|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5338 |
| Enzyme 1 Name |
Nucleoside diphosphate kinase, mitochondrial |
| Enzyme 1 Synonyms |
- NDK
- NDP kinase, mitochondrial
- Nucleoside diphosphate kinase D
- NDPKD
- nm23-H4
|
| Enzyme 1 Gene Name |
NME4 |
| Enzyme 1 Protein Sequence |
>Nucleoside diphosphate kinase, mitochondrial
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
|
| Enzyme 1 Number of Residues |
187 |
| Enzyme 1 Molecular Weight |
20658.5 |
| Enzyme 1 Theoretical pI |
10.75 |
| Enzyme 1 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 1 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
14336697  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O00746  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
NDKM_HUMAN  |
| Enzyme 1 PDB ID |
1EHW  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCG
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
|
| Enzyme 1 GenBank Gene ID |
AE006463  |
| Enzyme 1 GeneCard ID |
NME4  |
| Enzyme 1 GenAtlas ID |
NME4  |
| Enzyme 1 HGNC ID |
HGNC:7852  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
16p13.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed
]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [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
]
- Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [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 |
5341 |
| Enzyme 2 Name |
Nucleoside diphosphate kinase A |
| Enzyme 2 Synonyms |
- NDK A
- NDP kinase A
- Granzyme A-activated DNase
- GAAD
- Metastasis inhibition factor nm23
- Tumor metastatic process-associated protein
- nm23-H1
|
| Enzyme 2 Gene Name |
NME1 |
| Enzyme 2 Protein Sequence |
>Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
|
| Enzyme 2 Number of Residues |
152 |
| Enzyme 2 Molecular Weight |
17148.6 |
| Enzyme 2 Theoretical pI |
6.11 |
| Enzyme 2 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 2 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
4557797  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P15531  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
NDKA_HUMAN  |
| Enzyme 2 PDB ID |
1JXV  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>459 bp
ATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAACCAGATGGGGTCCAGCGGGGTCTT
GTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGATTCCGCCTTGTTGGTCTGAAATTC
ATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTACGTTGACCTGAAGGACCGTCCATTC
TTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCGGTAGTTGCCATGGTCTGGGAGGGG
CTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGGGAGACCAACCCTGCAGACTCCAAG
CCTGGGACCATCCGTGGAGACTTCTGCATACAAGTTGGCAGGAACATTATACATGGCAGT
GATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTGTGGTTTCACCCTGAGGAACTGGTA
GATTACACGAGCTGTGCTCAGAACTGGATCTATGAATGA
|
| Enzyme 2 GenBank Gene ID |
NM_000269.2  |
| Enzyme 2 GeneCard ID |
NME1  |
| Enzyme 2 GenAtlas ID |
NME1  |
| Enzyme 2 HGNC ID |
HGNC:7849  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
17q21.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed
]
- Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed
]
- Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed
]
- Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed
]
- Ni X, Gu S, Dai J, Cheng H, Guo L, Li L, Ji C, Xie Y, Ying K, Mao Y: Isolation and characterization of a novel human NM23-H1B gene, a different transcript of NM23-H1. J Hum Genet. 2003;48(2):96-100. [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
]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [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
]
- Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed
]
- MacDonald NJ, Freije JM, Stracke ML, Manrow RE, Steeg PS: Site-directed mutagenesis of nm23-H1. Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells. J Biol Chem. 1996 Oct 11;271(41):25107-16. [PubMed
]
- Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed
]
- Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed
]
- Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed
]
- Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed
]
- Garzia L, D'Angelo A, Amoresano A, Knauer SK, Cirulli C, Campanella C, Stauber RH, Steegborn C, Iolascon A, Zollo M: Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility. Oncogene. 2008 Mar 20;27(13):1853-64. Epub 2007 Oct 1. [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
]
- 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
]
- 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
]
- Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed
]
- Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed
]
- Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5344 |
| Enzyme 3 Name |
Nucleoside diphosphate kinase B |
| Enzyme 3 Synonyms |
- NDK B
- NDP kinase B
- C-myc purine-binding transcription factor PUF
- nm23-H2
|
| Enzyme 3 Gene Name |
NME2 |
| Enzyme 3 Protein Sequence |
>Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
|
| Enzyme 3 Number of Residues |
152 |
| Enzyme 3 Molecular Weight |
17297.9 |
| Enzyme 3 Theoretical pI |
8.69 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 3 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752) |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
4467843  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P22392  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NDKB_HUMAN  |
| Enzyme 3 PDB ID |
1NSK  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
|
| Enzyme 3 GenBank Gene ID |
X58965  |
| Enzyme 3 GeneCard ID |
