGCCTGCGCTTCCGGCCAGCAGGGCCCCGGGCCACCGTGAGGCTGGGGGGCTTT
GCTTCTGCCTCCCTGAAGCATGTTGCAGCCCAGCAGTTTGGTGAGGACACCTTCTTCGGC
ATCTGGACCTGCCTTGGGGCCCCTATCAAGGGCTACTCCTTCTTCCCTGGAGAGGAAGAG
GTGCTGATCCCCCCCTTTGAGACCTTCCAAGTGATCAATGCCAGCAGACTGGCCCAGGGC
CCCGCCCGCATCTACCTCCGAGCCCTGGGCAAGCACAGCACCTACAACTGCGAGTACATC
AAAGACAAGAAGTGCAAGTCTGGGCCTTGCCATCTGGATAATTCAGCCATGGGTCAGAGC
CCCCTCTCTGCAGTCTGGTCTTTGCTGCTGCTGCTCTGGTTCCTCGTGGTGAGGGCCTTT
CCAGATGGTCCAGGCCTCCTTTGA
Enzyme 7 GenBank Gene ID NM_004314.2 Link Image
Enzyme 7 GeneCard ID ART1 Link Image
Enzyme 7 GenAtlas ID ART1 Link Image
Enzyme 7 HGNC ID HGNC:723 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 11p15
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Okazaki IJ, Zolkiewska A, Nightingale MS, Moss J: Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases. Biochemistry. 1994 Nov 1;33(43):12828-36. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6200
Enzyme 8 Name Tankyrase-1
Enzyme 8 Synonyms
  1. TANK1
  2. Poly [ADP-ribose] polymerase 5A
  3. TNKS-1
  4. TRF1-interacting ankyrin-related ADP-ribose polymerase
  5. Tankyrase I
Enzyme 8 Gene Name TNKS
Enzyme 8 Protein Sequence >Tankyrase-1
MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPR
HGLALPEGDGSRDPPDRPRSPDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNP
AGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVSSTAPLGPGAAGPGTGVPAVS
GALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGA
NVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIV
LLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNV
NCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTEL
LLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPEL
RERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQV
TELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAAL
AGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILSESTPIRTSDVDYRLLEASKA
GDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVP
LHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKN
RDGNTPLDLVKEGDTDIQDLLRGDAALLDAAKKGCLARVQKLCTPENINCRDTQGRNSTP
LHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATD
KWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEA
LPTCFKPQATVVSASLISPASTPSCLSAASSIDNLTGPLAELAVGGASNAGDGAAGTERK
EGEVAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLI
KGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGG
IFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDER
HAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSF
LQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTA
TAAEQKT
Enzyme 8 Number of Residues 1327
Enzyme 8 Molecular Weight 142038.2
Enzyme 8 Theoretical pI 7.05
Enzyme 8 GO Classification
Function
  • NAD+ ADP-ribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
Component
Enzyme 8 General Function Involved in NAD+ ADP-ribosyltransferase activity
Enzyme 8 Specific Function May regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Has PARP activity and can modify TERF1, and thereby contribute to the regulation of telomere length
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ [RN:R04176]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 87239981 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O95271 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name TNKS1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >3984 bp
ATGGCGGCGTCGCGTCGCTCTCAGCATCATCACCACCATCATCAACAACAGCTCCAGCCC
GCCCCAGGGGCTTCAGCGCCGCCGCCGCCACCTCCTCCCCCACTCAGCCCTGGCCTGGCC
CCGGGGACCACCCCAGCCTCTCCCACGGCCAGCGGCCTGGCCCCCTTCGCCTCCCCGCGG
CACGGCCTAGCGCTGCCGGAGGGGGATGGCAGTCGGGATCCGCCCGACAGGCCCCGATCC
CCGGACCCGGTTGACGGTACCAGCTGTTGCAGTACCACCAGCACAATCTGTACCGTCGCC
GCCGCTCCCGTGGTCCCAGCGGTTTCTACTTCATCTGCCGCTGGGGTCGCTCCCAACCCA
GCCGGCAGTGGCAGTAACAATTCACCGTCGTCCTCTTCTTCCCCGACTTCTTCCTCATCT
TCCTCTCCATCCTCCCCTGGATCGAGCTTGGCGGAGAGCCCCGAGGCGGCCGGAGTTAGC
AGCACAGCACCACTGGGGCCTGGGGCAGCAGGACCTGGGACAGGGGTCCCAGCAGTGAGC
GGGGCCCTACGGGAACTGCTGGAGGCCTGTCGCAATGGGGACGTGTCCCGGGTAAAGAGG
CTGGTGGACGCGGCAAACGTAAATGCAAAGGACATGGCCGGCCGGAAGTCTTCTCCCCTG
CACTTCGCTGCAGGTTTTGGAAGGAAGGATGTTGTAGAACACTTACTACAGATGGGTGCT
AATGTCCACGCTCGTGATGATGGAGGTCTCATCCCGCTTCATAATGCCTGTTCTTTTGGC
CATGCTGAGGTTGTGAGTCTGTTATTGTGCCAAGGAGCTGATCCAAATGCCAGGGATAAC
TGGAACTATACACCTCTGCATGAAGCTGCTATTAAAGGGAAGATCGATGTGTGCATTGTG
CTGCTGCAGCACGGAGCTGACCCAAACATTCGGAACACTGATGGGAAATCAGCCCTGGAC
CTGGCAGATCCTTCAGCAAAAGCTGTCCTTACAGGTGAATACAAGAAAGACGAACTCCTA
GAAGCTGCTAGGAGTGGTAATGAAGAAAAACTAATGGCTTTACTGACTCCTCTAAATGTG
AATTGCCATGCAAGTGATGGGCGAAAGTCGACTCCTTTACATCTAGCAGCGGGCTACAAC
AGAGTTCGAATAGTTCAGCTTCTTCTTCAGCATGGTGCTGATGTTCATGCAAAAGACAAA
GGTGGACTTGTGCCTCTTCATAATGCATGTTCATATGGACATTATGAAGTCACAGAACTG
CTACTAAAGCATGGAGCTTGTGTTAATGCCATGGATCTCTGGCAGTTTACTCCACTGCAC
GAGGCTGCTTCCAAGAACCGTGTAGAAGTCTGCTCTTTGTTACTTAGCCATGGCGCTGAT
CCTACATTAGTCAACTGCCATGGCAAAAGTGCTGTGGATATGGCTCCAACTCCGGAGCTT
AGGGAGAGATTGACTTATGAATTTAAAGGTCATTCTTTACTACAAGCAGCCAGAGAAGCA
GACTTAGCTAAAGTTAAAAAAACACTCGCTCTGGAAATCATTAATTTCAAACAACCGCAG
TCTCATGAAACAGCACTGCACTGTGCTGTGGCCTCTCTGCATCCCAAACGTAAACAAGTG
ACAGAATTGTTACTTAGAAAAGGAGCAAATGTTAATGAAAAAAATAAAGATTTCATGACT
CCCCTGCATGTTGCAGCCGAAAGAGCCCATAATGATGTCATGGAAGTTCTGCATAAGCAT
GGCGCCAAGATGAATGCACTGGACACCCTTGGTCAGACTGCTTTGCATAGAGCCGCCCTA
GCAGGCCACCTGCAGACCTGCCGCCTCCTGCTGAGTTACGGCTCTGACCCCTCCATCATC
TCCTTACAAGGCTTCACAGCAGCACAGATGGGCAATGAAGCAGTGCAGCAGATTCTGAGT
GAGAGTACACCTATACGTACTTCTGATGTTGATTATCGACTCTTAGAGGCATCTAAAGCT
GGAGACTTGGAAACTGTGAAGCAACTTTGCAGCTCTCAAAATGTGAATTGTAGAGACTTA
GAGGGCCGGCATTCCACGCCCTTACACTTCGCAGCAGGCTACAACCGCGTGTCTGTTGTA
GAGTACCTGCTACACCACGGTGCCGATGTCCATGCCAAAGACAAGGGTGGCTTGGTGCCC
CTTCATAATGCCTGTTCATATGGACACTATGAGGTGGCTGAGCTTTTAGTAAGGCATGGG
GCTTCTGTCAATGTGGCGGACTTATGGAAATTTACCCCTCTCCATGAAGCAGCAGCTAAA
GGAAAGTATGAAATCTGCAAGCTCCTTTTAAAACATGGAGCAGATCCAACTAAAAAGAAC
AGAGATGGAAATACACCTTTGGATTTGGTAAAGGAAGGAGACACAGATATTCAGGACTTA
CTGAGAGGGGATGCTGCTTTGTTGGATGCTGCCAAGAAGGGCTGCCTGGCAAGAGTGCAG
AAGCTCTGTACCCCAGAGAATATCAACTGCAGAGACACCCAGGGCAGAAATTCAACCCCT
CTGCACCTGGCAGCAGGCTATAATAACCTGGAAGTAGCTGAATATCTTCTAGAGCATGGA
GCTGATGTTAATGCCCAGGACAAGGGTGGTTTAATTCCTCTTCATAATGCGGCATCTTAT
GGGCATGTTGACATAGCGGCTTTATTGATAAAATACAACACGTGTGTAAATGCAACAGAT
AAGTGGGCGTTTACTCCCCTCCATGAAGCAGCCCAGAAAGGAAGGACGCAGCTGTGCGCC
CTCCTCCTAGCGCATGGTGCAGACCCCACCATGAAGAACCAGGAAGGCCAGACGCCTCTG
GATCTGGCAACAGCTGACGATATCAGAGCTTTGCTGATAGATGCCATGCCCCCAGAGGCC
TTACCTACCTGTTTTAAACCTCAGGCTACTGTAGTGAGTGCCTCTCTGATCTCACCAGCA
TCCACCCCCTCCTGCCTCTCGGCTGCCAGCAGCATAGACAACCTCACTGGCCCTTTAGCA
GAGTTGGCCGTAGGAGGAGCCTCCAATGCAGGGGATGGCGCCGCGGGAACAGAAAGGAAG
GAAGGAGAAGTTGCTGGTCTTGACATGAATATCAGCCAATTTCTAAAAAGCCTTGGCCTT
GAACACCTTCGGGATATCTTTGAAACAGAACAGATTACACTAGATGTGTTGGCTGATATG
GGTCATGAAGAGTTGAAAGAAATAGGCATCAATGCATATGGGCACCGCCACAAATTAATC
AAAGGAGTAGAAAGACTCTTAGGTGGACAACAAGGCACCAATCCTTATTTGACTTTTCAC
TGTGTTAATCAGGGAACGATTTTGCTGGATCTTGCTCCAGAAGATAAAGAATATCAGTCA
GTGGAAGAAGAGATGCAAAGTACTATTCGAGAACACAGAGATGGTGGTAATGCTGGCGGC
ATCTTCAACAGATACAATGTCATTCGAATTCAAAAAGTTGTCAACAAGAAGTTGAGGGAG
