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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
SDF File Show
PDB File Show
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. Mono-ADP-ribosyltransferase sirtuin-6
  5. Poly [ADP-ribose] polymerase 3
  6. Ecto-ADP-ribosyltransferase 3 precursor
  7. GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 precursor
  8. Tankyrase-1
  9. ADP-ribosyl cyclase 2 precursor
  10. Poly [ADP-ribose] polymerase 2
  11. ADP-ribosyl cyclase 1
  12. Ecto-ADP-ribosyltransferase 4 precursor
  13. Pre-B-cell colony enhancing factor 1
  14. ART5 protein precursor (ADP-ribosyltransferase 5, isoform CRA_b)
  15. Poly (ADP-ribose) polymerase family, member 4
  16. cDNA, FLJ92858, highly similar to Homo sapiens bone marrow stromal cell antigen 1 (BST1), mRNA (Bone marrow stromal cell antigen 1)
  17. 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 29574
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 Not Available
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
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 11
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. 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]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5805
Enzyme 2 Name Purine nucleoside phosphorylase
Enzyme 2 Synonyms
  1. Inosine phosphorylase
  2. PNP
Enzyme 2 Gene Name NP
Enzyme 2 Protein Sequence >Purine nucleoside phosphorylase 
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Enzyme 2 Number of Residues 289
Enzyme 2 Molecular Weight 32118
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 metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
—
Enzyme 2 General Function Nucleotide transport and metabolism
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
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 NP Link Image
Enzyme 2 GenAtlas ID NP Link Image
Enzyme 2 HGNC ID HGNC:7892 Link Image
Enzyme 2 Chromosome Location 14
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. 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]
  5. 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]
  6. 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. Tankyrase II
  3. TNKS-2
  4. TRF1- interacting ankyrin-related ADP-ribose polymerase 2
  5. Tankyrase-like protein
  6. 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 126919
Enzyme 3 Theoretical pI 7.20
Enzyme 3 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
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid ADP-ribosylation
  • protein modification
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 3 General Function Not Available
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+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 10953952 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 >3800 bp 
GGCACGAGGCTGGACGGAGCTGGCAGGAGGGGCCTTGCCAGCTTCCGCCGCCGCGTCGTT
TCAGGACCCGGACGGCGGATTCGCGCTGCCTCCGCCGCCGCGGGGCAGCCGGGGGGCAGG
GAGCCCAGCGAGGGGCGCGCGTGGGCGGCCATGGGACTGCGCCGGATCCGGTGACAGCAG
GGAGCCAAGCGGCCCGGGCCCTGAGCGCGTCTTCTCCGGGGGGCCTCGCCCTCCTGCTCG
CGGGGCCGGGGCTCCTGCTCCGGTTGCTGGCGCTGTTGCTGGCTGTGGCGGCGGCCAGGA
TCATGTCGGGTCGCCGCTGCGCCGGCGGGGGAGCGGCCTGCGCGAGCGCCGCGGCCGAGG
CCGTGGAGCCGGCCGCCCGAGAGCTGTTCGAGGCGTGCCGCAACGGGGACGTGGAACGAG
TCAAGAGGCTGGTGACGCCTGAGAAGGTGAACAGCCGCGACACGGCGGGCAGGAAATCCA
CCCCGCTGCACTTCGCCGCAGNTTTTGGGCGGAAAGACGTAGTTGAATATTTGCTTCAGA
ATGGTGCAAATGTCCAAGCACGTGATGATGGGGGCCTTATTCCTCTTCATAATGCATGCT
CTTTTGGTCATGCTGAAGTAGTCAATCTCCTTTTGCGACATGGTGCAGACCCCAATGCTC
GAGATAATTGGAATTATACTCCTCTCCATGAAGCTGCAATTAAAGGAAAGATTGATGTTT
GCATTGTGCTGTTACAGCATGGAGCTGAGCCAACCATCCGAAATACAGATGGAAGGACAG
CATTGGATTTAGCAGATCCATCTGCCAAAGCAGTGCTTACTGGTGAATATAAGAAAGATG
AACTCTTAGAAAGTGCCAGGAGTGGCAATGAAGAAAAAATGATGGCTCTACTCACACCAT
TAAATGTCAACTGCCACGCAAGTGATGGCAGAAAGTCAACTCCATTACATTTGGCAGCAG
GATATAACAGAGTAAAGATTGTACAGCTGTTACTGCAACATGGAGCTGATGTCCATGCTA
AAGATAAAGGTGATCTGGTACCATTACACAATGCCTGTTCTTATGGTCATTATGAAGTAA
CTGAACTTTTGGTCAAGCATGGTGCCTGTGTAAATGCAATGGACTTGTGGCAATTCACTC
CTCTTCATGAGGCAGCTTCTAAGAACAGGGTTGAAGTATGTTCTCTTCTCTTAAGTTATG
GTGCAGACCCAACACTGCTCAATTGTCACAATAAAAGTGCTATAGACTTGGCTCCCACAC
CACAGTTAAAAGAAAGATTAGCATATGAATTTCAAAGGCCACTCGTTGCTGCAASTGCAC
GAGAAGCTGATGTTACTCGAATCAAAAAACATCTCTCTCTGGAAATGGTGATTCAAGCAT
CTCAAACACATGAAACAGCATTGCATTGTGCTGCTGCATCTCCATATCCCAAAAGAAAGC
AAATATGTGAACTGTTGCTAAGAAAAGGAGCAAACATCAATGAAAAGACTAAAGAATTCT
TGACTCCTCTGCACGTGGCATCTGAGAAAGCTCATAATGATGTTGTTGAAGTAGTGGTGA
AACATGAAGCAAAGGTTAATGCTCTGGATAATCTTGGTCAGACTTCTCTACACAGAGCTG
CATATTGTGGTCATCTACAAACCTGCCGCCTACTCCTGAGCTATGGGTGTGATCCTAACA
TTATATCCCTTCAGGGCTTTACTGCTTTACAGATGGGAAATGAAAATGTACAGCAACTCC
TCCAAGAGGGTATCTCATTAGGTAATTCAGAGGCAGACAGACAATTGCTGGAAGCTGCAA