NME2  |
| Enzyme 3 GenAtlas ID |
NME2  |
| Enzyme 3 HGNC ID |
HGNC:7850  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
17q21.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed
]
- Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed
]
- Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed
]
- Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed
]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [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
]
- Seifert M, Seib T, Engel M, Dooley S, Welter C: Characterization of the human nm23-H2 promoter region and localization of the microsatellite D17S396. Biochem Biophys Res Commun. 1995 Oct 24;215(3):910-4. [PubMed
]
- Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M: Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. [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
]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [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
]
- Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed
]
- Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5346 |
| Enzyme 4 Name |
Nucleoside diphosphate kinase 6 |
| Enzyme 4 Synonyms |
- NDK 6
- NDP kinase 6
- Inhibitor of p53-induced apoptosis-alpha
- IPIA-alpha
- nm23-H6
|
| Enzyme 4 Gene Name |
NME6 |
| Enzyme 4 Protein Sequence |
>Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
|
| Enzyme 4 Number of Residues |
186 |
| Enzyme 4 Molecular Weight |
21142.0 |
| Enzyme 4 Theoretical pI |
8.49 |
| Enzyme 4 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 4 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
3228530  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O75414  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
NDK6_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
|
| Enzyme 4 GenBank Gene ID |
AF051941  |
| Enzyme 4 GeneCard ID |
NME6  |
| Enzyme 4 GenAtlas ID |
NME6  |
| Enzyme 4 HGNC ID |
HGNC:20567  |
| Enzyme 4 Chromosome Location |
3 |
| Enzyme 4 Locus |
3p21 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [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
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6238 |
| Enzyme 5 Name |
DNA polymerase beta |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
POLB |
| Enzyme 5 Protein Sequence |
>DNA polymerase beta
MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAK
KLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIK
TLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGS
FRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQ
LPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRP
LGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
|
| Enzyme 5 Number of Residues |
335 |
| Enzyme 5 Molecular Weight |
38177.3 |
| Enzyme 5 Theoretical pI |
9.41 |
| Enzyme 5 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA repair
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in DNA binding |
| Enzyme 5 Specific Function |
Repair polymerase. Conducts "gap-filling" DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. Has a 5'-deoxyribose-5- phosphate lyase (dRP lyase) activity |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
292397  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P06746  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
DPOLB_HUMAN  |
| Enzyme 5 PDB ID |
8ICK  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1008 bp
ATGAGCAAACGGAAGGCGCCGCAGGAGACTCTCAACGGGGGAATCACCGACATGCTCACA
GAACTCGCAAACTTTGAGAAGAACGTGAGCCAAGCTATCCACAAGTACAATGCTTACAGA
AAAGCAGCATCTGTTATAGCAAAATACCCACACAAAATAAAGAGTGGAGCTGAAGCTAAG
AAATTGCCTGGAGTAGGAACAAAAATTGCTGAAAAGATTGATGAGTTTTTAGCAACTGGA
AAATTACGTAAACTGGAAAAGATTCGGCAGGATGATACGAGTTCATCCATCAATTTCCTG
ACTCGAGTTAGTGGCATTGGTCCATCTGCTGCAAGGAAGTTTGTAGATGAAGGAATTAAA
ACACTAGAAGATCTCAGAAAAAATGAAGATAAATTGAACCATCATCAGCGAATTGGGCTG
AAATATTTTGGGGACTTTGAAAAAAGAATTCCTCGTGAAGAGATGTTACAAATGCAAGAT
ATTGTACTAAATGAAGTTAAAAAAGTGGATTCTGAATACATTGCTACAGTCTGTGGCAGT
TTCAGAAGAGGTGCAGAGTCCAGTGGTGACATGGATGTTCTCCTGACCCATCCCAGCTTC
ACTTCAGAATCAACCAAACAGCCAAAACTGTTACATCAGGTTGTGGAGCAGTTACAAAAG
GTTCATTTTATCACAGATACCCTGTCAAAGGGTGAGACAAAGTTCATGGGTGTTTGCCAG
CTTCCCAGTAAAAATGATGAAAAAGAATATCCACACAGAAGAATTGATATCAGGTTGATA
CCCAAAGATCAGTATTACTGTGGTGTTCTCTATTTCACTGGGAGTGATATTTTCAATAAG
AATATGAGGGCTCATGCCCTAGAAAAGGGTTTCACAATCAATGAGTACACCATCCGTCCC
TTGGGAGTCACTGGAGTTGCAGGAGAACCCCTGCCAGTGGATAGTGAAAAAGACATCTTT
GATTACATCCAGTGGAAATACCGGGAACCCAAGGACCGGAGCGAATGA
|
| Enzyme 5 GenBank Gene ID |
L11607  |
| Enzyme 5 GeneCard ID |
POLB  |
| Enzyme 5 GenAtlas ID |
POLB  |
| Enzyme 5 HGNC ID |
HGNC:9174  |
| Enzyme 5 Chromosome Location |
8 |
| Enzyme 5 Locus |
8p11.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Patterson TA, Little W, Cheng X, Widen SG, Kumar A, Beard WA, Wilson SH: Molecular cloning and high-level expression of human polymerase beta cDNA and comparison of the purified recombinant human and rat enzymes. Protein Expr Purif. 2000 Feb;18(1):100-10. [PubMed
]
- Dobashi Y, Kubota Y, Shuin T, Torigoe S, Yao M, Hosaka M: Polymorphisms in the human DNA polymerase beta gene. Hum Genet. 1995 Apr;95(4):389-90. [PubMed
]
- Chyan YJ, Ackerman S, Shepherd NS, McBride OW, Widen SG, Wilson SH, Wood TG: The human DNA polymerase beta gene structure. Evidence of alternative splicing in gene expression. Nucleic Acids Res. 1994 Jul 25;22(14):2719-25. [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
]
- Widen SG, Kedar P, Wilson SH: Human beta-polymerase gene. Structure of the 5'-flanking region and active promoter. J Biol Chem. 1988 Nov 15;263(32):16992-8. [PubMed