CGGTTCTGCCACCGACAGAAGGAAGTGTCTGAGGAGAATCACAACCATCACAATGAGCGC
ATGTTGTTTCATGGTTCTCCTTTCATTAATGCCATTATTCATAAAGGGTTTGATGAGCGA
CATGCATACATAGGAGGAATGTTTGGGGCCGGGATTTATTTTGCTGAAAACTCCTCAAAA
AGCAACCAATATGTTTATGGAATTGGAGGAGGAACAGGCTGCCCTACACACAAGGACAGG
TCATGCTATATATGTCACAGACAAATGCTCTTCTGTAGAGTGACCCTTGGGAAATCCTTT
CTGCAGTTTAGCACCATGAAAATGGCCCACGCGCCTCCAGGGCACCACTCAGTCATTGGT
AGACCGAGCGTCAATGGGCTGGCATATGCTGAATATGTCATCTACAGAGGAGAACAGGCA
TACCCAGAGTATCTTATCACTTACCAGATCATGAAGCCAGAAGCCCCTTCCCAGACCGCA
ACAGCCGCAGAGCAGAAGACCTAG
Enzyme 8 GenBank Gene ID NM_003747.2 Link Image
Enzyme 8 GeneCard ID TNKS Link Image
Enzyme 8 GenAtlas ID TNKS Link Image
Enzyme 8 HGNC ID HGNC:11941 Link Image
Enzyme 8 Chromosome Location 8
Enzyme 8 Locus 8p23.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Smith S, Giriat I, Schmitt A, de Lange T: Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Science. 1998 Nov 20;282(5393):1484-7. [PubMed Link Image]
  2. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  3. Smith S, de Lange T: Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes. J Cell Sci. 1999 Nov;112 ( Pt 21):3649-56. [PubMed Link Image]
  4. Chi NW, Lodish HF: Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles. J Biol Chem. 2000 Dec 8;275(49):38437-44. [PubMed Link Image]
  5. Cook BD, Dynek JN, Chang W, Shostak G, Smith S: Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres. Mol Cell Biol. 2002 Jan;22(1):332-42. [PubMed Link Image]
  6. Loayza D, De Lange T: POT1 as a terminal transducer of TRF1 telomere length control. Nature. 2003 Jun 26;423(6943):1013-8. Epub 2003 May 25. [PubMed Link Image]
  7. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6201
Enzyme 9 Name Poly [ADP-ribose] polymerase 1
Enzyme 9 Synonyms
  1. PARP-1
  2. NAD(+) ADP-ribosyltransferase 1
  3. ADPRT 1
  4. Poly[ADP-ribose] synthase 1
Enzyme 9 Gene Name PARP1
Enzyme 9 Protein Sequence >Poly [ADP-ribose] polymerase 1
MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKV
GHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKS
NRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQ
LKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKA
QNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSG
QLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPE
TSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLT
GTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSP
WGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLE
HSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNK
LEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPG
TKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAV
SQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRG
GSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIE
REGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM
VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSA
NISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW
Enzyme 9 Number of Residues 1014
Enzyme 9 Molecular Weight 113082.9
Enzyme 9 Theoretical pI 9.34
Enzyme 9 GO Classification
Function
  • DNA binding
  • NAD or NADH binding
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • nucleotide binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
  • transition metal ion binding
  • zinc ion binding
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
Component
  • cell part
  • intracellular
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 9 General Function Involved in DNA binding
Enzyme 9 Specific Function Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP- ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ [RN:R04176]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 21693601 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P09874 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PARP1_HUMAN Link Image
Enzyme 9 PDB ID 1WOK Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >3045 bp
ATGGCGGAGTCTTCGGATAAGCTCTATCGAGTCGAGTACGCCAAGAGCGGGCGCGCCTCT
TGCAAGAAATGCAGCGAGAGCATCCCCAAGGACTCGCTCCGGATGGCCATCATGGTGCAG
TCGCCCATGTTTGATGGAAAAGTCCCACACTGGTACCACTTCTCCTGCTTCTGGAAGGTG
GGCCACTCCATCCGGCACCCTGACGTTGAGGTGGATGGGTTCTCTGAGCTTCGGTGGGAT
GACCAGCAGAAAGTCAAGAAGACAGCGGAAGCTGGAGGAGTGACAGGCAAAGGCCAGGAT
GGAATTGGTAGCAAGGCAGAGAAGACTCTGGGTGACTTTGCAGCAGAGTATGCCAAGTCC
AACAGAAGTACGTGCAAGGGGTGTATGGAGAAGATAGAAAAGGGCCAGGTGCGCCTGTCC
AAGAAGATGGTGGACCCGGAGAAGCCACAGCTAGGCATGATTGACCGCTGGTACCATCCA
GGCTGCTTTGTCAAGAACAGGGAGGAGCTGGGTTTCCGGCCCGAGTACAGTGCGAGTCAG
CTCAAGGGCTTCAGCCTCCTTGCTACAGAGGATAAAGAAGCCCTGAAGAAGCAGCTCCCA
GGAGTCAAGAGTGAAGGAAAGAGAAAAGGCGATGAGGTGGATGGAGTGGATGAAGTGGCG
AAGAAGAAATCTAAAAAAGAAAAAGACAAGGATAGTAAGCTTGAAAAAGCCCTAAAGGCT
CAGAACGACCTGATCTGGAACATCAAGGACGAGCTAAAGAAAGTGTGTTCAACTAATGAC
CTGAAGGAGCTACTCATCTTCAACAAGCAGCAAGTGCCTTCTGGGGAGTCGGCGATCTTG
GACCGAGTAGCTGATGGCATGGTGTTCGGTGCCCTCCTTCCCTGCGAGGAATGCTCGGGT
CAGCTGGTCTTCAAGAGCGATGCCTATTACTGCACTGGGGACGTCACTGCCTGGACCAAG
TGTATGGTCAAGACACAGACACCCAACCGGAAGGAGTGGGTAACCCCAAAGGAATTCCGA
GAAATCTCTTACCTCAAGAAATTGAAGGTTAAAAAGCAGGACCGTATATTCCCCCCAGAA
ACCAGCGCCTCCGTGGCGGCCACGCCTCCGCCCTCCACAGCCTCGGCTCCTGCTGCTGTG
AACTCCTCTGCTTCAGCAGATAAGCCATTATCCAACATGAAGATCCTGACTCTCGGGAAG
CTGTCCCGGAACAAGGATGAAGTGAAGGCCATGATTGAGAAACTCGGGGGGAAGTTGACG
GGGACGGCCAACAAGGCTTCCCTGTGCATCAGCACCAAAAAGGAGGTGGAAAAGATGAAT
AAGAAGATGGAGGAAGTAAAGGAAGCCAACATCCGAGTTGTGTCTGAGGACTTCCTCCAG
GACGTCTCCGCCTCCACCAAGAGCCTTCAGGAGTTGTTCTTAGCGCACATCTTGTCCCCT
TGGGGGGCAGAGGTGAAGGCAGAGCCTGTTGAAGTTGTGGCCCCAAGAGGGAAGTCAGGG
GCTGCGCTCTCCAAAAAAAGCAAGGGCCAGGTCAAGGAGGAAGGTATCAACAAATCTGAA
AAGAGAATGAAATTAACTCTTAAAGGAGGAGCAGCTGTGGATCCTGATTCTGGACTGGAA
CACTCTGCGCATGTCCTGGAGAAAGGTGGGAAGGTCTTCAGTGCCACCCTTGGCCTGGTG
GACATCGTTAAAGGAACCAACTCCTACTACAAGCTGCAGCTTCTGGAGGACGACAAGGAA
AACAGGTATTGGATATTCAGGTCCTGGGGCCGTGTGGGTACGGTGATCGGTAGCAACAAA
CTGGAACAGATGCCGTCCAAGGAGGATGCCATTGAGCACTTCATGAAATTATATGAAGAA
AAAACCGGGAACGCTTGGCACTCCAAAAATTTCACGAAGTATCCCAAAAAGTTCTACCCC
CTGGAGATTGACTATGGCCAGGATGAAGAGGCAGTGAAGAAGCTGACAGTAAATCCTGGC
ACCAAGTCCAAGCTCCCCAAGCCAGTTCAGGACCTCATCAAGATGATCTTTGATGTGGAA
AGTATGAAGAAAGCCATGGTGGAGTATGAGATCGACCTTCAGAAGATGCCCTTGGGGAAG
CTGAGCAAAAGGCAGATCCAGGCCGCATACTCCATCCTCAGTGAGGTCCAGCAGGCGGTG
TCTCAGGGCAGCAGCGACTCTCAGATCCTGGATCTCTCAAATCGCTTTTACACCCTGATC
CCCCACGACTTTGGGATGAAGAAGCCTCCGCTCCTGAACAATGCAGACAGTGTGCAGGCC
AAGGTGGAAATGCTTGACAACCTGCTGGACATCGAGGTGGCCTACAGTCTGCTCAGGGGA
GGGTCTGATGATAGCAGCAAGGATCCCATCGATGTCAACTATGAGAAGCTCAAAACTGAC
ATTAAGGTGGTTGACAGAGATTCTGAAGAAGCCGAGATCATCAGGAAGTATGTTAAGAAC
ACTCATGCAACCACACACAATGCGTATGACTTGGAAGTCATCGATATCTTTAAGATAGAG
CGTGAAGGCGAATGCCAGCGTTACAAGCCCTTTAAGCAGCTTCATAACCGAAGATTGCTG
TGGCACGGGTCCAGGACCACCAACTTTGCTGGGATCCTGTCCCAGGGTCTTCGGATAGCC
CCGCCTGAAGCGCCCGTGACAGGCTACATGTTTGGTAAAGGGATCTATTTCGCTGACATG
GTCTCCAAGAGTGCCAACTACTGCCATACGTCTCAGGGAGACCCAATAGGCTTAATCCTG
TTGGGAGAAGTTGCCCTTGGAAACATGTATGAACTGAAGCACGCTTCACATATCAGCAAG
TTACCCAAGGGCAAGCACAGTGTCAAAGGTTTGGGCAAAACTACCCCTGATCCTTCAGCT
AACATTAGTCTGGATGGTGTAGACGTTCCTCTTGGGACCGGGATTTCATCTGGTGTGAAT
GACACCTCTCTACTATATAACGAGTACATTGTCTATGATATTGCTCAGGTAAATCTGAAG