AGGCTGGAGATGTCGAAACTGTAAAAAAACTGTGTACTGTTCAGAGTGTCAACTGCAGAG
ACATTGAAGGGCGTCAGTCTACACCACTTCATTTTGCAGCTGGGTATAACAGAGTGTCCG
TGGTGGAATATCTGCTACAGCATGGAGCTGATGTGCATGCTAAAGATAAAGGAGGCCTTG
TACCTTTGCACAATGCATGTTCTTATGGACATTATGAAGTTGCAGAACTTCTTGTTAAAC
ATGGAGCAGTAGTTAATGTAGCTGATTTATGGAAATTTACACCTTTACATGAAGCAGCAG
CAAAAGGAAAATATGAAATTTGCAAACTTCTGCTCCAGCATGGTGCAGACCCTACAAAAA
AAAACAGGGATGGAAATACTCCTTTGGATCTTGTTAAAGATGGAGATACAGATATTCAAG
ATCTGCTTAGGGGAGATGCAGCTTTGCTAGATGCTGCCAAGAAGGGTTGTTTAGCCAGAG
TGAAGAAGTTGTCTTCTCCTGATAATGTAAATTGCCGCGATACCCAAGGCAGACATTCAA
CACCTTTACATTTAGCAGCTGGTTATAATAATTTAGAAGTTGCAGAGTATTTGTTACAAC
ACGGAGCTGATGTGAATGCCCAAGACAAAGGAGGACTTATTCCTTTACATAATGCAGCAT
CTTACGGGCATGTAGATGTAGCAGCTCTACTAATAAAGTATAATGCATGTGTCAATGCCA
CGGACAAATGGGCTTTCACACCTTTGCACGAAGCAGCCCAAAAGGGACGAACACAGCTTT
GTGCTTTGTTGCTAGCCCATGGAGCTGACCCGACTCTTAAAAATCAGGAAGGACAAACAC
CTTTAGATTTAGTTTCAGCGGATGATGTCAGCGCTCTTCTGACAGCAGCCATGCCCCCAT
CTGCTCTGCCCTCTTGTTACAAGCCTCAAGTGCTCAATGGTGTGAGAAGCCCAGGAGCCA
CTGCAGATGCTCTCTCTTCAGGTCCATCTAGCCCATCAAGCCTTTCTGCAGCCAGCAGTC
TTGACAACTTATCTGGGAGTTTTTCAGAACTGTCTTCAGTAGTTAGTTCAAGTGGAACAG
AGGGTGCTTCCAGTTTGGAGAAAAAGGAGGTTCCAGGAGTAGATTTTAGCATAACTCAAT
TCGTAAGGAATCTTGGACTTGAGCACCTAATGGATATATTTGAGAGAGAACAGATCACTT
TGGATGTATTAGTTGAGATGGGGCACAAGGAGCTGAAGGAGATTGGAATCAATGCTTATG
GACATAGGCACAAACTAATTAAAGGAGTCGAGAGACTTATCTCCGGACAACAAGGTCTTA
ACCCATATTTAACTTTGAACACCTCTGGTAGTGGAACAATTCTTATAGATCTGTCTCCTG
ATGATAAAGAGTTTCAGTCTGTGGAGGAAGAGATGCAAAGTACAGTTCGAGAGCACAGAG
ATGGAGGTCATGCAGGTGGAATCTTCAACAGATACAATATTCTCAAGATTCAGAAGGTTT
GTAACAAGAAACTATGGGAAAGATACACTCACCGGAGAAAAGAAGTTTCTGAAGAAAACC
ACAACCATGCCAATGAACGAATGCTATTTCATGGGTCTCCTTTTGTGAATGCAATTATCC
ACAAAGGCTTTGATGAAAGGCATGCGTACATAGGTGGTATGTTTGGAGCTGGCATTTATT
TTGCTGAAAACTCTTCCAAAAGCAATCAATATGTATATGGAATTGGAGGAGGTACTGGGT
GTCCAGTTCACAAAGACAGATCTTGTTACATTTGCCACAGGCAGCTGCTCTTTTGCCGGG
TAACCTTGGGAAAGTCTTTCCTGCAGTTCAGTGCAATGAAAATGGCACATTCTCCTCCAG
GTCATCACTCAGTCACTGGTAGGCCCAGTGTAAATGGCCTAGCATTAGCTGAATATGTTA
TTTACAGAGGAGAACAGGCTTATCCTGAGTATTTAATTACTTACCAGATTATGAGGCCTG
AAGGTATGGTCGATGGATAA
Enzyme 3 GenBank Gene ID AF305081 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 10
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. 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 Mono-ADP-ribosyltransferase sirtuin-6
Enzyme 4 Synonyms
  1. SIR2-like protein 6
Enzyme 4 Gene Name SIRT6
Enzyme 4 Protein Sequence >Mono-ADP-ribosyltransferase sirtuin-6 
MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVWQSSSVVFHTGAGISTASG
IPDFRGPHGVWTMEERGLAPKFDTTFESARPTQTHMALVQLERVGLLRFLVSQNVDGLHV
RSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKATGRLCTVAKARGLRACRGE
LRDTILDWEDSLPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVN
LQPTKHDRHADLRIHGYVDEVMTRLMKHLGLEIPAWDGPRVLERALPPLPRPPTPKLEPK
EESPTRINGSIPAGPKQEPCAQHNGSEPASPKRERPTSPAPHRPPKRVKAKAVPS
Enzyme 4 Number of Residues 355
Enzyme 4 Molecular Weight 39119
Enzyme 4 Theoretical pI 9.67
Enzyme 4 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
  • cellular metabolism
  • chromatin silencing
  • gene silencing
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • chromatin remodeling complex
  • chromatin silencing complex
  • protein complex
Enzyme 4 General Function Transcription
Enzyme 4 Specific Function NAD(P)(+) + protein-L-arginine = nicotinamide + omega-N-(ADP-D-ribosyl)-protein-L-arginine
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • NAD(P)+ + L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-L-arginine
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 19
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]
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. NAD(+ADP- ribosyltransferase 3
  3. Poly[ADP-ribose] synthetase 3
  4. pADPRT-3
  5. hPARP-3
  6. IRT1
Enzyme 5 Gene Name PARP3
Enzyme 5 Protein Sequence >Poly [ADP-ribose] polymerase 3 
MAPKPKPWVQTEGPEKKKGRQAGREEDPFRSTAEALKAIPAEKRIIRVDPTCPLSSNPGT
QVYEDYNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNRWGRVGEVGQSKINHFTRLED
AKKDFEKKFREKTKNNWAERDHFVSHPGKYTLIEVQAEDEAQEAVVKVDRGPVRTVTKRV
QPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEAL
KGPTDGGQSLEELSSHFYTVIPHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQA
VSEQEKTVEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQTGSNHRCPTLQHIWK
VNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHSGGRVGKGIYFASENS
KSAGYVIGMKCGAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPT
QDTELELDGQQVVVPQGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVHL
Enzyme 5 Number of Residues 533
Enzyme 5 Molecular Weight 60090
Enzyme 5 Theoretical pI 6.79
Enzyme 5 GO Classification
Function