]
- Abbotts J, SenGupta DN, Zmudzka B, Widen SG, Notario V, Wilson SH: Expression of human DNA polymerase beta in Escherichia coli and characterization of the recombinant enzyme. Biochemistry. 1988 Feb 9;27(3):901-9. [PubMed
]
- SenGupta DN, Zmudzka BZ, Kumar P, Cobianchi F, Skowronski J, Wilson SH: Sequence of human DNA polymerase beta mRNA obtained through cDNA cloning. Biochem Biophys Res Commun. 1986 Apr 14;136(1):341-7. [PubMed
]
- Matsumoto Y, Kim K, Katz DS, Feng JA: Catalytic center of DNA polymerase beta for excision of deoxyribose phosphate groups. Biochemistry. 1998 May 5;37(18):6456-64. [PubMed
]
- DeMott MS, Beyret E, Wong D, Bales BC, Hwang JT, Greenberg MM, Demple B: Covalent trapping of human DNA polymerase beta by the oxidative DNA lesion 2-deoxyribonolactone. J Biol Chem. 2002 Mar 8;277(10):7637-40. Epub 2002 Jan 22. [PubMed
]
- El-Andaloussi N, Valovka T, Toueille M, Steinacher R, Focke F, Gehrig P, Covic M, Hassa PO, Schar P, Hubscher U, Hottiger MO: Arginine methylation regulates DNA polymerase beta. Mol Cell. 2006 Apr 7;22(1):51-62. [PubMed
]
- Pelletier H, Sawaya MR, Wolfle W, Wilson SH, Kraut J: A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase beta. Biochemistry. 1996 Oct 1;35(39):12762-77. [PubMed
]
- Pelletier H, Sawaya MR: Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase beta by X-ray structural analysis. Biochemistry. 1996 Oct 1;35(39):12778-87. [PubMed
]
- Sawaya MR, Prasad R, Wilson SH, Kraut J, Pelletier H: Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism. Biochemistry. 1997 Sep 16;36(37):11205-15. [PubMed
]
- Krahn JM, Beard WA, Miller H, Grollman AP, Wilson SH: Structure of DNA polymerase beta with the mutagenic DNA lesion 8-oxodeoxyguanine reveals structural insights into its coding potential. Structure. 2003 Jan;11(1):121-7. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6239 |
| Enzyme 6 Name |
DNA polymerase alpha catalytic subunit |
| Enzyme 6 Synonyms |
- DNA polymerase alpha catalytic subunit p180
|
| Enzyme 6 Gene Name |
POLA1 |
| Enzyme 6 Protein Sequence |
>DNA polymerase alpha catalytic subunit
MAPVHGDDSLSDSGSFVSSRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDFTGVYEE
VDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDADEKGKDGKARNKDK
RNVKKLAVTKPNNIKSMFIACAGKKTADKAVDLSKDGLLGDILQDLNTETPQITPPPVMI
LKKKRSIGASPNPFSVHTATAVPSGKIASPVSRKEPPLTPVPLKRAEFAGDDVQVESTEE
EQESGAMEFEDGDFDEPMEVEEVDLEPMAAKAWDKESEPAEEVKQEADSGKGTVSYLGSF
LPDVSCWDIDQEGDSSFSVQEVQVDSSHLPLVKGADEEQVFHFYWLDAYEDQYNQPGVVF
LFGKVWIESAETHVSCCVMVKNIERTLYFLPREMKIDLNTGKETGTPISMKDVYEEFDEK
IATKYKIMKFKSKPVEKNYAFEIPDVPEKSEYLEVKYSAEMPQLPQDLKGETFSHVFGTN
TSSLELFLMNRKIKGPCWLEVKSPQLLNQPVSWCKVEAMALKPDLVNVIKDVSPPPLVVM
AFSMKTMQNAKNHQNEIIAMAALVHHSFALDKAAPKPPFQSHFCVVSKPKDCIFPYAFKE
VIEKKNVKVEVAATERTLLGFFLAKVHKIDPDIIVGHNIYGFELEVLLQRINVCKAPHWS
KIGRLKRSNMPKLGGRSGFGERNATCGRMICDVEISAKELIRCKSYHLSELVQQILKTER
VVIPMENIQNMYSESSQLLYLLEHTWKDAKFILQIMCELNVLPLALQITNIAGNIMSRTL
MGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQKLGDEDEEIDGDTNKYKKGRKKAAYA
GGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNICFTTVQRVASEAQKVTEDGEQEQIPE
LPDPSLEMGILPREIRKLVERRKQVKQLMKQQDLNPDLILQYDIRQKALKLTANSMYGCL
GFSYSRFYAKPLAALVTYKGREILMHTKEMVQKMNLEVIYGDTDSIMINTNSTNLEEVFK
LGNKVKSEVNKLYKLLEIDIDGVFKSLLLLKKKKYAALVVEPTSDGNYVTKQELKGLDIV
RRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKRLIEIGENVLNGSVPVSQFEINKALT
KDPQDYPDKKSLPHVHVALWINSQGGRKVKAGDTVSYVICQDGSNLTASQRAYAPEQLQK
QDNLTIDTQYYLAQQIHPVVARICEPIDGIDAVLIATWLGLDPTQFRVHHYHKDEENDAL
LGGPAQLTDEEKYRDCERFKCPCPTCGTENIYDNVFDGSGTDMEPSLYRCSNIDCKASPL
TFTVQLSNKLIMDIRRFIKKYYDGWLICEEPTCRNRTRHLPLQFSRTGPLCPACMKATLQ
PEYSDKSLYTQLCFYRYIFDAECALEKLTTDHEKDKLKKQFFTPKVLQDYRKLKNTAEQF
LSRSGYSEVNLSKLFAGCAVKS
|
| Enzyme 6 Number of Residues |
1462 |
| Enzyme 6 Molecular Weight |
165911.4 |
| Enzyme 6 Theoretical pI |
5.59 |
| Enzyme 6 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA replication
- cellular macromolecule metabolic process
- cellular nitrogen compound metabolic process
- macromolecule metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 6 General Function |
Involved in nucleotide binding |
| Enzyme 6 Specific Function |
Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
35568  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P09884  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
DPOLA_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>4389 bp
ATGGCACCTGTGCACGGCGACGACTCTCTGTCAGATTCAGGGAGTTTTGTATCTTCTCGA
GCCCGGCGAGAAAAAAAATCAAAGAAGGGGCGCCAAGAAGCCCTAGAAAGACTGAAAAAG
GCTAAAGCTGGTGAGAAGTATAAATATGAAGTCGAGGACTTCACAGGTGTTTATGAAGAA
GTTGATGAAGAACAGTATTCGAAGCTGGTTCAGGCACGCCAGGATGATGACTGGATTGTG
GATGATGATGGTATTGGCTATGTGGAAGATGGCCGAGAGATTTTTGATGATGACCTTGAA
GATGATGCCCTTGATGCTGATGAGAAAGGAAAAGATGGTAAAGCACGCAATAAAGACAAG
AGGAATGTAAAGAAGCTCGCAGTGACAAAACCGAACAACATTAAGTCAATGTTCATTGCT
TGTGCTGGAAAGAAAACTGCAGATAAAGCTGTAGACTTGTCCAAGGATGGTCTGCTAGGT
GACATTCTACAGGATCTTAACACTGAGACACCTCAAATAACTCCACCACCTGTAATGATA
CTGAAGAAGAAAAGATCCATTGGAGCTTCACCGAATCCTTTCTCTGTGCACACCGCCACG
GCAGTTCCTTCAGGAAAAATTGCTTCCCCTGTCTCCAGAAAGGAGCCTCCATTAACTCCT
GTTCCTCTTAAACGTGCTGAATTTGCTGGCGATGATGTACAGGTCGAGAGTACAGAAGAA
GAGCAGGAGTCAGGGGCAATGGAGTTTGAAGATGGTGACTTTGATGAGCCCATGGAAGTT
GAAGAGGTGGACCTGGAGCCTATGGCTGCCAAGGCTTGGGACAAAGAGAGTGAGCCAGCA
GAGGAAGTGAAACAAGAGGCGGATTCTGGGAAAGGGACCGTGTCCTACTTAGGAAGTTTT
CTCCCGGATGTCTCTTGTTGGGACATTGATCAAGAAGGTGATAGCAGTTTCTCAGTGCAA
GAAGTTCAAGTGGATTCCAGTCACCTCCCATTGGTAAAAGGGGCAGATGAGGAACAAGTA
TTCCACTTTTATTGGTTGGATGCTTATGAGGATCAGTACAACCAACCAGGTGTGGTATTT