TATCTGCTGAAACTGAAATTCAATTTTAAGACCTCCCTGTGGTAA
Enzyme 9 GenBank Gene ID AF524947 Link Image
Enzyme 9 GeneCard ID PARP1 Link Image
Enzyme 9 GenAtlas ID PARP1 Link Image
Enzyme 9 HGNC ID HGNC:270 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1q41-q42
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Uchida K, Morita T, Sato T, Ogura T, Yamashita R, Noguchi S, Suzuki H, Nyunoya H, Miwa M, Sugimura T: Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase. Biochem Biophys Res Commun. 1987 Oct 29;148(2):617-22. [PubMed Link Image]
  2. Kurosaki T, Ushiro H, Mitsuuchi Y, Suzuki S, Matsuda M, Matsuda Y, Katunuma N, Kangawa K, Matsuo H, Hirose T, et al.: Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence. J Biol Chem. 1987 Nov 25;262(33):15990-7. [PubMed Link Image]
  3. Cherney BW, McBride OW, Chen DF, Alkhatib H, Bhatia K, Hensley P, Smulson ME: cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8370-4. [PubMed Link Image]
  4. Auer B, Nagl U, Herzog H, Schneider R, Schweiger M: Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization of the gene. DNA. 1989 Oct;8(8):575-80. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Yokoyama Y, Kawamoto T, Mitsuuchi Y, Kurosaki T, Toda K, Ushiro H, Terashima M, Sumimoto H, Kuribayashi I, Yamamoto Y, et al.: Human poly(ADP-ribose) polymerase gene. Cloning of the promoter region. Eur J Biochem. 1990 Dec 12;194(2):521-6. [PubMed Link Image]
  8. Ogura T, Nyunoya H, Takahashi-Masutani M, Miwa M, Sugimura T, Esumi H: Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene: structural similarity to that of the DNA polymerase beta gene. Biochem Biophys Res Commun. 1990 Mar 16;167(2):701-10. [PubMed Link Image]
  9. Schneider R, Auer B, Kuhne C, Herzog H, Klocker H, Burtscher HJ, Hirsch-Kauffmann M, Wintersberger U, Schweiger M: Isolation of a cDNA clone for human NAD+: protein ADP-ribosyltransferase. Eur J Cell Biol. 1987 Oct;44(2):302-7. [PubMed Link Image]
  10. Suzuki H, Uchida K, Shima H, Sato T, Okamoto T, Kimura T, Miwa M: Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation. Biochem Biophys Res Commun. 1987 Jul 31;146(2):403-9. [PubMed Link Image]
  11. Gradwohl G, Menissier de Murcia JM, Molinete M, Simonin F, Koken M, Hoeijmakers JH, de Murcia G: The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA. Proc Natl Acad Sci U S A. 1990 Apr;87(8):2990-4. [PubMed Link Image]
  12. Ikejima M, Noguchi S, Yamashita R, Ogura T, Sugimura T, Gill DM, Miwa M: The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA. J Biol Chem. 1990 Dec 15;265(35):21907-13. [PubMed Link Image]
  13. Simonin F, Menissier-de Murcia J, Poch O, Muller S, Gradwohl G, Molinete M, Penning C, Keith G, de Murcia G: Expression and site-directed mutagenesis of the catalytic domain of human poly(ADP-ribose)polymerase in Escherichia coli. Lysine 893 is critical for activity. J Biol Chem. 1990 Nov 5;265(31):19249-56. [PubMed Link Image]
  14. Schreiber V, Molinete M, Boeuf H, de Murcia G, Menissier-de Murcia J: The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity. EMBO J. 1992 Sep;11(9):3263-9. [PubMed Link Image]
  15. Rolli V, O'Farrell M, Menissier-de Murcia J, de Murcia G: Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching. Biochemistry. 1997 Oct 7;36(40):12147-54. [PubMed Link Image]
  16. Dantzer F, Nasheuer HP, Vonesch JL, de Murcia G, Menissier-de Murcia J: Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication. Nucleic Acids Res. 1998 Apr 15;26(8):1891-8. [PubMed Link Image]
  17. Ariumi Y, Masutani M, Copeland TD, Mimori T, Sugimura T, Shimotohno K, Ueda K, Hatanaka M, Noda M: Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro. Oncogene. 1999 Aug 12;18(32):4616-25. [PubMed Link Image]
  18. Gueven N, Becherel OJ, Kijas AW, Chen P, Howe O, Rudolph JH, Gatti R, Date H, Onodera O, Taucher-Scholz G, Lavin MF: Aprataxin, a novel protein that protects against genotoxic stress. Hum Mol Genet. 2004 May 15;13(10):1081-93. Epub 2004 Mar 25. [PubMed Link Image]
  19. Li Y, Oh HJ, Lau YF: The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its biological functions. Mol Cell Endocrinol. 2006 Sep 26;257-258:35-46. Epub 2006 Aug 9. [PubMed Link Image]
  20. Kanno S, Kuzuoka H, Sasao S, Hong Z, Lan L, Nakajima S, Yasui A: A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. EMBO J. 2007 Apr 18;26(8):2094-103. Epub 2007 Mar 29. [PubMed Link Image]
  21. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  22. Ahel I, Ahel D, Matsusaka T, Clark AJ, Pines J, Boulton SJ, West SC: Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature. 2008 Jan 3;451(7174):81-5. [PubMed Link Image]
  23. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  24. Reinemund J, Seidel K, Steckelings UM, Zaade D, Klare S, Rompe F, Katerbaum M, Schacherl J, Li Y, Menk M, Schefe JH, Goldin-Lang P, Szabo C, Olah G, Unger T, Funke-Kaiser H: Poly(ADP-ribose) polymerase-1 (PARP-1) transcriptionally regulates angiotensin AT2 receptor (AT2R) and AT2R binding protein (ATBP) genes. Biochem Pharmacol. 2009 Jun 15;77(12):1795-805. Epub 2009 Mar 19. [PubMed Link Image]
  25. Martin N, Schwamborn K, Schreiber V, Werner A, Guillier C, Zhang XD, Bischof O, Seeler JS, Dejean A: PARP-1 transcriptional activity is regulated by sumoylation upon heat shock. EMBO J. 2009 Nov 18;28(22):3534-48. Epub 2009 Sep 24. [PubMed Link Image]
  26. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  27. Ahel D, Horejsi Z, Wiechens N, Polo SE, Garcia-Wilson E, Ahel I, Flynn H, Skehel M, West SC, Jackson SP, Owen-Hughes T, Boulton SJ: Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1. Science. 2009 Sep 4;325(5945):1240-3. Epub 2009 Aug 6. [PubMed Link Image]
  28. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  29. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6203
Enzyme 10 Name ADP-ribosyl cyclase 2
Enzyme 10 Synonyms
  1. Bone marrow stromal antigen 1
  2. BST-1
  3. Cyclic ADP-ribose hydrolase 2
  4. cADPr hydrolase 2
  5. CD157 antigen
Enzyme 10 Gene Name BST1
Enzyme 10 Protein Sequence >ADP-ribosyl cyclase 2
MAAQGCAASRLLQLLLQLLLLLLLLAAGGARARWRGEGTSAHLRDIFLGRCAEYRALLSP
EQRNKNCTAIWEAFKVALDKDPCSVLPSDYDLFINLSRHSIPRDKSLFWENSHLLVNSFA
DNTRRFMPLSDVLYGRVADFLSWCRQKNDSGLDYQSCPTSEDCENNPVDSFWKRASIQYS
KDSSGVIHVMLNGSEPTGAYPIKGFFADYEIPNLQKEKITRIEIWVMHEIGGPNVESCGE
GSMKVLEKRLKDMGFQYSCINDYRPVKLLQCVDHSTHPDCALKSAAAATQRKAPSLYTEQ
RAGLIIPLFLVLASRTQL
Enzyme 10 Number of Residues 318
Enzyme 10 Molecular Weight 35723.5
Enzyme 10 Theoretical pI 7.86
Enzyme 10 GO Classification
Function
  • NAD+ nucleosidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing N-glycosyl compounds
Process
  • metabolic process
Component
Enzyme 10 General Function Involved in NAD+ nucleosidase activity
Enzyme 10 Specific Function Synthesizes cyclic ADP-ribose, a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth
Enzyme 10 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 10 Reactions
  • NAD+ + H2O = ADP-ribose + nicotinamide [RN:R00102]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-28
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 63991381 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q10588 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name BST1_HUMAN Link Image
Enzyme 10 PDB ID 1ISM Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >957 bp
ATGGCGGCCCAGGGGTGCGCGGCATCGCGGCTGCTCCAGCTGCTGCTGCAGCTTCTGCTT
CTACTGTTGCTGCTGGCGGCGGGCGGGGCGCGCGCGCGGTGGCGCGGGGAGGGCACCAGC
GCACACTTGCGGGACATCTTCCTGGGCCGCTGCGCCGAGTACCGCGCACTGCTGAGTCCC
GAGCAGCGGAACAAGAACTGCACAGCCATCTGGGAAGCCTTTAAAGTGGCGCTGGACAAG
GATCCCTGCTCCGTGCTGCCCTCAGACTATGACCTTTTTATTAACTTGTCCAGGCACTCT
ATTCCCAGAGATAAGTCCCTGTTCTGGGAAAATAGCCACCTCCTTGTTAACAGCTTTGCA
GACAACACCCGTCGTTTTATGCCCCTGAGCGATGTTCTGTATGGCAGGGTTGCAGATTTC
TTGAGCTGGTGTCGACAGAAAAATGACTCTGGACTCGATTACCAATCCTGCCCTACATCA
GAAGACTGTGAAAATAATCCTGTGGATTCCTTTTGGAAAAGGGCATCCATCCAGTATTCC
AAGGATAGTTCTGGGGTGATCCACGTCATGCTGAATGGTTCAGAGCCAACAGGAGCCTAT
CCCATCAAAGGTTTTTTTGCAGATTATGAAATTCCAAACCTCCAGAAGGAAAAAATTACA
CGAATCGAGATCTGGGTTATGCATGAAATTGGGGGACCCAATGTGGAATCCTGCGGGGAA
GGCAGCATGAAAGTCCTGGAAAAGAGGCTGAAGGACATGGGGTTCCAGTACAGCTGTATT
AATGATTACCGACCAGTGAAGCTCTTACAGTGCGTGGACCACAGCACCCATCCTGACTGT
GCCTTAAAGTCGGCAGCAGCCGCTACTCAAAGAAAAGCCCCAAGTCTTTATACAGAACAA
AGGGCGGGTCTTATCATTCCCCTCTTTCTGGTGCTGGCTTCCAGGACTCAACTGTAA
Enzyme 10 GenBank Gene ID AC114744 Link Image
Enzyme 10 GeneCard ID BST1 Link Image
Enzyme 10 GenAtlas ID BST1 Link Image
Enzyme 10 HGNC ID HGNC:1118 Link Image
Enzyme 10 Chromosome Location 4
Enzyme 10 Locus 4p15
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Kaisho T, Ishikawa J, Oritani K, Inazawa J, Tomizawa H, Muraoka O, Ochi T, Hirano T: BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre-B-cell growth. Proc Natl Acad Sci U S A. 1994 Jun 7;91(12):5325-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  7. Yamamoto-Katayama S, Ariyoshi M, Ishihara K, Hirano T, Jingami H, Morikawa K: Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities. J Mol Biol. 2002 Feb 22;316(3):711-23. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6204
Enzyme 11 Name Poly [ADP-ribose] polymerase 2
Enzyme 11 Synonyms
  1. PARP-2
  2. hPARP-2
  3. NAD(+) ADP-ribosyltransferase 2
  4. ADPRT-2
  5. Poly[ADP-ribose] synthase 2
  6. pADPRT-2
Enzyme 11 Gene Name PARP2
Enzyme 11 Protein Sequence >Poly [ADP-ribose] polymerase 2
MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKD
RTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLN
QTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKF
LDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQE
LIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALME
ACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQ
HYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDL
HNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLK
NTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGP
ASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW
Enzyme 11 Number of Residues 583
Enzyme 11 Molecular Weight 66205.3
Enzyme 11 Theoretical pI 9.22
Enzyme 11 GO Classification
Function
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
Component
Enzyme 11 General Function Involved in NAD+ ADP-ribosyltransferase activity
Enzyme 11 Specific Function Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ [RN:R04176]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 110825961 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9UGN5 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PARP2_HUMAN Link Image
Enzyme 11 PDB ID 1GS0 Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1752 bp
ATGGCGGCGCGGCGGCGACGGAGCACCGGCGGCGGCAGGGCGAGAGCATTAAATGAAAGC
AAAAGAGTTAATAATGGCAACACGGCTCCAGAAGACTCTTCCCCTGCCAAGAAAACTCGT
AGATGCCAGAGACAGGAGTCGAAAAAGATGCCTGTGGCTGGAGGAAAAGCTAATAAGGAC
AGGACAGAAGACAAGCAAGATGGTATGCCAGGAAGGTCATGGGCCAGCAAAAGGGTCTCT
GAATCTGTGAAGGCCTTGCTGTTAAAGGGCAAAGCTCCTGTGGACCCAGAGTGTACAGCC
AAGGTGGGGAAGGCTCATGTGTATTGTGAAGGAAATGATGTCTATGATGTCATGCTAAAT
CAGACCAATCTCCAGTTCAACAACAACAAGTACTATCTGATTCAGCTATTAGAAGATGAT
GCCCAGAGGAACTTCAGTGTTTGGATGAGATGGGGCCGAGTTGGGAAAATGGGACAGCAC
AGCCTGGTGGCTTGTTCAGGCAATCTCAACAAGGCCAAGGAAATCTTTCAGAAGAAATTC
CTTGACAAAACGAAAAACAATTGGGAAGATCGAGAAAAGTTTGAGAAGGTGCCTGGAAAA
TATGATATGCTACAGATGGACTATGCCACCAATACTCAGGATGAAGAGGAAACAAAGAAA
GAGGAATCTCTTAAATCTCCCTTGAAGCCAGAGTCACAGCTAGATCTTCGGGTACAGGAG
TTAATAAAGTTGATCTGTAATGTTCAGGCCATGGAAGAAATGATGATGGAAATGAAGTAT
AATACCAAGAAAGCCCCACTTGGGAAGCTGACAGTGGCACAAATCAAGGCAGGTTACCAG
TCTCTTAAGAAGATTGAGGATTGTATTCGGGCTGGCCAGCATGGACGAGCTCTCATGGAA
GCATGCAATGAATTCTACACCAGGATTCCGCATGACTTTGGACTCCGTACTCCTCCACTA
ATCCGGACACAGAAGGAACTGTCAGAAAAAATACAATTACTAGAGGCTTTGGGAGACATT
GAAATTGCTATTAAGCTGGTGAAAACAGAGCTACAAAGCCCAGAACACCCATTGGACCAA
CACTATAGAAACCTACATTGTGCCTTGCGCCCCCTTGACCATGAAAGTTATGAGTTCAAA
GTGATTTCCCAGTACCTACAATCTACCCATGCTCCCACACACAGCGACTATACCATGACC
TTGCTGGATTTGTTTGAAGTGGAGAAGGATGGTGAGAAAGAAGCCTTCAGAGAGGACCTT
CATAACAGGATGCTTCTATGGCATGGTTCCAGGATGAGTAACTGGGTGGGAATCTTGAGC
CATGGGCTTCGAATTGCCCCACCTGAAGCTCCCATCACAGGTTACATGTTTGGGAAAGGA
ATCTACTTTGCTGACATGTCTTCCAAGAGTGCCAATTACTGCTTTGCCTCTCGCCTAAAG
AATACAGGACTGCTGCTCTTATCAGAGGTAGCTCTAGGTCAGTGTAATGAACTACTAGAG
GCCAATCCTAAGGCCGAAGGATTGCTTCAAGGTAAACATAGCACCAAGGGGCTGGGCAAG
ATGGCTCCCAGTTCTGCCCACTTCGTCACCCTGAATGGGAGTACAGTGCCATTAGGACCA
GCAAGTGACACAGGAATTCTGAATCCAGATGGTTATACCCTCAACTACAATGAATATATT
GTATATAACCCCAACCAGGTCCGTATGCGGTACCTTTTAAAGGTTCAGTTTAATTTCCTT
CAGCTGTGGTGA
Enzyme 11 GenBank Gene ID NM_005484.3 Link Image
Enzyme 11 GeneCard ID PARP2 Link Image
Enzyme 11 GenAtlas ID PARP2 Link Image
Enzyme 11 HGNC ID HGNC:272 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 14q11.2-q12
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Ame JC, Rolli V, Schreiber V, Niedergang C, Apiou F, Decker P, Muller S, Hoger T, Menissier-de Murcia J, de Murcia G: PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase. J Biol Chem. 1999 Jun 18;274(25):17860-8. [PubMed Link Image]
  2. Johansson M: A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues. Genomics. 1999 May 1;57(3):442-5. [PubMed Link Image]
  3. Berghammer H, Ebner M, Marksteiner R, Auer B: pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans. FEBS Lett. 1999 Apr 23;449(2-3):259-63. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Schreiber V, Ame JC, Dolle P, Schultz I, Rinaldi B, Fraulob V, Menissier-de Murcia J, de Murcia G: Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. J Biol Chem. 2002 Jun 21;277(25):23028-36. Epub 2002 Apr 10. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6206
Enzyme 12 Name ADP-ribosyl cyclase 1
Enzyme 12 Synonyms
  1. Cyclic ADP-ribose hydrolase 1
  2. cADPr hydrolase 1
  3. T10
  4. CD38 antigen
Enzyme 12 Gene Name CD38
Enzyme 12 Protein Sequence >ADP-ribosyl cyclase 1
MANCEFSPVSGDKPCCRLSRRAQLCLGVSILVLILVVVLAVVVPRWRQQWSGPGTTKRFP
ETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCN
KILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDC
SNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEA
WVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI
Enzyme 12 Number of Residues 300
Enzyme 12 Molecular Weight 34328.1
Enzyme 12 Theoretical pI 7.72
Enzyme 12 GO Classification
Function
  • NAD+ nucleosidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing N-glycosyl compounds
Process
  • metabolic process
Component
Enzyme 12 General Function Involved in NAD+ nucleosidase activity
Enzyme 12 Specific Function Synthesizes cyclic ADP-ribose, a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity. Also moonlights as a receptor in cells of the immune system
Enzyme 12 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 12 Reactions
  • NAD+ + H2O = ADP-ribose + nicotinamide [RN:R00102]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 22-42
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 14044085 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P28907 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name CD38_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >903 bp
ATGGCCAACTGCGAGTTCAGCCCGGTGTCCGGGGACAAACCCTGCTGCCGGCTCTCTAGG
AGAGCCCAACTCTGTCTTGGCGTCAGTATCCTGGTCCTGATCCTCGTCGTGGTGCTCGCG
GTGGTCGTCCCGAGGTGGCGCCAGCAGTGGAGCGGTCCGGGCACCACCAAGCGCTTTCCC
GAGACCGTCCTGGCGCGATGCGTCAAGTACACTGAAATTCATCCTGAGATGAGACATGTA
GACTGCCAAAGTGTATGGGATGCTTTCAAGGGTGCATTTATTTCAAAACATCCTTGCAAC
ATTACTGAAGAAGACTATCAGCCACTAATGAAGTTGGGAACTCAGACCGTACCTTGCAAC
AAGATTCTTCTTTGGAGCAGAATAAAAGATCTGGCCCATCAGTTCACACAGGTCCAGCGG
GACATGTTCACCCTGGAGGACACGCTGCTAGGCTACCTTGCTGATGACCTCACATGGTGT
GGTGAATTCAACACTTCCAAAATAAACTATCAATCTTGCCCAGACTGGAGAAAGGACTGC
AGCAACAACCCTGTTTCAGTATTCTGGAAAACGGTTTCCCGCAGGTTTGCAGAAGCTGCC
TGTGATGTGGTCCATGTGATGCTCAATGGATCCCGCAGTAAAATCTTTGACAAAAACAGC
ACTTTTGGGAGTGTGGAAGTCCATAATTTGCAACCAGAGAAGGTTCAGACACTAGAGGCC
TGGGTGATACATGGTGGAAGAGAAGATTCCAGAGACTTATGCCAGGATCCCACCATAAAA
GAGCTGGAATCGATTATAAGCAAAAGGAATATTCAATTTTCCTGCAAGAATATCTACAGA
CCTGACAAGTTTCTTCAGTGTGTGAAAAATCCTGAGGATTCATCTTGCACATCTGAGATC
TGA
Enzyme 12 GenBank Gene ID BC007964 Link Image
Enzyme 12 GeneCard ID CD38 Link Image
Enzyme 12 GenAtlas ID CD38 Link Image
Enzyme 12 HGNC ID HGNC:1667 Link Image
Enzyme 12 Chromosome Location 4
Enzyme 12 Locus 4p15
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Jackson DG, Bell JI: Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation. J Immunol. 1990 Apr 1;144(7):2811-5. [PubMed Link Image]
  2. Nata K, Takamura T, Karasawa T, Kumagai T, Hashioka W, Tohgo A, Yonekura H, Takasawa S, Nakamura S, Okamoto H: Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing. Gene. 1997 Feb 28;186(2):285-92. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. States DJ, Walseth TF, Lee HC: Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38. Trends Biochem Sci. 1992 Dec;17(12):495. [PubMed Link Image]
  5. Takasawa S, Tohgo A, Noguchi N, Koguma T, Nata K, Sugimoto T, Yonekura H, Okamoto H: Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP. J Biol Chem. 1993 Dec 15;268(35):26052-4. [PubMed Link Image]
  6. Tohgo A, Takasawa S, Noguchi N, Koguma T, Nata K, Sugimoto T, Furuya Y, Yonekura H, Okamoto H: Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38. J Biol Chem. 1994 Nov 18;269(46):28555-7. [PubMed Link Image]
  7. Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [PubMed Link Image]
  8. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  9. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed Link Image]
  10. Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q: Crystal structure of human CD38 extracellular domain. Structure. 2005 Sep;13(9):1331-9. [PubMed Link Image]
  11. Yagui K, Shimada F, Mimura M, Hashimoto N, Suzuki Y, Tokuyama Y, Nata K, Tohgo A, Ikehata F, Takasawa S, Okamoto H, Makino H, Saito Y, Kanatsuka A: A missense mutation in the CD38 gene, a novel factor for insulin secretion: association with Type II diabetes mellitus in Japanese subjects and evidence of abnormal function when expressed in vitro. Diabetologia. 1998 Sep;41(9):1024-8. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6207
Enzyme 13 Name Ecto-ADP-ribosyltransferase 4
Enzyme 13 Synonyms
  1. Dombrock blood group carrier molecule
  2. Mono(ADP-ribosyl)transferase 4
  3. NAD(P)(+)--arginine ADP-ribosyltransferase 4
  4. CD297 antigen
Enzyme 13 Gene Name ART4
Enzyme 13 Protein Sequence >Ecto-ADP-ribosyltransferase 4
MGPLINRCKKILLPTTVPPATMRIWLLGGLLPFLLLLSGLQRPTEGSEVAIKIDFDFAPG
SFDDQYQGCSKQVMEKLTQGDYFTKDIEAQKNYFRMWQKAHLAWLNQGKVLPQNMTTTHA
VAILFYTLNSNVHSDFTRAMASVARTPQQYERSFHFKYLHYYLTSAIQLLRKDSIMENGT
LCYEVHYRTKDVHFNAYTGATIRFGQFLSTSLLKEEAQEFGNQTLFTIFTCLGAPVQYFS
LKKEVLIPPYELFKVINMSYHPRGNWLQLRSTGNLSTYNCQLLKASSKKCIPDPIAIASL
SFLTSVIIFSKSRV
Enzyme 13 Number of Residues 314
Enzyme 13 Molecular Weight 35877.3
Enzyme 13 Theoretical pI 9.57
Enzyme 13 GO Classification
Function
  • NAD(P)+-protein-arginine ADP-ribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
Component
Enzyme 13 General Function Involved in NAD(P)+-protein-arginine ADP-ribosyltransferase activity
Enzyme 13 Specific Function NAD(+) + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • NAD+ + protein L-arginine = nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine [RN:R00555]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-46
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 10444285 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q93070 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name NAR4_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >945 bp
ATGGGTCCATTGATCAACAGATGCAAGAAGATTCTTCTCCCAACTACTGTACCTCCTGCA
ACGATGAGAATCTGGCTCCTTGGAGGCCTGCTGCCATTCCTGCTGCTCCTCTCTGGCCTG
CAGAGACCCACAGAGGGTTCTGAGGTTGCAATTAAAATCGACTTCGACTTCGCACCAGGT
TCTTTTGATGATCAGTACCAAGGCTGTAGCAAACAGGTTATGGAGAAACTAACTCAAGGG
GATTATTTCACAAAAGACATAGAAGCCCAGAAGAATTATTTTAGGATGTGGCAAAAAGCC
CACTTAGCCTGGCTTAACCAAGGAAAAGTTCTACCCCAGAACATGACTACCACACACGCT
GTGGCTATTTTGTTTTACACATTGAACAGCAATGTTCATTCTGACTTTACTAGAGCCATG
GCCTCTGTTGCCAGGACTCCACAGCAGTATGAACGTTCATTCCACTTCAAATATTTACAC
TACTACCTCACCTCAGCAATCCAGCTGCTGAGGAAAGACAGCATCATGGAGAATGGCACT
CTGTGCTATGAGGTGCATTATAGGACGAAGGATGTCCACTTTAATGCCTACACAGGGGCC
ACCATTCGATTTGGCCAATTCCTTTCCACATCCCTCCTGAAAGAAGAGGCACAGGAGTTT
GGGAACCAGACACTATTTACCATATTCACCTGCCTGGGTGCACCTGTACAGTACTTCTCC
CTCAAGAAGGAAGTCTTGATCCCTCCCTATGAGCTGTTTAAAGTTATAAATATGAGCTAC
CACCCAAGAGGAAACTGGTTGCAGTTGAGGTCAACTGGGAACCTGAGCACATATAACTGT
CAGCTGCTAAAAGCTTCCAGCAAGAAATGCATCCCTGATCCTATAGCTATTGCATCTCTC
TCCTTTTTGACCAGTGTCATCATCTTTTCCAAAAGCAGAGTATAA
Enzyme 13 GenBank Gene ID AF290204 Link Image
Enzyme 13 GeneCard ID ART4 Link Image
Enzyme 13 GenAtlas ID ART4 Link Image
Enzyme 13 HGNC ID HGNC:726 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 12p13-p12