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ 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
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 5 General Function Not Available
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
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 4808552 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
CAGGTGTATGAGGACTACAACTGCACCCTGAACCAGACCAACATCGAGAACAACAACAAG
AAGTTCTACATCATCCAGCTGCTCCAAGACAGCAACCGCTTCTTCACCTGCTGGAACCGC
TGGGGCCGTGTGGGAGAGGTCGGCCAGTCAAAGATCAACCACTTCACAAGGCTAGAAGAT
GCAAAGAAGGACTTTGAGAAGAAATTTCGGGAAAAGACCAAGAACAACTGGGCAGAGCGG
GACCACTTTGTGTCTCACCCGGGCAAGTACACACTTATCGAAGTACAGGCAGAGGATGAG
GCCCAGGAAGCTGTGGTGAAGGTGGACAGAGCCCCAGTGAGGACTGTGACTAAGCGGGTG
CAGCCCTGCTCCCTGGACCCAGCCACGCAGAAGCTCATCACTAACATCTTCAGCAAGGAG
ATGTTCAAGAACACCATGGCCCTCATGGACCTGGATGTGAAGAAGATGCCCCTGGGAAAG
CTGAGCAAGCAACAGATTGCACGGGGTTTCGAGGCCTTGGAGGCGCTGGAGGAGGCCCTG
AAAGGCCCCACGGATGGTGGCCAAAGCCTGGAGGAGCTGTCCTCACACTTTTACACCGTC
ATCCCGCACAACTTCGGCCACAGCCAGCCCCCGCCCATCAATTCCCCTGAGCTTCTGCAG
GCCAAGAAGGACATGCTGCTGGTGCTGGCGGACATCGAGCTGGCCCAGGCCCTGCAGGCA
GTCTCTGAGCAGGAGAAGACGGTGGAGGAGGTGCCACACCCCCTGGACCGAGACTACCAG
CTTCTCAAGTGCCAGCTGCAGCTGCTAGACTCTGGAGCACCTGAGTACAAGGTGATACAG
ACCTACTTAGAACAGACTGGCAGCAACCACAGGTGCCCTACACTTCAACACATCTGGAAA
GTAAACCAAGAAGGGGAGGAAGACAGATTCCAGGCCCACTCCAAACTGGGTAATCGGAAG
CTGCTGTGGCATGGCACCAACATGGCCGTGGTGGCCGCCATCCTCACTAGTGGGCTCCGC
ATCATGCCACATTCTGGTGGGCGTGTTGGCAAGGGCATCTACTTTGCCTCAGAGAACAGC
AAGTCAGCTGGATATGTTATTGGCATGAAGTGTGGGGCCCACCATGTCGGCTACATGTTC
CTGGGTGAGGTGGCCCTGGGCAGAGAGCACCATATCAACACGGACAACCCCAGCTTGAAG
AGCCCACCTCCTGGCTTCGACAGTGTCATTGCCCGAGGCCACACCGAGCCTGATCCGACC
CAGGACACTGAGTTGGAGCTGGATGGCCAGCAAGTGGTGGTGCCCCAGGGCCAGCCTGTG
CCCTGCCCAGAGTTCAGCAGCTCCACATTCTCCCAGAGCGAGTACCTCATCTACCAGGAG
AGCCAGTGTCGCCTGCGCTACCTGCTGGAGGTCCACCTCTGA
Enzyme 5 GenBank Gene ID AF083068 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]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6194
Enzyme 6 Name Ecto-ADP-ribosyltransferase 3 precursor
Enzyme 6 Synonyms
  1. NAD(P(+-- arginine ADP-ribosyltransferase 3
  2. Mono(ADP-ribosyltransferase 3
Enzyme 6 Gene Name ART3
Enzyme 6 Protein Sequence >Ecto-ADP-ribosyltransferase 3 precursor 
MKTGHFEIVTMLLATMILVDIFQVKAEVLDMADNAFDDEYLKCTDRMEIKYVPQLLKEEK
ASHQQLDTVWENAKAKWAARKTQIFLPMNFKDNHGIALMAYISEAQEQTPFYHLFSEAVK
MAGQSREDYIYGFQFKAFHFYLTRALQLLRKPCEASSKTVVYRTSQGTSFTFGGLNQARF
GHFTLAYSAKPQAANDQLTVLSIYTCLGVDIENFLDKESERITLIPLNEVFQVSQEGAGN
NLILQSINKTCSHYECAFLGGLKTENCIENLEYFQPIYVYNPGEKNQKLEDHSEKNWKLE
DHGEKNQKLEDHGVKILEPTQIPGMKIPEPFPLPEDKSQGNINNPTPGPVPVPGPKSHPS
ASSGKLLLPQFGMVIILISVSAINLFVAL
Enzyme 6 Number of Residues 389
Enzyme 6 Molecular Weight 43924
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
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid ADP-ribosylation
  • protein modification
Component
—
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function NAD(P)(+) + protein-L-arginine = nicotinamide + omega-N-(ADP-D-ribosyl)-protein-L-arginine
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • NAD(P)+ + L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-L-arginine
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-26
Enzyme 6 Transmembrane Regions
  • 366-388
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1226246 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 >1104 bp 
ATGAAGACGGGACATTTTGAAATAGTCACCATGCTGCTGGCAACCATGATTCTAGTGGAC
ATTTTCCAGGTGAAGGCTGAAGTGTTAGACATGGCAGATAATGCATTTGATGATGAATAC
CTGAAATGTACGGACAGGATGGAAATTAAATACGTTCCCCAACTGCTAAAGGAGGAAAAA
GCAAGCCACCAGCAATTAGATACTGTGTGGGAAAATGCAAAAGCCAAATGGGCAGCCCGA
AAGACTCAAATCTTTCTCCCTATGAATTTTAAGGATAACCATGGAATAGCCCTGATGGCA
TATATTTCCGAAGCTCAAGAGCAAACTCCCTTTTACCATCTGTTCAGTGAAGCTGTGAAG
ATGGCTGGCCAATCTCGAGAAGATTATATCTATGGCTTCCAGTTCAAAGCTTTCCACTTT
TACCTCACAAGAGCCCTGCAGTTGCTGAGAAAACCTTGTGAGGCCAGTTCCAAAACTGTG
GTATATAGAACAAGCCAGGGCACTTCATTTACATTTGGAGGGCTAAACCAAGCCAGGTTT
GGCCATTTTACCTTGGCATATTCAGCCAAACCTCAGGCTGCTAATGACCAGCTCACTGTG
TTATCCATCTACACATGCCTTGGAGTTGACATTGAAAATTTTCTTGATAAAGAAAGTGAA
AGAATTACTTTAATACCTCTGAATGAGGTTTTTCAAGTGTCACAGGAGGGGGCTGGCAAT
AACCTTATCCTTCAAAGCATAAACAAGACCTGCAGCCATTATGAGTGTGCATTTCTAGGT
GGACTAAAAACCGAAAACTGTATTGAGAACCTAGAATATTTTCAACCCATCTATGTCTAC
AACCCTGGTGAGAAAAACCAGAAGCTTGAAGACCATAGTGAGAAAAACTGGAAGCTTGAA
GACCATGGTGAGAAAAACCAGAAGCTTGAAGACCATGGTGTGAAAATCCTTGAACCCACC
CAAATACCTGCTCCAGGTCCAGTTCCTGTTCCAGGTCCCAAAAGCCATCCTTCTGCATCC
TCGGGCAAACTGCTGCTTCCACAGTTTGGGATGGTCATCATTTTAATCAGTGTTTCTGCT
ATAAATCTCTTTGTTGCTCTGTAG
Enzyme 6 GenBank Gene ID U47054 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]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6197
Enzyme 7 Name GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 precursor
