|
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
)
|
| Enzyme 1 Reactions |
- S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide [RN:R01269]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
494989  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P40261  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
NNMT_HUMAN  |
| 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  |
| Enzyme 1 GeneCard ID |
NNMT  |
| Enzyme 1 GenAtlas ID |
NNMT  |
| Enzyme 1 HGNC ID |
HGNC:7861  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
11q23.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5805 |
| Enzyme 2 Name |
Purine nucleoside phosphorylase |
| Enzyme 2 Synonyms |
- PNP
- 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 |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
35565  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P00491  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PNPH_HUMAN  |
| Enzyme 2 PDB ID |
1RT9  |
| 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  |
| Enzyme 2 GeneCard ID |
PNP  |
| Enzyme 2 GenAtlas ID |
PNP  |
| Enzyme 2 HGNC ID |
HGNC:7892  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
14q13.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6189 |
| Enzyme 3 Name |
Tankyrase-2 |
| Enzyme 3 Synonyms |
- TANK2
- Poly [ADP-ribose] polymerase 5B
- TNKS-2
- TRF1-interacting ankyrin-related ADP-ribose polymerase 2
- Tankyrase II
- Tankyrase-like protein
- 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 |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
12005976  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q9H2K2  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
TNKS2_HUMAN  |
| 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  |
| Enzyme 3 GeneCard ID |
TNKS2  |
| Enzyme 3 GenAtlas ID |
TNKS2  |
| Enzyme 3 HGNC ID |
HGNC:15677  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
10q23.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6191 |
| Enzyme 4 Name |
NAD-dependent deacetylase sirtuin-6 |
| Enzyme 4 Synonyms |
- 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 |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
7243749  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q8N6T7  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SIRT6_HUMAN  |
| 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  |
| Enzyme 4 GeneCard ID |
SIRT6  |
| Enzyme 4 GenAtlas ID |
SIRT6  |
| Enzyme 4 HGNC ID |
HGNC:14934  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
19p13.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Frye RA: Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun. 2000 Jul 5;273(2):793-8. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6193 |
| Enzyme 5 Name |
Poly [ADP-ribose] polymerase 3 |
| Enzyme 5 Synonyms |
- PARP-3
- hPARP-3
- IRT1
- NAD(+) ADP-ribosyltransferase 3
- ADPRT-3
- Poly[ADP-ribose] synthase 3
- 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 |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
158634482  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9Y6F1  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
PARP3_HUMAN  |
| 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  |
| Enzyme 5 GeneCard ID |
PARP3  |
| Enzyme 5 GenAtlas ID |
PARP3  |
| Enzyme 5 HGNC ID |
HGNC:273  |
| Enzyme 5 Chromosome Location |
3 |
| Enzyme 5 Locus |
3p21.31-p21.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6194 |
| Enzyme 6 Name |
Ecto-ADP-ribosyltransferase 3 |
| Enzyme 6 Synonyms |
- Mono(ADP-ribosyl)transferase 3
- 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 |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
14250010  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q13508  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
NAR3_HUMAN  |
| 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  |
| Enzyme 6 GeneCard ID |
ART3  |
| Enzyme 6 GenAtlas ID |
ART3  |
| Enzyme 6 HGNC ID |
HGNC:725  |
| Enzyme 6 Chromosome Location |
4 |
| Enzyme 6 Locus |
4p15.1-p14|4p15.1-p14|4p15.1-p14 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
- 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
]
- 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
]
|
| 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 |
- Mono(ADP-ribosyl)transferase 1
- 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 |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
158634472  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P52961  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
NAR1_HUMAN  |
| 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  |
| Enzyme 7 GeneCard ID |
ART1  |
| Enzyme 7 GenAtlas ID |
ART1  |
| Enzyme 7 HGNC ID |
HGNC:723  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
11p15 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
- 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6200 |
| Enzyme 8 Name |
Tankyrase-1 |
| Enzyme 8 Synonyms |
- TANK1
- Poly [ADP-ribose] polymerase 5A
- TNKS-1
- TRF1-interacting ankyrin-related ADP-ribose polymerase
- 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 |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
87239981  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O95271  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
TNKS1_HUMAN  |
| 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  |
| Enzyme 8 GeneCard ID |
TNKS  |
| Enzyme 8 GenAtlas ID |
TNKS  |
| Enzyme 8 HGNC ID |
HGNC:11941  |
| Enzyme 8 Chromosome Location |
8 |
| Enzyme 8 Locus |
8p23.1 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6201 |
| Enzyme 9 Name |
Poly [ADP-ribose] polymerase 1 |
| Enzyme 9 Synonyms |
- PARP-1
- NAD(+) ADP-ribosyltransferase 1
- ADPRT 1
- 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 |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
21693601  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P09874  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PARP1_HUMAN  |
| Enzyme 9 PDB ID |
1WOK  |
| 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  |
| Enzyme 9 GeneCard ID |
PARP1  |
| Enzyme 9 GenAtlas ID |
PARP1  |
| Enzyme 9 HGNC ID |
HGNC:270  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1q41-q42 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6203 |
| Enzyme 10 Name |
ADP-ribosyl cyclase 2 |
| Enzyme 10 Synonyms |
- Bone marrow stromal antigen 1
- BST-1
- Cyclic ADP-ribose hydrolase 2
- cADPr hydrolase 2
- 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 |