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Gubin AN, Njoroge JM, Wojda U, Pack SD, Rios M, Reid ME, Miller JL: Identification of the dombrock blood group glycoprotein as a polymorphic member of the ADP-ribosyltransferase gene family. Blood. 2000 Oct 1;96(7):2621-7. [PubMed Link Image]
  2. Rios M, Hue-Roye K, Oyen R, Miller J, Reid ME: Insights into the Holley- and Joseph- phenotypes. Transfusion. 2002 Jan;42(1):52-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Koch-Nolte F, Haag F, Braren R, Kuhl M, Hoovers J, Balasubramanian S, Bazan F, Thiele HG: Two novel human members of an emerging mammalian gene family related to mono-ADP-ribosylating bacterial toxins. Genomics. 1997 Feb 1;39(3):370-6. [PubMed Link Image]
  5. Wu GG, Jin SZ, Deng ZH, Zhao TM: Polymerase chain reaction with sequence-specific primers-based genotyping of the human Dombrock blood group DO1 and DO2 alleles and the DO gene frequencies in Chinese blood donors. Vox Sang. 2001 Jul;81(1):49-51. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 13072
Enzyme 14 Name Pre-B-cell colony enhancing factor 1
Enzyme 14 Synonyms
  1. Pre-B-cell colony enhancing factor 1, isoform CRA_a
  2. cDNA FLJ76475, highly similar to Homo sapiens pre-B-cell colony enhancing factor 1
  3. PBEF1, transcript variant 1, mRNA
Enzyme 14 Gene Name PBEF1
Enzyme 14 Protein Sequence >Pre-B-cell colony enhancing factor 1
MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFY
GLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVP
EGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETS
GNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGY
SVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIV
SRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINT
LQEIVEGMKQKMWSIENIAFGSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVAD
PNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHTVFKNGKVTKSYSFDEIRKNA
QLNIELEAAHH
Enzyme 14 Number of Residues 491
Enzyme 14 Molecular Weight 55522
Enzyme 14 Theoretical pI 7.18
Enzyme 14 GO Classification
Function
  • catalytic activity
  • nicotinate phosphoribosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
Component
Enzyme 14 General Function Coenzyme transport and metabolism
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 158259163 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID A4D0Q9 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name A4D0Q9_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID AK292851 Link Image
Enzyme 14 GeneCard ID A4D0Q9 Link Image
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 14591
Enzyme 15 Name Nicotinamide phosphoribosyltransferase
Enzyme 15 Synonyms
  1. NAmPRTase
  2. Nampt
  3. Pre-B-cell colony-enhancing factor 1
  4. Pre-B cell-enhancing factor
  5. Visfatin
Enzyme 15 Gene Name NAMPT
Enzyme 15 Protein Sequence >Nicotinamide phosphoribosyltransferase
MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFY
GLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVP
EGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETS
GNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGY
SVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIV
SRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINT
LQEIVEGMKQKMWSIENIAFGSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVAD
PNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHTVFKNGKVTKSYSFDEIRKNA
QLNIELEAAHH
Enzyme 15 Number of Residues 491
Enzyme 15 Molecular Weight 55520.8
Enzyme 15 Theoretical pI 7.18
Enzyme 15 GO Classification
Function
  • catalytic activity
  • nicotinate phosphoribosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • NAD biosynthetic process
  • cellular metabolic process
  • coenzyme biosynthetic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • metabolic process
  • nicotinamide nucleotide biosynthetic process
  • pyridine nucleotide biosynthetic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 15 General Function Involved in nicotinate phosphoribosyltransferase activity
Enzyme 15 Specific Function Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway
Enzyme 15 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 15 Reactions
  • nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R01271]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID P43490 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name NAMPT_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1476 bp
ATGAATCCTGCGGCAGAAGCCGAGTTCAACATCCTCCTGGCCACCGACTCCTACAAGGTT
ACTCACTATAAACAATATCCACCCAACACAAGCAAAGTTTATTCCTACTTTGAATGCCGT
GAAAAGAAGACAGAAAACTCCAAATTAAGGAAGGTGAAATATGAGGAAACAGTATTTTAT
GGGTTGCAGTACATTCTTAATAAGTACTTAAAAGGTAAAGTAGTAACCAAAGAGAAAATC
CAGGAAGCCAAAGATGTCTACAAAGAACATTTCCAAGATGATGTCTTTAATGAAAAGGGA
TGGAACTACATTCTTGAGAAGTATGATGGGCATCTTCCAATAGAAATAAAAGCTGTTCCT
GAGGGCTTTGTCATTCCCAGAGGAAATGTTCTCTTCACGGTGGAAAACACAGATCCAGAG
TGTTACTGGCTTACAAATTGGATTGAGACTATTCTTGTTCAGTCCTGGTATCCAATCACA
GTGGCCACAAATTCTAGAGAGCAGAAGAAAATATTGGCCAAATATTTGTTAGAAACTTCT
GGTAACTTAGATGGTCTGGAATACAAGTTACATGATTTTGGCTACAGAGGAGTCTCTTCC
CAAGAGACTGCTGGCATAGGAGCATCTGCTCACTTGGTTAACTTCAAAGGAACAGATACA
GTAGCAGGACTTGCTCTAATTAAAAAATATTATGGAACGAAAGATCCTGTTCCAGGCTAT
TCTGTTCCAGCAGCAGAACACAGTACCATAACAGCTTGGGGGAAAGACCATGAAAAAGAT
GCTTTTGAACATATTGTAACACAGTTTTCATCAGTGCCTGTATCTGTGGTCAGCGATAGC
TATGACATTTATAATGCGTGTGAGAAAATATGGGGTGAAGATCTAAGACATTTAATAGTA
TCGAGAAGTACACAGGCACCACTAATAATCAGACCTGATTCTGGAAACCCTCTTGACACT
GTGTTAAAGGTTTTGGAGATTTTAGGTAAGAAGTTTCCTGTTACTGAGAACTCAAAGGGT
TACAAGTTGCTGCCACCTTATCTTAGAGTTATTCAAGGGGATGGAGTAGATATTAATACC
TTACAAGAGATTGTAGAAGGCATGAAACAAAAAATGTGGAGTATTGAAAATATTGCCTTC
GGTTCTGGTGGAGGTTTGCTACAGAAGTTGACAAGAGATCTCTTGAATTGTTCCTTCAAG
TGTAGCTATGTTGTAACTAATGGCCTTGGGATTAACGTCTTCAAGGACCCAGTTGCTGAT
CCCAACAAAAGGTCCAAAAAGGGCCGATTATCTTTACATAGGACGCCAGCAGGGAATTTT
GTTACACTGGAGGAAGGAAAAGGAGACCTTGAGGAATATGGTCAGGATCTTCTCCATACT
GTCTTCAAGAATGGCAAGGTGACAAAAAGCTATTCATTTGATGAAATAAGAAAAAATGCA
CAGCTGAATATTGAACTGGAAGCAGCACATCATTAG
Enzyme 15 GenBank Gene ID U02020 Link Image
Enzyme 15 GeneCard ID NAMPT Link Image
Enzyme 15 GenAtlas ID NAMPT Link Image
Enzyme 15 HGNC ID HGNC:30092 Link Image
Enzyme 15 Chromosome Location 7
Enzyme 15 Locus 7q22.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Samal B, Sun Y, Stearns G, Xie C, Suggs S, McNiece I: Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor. Mol Cell Biol. 1994 Feb;14(2):1431-7. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Khan JA, Tao X, Tong L: Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents. Nat Struct Mol Biol. 2006 Jul;13(7):582-8. Epub 2006 Jun 18. [PubMed Link Image]
  10. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 15317
Enzyme 16 Name ART5 protein precursor (ADP-ribosyltransferase 5, isoform CRA_b)
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name ART5
Enzyme 16 Protein Sequence >ART5 protein precursor (ADP-ribosyltransferase 5, isoform CRA_b)
MALAALMIALGSLGLHTWQAQAVPTILPLGLAPDTFDDTYVGCAEEMEEKAAPLLKEEMA
HHALLRESWEAAQETWEDKRRGLTLPPGFKAQNGIAIMVYTNSSNTLYWELNQAVRTGGG