CTGTTTGGGAAAGTTTGGATTGAATCAGCCGAGACCCATGTGAGCTGTTGTGTCATGGTG
AAAAATATCGAGCGAACGCTTTACTTCCTTCCCCGTGAAATGAAAATTGATCTAAATACG
GGGAAAGAAACAGGAACTCCAATTTCAATGAAGGATGTTTATGAGGAATTTGATGAGAAA
ATAGCAACAAAATATAAAATTATGAAGTTCAAGTCTAAGCCAGTGGAAAAGAACTATGCT
TTTGAGATACCTGATGTTCCAGAAAAATCTGAGTACTTGGAAGTTAAATACTCGGCTGAA
ATGCCACAGCTTCCTCAAGATTTGAAAGGAGAAACTTTTTCTCATGTATTTGGGACCAAC
ACATCTAGCCTGGAACTGTTCTTGATGAACAGAAAGATCAAAGGACCTTGTTGGCTTGAA
GTAAAAAAGTCCACAGCTCTTAATCAGCCAGTCAGTTGGTGTAAAGTTGAGGCAATGGCT
TTGAAACCAGACCTGGTGAATGTAATTAAGGATGTCAGTCCACCACCGCTTGTCGTGATG
GCTTTCAGCATGAAGACAATGCAGAATGCAAAGAACCATCAAAATGAGATTATTGCTATG
GCAGCTTTGGTCCATCACAGTTTTGCATTGGATAAAGCAGCCCCAAAGCCTCCCTTTCAG
TCACACTTCTGTGTTGTGTCTAAACCAAAGGACTGTATTTTTCCATATGCTTTCAAAGAA
GTCATTGAGAAAAAGAATGTGAAGGTTGAGGTTGCTGCAACAGAAAGAACACTGCTAGGT
TTTTTCCTTGCAAAAGTTCACAAAATTGATCCTGATATCATTGTGGGTCATAATATTTAT
GGGTTTGAACTGGAAGTACTACTGCAGAGAATTAATGTGTGCAAAGCTCCTCACTGGTCC
AAGATAGGTCGACTGAAGCGATCCAACATGCCAAAGCTTGGGGGCCGGAGTGGATTTGGT
GAAAGAAATGCTACCTGTGGTCGAATGATCTGTGATGTGGAAATTTCAGCAAAGGAATTG
ATTCGTTGTAAAAGCTACCATCTGTCTGAACTTGTTCAGCAGATTCTAAAAACTGAAAGG
GTTGTAATCCCAATGGAAAATATACAAAATATGTACAGTGAATCTTCTCAACTGTTATAC
CTGTTGGAACACACCTGGAAAGATGCCAAGTTCATTTTGCAGATCATGTGTGAGCTAAAT
GTTCTTCCATTAGCATTGCAGATCACTAACATCGCTGGGAACATTATGTCCAGGACGCTG
ATGGGTGGACGATCCGAGCGTAACGAGTTCTTGTTGCTTCATGCATTTTACGAAAACAAC
TATATTGTGCCTGACAAGCAGATTTTCAGAAAGCCTCAGCAAAAACTGGGAGATGAAGAT
GAAGAAATTGATGGAGATACCAATAAATACAAGAAAGGACGTAAGAAAGGAGCTTATGCT
GGAGGCTTGGTTTTGGACCCCAAAGTTGGTTTTTATGATAAGTTCATTTTGCTTCTGGAC
TTCAACAGTCTATATCCTTCCATCATTCAGGAATTTAACATTTGTTTTACAACAGTACAA
AGAGTTGCTTCAGAGGCACAGAAAGTTACAGAGGATGGAGAACAAGAACAGATCCCTGAG
TTGCCAGATCCAAGCTTAGAAATGGGCATTTTGCCCAGAGAGATCCGGAAACTGGTAGAA
CGGAGAAAACAAGTCAAACAGCTAATGAAACAGCAAGACTTAAATCCAGACCTTATTCTT
CAGTATGACATTCGACAGAAGGCTTTGAAGCTCACAGCGAACAGTATGTATGGTTGCCTG
GGATTTTCCTATAGCAGATTTTACGCCAAACCACTGGCTGCCTTGGTGACATACAAAGGA
AGGGAGATTTTGATGCATACGAAAGAGATGGTACAAAAGATGAATCTTGAAGTTATTTAT
GGAGATACAGATTCAATTATGATAAACACCAATAGCACCAATCTGGAAGAAGTATTTAAG
TTGGGAAACAAGGTAAAAAGTGAAGTGAATAAGTTGTACAAACTGCTTGAAATAGACATT
GATGGGGTTTTCAAGTCTCTGCTACTGCTGAAAAAAAAGAAGTACGCTGCTCTGGTTGTT
GAGCCAACGTCGGATGGGAATTATGTCACCAAACAGGAGCTCAAAGGATTAGATATAGTT
AGAAGAGATTGGTGTGATCTTGCTAAAGACACTGGAAACTTTGTGATTGGCCAGATTCTT
TCTGATCAAAGCCGGGACACTATAGTGGAAAACATTCAGAAGAGGCTGATAGAAATTGGA
GAAAATGTGCTAAATGGCAGTGTCCCAGTGAGCCAGTTTGAAATTAACAAGGCATTGACA
AAGGATCCCCAGGATTACCCTGATAAAAAAAGCCTACCTCATGTACATGTTGCCCTCTGG
ATAAATTCTCAAGGAGGCAGAAAGGTGAAAGCTGGAGATACTGTGTCATATGTCATCTGT
CAGGATGGATCAAACCTCACTGCAAGTCAGAGGGCCTATGCGCCTGAGCAGCTGCAGAAA
CAGGATAATCTAACCATTGACACCCAGTACTACCTGGCCCAGCAGATCCACCCAGTCGTG
GCTCGGATCTGTGAACCAATAGACGGAATTGATGCTGTCCTCATTGCAACGTGGTTGGGA
CTTGACCCCACCCAATTTAGAGTTCATCATTATCATAAAGATGAAGAGAATGATGCTCTA
CTTGGTGGCCCAGCACAGCTCACTGATGAAGAGAAATACAGGGACTGTGAAAGATTCAAA
TGTCCATGCCCTACATGTGGAACTGAGAATATTTATGATAATGTCTTTGATGGTTCGGGA
ACAGATATGGAGCCCAGCTTGTATCGTTGCAGTAACATCGATTGTAAGGCTTCACCTCTG
ACCTTTACAGTACAACTGAGCAACAAATTGATCATGGACATTAGACGTTTCATTAAAAAG
TACTATGATGGCTGGTTGATATGTGAAGAGCCAACCTGTCGCAATCGAACTCGTCACCTT
CCCCTTCAATTCTCCCGAACTGGGCCTCTTTGCCCAGCCTGCATGAAAGCTACACTTCAA
CCAGAGTATTCTGACAAGTCCCTGTACACCCAGCTGTGCTTTTACCGGTACATTTTTGAT
GCGGAGTGTGCACTGGAGAAACTTACTACCGATCATGAGAAAGATAAATTGAAGAAGCAA
TTTTTTACCCCCAAAGTTCTGCAGGACTACAGAAAACTCAAGAACACAGCAGAGCAATTC
TTGTCCCGAAGTGGCTACTCCGAAGTGAATCTGAGCAAACTCTTCGCTGGTTGTGCCGTG
AAATCCTAA
|
| Enzyme 6 GenBank Gene ID |
X06745  |
| Enzyme 6 GeneCard ID |
POLA1  |
| Enzyme 6 GenAtlas ID |
POLA1  |
| Enzyme 6 HGNC ID |
HGNC:9173  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Wong SW, Wahl AF, Yuan PM, Arai N, Pearson BE, Arai K, Korn D, Hunkapiller MW, Wang TS: Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases. EMBO J. 1988 Jan;7(1):37-47. [PubMed
]
- Pearson BE, Nasheuer HP, Wang TS: Human DNA polymerase alpha gene: sequences controlling expression in cycling and serum-stimulated cells. Mol Cell Biol. 1991 Apr;11(4):2081-95. [PubMed
]
- Hsi KL, Copeland WC, Wang TS: Human DNA polymerase alpha catalytic polypeptide binds ConA and RCA and contains a specific labile site in the N-terminus. Nucleic Acids Res. 1990 Nov 11;18(21):6231-7. [PubMed
]
- Smale ST, Tjian R: T-antigen-DNA polymerase alpha complex implicated in simian virus 40 DNA replication. Mol Cell Biol. 1986 Nov;6(11):4077-87. [PubMed
]
- Lee SS, Dong Q, Wang TS, Lehman IR: Interaction of herpes simplex virus 1 origin-binding protein with DNA polymerase alpha. Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7882-6. [PubMed
]
- Braun KA, Lao Y, He Z, Ingles CJ, Wold MS: Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms. Biochemistry. 1997 Jul 15;36(28):8443-54. [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
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [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
]
- Warren EM, Huang H, Fanning E, Chazin WJ, Eichman BF: Physical interactions between Mcm10, DNA, and DNA polymerase alpha. J Biol Chem. 2009 Sep 4;284(36):24662-72. Epub 2009 Jul 16. [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
]
- Evanics F, Maurmann L, Yang WW, Bose RN: Nuclear magnetic resonance structures of the zinc finger domain of human DNA polymerase-alpha. Biochim Biophys Acta. 2003 Sep 23;1651(1-2):163-71. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6240 |
| Enzyme 7 Name |
DNA polymerase delta subunit 3 |
| Enzyme 7 Synonyms |
- DNA polymerase delta subunit p66
|
| Enzyme 7 Gene Name |
POLD3 |
| Enzyme 7 Protein Sequence |
>DNA polymerase delta subunit 3
MADQLYLENIDEFVTDQNKIVTYKWLSYTLGVHVNQAKQMLYDYVERKRKENSGAQLHVT