|
| 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
)
|
| Enzyme 10 Reactions |
- NAD+ + H2O = ADP-ribose + nicotinamide [RN:R00102]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
63991381  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q10588  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
BST1_HUMAN  |
| Enzyme 10 PDB ID |
1ISM  |
| 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  |
| Enzyme 10 GeneCard ID |
BST1  |
| Enzyme 10 GenAtlas ID |
BST1  |
| Enzyme 10 HGNC ID |
HGNC:1118  |
| Enzyme 10 Chromosome Location |
4 |
| Enzyme 10 Locus |
4p15 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6204 |
| Enzyme 11 Name |
Poly [ADP-ribose] polymerase 2 |
| Enzyme 11 Synonyms |
- PARP-2
- hPARP-2
- NAD(+) ADP-ribosyltransferase 2
- ADPRT-2
- Poly[ADP-ribose] synthase 2
- 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 |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
110825961  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9UGN5  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PARP2_HUMAN  |
| Enzyme 11 PDB ID |
1GS0  |
| 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  |
| Enzyme 11 GeneCard ID |
PARP2  |
| Enzyme 11 GenAtlas ID |
PARP2  |
| Enzyme 11 HGNC ID |
HGNC:272  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
14q11.2-q12 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6206 |
| Enzyme 12 Name |
ADP-ribosyl cyclase 1 |
| Enzyme 12 Synonyms |
- Cyclic ADP-ribose hydrolase 1
- cADPr hydrolase 1
- T10
- 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 |
|
| 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
)
|
| Enzyme 12 Reactions |
- NAD+ + H2O = ADP-ribose + nicotinamide [RN:R00102]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
14044085  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P28907  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
CD38_HUMAN  |
| 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  |
| Enzyme 12 GeneCard ID |
CD38  |
| Enzyme 12 GenAtlas ID |
CD38  |
| Enzyme 12 HGNC ID |
HGNC:1667  |
| Enzyme 12 Chromosome Location |
4 |
| Enzyme 12 Locus |
4p15 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6207 |
| Enzyme 13 Name |
Ecto-ADP-ribosyltransferase 4 |
| Enzyme 13 Synonyms |
- Dombrock blood group carrier molecule
- Mono(ADP-ribosyl)transferase 4
- NAD(P)(+)--arginine ADP-ribosyltransferase 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 |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
10444285  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q93070  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
NAR4_HUMAN  |
| 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  |
| Enzyme 13 GeneCard ID |
ART4  |
| Enzyme 13 GenAtlas ID |
ART4  |
| Enzyme 13 HGNC ID |
HGNC:726  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
12p13-p12 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Pre-B-cell colony enhancing factor 1, isoform CRA_a
- cDNA FLJ76475, highly similar to Homo sapiens pre-B-cell colony enhancing factor 1
- 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 |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
158259163  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
A4D0Q9  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
A4D0Q9_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
Not Available |
| Enzyme 14 GenBank Gene ID |
AK292851  |
| Enzyme 14 GeneCard ID |
A4D0Q9  |
| 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  |
| Enzyme 14 General References |
- 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
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
14591 |
| Enzyme 15 Name |
Nicotinamide phosphoribosyltransferase |
| Enzyme 15 Synonyms |
- NAmPRTase
- Nampt
- Pre-B-cell colony-enhancing factor 1
- Pre-B cell-enhancing factor
- 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
)
|
| 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 |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
Not Available |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P43490  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
NAMPT_HUMAN  |
| 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  |
| Enzyme 15 GeneCard ID |
NAMPT  |
| Enzyme 15 GenAtlas ID |
NAMPT  |
| Enzyme 15 HGNC ID |
HGNC:30092  |
| Enzyme 15 Chromosome Location |
7 |
| Enzyme 15 Locus |
7q22.3 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
29788058  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q86W02  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
Q86W02_HUMAN  |
| 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  |
| Enzyme 16 GeneCard ID |
Q86W02  |
| Enzyme 16 GenAtlas ID |
ART5  |
| Enzyme 16 HGNC ID |
HGNC:24049  |
| Enzyme 16 Chromosome Location |
11 |
| Enzyme 16 Locus |
11p15.4 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- 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
]
|
| 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 |
|
|
| 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 |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
55959320  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q5QNZ9  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
Q5QNZ9_HUMAN  |
| 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  |
| Enzyme 17 GeneCard ID |
PARP4  |
| Enzyme 17 GenAtlas ID |
PARP4  |
| Enzyme 17 HGNC ID |
HGNC:271  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
13q11 |
| Enzyme 17 SNPs |
SNPJam Report  |
| 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 |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
Not Available |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
B2R6A2  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
B2R6A2_HUMAN  |
| Enzyme 18 PDB ID |
1ISM  |
| 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  |
| Enzyme 18 GeneCard ID |
B2R6A2  |
| 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  |
| 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 |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
Not Available |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
B1ANJ4  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
B1ANJ4_HUMAN  |
| Enzyme 19 PDB ID |
1WOK  |
| 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  |
| Enzyme 19 GeneCard ID |
B1ANJ4  |
| 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  |
| Enzyme 19 General References |
Not Available |
| Enzyme 19 Metabolite References |
Not Available |