Enzyme 7 Synonyms
  1. Mono(ADP-ribosyltransferase
  2. CD296 antigen
Enzyme 7 Gene Name ART1
Enzyme 7 Protein Sequence >GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 precursor 
MQMPAMMSLLLVSVGLMEALQAQSHPITRRDLFSQEIQLDMALASFDDQYAGCAAAMTAA
LPDLNHTEFQANQVYADSWTLASSQWQERQARWPEWSLSPTRPSPPPLGFRDEHGVALLA
YTANSPLHKEFNAAVREAGRSRAHYLHHFSFKTLHFLLTEALQLLGSGQRPPRCHQVFRG
VHGLRFRPAGPRATVRLGGFASASLKHVAAQQFGEDTFFGIWTCLGAPIKGYSFFPGEEE
VLIPPFETFQVINASRPAQGPARIYLRALGKHSTYNCEYIKDKKCKSGPCHLDNSAMGQS
PLSAVWSLLLLLWFLVVRAFPDGPGLL
Enzyme 7 Number of Residues 327
Enzyme 7 Molecular Weight 36319
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
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid ADP-ribosylation
  • protein modification
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function NAD(P)(+) + protein-L-arginine = nicotinamide + omega-N-(ADP-D-ribosyl)-protein-L-arginine
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • NAD(P)+ + L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-L-arginine
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-22
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 807100 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
GTGCTGATCCCCCCCTTTGAGACCTTCCAAGTGATCAATGCCAGCAGACCGGCCCAGGGC
CCCGCCCGCATCTACCTCCGAGCCCTGGGCAAGCACAGCACCTACAACTGCGAGTACATC
AAAGACAAGAAGTGCAAGTCTGGGCCTTGCCATCTGGATAATTCAGCCATGGGTCAGAGC
CCCCTCTCTGCAGTCTGGTCTTTGCTGCTGCTGCTCTGGTTCCTCGTGGTGAGGGCCTTT
CCAGATGGTCCAGGCCTCCTTTGA
Enzyme 7 GenBank Gene ID S74683 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 11
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]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6200
Enzyme 8 Name Tankyrase-1
Enzyme 8 Synonyms
  1. TANK1
  2. Tankyrase I
  3. TNKS-1
  4. TRF1- interacting ankyrin-related ADP-ribose polymerase
Enzyme 8 Gene Name TNKS
Enzyme 8 Protein Sequence >Tankyrase-1 
MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPR
HGLALPEGDGSRDPPDRPRSPDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNP
AGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVSSTAPLGPGAAGPGTGVPAVS
GALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGA
NVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIV
LLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNV
NCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTEL
LLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPEL
RERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQV
TELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAAL
AGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILSESTPIRTSDVDYRLLEASKA
GDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVP
LHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKN
RDGNTPLDLVKEGDTDIQDLLKGDAALLDAAKKGCLARVQKLCTPENINCRDTQGRNSTP
LHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATD
KWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEA
LPTCFKPQATVVSASLISPASTPSCLSAASSIDNLTGPLAELAVGGASNAGDGAAGTERK
EGEVAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLI
KGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGG
IFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDER
HAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSF
LQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTA
TAAEQKT
Enzyme 8 Number of Residues 1327
Enzyme 8 Molecular Weight 142013
Enzyme 8 Theoretical pI 7.05
Enzyme 8 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
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid ADP-ribosylation
  • protein modification
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 8 General Function Not Available
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+
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 3929219 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
CCTACGTTAGTCAACTGCCATGGCAAAAGTGCTGTGGATATGGCTCCAACTCCGGAGCTT
AGGGAGAGATTGACTTATGAATTTAAAGGTCATTCTTTACTACAAGCAGCCAGAGAAGCA
GACTTAGCTAAAGTTAAAAAAACACTCGCTCTGGAAATCATTAATTTCAAACAACCGCAG
TCTCATGAAACAGCACTGCACTGTGCTGTGGCCTCTCTGCATCCCAAACGTAAACAAGTG
ACAGAATTGTTACTTAGAAAAGGAGCAAATGTTAATGAAAAAAATAAAGATTTCATGACT
CCCCTGCATGTTGCAGCCGAAAGAGCCCATAATGATGTCATGGAAGTTCTGCATAAGCAT
GGCGCCAAGATGAATGCACTGGACACCCTTGGTCAGACTGCTTTGCATAGAGCCGCCCTA
GCAGGCCACCTGCAGACCTGCCGCCTCCTGCTGAGTTACGGCTCTGACCCCTCCATCATC
TCCTTACAAGGCTTCACAGCAGCACAGATGGGCAATGAAGCAGTGCAGCAGATTCTGAGT
GAGAGTACACCTATACGTACTTCTGATGTTGATTATCGACTCTTAGAGGCATCTAAAGCT
GGAGACTTGGAAACTGTGAAGCAACTTTGCAGCTCTCAAAATGTGAATTGTAGAGACTTA
GAGGGCCGGCATTCCACGCCCTTACACTTCGCAGCAGGCTACAACCGCGTGTCTGTTGTA
GAGTACCTGCTACACCACGGTGCCGATGTCCATGCCAAAGACAAGGGTGGCTTGGTGCCC
CTTCATAATGCCTGTTCATATGGACACTATGAGGTGGCTGAGCTTTTAGTAAGGCATGGG