SRELYMRHFPFKALHFYLIRALQLLRGSGGCSRGPGEVVFRGVGSLRFEPKRLGDSVRLG
QFASSSLDKAVAHRFGNATLFSLTTCFGAPIQAFSVFPKEREVLIPPHEVFLVTRFSQDG
AQSLVTLWSYNQTCSHFNCAYLGGEKRRGCVSAPGALGTGDLHMTKRHLQQP
Enzyme 16 Number of Residues 292
Enzyme 16 Molecular Weight 32155
Enzyme 16 Theoretical pI 8.38
Enzyme 16 GO Classification
Function
  • NAD(P)+-protein-arginine ADP-ribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid ADP-ribosylation
  • protein modification
Component
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-21
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 29788058 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q86W02 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name Q86W02_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >879 bp
ATGGCGCTGGCGGCTTTGATGATCGCCCTCGGCAGCCTCGGCCTCCACACCTGGCAGGCC
CAGGCTGTTCCCACCATCCTGCCCCTGGGCCTGGCTCCAGACACCTTTGACGATACCTAT
GTGGGTTGTGCAGAGGAGATGGAGGAGAAGGCAGCCCCCCTGCTAAAGGAGGAAATGGCC
CACCATGCCCTGCTGCGGGAATCCTGGGAGGCAGCCCAGGAGACCTGGGAGGACAAGCGT
CGAGGGCTTACCTTGCCCCCTGGCTTCAAAGCCCAGAATGGAATAGCCATTATGGTCTAC
ACCAACTCATCGAACACCTTGTACTGGGAGTTGAATCAGGCCGTGCGGACGGGCGGAGGC
TCCCGGGAGCTCTACATGAGGCACTTTCCCTTCAAGGCCCTGCATTTCTACCTGATCCGG
GCCCTGCAGCTGCTGCGAGGCAGTGGGGGCTGCAGCAGGGGACCTGGGGAGGTGGTGTTC
CGAGGTGTGGGCAGCCTTCGCTTTGAACCCAAGAGGCTGGGGGACTCTGTCCGCTTGGGC
CAGTTTGCCTCCAGCTCCCTGGATAAGGCAGTGGCCCACAGATTTGGTAATGCCACCCTC
TTCTCTCTAACAACTTGCTTTGGGGCCCCTATACAGGCCTTCTCTGTCTTTCCCAAGGAG
CGCGAGGTGCTGATTCCCCCCCATGAAGTCTTTTTGGTTACCAGATTCTCTCAGGATGGA
GCCCAGAGCTTGGTGACTCTCTGGAGCTATAATCAGACCTGTAGCCATTTTAACTGCGCC
TATCTGGGTGGGGAGAAGAGGCGGGGCTGTGTGTCTGCGCCAGGAGCCCTGGGAACGGGT
GACCTTCATATGACGAAGAGGCACCTCCAGCAGCCTTGA
Enzyme 16 GenBank Gene ID Y16835 Link Image
Enzyme 16 GeneCard ID Q86W02 Link Image
Enzyme 16 GenAtlas ID ART5 Link Image
Enzyme 16 HGNC ID HGNC:24049 Link Image
Enzyme 16 Chromosome Location 11
Enzyme 16 Locus 11p15.4
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Glowacki G, Braren R, Firner K, Nissen M, Kuhl M, Reche P, Bazan F, Cetkovic-Cvrlje M, Leiter E, Haag F, Koch-Nolte F: The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse. Protein Sci. 2002 Jul;11(7):1657-70. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 15855
Enzyme 17 Name Poly (ADP-ribose) polymerase family, member 4
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name PARP4
Enzyme 17 Protein Sequence >Poly (ADP-ribose) polymerase family, member 4
MVMGIFANCIFCLKVKYLPQQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNADVLSQYQ
LNSIQKNHVHIANPDFIWKSIREKRLLDVKNYDPYKPLDITPPPDQKASSSEVKTEGLCP
DSATEEEDTVELTEFGMQNVEIPHLPQDFEVAKYNTLEKVGMEGGQEAVVVELQCSRDSR
DCPFLISSHFLLDDGMETRRQFAIKKTSEDASEYFENYIEELKKQGFLLREHFTPEATQL
ASEQLQALLLEEVMNSSTLSQEVSDLVEMIWAEALGHLEHMLLKPVNRISLNDVSKAEGI
LLLVKAALKNGETAEQLQKMMTEFYRLIPHKGTMPKEVNLGLLAKKADLCQLIRDMVNVC
ETNLSKPNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNHHSKSPVDVLQIFRVGRV
NETTEFLSKLGNVRPLLHGSPVQNIVGILCRGLLLPKVVEDRGVQRTDVGNLGSGIYFSD
SLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFSLTEAPPGYDSVHGVSQTASVT
TDFEDDEFVVYKTNQVKMKYIIKFSMPGDQIKDFHPSDHTELEEYRPEFSNFSKVEDYQL
PDAKTSSSTKAGLQDASGNLVPLEDVHIKGRIIDTVAQVIVFQTYTNKSHVPIEAKYIFP
LDDKAAVCGFEAFINGKHIVGEIKEKEEAQQEYLEAVTQGHGAYLMSQDAPDVFTVSVGN
LPPKAKVLIKITYITELSILGTVGVFFMPATVAPWQQDKALNENLQDTVEKICIKEIGTK
QSFSLTMSIEMPYVIEFIFSDTHELKQKRTDCKAVISTMEGSSLDSSGFSLHIGLSAAYL
PRMWVEKHPEKESEACMLVFQPDLDVDLPDLASESEVIICLDCSSSMEGVTFLQAKQIAL
HALSLVGEKQKVNIIQFGTGYKELFSYPKHITSNTMAAEFIMSATPTMGNTDFWKTLRYL
SLLYPARGSRNILLVSDGHLQDESLTLQLVKRSRPHTRLFACGIGSTANRHVLRILSQCG
AGVFEYFNAKSKHSWRKQIEDQMTRLCSPSCHSVSVKWQQLNPDVPEALQAPAQVPSLFL
NDRLLVYGFIPHCTQATLCALIQEKEFRTMVSTTELQKTTGTMIHKLAARALIRDYEDGI
LHENETSHEMKKQTLKSLIIKLSKENSLITQFTSFVAVEKRDENESPFPDIPKVSELIAK
EDVDFLPYMSWQGEPQEAVRNQSLLASSEWPELRLSKRKHRKIPFSKRKMELSQPEVSED
FEEDGLGVLPAFTSNLERGGVEKLLDLSWTESCKPTATEPLFKKVSPWETSTSSFFPILA
PAVGSYLPPTARAHSPASLSFASYRQVASFGSAAPPRQFDASQFSQGPVPGTCADWIPQS
ASCPTGPPQNPPSSPYCGIVFSGSSLSSAQSAPLQHPGGFTTRPSAGTFPELDSPQLHFS
LPTDPDPIRGFGSYHPSASSPFHFQPSAASLTANLRLPMASALPEALCSQSRTTPVDLCL
LEESVGSLEGSRCPVFAFQSSDTESDELSEVLQDSCFLQIKCDTKDDSILCFLEVKEEDE
IVCIQHWQDAVPWTELLSLQTEDGFWKLTPELGLILNLNTNGLHSFLKQKGIQSLGVKGR
ECLLDLIATMLVLQFIRTRLEKEGIVFKSLMKMDDASISRNIPWAFEAIKQASEWVRRTE
GQYPSICPRLELGNDWDSATKQLLGLQPISTVSPLHRVLHYSQG
Enzyme 17 Number of Residues 1724
Enzyme 17 Molecular Weight 192592.9
Enzyme 17 Theoretical pI 5.39
Enzyme 17 GO Classification
Function
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
Component
  • cell part
  • intracellular
Enzyme 17 General Function Involved in NAD+ ADP-ribosyltransferase activity
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 55959320 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q5QNZ9 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name Q5QNZ9_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >5175 bp
ATGGTGATGGGAATCTTTGCAAATTGTATCTTCTGTTTGAAAGTGAAGTACTTACCTCAG
CAGCAGAAGAAAAAGCTACAAACTGACATTAAGGAAAATGGCGGAAAGTTTTCCTTTTCG
TTAAATCCTCAGTGCACACATATAATCTTAGATAATGCTGATGTTCTGAGTCAGTACCAA
CTGAATTCTATCCAAAAGAACCACGTTCATATTGCAAACCCAGATTTTATATGGAAATCT
ATCAGGGAAAAGAGACTCTTGGATGTAAAGAATTATGATCCTTATAAGCCCCTGGACATC
ACACCACCTCCTGATCAGAAGGCGAGCAGTTCTGAAGTGAAAACAGAAGGTCTATGCCCG
GACAGTGCCACAGAGGAGGAAGACACTGTGGAACTCACTGAGTTTGGTATGCAGAATGTT
GAAATTCCTCATCTTCCTCAAGATTTTGAAGTTGCAAAATATAACACCTTGGAGAAAGTG
GGAATGGAGGGAGGCCAGGAAGCTGTGGTGGTGGAGCTTCAGTGTTCGCGGGACTCCAGG
GACTGTCCTTTCCTGATATCCTCACACTTCCTCCTGGATGATGGCATGGAGACTAGAAGA
CAGTTTGCTATAAAGAAAACCTCTGAAGATGCAAGTGAATACTTTGAAAATTACATTGAA
GAACTGAAGAAACAAGGATTTCTACTAAGAGAACATTTCACACCTGAAGCAACCCAATTA
GCATCTGAACAATTGCAAGCATTGCTTTTGGAGGAAGTCATGAATTCAAGCACTCTGAGC
CAAGAGGTGAGCGATTTAGTAGAGATGATTTGGGCAGAGGCCCTGGGCCACCTGGAACAC
ATGCTTCTCAAGCCAGTGAACAGGATTAGCCTCAACGATGTGAGCAAGGCAGAGGGGATT
CTCCTTCTAGTAAAGGCAGCACTGAAAAATGGAGAAACAGCAGAGCAATTGCAAAAGATG
ATGACAGAGTTTTACAGACTGATACCTCACAAAGGCACAATGCCCAAAGAAGTGAACCTG
GGACTATTGGCTAAGAAAGCAGACCTCTGCCAGCTAATAAGAGACATGGTTAATGTCTGT
GAAACTAATTTGTCCAAACCCAACCCACCATCCCTGGCCAAATACCGAGCTTTGAGGTGC
AAAATTGAGCATGTTGAACAGAATACTGAAGAATTTCTCAGGGTTAGAAAAGAGGTTTTG
CAGAATCATCACAGTAAGAGCCCAGTGGATGTCTTGCAGATATTTAGAGTTGGCAGAGTG
AATGAAACCACAGAGTTTTTGAGCAAACTTGGTAATGTGAGGCCCTTGTTGCATGGTTCT
CCTGTACAAAACATCGTGGGAATCTTGTGTCGAGGGTTGCTTTTACCCAAAGTAGTGGAA
GATCGTGGTGTGCAAAGAACAGACGTCGGAAACCTTGGAAGTGGGATTTATTTCAGTGAT
TCGCTCAGTACAAGTATCAAGTACTCACACCCGGGAGAGACAGATGGCACCAGACTCCTG
CTCATTTGTGACGTAGCCCTCGGAAAGTGTATGGACTTACATGAGAAGGACTTTTCCTTA
ACTGAAGCACCACCAGGCTACGACAGTGTGCATGGAGTTTCGCAAACAGCCTCTGTCACC
ACAGACTTTGAGGATGATGAATTTGTTGTCTATAAAACCAATCAGGTTAAAATGAAATAT
ATTATTAAATTTTCCATGCCTGGAGATCAGATAAAGGACTTTCATCCTAGTGATCATACT
GAATTAGAGGAATACAGACCTGAGTTTTCAAATTTTTCAAAGGTTGAAGATTACCAGTTA
CCAGATGCCAAAACTTCCAGCAGCACCAAGGCCGGCCTCCAGGATGCCTCTGGGAACTTG
GTTCCTCTGGAGGATGTCCACATCAAAGGGAGAATCATAGACACTGTAGCCCAGGTCATT
GTTTTTCAGACATACACAAATAAAAGTCACGTGCCCATTGAGGCAAAATATATCTTTCCT
TTGGATGACAAGGCCGCTGTGTGTGGCTTCGAAGCCTTCATCAATGGGAAGCACATAGTT
GGAGAGATTAAAGAGAAGGAAGAAGCCCAGCAAGAGTACCTAGAAGCCGTGACCCAGGGC