YLVSGSLIQNGHSCHKVAVVREDKLEAVKSKLAVTASIHVYSIQKAMLKDSGPLFNTDYD
ILKSNLQNCSKFSAIQCAAAVPRAPAESSSSSKKFEQSHLHMSSETQANNELTTNGHGPP
ASKQVSQQPKGIMGMFASKAAAKTQETNKETKTEAKEVTNASAAGNKAPGKGNMMSNFFG
KAAMNKFKVNLDSEQAVKEEKIVEQPTVSVTEPKLATPAGLKKSSKKAEPVKVLQKEKKR
GKRVALSDDETKETENMRKKRRRIKLPESDSSEDEVFPDSPGAYEAESPSPPPPPSPPLE
PVPKTEPEPPSVKSSSGENKRKRKRVLKSKTYLDGEGCIVTEKVYESESCTDSEEELNMK
TSSVHRPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK
|
| Enzyme 7 Number of Residues |
466 |
| Enzyme 7 Molecular Weight |
51400.0 |
| Enzyme 7 Theoretical pI |
9.96 |
| Enzyme 7 GO Classification |
| Function |
|
| Process |
- DNA metabolic process
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 7 General Function |
Involved in protein binding |
| Enzyme 7 Specific Function |
Required for optimal DNA polymerase delta activity |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
221045990  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q15054  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
DPOD3_HUMAN  |
| Enzyme 7 PDB ID |
1U76  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1401 bp
ATGGCGGACCAGCTTTATCTGGAAAATATAGACGAGTTCGTCACGGACCAAAACAAGATC
GTGACATACAAATGGCTGAGCTATACACTAGGGGTTCATGTTAACCAGGCCAAACAGATG
CTGTATGATTATGTTGAAAGGAAACGAAAAGAAAATTCAGGAGCCCAACTGCATGTTACC
TACTTGGTGTCTGGCAGTCTCATTCAGAATGGACATTCCTGCCACAAGGTTGCAGTAGTG
AGAGAAGATAAATTGGAAGCAGTGAAGTCCAAGCTAGCTGTGACTGCCAGCATCCATGTG
TACAGCATCCAGAAAGCCATGCTAAAGGACAGTGGGCCTCTGTTCAATACTGACTATGAC
ATCCTTAAAAGCAACTTGCAGAACTGCAGCAAATTTAGTGCTATACAATGTGCAGCTGCC
GTCCCTAGAGCTCCTGCTGAATCCTCTTCGTCTTCCAAAAAGTTTGAGCAGTCACATCTT
CACATGTCAAGTGAGACACAAGCCAACAATGAGCTGACCACCAATGGTCATGGCCCACCT
GCATCCAAGCAGGTTTCCCAGCAGCCCAAAGGAATTATGGGAATGTTTGCCTCCAAAGCT
GCTGCTAAAACCCAAGAAACCAACAAGGAAACGAAAACAGAGGCTAAAGAAGTAACAAAT
GCATCTGCAGCAGGCAACAAGGCACCAGGGAAAGGGAATATGATGAGCAACTTTTTTGGA
AAAGCTGCTATGAATAAATTTAAAGTCAATTTGGACTCAGAACAAGCAGTGAAAGAAGAA
AAAATAGTGGAGCAGCCTACAGTGTCTGTCACGGAACCAAAGCTGGCAACTCCTGCAGGC
CTGAAAAAATCCAGCAAAAAAGCAGAGCCTGTTAAGGTGCTGCAGAAGGAAAAAAAAAGG
GGGAAGCGAGTAGCATTATCTGATGATGAGACAAAGGAAACTGAAAACATGAGGAAAAAG
AGGAGAAGAATCAAACTTCCTGAATCTGATAGCAGTGAAGATGAAGTCTTTCCAGACTCT
CCTGGGGCTTATGAAGCTGAGTCACCATCCCCACCTCCTCCTCCGTCTCCACCTCTTGAA
CCAGTGCCAAAGACTGAGCCTGAACCTCCTTCTGTCAAGAGCTCAAGTGGAGAAAACAAA
AGAAAACGAAAACGCGTACTAAAATCTAAAACTTACCTGGATGGGGAAGGCTGCATAGTG
ACTGAAAAAGTCTACGAGAGTGAATCCTGCACAGATAGTGAAGAGGAGCTTAACATGAAG
ACATCCTCAGTACACAGACCCCCTGCCATGACTGTGAAAAAAGAACCCAGAGAGGAACGA
AAGGGCCCCAAGAAAGGGACTGCTGCTCTGGGCAAAGCCAACAGACAGGTGTCCATTACT
GGCTTCTTCCAGAGGAAATAA
|
| Enzyme 7 GenBank Gene ID |
AK316301  |
| Enzyme 7 GeneCard ID |
POLD3  |
| Enzyme 7 GenAtlas ID |
POLD3  |
| Enzyme 7 HGNC ID |
HGNC:20932  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
11q14 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [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
]
- Hughes P, Tratner I, Ducoux M, Piard K, Baldacci G: Isolation and identification of the third subunit of mammalian DNA polymerase delta by PCNA-affinity chromatography of mouse FM3A cell extracts. Nucleic Acids Res. 1999 May 15;27(10):2108-14. [PubMed
]
- Mo J, Liu L, Leon A, Mazloum N, Lee MY: Evidence that DNA polymerase delta isolated by immunoaffinity chromatography exhibits high-molecular weight characteristics and is associated with the KIAA0039 protein and RPA. Biochemistry. 2000 Jun 20;39(24):7245-54. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Li H, Xie B, Zhou Y, Rahmeh A, Trusa S, Zhang S, Gao Y, Lee EY, Lee MY: Functional roles of p12, the fourth subunit of human DNA polymerase delta. J Biol Chem. 2006 May 26;281(21):14748-55. Epub 2006 Feb 28. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [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
]
- 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
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6243 |
| Enzyme 8 Name |
DNA polymerase lambda |
| Enzyme 8 Synonyms |
- Pol Lambda
- DNA polymerase beta-2
- Pol beta2
- DNA polymerase kappa
|
| Enzyme 8 Gene Name |
POLL |
| Enzyme 8 Protein Sequence |
>DNA polymerase lambda
MDPRGILKAFPKRQKIHADASSKVLAKIPRREEGEEAEEWLSSLRAHVVRTGIGRARAEL
FEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYERALRLLRLPQLPPGAQLVKSAWLSLCLQ
ERRLVDVAGFSIFIPSRYLDHPQPSKAEQDASIPPGTHEALLQTALSPPPPPTRPVSPPQ
KAKEAPNTQAQPISDDEASDGEETQVSAADLEALISGHYPTSLEGDCEPSPAPAVLDKWV
CAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEAC
SIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSL
EDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRR
GKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLP
GPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNT
HGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
|
| Enzyme 8 Number of Residues |
575 |
| Enzyme 8 Molecular Weight |
63481.7 |
| Enzyme 8 Theoretical pI |
7.94 |
| Enzyme 8 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA repair
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
|
|
| Enzyme 8 General Function |
Involved in DNA binding |
| Enzyme 8 Specific Function |
Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
6746387  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q9UGP5  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
DPOLL_HUMAN  |
| Enzyme 8 PDB ID |
1XSL  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1728 bp
ATGGATCCCAGGGGTATCTTGAAGGCATTTCCCAAGCGGCAGAAAATTCATGCTGATGCA
TCATCAAAAGTACTTGCAAAGATTCCTAGGAGGGAAGAGGGAGAAGAAGCAGAAGAGTGG
CTGAGCTCCCTTCGGGCCCATGTTGTGCGCACTGGCATTGGACGAGCCCGGGCAGAACTC
TTTGAGAAGCAGATTGTTCAGCATGGCGGCCAGCTATGCCCTGCCCAGGGCCCAGGTGTC