GCTTCTGTCAATGTGGCGGACTTATGGAAATTTACCCCTCTCCATGAAGCAGCAGCTAAA
GGAAAGTATGAAATCTGCAAGCTCCTTTTAAAACATGGAGCAGATCCAACTAAAAAGAAC
AGAGATGGAAATACACCTTTGGATTTGGTAAAGGAAGGAGACACAGATATTCAGGACTTA
CTGAAAGGGGATGCTGCTTTGTTGGATGCTGCCAAGAAGGGCTGCCTGGCAAGAGTGCAG
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 AF082556 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. 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]
  3. 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]
  4. 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6203
Enzyme 9 Name ADP-ribosyl cyclase 2 precursor
Enzyme 9 Synonyms
  1. Cyclic ADP-ribose hydrolase 2
  2. cADPr hydrolase 2
  3. Bone marrow stromal antigen 1
  4. BST- 1
  5. CD157 antigen
Enzyme 9 Gene Name BST1
Enzyme 9 Protein Sequence >ADP-ribosyl cyclase 2 precursor 
MAAQGCAASRLLQLLLQLLLLLLLLAAGGARARWRGEGTSAHLRDIFLGRCAEYRALLSP
EQRNKNCTAIWEAFKVALDKDPCSVLPSDYDLFINLSRHSIPRDKSLFWENSHLLVNSFA
DNTRRFMPLSDVLYGRVADFLSWCRQKNDSGLDYQSCPTSEDCENNPVDSFWKRASIQYS
KDSSGVIHVMLNGSEPTGAYPIKGFFADYEIPNLQKEKITRIEIWVMHEIGGPNVESCGE
GSMKVLEKRLKDMGFQYSCINDYRPVKLLQCVDHSTHPDCALKSAAAATQRKAPSLYTEQ
RAGLIIPLFLVLASRTQL
Enzyme 9 Number of Residues 318
Enzyme 9 Molecular Weight 35724
Enzyme 9 Theoretical pI 7.86
Enzyme 9 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 9 General Function Not Available
Enzyme 9 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 9 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 9 Reactions
  • NAD+ + H2O = ADP-ribose + nicotinamide
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-28
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 999429 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q10588 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name BST1_HUMAN Link Image
Enzyme 9 PDB ID 1ISM Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >957 bp 
ATGGCGGCCCAGGGGTGCGCGGCATCGCGGCTGCTCCAGCTGCTGCTGCAGCTTCTGCTT
CTACTGTTGCTGCTGGCGGCGGGCGGGGCGCGCGCGCGGTGGCGCGCGGAGGGCACCAGC
GCACACTTGCGGGACATCTTCCTGGGCCGCTGCGCCGAGTACCGCGCACTGCTGAGTCCC
GAGCAGCGGAACAAGAACTGCACAGCCATCTGGGAAGCCTTTAAAGTGGCGCTGGACAAG
GATCCCTGCTCCGTGCTGCCCTCAGACTATGACCTTTTTATTAACTTGTCCAGGCACTCT
ATTCCCAGAGATAAGTCCCTGTTCTGGGAAAATAGCCACCTCCTTGTTAACAGCTTTGCA
GACAACACCCGTCGTTTTATGCCCCTGAGCGATGTTCTGTATGGCAGGGTTGCAGATTTC
TTGAGCTGGTGTCGACAGAAAAATGACTCTGGACTCGATTACCAATCCTGCCCTACATCA
GAAGACTGTGAAAATAATCCTGTGGATTCCTTTTGGAAAAGGGCATCCATCCAGTATTCC
AAGGATAGTTCTGGGGTGATCCACGTCATGCTGAATGGTTCAGAGCCAACAGGAGCCTAT
CCCATCAAAGGTTTTTTTGCAGATTATGAAATTCCAAACCTCCAGAAGGAAAAAATTACA
CGAATCGAGATCTGGGTTATGCATGAAATTGGGGGACCCAATGTGGAATCCTGCGGGGAA
GGCAGCATGAAAGTCCTGGAAAAGAGGCTGAAGGACATGGGGTTCCAGTACAGCTGTATT
AATGATTACCGACCAGTGAAGCTCTTACAGTGCGTGGACCACAGCACCCATCCTGACTGT
GCCTTAAAGTCGGCAGCAGCCGCTACTCAAAGAAAAGCCCCAAGTCTTTATACAGAACAA
AGGGCGGGTCTTATCATTCCCCTCTTTCTGGTGCTGGCTTCCCGGACTCAACTGTAA
Enzyme 9 GenBank Gene ID D21878 Link Image
Enzyme 9 GeneCard ID BST1 Link Image
Enzyme 9 GenAtlas ID BST1 Link Image
Enzyme 9 HGNC ID HGNC:1118 Link Image
Enzyme 9 Chromosome Location 4
Enzyme 9 Locus 4p15
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6204
Enzyme 10 Name Poly [ADP-ribose] polymerase 2
Enzyme 10 Synonyms
  1. PARP-2
  2. NAD(+ADP- ribosyltransferase 2
  3. Poly[ADP-ribose] synthetase 2
  4. pADPRT-2
  5. hPARP-2
Enzyme 10 Gene Name PARP2
Enzyme 10 Protein Sequence >Poly [ADP-ribose] polymerase 2 
MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKD
RTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLN
QTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKF
LDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQE
LIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALME
ACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQ
HYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDL
HNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLK
NTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGP
ASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW
Enzyme 10 Number of Residues 583
Enzyme 10 Molecular Weight 66207
Enzyme 10 Theoretical pI 9.22
Enzyme 10 GO Classification
Function
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ 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
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 10 General Function Not Available
Enzyme 10 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 10 Pathways Not Available
Enzyme 10 Reactions
  • NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 6688130 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9UGN5 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PARP2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1713 bp 
ATGGCGGCGCGGCGGCGACGGAGCACCGGCGGCGGCAGGGCGAGAGCATTAAATGAAAGC