CATGGCGCTTACCTGATGAGTCAGGATGCTCCGGACGTTTTTACTGTAAGTGTTGGAAAC
TTACCCCCTAAGGCTAAGGTTCTTATAAAAATTACCTACATCACAGAACTCAGCATCCTG
GGCACTGTTGGTGTCTTTTTCATGCCCGCCACCGTAGCACCCTGGCAACAGGACAAGGCT
TTGAATGAAAACCTTCAGGATACAGTAGAGAAGATTTGTATAAAAGAAATAGGAACAAAG
CAAAGCTTCTCTTTGACTATGTCTATTGAGATGCCGTATGTGATTGAATTCATTTTCAGT
GATACACATGAACTGAAACAAAAGCGCACAGACTGCAAAGCTGTCATTAGCACCATGGAA
GGCAGCTCCTTAGACAGCAGTGGATTTTCTCTCCACATCGGTTTGTCTGCTGCCTATCTC
CCAAGAATGTGGGTTGAAAAACATCCAGAAAAAGAAAGCGAGGCTTGCATGCTTGTCTTT
CAACCCGATCTCGATGTCGACCTCCCTGACCTAGCCAGTGAGAGCGAAGTGATTATTTGT
CTTGACTGCTCCAGTTCCATGGAGGGTGTGACATTCTTGCAAGCCAAGCAAATCGCCTTG
CATGCGCTGTCCTTGGTGGGTGAGAAGCAGAAAGTAAATATTATCCAGTTCGGCACAGGT
TACAAGGAGCTATTTTCGTATCCTAAGCATATCACAAGCAATACCATGGCAGCAGAGTTC
ATCATGTCTGCCACACCTACCATGGGGAACACAGACTTCTGGAAAACACTCCGATATCTT
AGCTTATTGTACCCTGCTCGAGGGTCACGGAACATCCTCCTGGTGTCTGATGGGCACCTC
CAGGATGAGAGCCTGACATTACAGCTCGTGAAGAGGAGCCGCCCGCACACCAGGTTATTC
GCCTGCGGTATCGGTTCTACAGCAAATCGTCACGTCTTAAGGATTTTGTCCCAGTGTGGT
GCCGGAGTATTTGAATATTTTAATGCAAAATCCAAGCATAGTTGGAGAAAACAGATAGAA
GACCAAATGACCAGGCTATGTTCTCCGAGTTGCCACTCTGTCTCCGTCAAATGGCAGCAA
CTCAATCCAGATGTGCCCGAGGCCCTGCAGGCCCCAGCCCAGGTGCCGTCCTTGTTTCTC
AATGATCGACTCCTTGTCTATGGATTCATTCCTCACTGCACACAGGCAACTCTGTGTGCA
CTAATTCAAGAGAAAGAATTTCGTACAATGGTGTCGACTACTGAGCTTCAGAAGACAACT
GGAACTATGATCCACAAGCTGGCAGCCCGAGCTCTAATCAGAGATTATGAAGATGGCATT
CTTCACGAAAATGAAACCAGTCATGAGATGAAAAAACAAACCTTGAAATCTCTGATTATT
AAACTCAGTAAAGAAAACTCTCTCATAACACAATTTACAAGCTTTGTGGCAGTTGAGAAA
AGGGATGAGAATGAGTCGCCTTTTCCTGATATTCCAAAAGTTTCTGAACTTATTGCCAAA
GAAGATGTAGACTTCCTGCCCTACATGAGCTGGCAGGGGGAGCCCCAAGAAGCCGTCAGG
AACCAGTCTCTTTTAGCATCCTCTGAGTGGCCAGAATTACGTTTATCCAAACGAAAACAT
AGGAAAATTCCATTTTCCAAAAGAAAAATGGAATTATCTCAGCCAGAAGTTTCTGAAGAT
TTTGAAGAGGATGGCTTAGGTGTACTACCAGCTTTCACATCAAATTTGGAACGTGGAGGT
GTGGAAAAGCTATTGGATTTAAGTTGGACAGAGTCATGTAAACCAACAGCAACTGAACCA
CTATTTAAGAAAGTCAGTCCATGGGAAACATCTACTTCTAGCTTTTTTCCTATTTTGGCT
CCGGCCGTTGGTTCCTATCTTCCCCCGACTGCCCGCGCTCACAGTCCTGCTTCCTTGTCT
TTTGCCTCATATCGTCAGGTAGCTAGTTTCGGTTCAGCTGCTCCTCCCAGACAGTTTGAT
GCATCTCAATTCAGCCAAGGCCCTGTGCCTGGCACTTGTGCTGACTGGATCCCACAGTCG
GCGTCTTGTCCCACAGGACCTCCCCAGAACCCACCTTCTTCACCCTATTGTGGCATTGTT
TTTTCAGGGAGCTCATTAAGCTCTGCACAGTCTGCTCCACTGCAACATCCTGGAGGCTTT
ACTACCAGGCCTTCTGCTGGCACCTTCCCTGAGCTGGATTCTCCCCAGCTTCATTTCTCT
CTTCCTACAGACCCTGATCCCATCAGAGGTTTTGGGTCTTATCATCCCTCTGCTTCCTCT
CCTTTTCATTTTCAACCTTCCGCAGCCTCTTTGACTGCCAACCTTAGGCTGCCAATGGCC
TCTGCTTTACCTGAGGCTCTTTGCAGTCAGTCCCGGACTACCCCAGTAGATCTCTGTCTT
CTAGAAGAATCAGTAGGCAGTCTCGAAGGAAGTCGATGTCCTGTCTTTGCTTTTCAAAGT
TCTGACACAGAAAGTGATGAGCTATCAGAAGTACTTCAAGACAGCTGCTTTTTACAAATA
AAATGTGATACAAAAGATGACAGTATCCTGTGCTTTCTGGAAGTAAAAGAAGAGGATGAA
ATAGTGTGCATACAACACTGGCAGGATGCTGTGCCTTGGACAGAACTCCTCAGTCTACAG
ACAGAGGATGGCTTCTGGAAACTTACACCAGAACTGGGACTTATATTAAATCTTAATACA
AATGGTTTGCACAGCTTTCTTAAACAAAAAGGCATTCAATCTCTAGGTGTAAAAGGAAGA
GAATGTCTCCTGGACCTAATTGCCACAATGCTGGTACTACAGTTTATTCGCACCAGGTTG
GAAAAAGAGGGAATAGTGTTCAAATCACTGATGAAAATGGATGACGCTTCTATTTCCAGG
AATATTCCCTGGGCTTTTGAGGCAATAAAGCAAGCAAGTGAATGGGTAAGAAGAACTGAA
GGACAGTACCCATCTATCTGCCCACGGCTTGAACTGGGGAACGACTGGGACTCTGCCACC
AAGCAGTTGCTGGGACTCCAGCCCATAAGCACTGTGTCCCCTCTTCATAGAGTCCTCCAT
TACAGTCAAGGCTAA
Enzyme 17 GenBank Gene ID AL359763 Link Image
Enzyme 17 GeneCard ID PARP4 Link Image
Enzyme 17 GenAtlas ID PARP4 Link Image
Enzyme 17 HGNC ID HGNC:271 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 13q11
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References Not Available
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 16525
Enzyme 18 Name cDNA, FLJ92858, highly similar to Homo sapiens bone marrow stromal cell antigen 1 (BST1), mRNA (Bone marrow stromal cell antigen 1)
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name BST1
Enzyme 18 Protein Sequence >cDNA, FLJ92858, highly similar to Homo sapiens bone marrow stromal cell antigen 1 (BST1), mRNA (Bone marrow stromal cell antigen 1)
MAAQGCAASRLLQLLLQLLLLLLLLAAGGARARWRGEGTSAHLRDIFLGRCAEYRALLSP
EQRNKNCTAIWEAFKVALDKDPCSVLPSDYDLFINLSRHSIPRDKSLFWENSHLLVNSFA
DNTRRFMPLSDVLYGRVADFLSWCRQKNDSGLDYQSCPTSEDCENNPVDSFWKRASIQYS
KDSSGVIHVMLNGSEPTGAYPIKGFFADYEIPNLQKEKITRIEIWVMHEIGGPNVESCGE
GSMKVLEKRLKDMGFQYSCINDYRPVKLLQCVDHSTHPDCALKSAAAATQRKAPSLYTEQ
RAGLIIPLFLVLASRTQL
Enzyme 18 Number of Residues 318
Enzyme 18 Molecular Weight 35724
Enzyme 18 Theoretical pI 7.86
Enzyme 18 GO Classification
Function
  • NAD+ nucleosidase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing N-glycosyl compounds
Process
Component
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID B2R6A2 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name B2R6A2_HUMAN Link Image
Enzyme 18 PDB ID 1ISM Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID AK312497 Link Image
Enzyme 18 GeneCard ID B2R6A2 Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 16699
Enzyme 19 Name Poly (ADP-ribose) polymerase family, member 1 (Poly (ADP-ribose) polymerase family, member 1, isoform CRA_a)
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name PARP1
Enzyme 19 Protein Sequence >Poly (ADP-ribose) polymerase family, member 1 (Poly (ADP-ribose) polymerase family, member 1, isoform CRA_a)
MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKV
GHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKS
NRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQ
LKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKA
QNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSG
QLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPE
TSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLT
GTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSP
WGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLE
HSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNK
LEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPG
TKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAV
SQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRG
GSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIE
REGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM
VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSA
NISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW
Enzyme 19 Number of Residues 1014
Enzyme 19 Molecular Weight 113085
Enzyme 19 Theoretical pI 9.34
Enzyme 19 GO Classification
Function
  • DNA binding
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • DNA metabolism
  • biopolymer metabolism
  • biopolymer modification
  • cellular metabolism
  • macromolecule metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • protein amino acid ADP-ribosylation
  • protein modification
Component
  • cell
  • intracellular
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID B1ANJ4 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name B1ANJ4_HUMAN Link Image
Enzyme 19 PDB ID 1WOK Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AL359704 Link Image
Enzyme 19 GeneCard ID B1ANJ4 Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available