ACTCACATTGTGGTGGATGAAGGCATGGACTATGAGCGAGCCCTCCGCCTTCTCAGACTA
CCCCAGCTGCCCCCGGGTGCTCAGCTGGTGAAGTCAGCCTGGCTGAGCTTGTGCCTTCAG
GAGAGGAGGCTGGTGGATGTAGCTGGATTCAGCATCTTCATCCCCAGTAGGTACTTGGAC
CATCCACAGCCCAGCAAGGCAGAGCAGGATGCTTCTATTCCTCCTGGCACCCATGAGGCC
CTGCTTCAGACAGCCCTTTCTCCTCCTCCTCCTCCCACCAGGCCTGTGTCTCCTCCCCAA
AAGGCAAAAGAGGCACCAAACACCCAAGCCCAGCCCATCTCTGATGATGAAGCCAGTGAT
GGGGAAGAAACCCAGGTTAGTGCAGCTGATCTGGAAGCCCTCATCAGTGGCCACTACCCC
ACCTCCCTTGAGGGAGATTGTGAGCCTAGCCCAGCCCCTGCTGTCCTGGATAAGTGGGTC
TGTGCACAGCCCTCAAGCCAGAAGGCGACCAATCACAACCTCCATATCACAGAGAAGCTG
GAAGTTCTGGCCAAAGCCTACAGTGTTCAGGGAGACAAGTGGAGGGCCCTGGGCTATGCC
AAGGCCATCAATGCCCTCAAGAGCTTCCATAAGCCTGTCACCTCGTACCAGGAGGCCTGC
AGTATCCCTGGGATTGGGAAGCGGATGGCTGAGAAAATCATAGAGATCCTGGAGAGCGGG
CATTTGCGGAAGCTGGACCATATCAGTGAGAGCGTGCCTGTCTTGGAGCTCTTCTCCAAC
ATCTGGGGAGCTGGGACCAAGACTGCCCAGATGTGGTACCAACAGGGCTTCCGAAGTCTG
GAAGACATCCGCAGCCAGGCCTCCCTGACAACCCAGCAGGCCATCGGCCTGAAGCATTAC
AGTGACTTCCTGGAACGTATGCCCAGGGAGGAGGCTACAGAGATTGAGCAGACAGTCCAG
AAAGCAGCCCAGGCCTTTAACTCTGGGCTGCTGTGTGTGGCATGTGGTTCATACCGACGG
GGAAAGGCGACCTGTGGTGATGTCGACGTGCTCATCACTCACCCAGATGGCCGGTCCCAC
CGGGGTATCTTCAGCCGCCTCCTTGACAGTCTTCGGCAGGAAGGGTTCCTCACAGATGAC
TTGGTGAGCCAAGAGGAGAATGGTCAGCAACAGAAGTACTTGGGGGTGTGCCGGCTCCCA
GGGCCAGGGCGGCGGCACCGGCGCCTGGACATCATCGTGGTGCCCTATAGCGAGTTTGCC
TGTGCCCTGCTCTACTTCACCGGCTCTGCACACTTCAACCGCTCCATGCGAGCCCTGGCC
AAAACCAAGGGCATGAGTCTGTCAGAACATGCCCTCAGCACTGCTGTGGTCCGGAACACC
CATGGCTGCAAGGTGGGGCCTGGCCGAGTGCTGCCCACTCCCACTGAGAAGGATGTCTTC
AGGCTCTTAGGCCTCCCCTACCGAGAACCTGCTGAGCGGGACTGGTGA
|
| Enzyme 8 GenBank Gene ID |
AF161019  |
| Enzyme 8 GeneCard ID |
POLL  |
| Enzyme 8 GenAtlas ID |
POLL  |
| Enzyme 8 HGNC ID |
HGNC:9184  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
10q23 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Aoufouchi S, Flatter E, Dahan A, Faili A, Bertocci B, Storck S, Delbos F, Cocea L, Gupta N, Weill JC, Reynaud CA: Two novel human and mouse DNA polymerases of the polX family. Nucleic Acids Res. 2000 Sep 15;28(18):3684-93. [PubMed
]
- Nagasawa K, Kitamura K, Yasui A, Nimura Y, Ikeda K, Hirai M, Matsukage A, Nakanishi M: Identification and characterization of human DNA polymerase beta 2, a DNA polymerase beta -related enzyme. J Biol Chem. 2000 Oct 6;275(40):31233-8. [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
]
- 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
]
- 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
]
- Garcia-Diaz M, Bebenek K, Kunkel TA, Blanco L: Identification of an intrinsic 5'-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. J Biol Chem. 2001 Sep 14;276(37):34659-63. Epub 2001 Jul 16. [PubMed
]
- Blanca G, Shevelev I, Ramadan K, Villani G, Spadari S, Hubscher U, Maga G: Human DNA polymerase lambda diverged in evolution from DNA polymerase beta toward specific Mn(++) dependence: a kinetic and thermodynamic study. Biochemistry. 2003 Jun 24;42(24):7467-76. [PubMed
]
- Shevelev I, Blanca G, Villani G, Ramadan K, Spadari S, Hubscher U, Maga G: Mutagenesis of human DNA polymerase lambda: essential roles of Tyr505 and Phe506 for both DNA polymerase and terminal transferase activities. Nucleic Acids Res. 2003 Dec 1;31(23):6916-25. [PubMed
]
- Maga G, Blanca G, Shevelev I, Frouin I, Ramadan K, Spadari S, Villani G, Hubscher U: The human DNA polymerase lambda interacts with PCNA through a domain important for DNA primer binding and the interaction is inhibited by p21/WAF1/CIP1. FASEB J. 2004 Nov;18(14):1743-5. Epub 2004 Sep 9. [PubMed
]
- Maga G, Ramadan K, Locatelli GA, Shevelev I, Spadari S, Hubscher U: DNA elongation by the human DNA polymerase lambda polymerase and terminal transferase activities are differentially coordinated by proliferating cell nuclear antigen and replication protein A. J Biol Chem. 2005 Jan 21;280(3):1971-81. Epub 2004 Nov 10. [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
]
- DeRose EF, Kirby TW, Mueller GA, Bebenek K, Garcia-Diaz M, Blanco L, Kunkel TA, London RE: Solution structure of the lyase domain of human DNA polymerase lambda. Biochemistry. 2003 Aug 19;42(32):9564-74. [PubMed
]
- Garcia-Diaz M, Bebenek K, Krahn JM, Blanco L, Kunkel TA, Pedersen LC: A structural solution for the DNA polymerase lambda-dependent repair of DNA gaps with minimal homology. Mol Cell. 2004 Feb 27;13(4):561-72. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6244 |
| Enzyme 9 Name |
DNA polymerase epsilon subunit 4 |
| Enzyme 9 Synonyms |
- DNA polymerase II subunit 4
- DNA polymerase epsilon subunit p12
|
| Enzyme 9 Gene Name |
POLE4 |
| Enzyme 9 Protein Sequence |
>DNA polymerase epsilon subunit 4
MAAAAAAGSGTPREEEGPAGEAAASQPQAPTSVPGARLSRLPLARVKALVKADPDVTLAG
QEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD
|
| Enzyme 9 Number of Residues |
117 |
| Enzyme 9 Molecular Weight |
12208.6 |
| Enzyme 9 Theoretical pI |
4.55 |
| Enzyme 9 GO Classification |
| Function |
- DNA binding
- binding
- nucleic acid binding
- sequence-specific DNA binding
|
| Process |
| — |
| Component |
|
|
| Enzyme 9 General Function |
Involved in sequence-specific DNA binding |
| Enzyme 9 Specific Function |
May play a role in allowing polymerase epsilon to carry out its replication and/or repair function |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
62822482  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q9NR33  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
DPOE4_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>354 bp
ATGGCGGCGGCGGCGGCGGCAGGAAGCGGGACGCCCCGAGAGGAGGAGGGACCTGCTGGG