AAAAGAGTTAATAATGGCAACACGGCTCCAGAAGACTCTTCCCCTGCCAAGAAAACTCGT
AGATGCCAGAGACAGGAGTCGAAAAAGATGCCTGTGGCTGGAGGAAAAGCTAATAAGGAC
AGGACAGAAGACAAGCAAGATGAATCTGTGAAGGCCTTGCTGTTAAAGGGCAAAGCTCCT
GTGGACCCAGAGTGTACAGCCAAGGTGGGGAAGGCTCATGTGTATTGTGAAGGAAATGAT
GTCTATGATGTCATGCTAAATCAGACCAATCTCCAGTTCAACAACAACAAGTACTATCTG
ATTCAGCTATTAGAAGATGATGCCCAGAGGAACTTCAGTGTTTGGATGAGATGGGGCCGA
GTTGGGAAAATGGGACAGCACAGCCTGGTGGCTTGTTCAGGCAATCTCAACAAGGCCAAG
GAAATCTTTCAGAAGAAATTCCTTGACAAAACGAAAAACAATTGGGAAGATCGAGAAAAG
TTTGAGAAGGTGCCTGGAAAATATGATATGCTACAGATGGACTATGCCACCAATACTCAG
GATGAAGAGGAAACAAAGAAAGAGGAATCTCTTAAATCTCCCTTGAAGCCAGAGTCACAG
CTAGATCTTCGGGTACAGGAGTTAATAAAGTTGATCTGTAATGTTCAGGCCATGGAAGAA
ATGATGATGGAAATGAAGTATAATACCAAGAAAGCCCCACTTGGGAAGCTGACAGTGGCA
CAAATCAAGGCAGGTTACCAGTCTCTTAAGAAGATTGAGGATTGTATTCGGGCTGGCCAG
CATGGACGAGCTCTCATGGAAGCATGCAATGAATTCTACACCAGGATTCCGCATGACTTT
GGACTCCGTACTCCTCCACTAATCCGGACACAGAAGGAACTGTCAGAAAAAATACAATTA
CTAGAGGCTTTGGGAGACATTGAAATTGCTATTAAGCTGGTGAAAACAGAGCTACAAAGC
CCAGAACACCCATTGGACCAACACTATAGAAACCTACATTGTGCCTTGCGCCCCCTTGAC
CATGAAAGTTATGAGTTCAAAGTGATTTCCCAGTACCTACAATCTACCCATGCTCCCACA
CACAGCGACTATACCATGACCTTGCTGGATTTGTTTGAAGTGGAGAAGGATGGTGAGAAA
GAAGCCTTCAGAGAGGACCTTCATAACAGGATGCTTCTATGGCATGGTTCCAGGATGAGT
AACTGGGTGGGAATCTTGAGCCATGGGCTTCGAATTGCCCCACCTGAAGCTCCCATCACA
GGTTACATGTTTGGGAAAGGAATCTACTTTGCTGACATGTCTTCCAAGAGTGCCAATTAC
TGCTTTGCCTCTCGCCTAAAGAATACAGGACTGCTGCTCTTATCAGAGGTAGCTCTAGGT
CAGTGTAATGAACTACTAGAGGCCAATCCTAAGGCCGAAGGATTGCTTCAAGGTAAACAT
AGCACCAAGGGGCTGGGCAAGATGGCTCCCAGTTCTGCCCACTTCGTCACCCTGAATGGG
AGTACAGTGCCATTAGGACCAGCAAGTGACACAGGAATTCTGAATCCAGATGGTTATACC
CTCAACTACAATGAATATATTGTATATAACCCCAACCAGGTCCGTATGCGGTACCTTTTA
AAGGTTCAGTTTAATTTCCTTCAGCTGTGGTGA
Enzyme 10 GenBank Gene ID AJ236912 Link Image
Enzyme 10 GeneCard ID PARP2 Link Image
Enzyme 10 GenAtlas ID PARP2 Link Image
Enzyme 10 HGNC ID HGNC:272 Link Image
Enzyme 10 Chromosome Location 14
Enzyme 10 Locus 14q11.2-q12
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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. 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6206
Enzyme 11 Name ADP-ribosyl cyclase 1
Enzyme 11 Synonyms
  1. Cyclic ADP-ribose hydrolase 1
  2. cADPr hydrolase 1
  3. Lymphocyte differentiation antigen CD38
  4. T10
  5. Acute lymphoblastic leukemia cells antigen CD38
Enzyme 11 Gene Name CD38
Enzyme 11 Protein Sequence >ADP-ribosyl cyclase 1 
MANCEFSPVSGDKPCCRLSRRAQLCLGVSILVLILVVVLAVVVPRWRQQWSGPGTTKRFP
ETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCN
KILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDC
SNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEA
WVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI
Enzyme 11 Number of Residues 300
Enzyme 11 Molecular Weight 34329
Enzyme 11 Theoretical pI 7.72
Enzyme 11 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 11 General Function Not Available
Enzyme 11 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 11 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 11 Reactions
  • NAD+ + H2O = ADP-ribose + nicotinamide
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-40
Enzyme 11 Transmembrane Regions Not Available
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 180119 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P28907 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name CD38_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >903 bp 
ATGGCCAACTGCGAGTTCAGCCCGGTGTCCGGGGACAAACCCTGCTGCCGGCTCTCTAGG
AGAGCCCAACTCTGTCTTGGCGTCAGTATCCTGGTCCTGATCCTCGTCGTGGTGCTCGCG
GTGGTCGTCCCGAGGTGGCGCCAGACGTGGAGCGGTCCGGGCACCACCAAGCGCTTTCCC
GAGACCGTCCTGGCGCGATGCGTCAAGTACACTGAAATTCATCCTGAGATGAGACATGTA
GACTGCCAAAGTGTATGGGATGCTTTCAAGGGTGCATTTATTTCAAAACATCCTTGCAAC
ATTACTGAAGAAGACTATCAGCCACTAATGAAGTTGGGAACTCAGACCGTACCTTGCAAC
AAGATTCTTCTTTGGAGCAGAATAAAAGATCTGGCCCATCAGTTCACACAGGTCCAGCGG
GACATGTTCACCCTGGAGGACACGCTGCTAGGCTACCTTGCTGATGACCTCACATGGTGT
GGTGAATTCAACACTTCCAAAATAAACTATCAATCTTGCCCAGACTGGAGAAAGGACTGC
AGCAACAACCCTGTTTCAGTATTCTGGAAAACGGTTTCCCGCAGGTTTGCAGAAGCTGCC
TGTGATGTGGTCCATGTGATGCTCAATGGATCCCGCAGTAAAATCTTTGACAAAAACAGC
ACTTTTGGGAGTGTGGAAGTCCATAATTTGCAACCAGAGAAGGTTCAGACACTAGAGGCC
TGGGTGATACATGGTGGAAGAGAAGATTCCAGAGACTTATGCCAGGATCCCACCATAAAA
GAGCTGGAATCGATTATAAGCAAAAGGAATATTCAATTTTCCTGCAAGAATATCTACAGA
CCTGACAAGTTTCTTCAGTGTGTGAAAAATCCTGAGGATTCATCTTGCACATCTGAGATC
TGA
Enzyme 11 GenBank Gene ID M34461 Link Image
Enzyme 11 GeneCard ID CD38 Link Image
Enzyme 11 GenAtlas ID CD38 Link Image
Enzyme 11 HGNC ID HGNC:1667 Link Image
Enzyme 11 Chromosome Location 4
Enzyme 11 Locus 4p15
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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. 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]
  4. 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]
  5. 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]
  6. 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6207
Enzyme 12 Name Ecto-ADP-ribosyltransferase 4 precursor
Enzyme 12 Synonyms
  1. NAD(P(+-- arginine ADP-ribosyltransferase 4
  2. Mono(ADP-ribosyltransferase 4
  3. Dombrock blood group carrier molecule
  4. CD297 antigen
Enzyme 12 Gene Name ART4
Enzyme 12 Protein Sequence >Ecto-ADP-ribosyltransferase 4 precursor 
MGPLINRCKKILLPTTVPPATMRIWLLGGLLPFLLLLSGLQRPTEGSEVAIKIDFDFAPG
SFDDQYQGCSKQVMEKLTQGDYFTKDIEAQKNYFRMWQKAHLAWLNQGKVLPQNMTTTHA
VAILFYTLNSNVHSDFTRAMASVARTPQQYERSFHFKYLHYYLTSAIQLLRKDSIMENGT
LCYEVHYRTKDVHFNAYTGATIRFGQFLSTSLLKEEAQEFGNQTLFTIFTCLGAPVQYFS
LKKEVLIPPYELFKVINMSYHPRGNWLQLRSTGNLSTYNCQLLKASSKKCIPDPIAIASL
SFLTSVIIFSKSRV
Enzyme 12 Number of Residues 314
Enzyme 12 Molecular Weight 35878
Enzyme 12 Theoretical pI 9.57
Enzyme 12 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 12 General Function Not Available
Enzyme 12 Specific Function NAD(P)(+) + protein-L-arginine = nicotinamide + omega-N-(ADP-D-ribosyl)-protein-L-arginine
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • NAD(P)+ + L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-L-arginine
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 10444285 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q93070 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name NAR4_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >945 bp 
ATGGGTCCATTGATCAACAGATGCAAGAAGATTCTTCTCCCAACTACTGTACCTCCTGCA
ACGATGAGAATCTGGCTCCTTGGAGGCCTGCTGCCATTCCTGCTGCTCCTCTCTGGCCTG
CAGAGACCCACAGAGGGTTCTGAGGTTGCAATTAAAATCGACTTCGACTTCGCACCAGGT
TCTTTTGATGATCAGTACCAAGGCTGTAGCAAACAGGTTATGGAGAAACTAACTCAAGGG
GATTATTTCACAAAAGACATAGAAGCCCAGAAGAATTATTTTAGGATGTGGCAAAAAGCC
CACTTAGCCTGGCTTAACCAAGGAAAAGTTCTACCCCAGAACATGACTACCACACACGCT
GTGGCTATTTTGTTTTACACATTGAACAGCAATGTTCATTCTGACTTTACTAGAGCCATG
GCCTCTGTTGCCAGGACTCCACAGCAGTATGAACGTTCATTCCACTTCAAATATTTACAC
TACTACCTCACCTCAGCAATCCAGCTGCTGAGGAAAGACAGCATCATGGAGAATGGCACT
CTGTGCTATGAGGTGCATTATAGGACGAAGGATGTCCACTTTAATGCCTACACAGGGGCC
ACCATTCGATTTGGCCAATTCCTTTCCACATCCCTCCTGAAAGAAGAGGCACAGGAGTTT
GGGAACCAGACACTATTTACCATATTCACCTGCCTGGGTGCACCTGTACAGTACTTCTCC
CTCAAGAAGGAAGTCTTGATCCCTCCCTATGAGCTGTTTAAAGTTATAAATATGAGCTAC
CACCCAAGAGGAAACTGGTTGCAGTTGAGGTCAACTGGGAACCTGAGCACATATAACTGT
CAGCTGCTAAAAGCTTCCAGCAAGAAATGCATCCCTGATCCTATAGCTATTGCATCTCTC
TCCTTTTTGACCAGTGTCATCATCTTTTCCAAAAGCAGAGTATAA
Enzyme 12 GenBank Gene ID AF290204 Link Image
Enzyme 12 GeneCard ID ART4 Link Image
Enzyme 12 GenAtlas ID ART4 Link Image
Enzyme 12 HGNC ID HGNC:726 Link Image
Enzyme 12 Chromosome Location 12
Enzyme 12 Locus 12p13-p12
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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. 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]
  4. 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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 13072
Enzyme 13 Name Pre-B-cell colony enhancing factor 1
Enzyme 13 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 13 Gene Name PBEF1
Enzyme 13 Protein Sequence >Pre-B-cell colony enhancing factor 1 
MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFY
GLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVP
EGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETS
GNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGY
SVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIV
SRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINT
LQEIVEGMKQKMWSIENIAFGSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVAD
PNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHTVFKNGKVTKSYSFDEIRKNA
QLNIELEAAHH
Enzyme 13 Number of Residues 491
Enzyme 13 Molecular Weight 55522
Enzyme 13 Theoretical pI 7.18
Enzyme 13 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 13 General Function Coenzyme transport and metabolism
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 158259163 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID A4D0Q9 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name A4D0Q9_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID AK292851 Link Image
Enzyme 13 GeneCard ID A4D0Q9 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 15317
Enzyme 14 Name ART5 protein precursor (ADP-ribosyltransferase 5, isoform CRA_b)
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name ART5
Enzyme 14 Protein Sequence >ART5 protein precursor (ADP-ribosyltransferase 5, isoform CRA_b) 
MALAALMIALGSLGLHTWQAQAVPTILPLGLAPDTFDDTYVGCAEEMEEKAAPLLKEEMA