GAGGCAGCGGCCTCGCAGCCCCAGGCCCCAACGAGTGTGCCTGGGGCTCGTCTCTCGAGG
TTGCCTCTGGCGCGAGTGAAGGCCTTGGTGAAGGCAGATCCCGACGTGACGCTAGCGGGA
CAGGAAGCCATCTTCATTCTGGCACGAGCCGCGGAACTGTTTGTGGAGACCATTGCAAAA
GATGCCTACTGTTGCGCTCAGCAGGGAAAAAGGAAAACCCTTCAGAGGAGAGACTTGGAT
AATGCAATAGAAGCTGTGGATGAATTTGCTTTTCTGGAAGGTACTTTAGATTGA
|
| Enzyme 9 GenBank Gene ID |
AC007400  |
| Enzyme 9 GeneCard ID |
POLE4  |
| Enzyme 9 GenAtlas ID |
POLE4  |
| Enzyme 9 HGNC ID |
HGNC:18755  |
| Enzyme 9 Chromosome Location |
2 |
| Enzyme 9 Locus |
2p12 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Li Y, Pursell ZF, Linn S: Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon. J Biol Chem. 2000 Jul 28;275(30):23247-52. [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
]
- 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
]
- 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
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6245 |
| Enzyme 10 Name |
DNA polymerase eta |
| Enzyme 10 Synonyms |
- RAD30 homolog A
- Xeroderma pigmentosum variant type protein
|
| Enzyme 10 Gene Name |
POLH |
| Enzyme 10 Protein Sequence |
>DNA polymerase eta
MATGQDRVVALVDMDCFFVQVEQRQNPHLRNKPCAVVQYKSWKGGGIIAVSYEARAFGVT
RSMWADDAKKLCPDLLLAQVRESRGKANLTKYREASVEVMEIMSRFAVIERASIDEAYVD
LTSAVQERLQKLQGQPISADLLPSTYIEGLPQGPTTAEETVQKEGMRKQGLFQWLDSLQI
DNLTSPDLQLTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSH
GSVPQLFSQMPIRKIRSLGGKLGASVIEILGIEYMGELTQFTESQLQSHFGEKNGSWLYA
MCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATREQVQWWLLQLAQELEERLTKDRNDND
RVATQLVVSIRVQGDKRLSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLT
MLFLCATKFSASAPSSSTDITSFLSSDPSSLPKVPVTSSEAKTQGSGPAVTATKKATTSL
ESFFQKAAERQKVKEASLSSLTAPTQAPMSNSPSKPSLPFQTSQSTGTEPFFKQKSLLLK
QKQLNNSSVSSPQQNPWSNCKALPNSLPTEYPGCVPVCEGVSKLEESSKATPAEMDLAHN
SQSMHASSASKSVLEVTQKATPNPSLLAAEDQVPCEKCGSLVPVWDMPEHMDYHFALELQ
KSFLQPHSSNPQVVSAVSHQGKRNPKSPLACTNKRPRPEGMQTLESFFKPLTH
|
| Enzyme 10 Number of Residues |
713 |
| Enzyme 10 Molecular Weight |
78412.8 |
| Enzyme 10 Theoretical pI |
8.56 |
| Enzyme 10 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- damaged DNA binding
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA repair
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in damaged DNA binding |
| Enzyme 10 Specific Function |
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
5138988  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q9Y253  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
POLH_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>2142 bp
ATGGCTACTGGACAGGATCGAGTGGTTGCTCTCGTGGACATGGACTGTTTTTTTGTTCAA
GTGGAGCAGCGGCAAAATCCTCATTTGAGGAATAAACCTTGTGCAGTTGTACAGTACAAA
TCATGGAAGGGTGGTGGAATAATTGCAGTGAGTTATGAAGCTCGTGCATTTGGAGTCACT
AGAAGTATGTGGGCAGATGATGCTAAGAAGTTATGTCCAGATCTTCTACTGGCACAAGTT
CGTGAGTCCCGTGGGAAAGCTAACCTCACCAAGTACCGGGAAGCCAGTGTTGAAGTGATG
GAGATAATGTCTCGTTTTGCTGTGATTGAACGTGCCAGCATTGATGAGGCTTACGTAGAT
CTGACCAGTGCTGTACAAGAGAGACTACAAAAGCTACAAGGTCAGCCTATCTCGGCAGAC
TTGTTGCCAAGCACTTACATTGAAGGGTTGCCCCAAGGCCCTACAACGGCAGAAGAGACT
GTTCAGAAAGAGGGGATGCGAAAACAAGGCTTATTTCAATGGCTCGATTCTCTTCAGATT
GATAACCTCACCTCTCCAGACCTGCAGCTCACCGTGGGAGCAGTGATTGTGGAGGAAATG
AGAGCAGCCATAGAGAGGGAGACTGGTTTTCAGTGTTCAGCTGGAATTTCACACAATAAG
GTCCTGGCAAAACTGGCCTGTGGACTAAACAAGCCCAACCGCCAAACCCTGGTTTCACAT
GGGTCAGTCCCACAGCTCTTCAGCCAAATGCCCATTCGCAAAATCCGTAGTCTTGGAGGA
AAGCTAGGGGCCTCTGTCATTGAGATCCTAGGGATAGAATACATGGGTGAACTGACCCAG
TTCACTGAATCCCAGCTCCAGAGTCATTTTGGGGAGAAGAATGGGTCTTGGCTATATGCC
ATGTGCCGAGGGATTGAACATGATCCAGTTAAACCCAGGCAACTACCCAAAACCATTGGC
TGTAGTAAGAACTTCCCAGGAAAAACAGCTCTTGCTACTCGGGAACAGGTACAATGGTGG
CTGTTGCAATTAGCCCAGGAACTAGAGGAGAGACTGACTAAAGACCGAAATGATAATGAC
AGGGTAGCCACCCAGCTGGTTGTGAGCATTCGTGTACAAGGAGACAAACGCCTCAGCAGC
CTGCGCCGCTGCTGTGCCCTTACCCGCTATGATGCTCACAAGATGAGCCATGATGCATTT
ACTGTCATCAAGAACTGTAATACTTCTGGAATCCAGACAGAATGGTCTCCTCCTCTCACA
ATGCTTTTCCTCTGTGCTACAAAATTTTCTGCCTCTGCCCCTTCATCTTCTACAGACATC
ACCAGCTTCTTGAGCAGTGACCCAAGTTCTCTGCCAAAGGTGCCAGTTACCAGCTCAGAA
GCTAAGACCCAGGGAAGTGGCCCAGCGGTGACAGCCACTAAGAAAGCAACCACGTCTCTG
GAATCATTCTTCCAAAAAGCTGCAGAAAGGCAGAAAGTTAAAGAAGCTTCGCTTTCATCT
CTTACTGCTCCCACTCAGGCTCCCATGAGCAATTCACCATCCAAGCCCTCATTACCTTTT
CAAACCAGTCAAAGTACAGGAACTGAGCCCTTCTTTAAGCAGAAAAGTCTGCTTCTAAAG
CAGAAACAGCTTAATAATTCTTCAGTTTCTTCCCCCCAACAAAACCCATGGTCCAACTGT
AAAGCATTACCAAACTCTTTACCAACAGAGTATCCAGGGTGTGTCCCTGTTTGTGAAGGG
GTGTCGAAGCTAGAAGAATCCTCTAAAGCAACTCCTGCAGAGATGGATTTGGCCCACAAC
AGCCAAAGCATGCACGCCTCTTCAGCTTCCAAATCTGTGCTGGAGGTGACTCAGAAAGCA
ACCCCAAATCCAAGTCTTCTAGCTGCTGAGGACCAAGTGCCCTGTGAGAAGTGTGGCTCC
CTGGTACCGGTATGGGATATGCCAGAACACATGGACTATCATTTTGCATTGGAGTTGCAG
AAATCCTTTTTGCAGCCCCACTCTTCAAACCCCCAGGTTGTTTCTGCCGTATCTCATCAA
GGCAAAAGAAATCCCAAGAGCCCTTTGGCCTGCACTAATAAACGCCCCAGGCCTGAGGGC
ATGCAAACATTGGAATCATTTTTTAAGCCATTAACACATTAG
|
| Enzyme 10 GenBank Gene ID |
AB024313  |
| Enzyme 10 GeneCard ID |
POLH  |
| Enzyme 10 GenAtlas ID |
POLH  |
| Enzyme 10 HGNC ID |
HGNC:9181  |
| Enzyme 10 Chromosome Location |
6 |
| Enzyme 10 Locus |
6p21.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Masutani C, Kusumoto R, Yamada A, Dohmae N, Yokoi M, Yuasa M, Araki M, Iwai S, Takio K, Hanaoka F: The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase eta. Nature. 1999 Jun 17;399(6737):700-4. [PubMed
]
- Johnson RE, Kondratick CM, Prakash S, Prakash L: hRAD30 mutations in the variant form of xeroderma pigmentosum. Science. 1999 Jul 9;285(5425):263-5. [PubMed
]
- Yuasa M, Masutani C, Eki T, Hanaoka F: Genomic structure, chromosomal localization and identification of mutations in the xeroderma pigmentosum variant (XPV) gene. Oncogene. 2000 Sep 28;19(41):4721-8. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [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