HHALLRESWEAAQETWEDKRRGLTLPPGFKAQNGIAIMVYTNSSNTLYWELNQAVRTGGG
SRELYMRHFPFKALHFYLIRALQLLRGSGGCSRGPGEVVFRGVGSLRFEPKRLGDSVRLG
QFASSSLDKAVAHRFGNATLFSLTTCFGAPIQAFSVFPKEREVLIPPHEVFLVTRFSQDG
AQSLVTLWSYNQTCSHFNCAYLGGEKRRGCVSAPGALGTGDLHMTKRHLQQP
Enzyme 14 Number of Residues 292
Enzyme 14 Molecular Weight 32155
Enzyme 14 Theoretical pI 8.38
Enzyme 14 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 14 General Function Not Available
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-21
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 29788058 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q86W02 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name Q86W02_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >879 bp 
ATGGCGCTGGCGGCTTTGATGATCGCCCTCGGCAGCCTCGGCCTCCACACCTGGCAGGCC
CAGGCTGTTCCCACCATCCTGCCCCTGGGCCTGGCTCCAGACACCTTTGACGATACCTAT
GTGGGTTGTGCAGAGGAGATGGAGGAGAAGGCAGCCCCCCTGCTAAAGGAGGAAATGGCC
CACCATGCCCTGCTGCGGGAATCCTGGGAGGCAGCCCAGGAGACCTGGGAGGACAAGCGT
CGAGGGCTTACCTTGCCCCCTGGCTTCAAAGCCCAGAATGGAATAGCCATTATGGTCTAC
ACCAACTCATCGAACACCTTGTACTGGGAGTTGAATCAGGCCGTGCGGACGGGCGGAGGC
TCCCGGGAGCTCTACATGAGGCACTTTCCCTTCAAGGCCCTGCATTTCTACCTGATCCGG
GCCCTGCAGCTGCTGCGAGGCAGTGGGGGCTGCAGCAGGGGACCTGGGGAGGTGGTGTTC
CGAGGTGTGGGCAGCCTTCGCTTTGAACCCAAGAGGCTGGGGGACTCTGTCCGCTTGGGC
CAGTTTGCCTCCAGCTCCCTGGATAAGGCAGTGGCCCACAGATTTGGTAATGCCACCCTC
TTCTCTCTAACAACTTGCTTTGGGGCCCCTATACAGGCCTTCTCTGTCTTTCCCAAGGAG
CGCGAGGTGCTGATTCCCCCCCATGAAGTCTTTTTGGTTACCAGATTCTCTCAGGATGGA
GCCCAGAGCTTGGTGACTCTCTGGAGCTATAATCAGACCTGTAGCCATTTTAACTGCGCC
TATCTGGGTGGGGAGAAGAGGCGGGGCTGTGTGTCTGCGCCAGGAGCCCTGGGAACGGGT
GACCTTCATATGACGAAGAGGCACCTCCAGCAGCCTTGA
Enzyme 14 GenBank Gene ID Y16835 Link Image
Enzyme 14 GeneCard ID Q86W02 Link Image
Enzyme 14 GenAtlas ID ART5 Link Image
Enzyme 14 HGNC ID HGNC:24049 Link Image
Enzyme 14 Chromosome Location 11
Enzyme 14 Locus 11p15.4
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 15855
Enzyme 15 Name Poly (ADP-ribose) polymerase family, member 4
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name PARP4
Enzyme 15 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 15 Number of Residues 1724
Enzyme 15 Molecular Weight 192596
Enzyme 15 Theoretical pI 5.39
Enzyme 15 GO Classification
Function
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ ADP-ribosyltransferase activity
  • NAD+ 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
  • cell
  • intracellular
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
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 Q5QNZ9 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q5QNZ9_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID AL359763 Link Image
Enzyme 15 GeneCard ID Q5QNZ9 Link Image
Enzyme 15 GenAtlas ID PARP4 Link Image
Enzyme 15 HGNC ID HGNC:271 Link Image
Enzyme 15 Chromosome Location 13
Enzyme 15 Locus 13q11
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 16525
Enzyme 16 Name cDNA, FLJ92858, highly similar to Homo sapiens bone marrow stromal cell antigen 1 (BST1), mRNA (Bone marrow stromal cell antigen 1)
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name BST1
Enzyme 16 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 16 Number of Residues 318
Enzyme 16 Molecular Weight 35724
Enzyme 16 Theoretical pI 7.86
Enzyme 16 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 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
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID B2R6A2 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name B2R6A2_HUMAN Link Image
Enzyme 16 PDB ID 1ISM Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID AK312497 Link Image
Enzyme 16 GeneCard ID B2R6A2 Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 16699
Enzyme 17 Name Poly (ADP-ribose) polymerase family, member 1 (Poly (ADP-ribose) polymerase family, member 1, isoform CRA_a)
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name PARP1
Enzyme 17 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 17 Number of Residues 1014
Enzyme 17 Molecular Weight 113085
Enzyme 17 Theoretical pI 9.34
Enzyme 17 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 17 General Function Not Available
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 Not Available
Enzyme 17 UniProtKB/Swiss-Prot ID B1ANJ4 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name B1ANJ4_HUMAN Link Image
Enzyme 17 PDB ID 1WOK Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence Not Available
Enzyme 17 GenBank Gene ID AL359704 Link Image
Enzyme 17 GeneCard ID B1ANJ4 Link Image
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References Not Available
Enzyme 17 Metabolite References Not Available