]
- Glick E, Vigna KL, Loeb LA: Mutations in human DNA polymerase eta motif II alter bypass of DNA lesions. EMBO J. 2001 Dec 17;20(24):7303-12. [PubMed
]
- Zeng X, Winter DB, Kasmer C, Kraemer KH, Lehmann AR, Gearhart PJ: DNA polymerase eta is an A-T mutator in somatic hypermutation of immunoglobulin variable genes. Nat Immunol. 2001 Jun;2(6):537-41. [PubMed
]
- Kannouche P, Fernandez de Henestrosa AR, Coull B, Vidal AE, Gray C, Zicha D, Woodgate R, Lehmann AR: Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells. EMBO J. 2003 Mar 3;22(5):1223-33. [PubMed
]
- Haracska L, Prakash L, Prakash S: A mechanism for the exclusion of low-fidelity human Y-family DNA polymerases from base excision repair. Genes Dev. 2003 Nov 15;17(22):2777-85. [PubMed
]
- Glick E, Chau JS, Vigna KL, McCulloch SD, Adman ET, Kunkel TA, Loeb LA: Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta. J Biol Chem. 2003 May 23;278(21):19341-6. Epub 2003 Mar 18. [PubMed
]
- Faili A, Aoufouchi S, Weller S, Vuillier F, Stary A, Sarasin A, Reynaud CA, Weill JC: DNA polymerase eta is involved in hypermutation occurring during immunoglobulin class switch recombination. J Exp Med. 2004 Jan 19;199(2):265-70. [PubMed
]
- Kannouche PL, Wing J, Lehmann AR: Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage. Mol Cell. 2004 May 21;14(4):491-500. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [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
]
- Itoh T, Linn S, Kamide R, Tokushige H, Katori N, Hosaka Y, Yamaizumi M: Xeroderma pigmentosum variant heterozygotes show reduced levels of recovery of replicative DNA synthesis in the presence of caffeine after ultraviolet irradiation. J Invest Dermatol. 2000 Dec;115(6):981-5. [PubMed
]
- Broughton BC, Cordonnier A, Kleijer WJ, Jaspers NG, Fawcett H, Raams A, Garritsen VH, Stary A, Avril MF, Boudsocq F, Masutani C, Hanaoka F, Fuchs RP, Sarasin A, Lehmann AR: Molecular analysis of mutations in DNA polymerase eta in xeroderma pigmentosum-variant patients. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):815-20. Epub 2002 Jan 2. [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 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6246 |
| Enzyme 11 Name |
DNA polymerase delta catalytic subunit |
| Enzyme 11 Synonyms |
- DNA polymerase subunit delta p125
|
| Enzyme 11 Gene Name |
POLD1 |
| Enzyme 11 Protein Sequence |
>DNA polymerase delta catalytic subunit
MDGKRRPGPGPGVPPKRARGGLWDDDDAPRPSQFEEDLALMEEMEAEHRLQEQEEEELQS
VLEGVADGQVPPSAIDPRWLRPTPPALDPQTEPLIFQQLEIDHYVGPAQPVPGGPPPSRG
SVPVLRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGPEHMGDLQRELNLAISRDSRGGR
ELTGPAVLAVELCSRESMFGYHGHGPSPFLRITVALPRLVAPARRLLEQGIRVAGLGTPS
FAPYEANVDFEIRFMVDTDIVGCNWLELPAGKYALRLKEKATQCQLEADVLWSDVVSHPP
EGPWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPC
APILGAKVQSYEKEEDLLQAWSTFIRIMDPDVITGYNIQNFDLPYLISRAQTLKVQTFPF
LGRVAGLCSNIRDSSFQSKQTGRRDTKVVSMVGRVQMDMLQVLLREYKLRSYTLNAVSFH
FLGEQKEDVQHSIITDLQNGNDQTRRRLAVYCLKDAYLPLRLLERLMVLVNAVEMARVTG
VPLSYLLSRGQQVKVVSQLLRQAMHEGLLMPVVKSEGGEDYTGATVIEPLKGYYDVPIAT
LDFSSLYPSIMMAHNLCYTTLLRPGTAQKLGLTEDQFIRTPTGDEFVKTSVRKGLLPQIL
ENLLSARKRAKAELAKETDPLRRQVLDGRQLALKVSANSVYGFTGAQVGKLPCLEISQSV
TGFGRQMIEKTKQLVESKYTVENGYSTSAKVVYGDTDSVMCRFGVSSVAEAMALGREAAD
WVSGHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRPDAHDRMDCKGLEAVRRDNCPLV
ANLVTASLRRLLIDRDPEGAVAHAQDVISDLLCNRIDISQLVITKELTRAASDYAGKQAH
VELAERMRKRDPGSAPSLGDRVPYVIISAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQ
QLAKPLLRIFEPILGEGRAEAVLLRGDHTRCKTVLTGKVGGLLAFAKRRNCCIGCRTVLS
HQGAVCEFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFY
MRKKVRKDLEDQEQLLRRFGPPGPEAW
|
| Enzyme 11 Number of Residues |
1107 |
| Enzyme 11 Molecular Weight |
123629.9 |
| Enzyme 11 Theoretical pI |
7.03 |
| Enzyme 11 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA replication
- cellular macromolecule metabolic process
- cellular nitrogen compound metabolic process
- macromolecule metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in nucleotide binding |
| Enzyme 11 Specific Function |
Possesses two enzymatic activities:DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
21885469  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P28340  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
DPOD1_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>3324 bp
ATGGATGGCAAGCGGCGGCCAGGCCCAGGGCCCGGGGTGCCCCCAAAGCGGGCCCGTGGG
GGCCTCTGGGATGATGATGATGCACCTCGGCCATCCCAATTCGAGGAGGACCTGGCACTG
ATGGAGGAGATGGAGGCAGAACACAGGCTGCAGGAGCAGGAGGAGGAGGAGCTGCAGTCA
GTCCTGGAGGGGGTTGCAGACGGGCAGGTCCCACCATCAGCCATAGATCCTCGCTGGCTT
CGGCCCACACCACCAGCGCTGGACCCCCAGACAGAGCCCCTCATCTTCCAACAGTTGGAG
ATTGACCATTATGTGGGCCCAGCGCAGCCTGTGCCTGGGGGGCCCCCACCATCCCGCGGC
TCCGTGCCTGTGCTCCGCGCCTTCGGGGTCACCGATGAGGGGTTCTCTGTCTGCTGCCAC
ATCCACGGCTTCGCTCCCTACTTCTACACCCCAGCGCCCCCTGGTTTCGGGCCCGAGCAC
ATGGGTGACCTGCAACGGGAGCTGAACTTGGCCATCAGCCGGGACAGTCGCGGGGGGAGG
GAGCTGACTGGGCCGGCCGTGCTGGCTGTGGAACTGTGCTCCCGAGAGAGCATGTTTGGG
TACCACGGGCACGGCCCCTCCCCGTTCCTGCGCATCACCGTGGCGCTGCCGCGCCTCGTG
GCCCCGGCCCGCCGTCTCCTGGAACAGGGCATCCGTGTGGCAGGCCTGGGCACGCCCAGC
TTCGCGCCCTACGAGGCCAACGTCGACTTTGAGATCCGGTTCATGGTGGACACGGACATC
GTCGGCTGCAACTGGCTGGAGCTCCCAGCTGGGAAATACGCCCTGAGGCTGAAGGAGAAG
GCTACGCAGTGCCAGCTGGAGGCGGACGTGCTGTGGTCTGACGTGGTCAGTCACCCACCG
GAAGGGCCATGGCAGCGCATTGCGCCCTTGCGCGTGCTCAGCTTCGATATCGAGTGCGCC
GGCCGCAAAGGCATCTTCCCTGAGCCTGAGCGGGACCCTGTCATCCAGATCTGCTCGCTG
GGCCTGCGCTGGGGGGAGCCGGAGCCCTTCCTACGCCTGGCGCTCACCCTGCGGCCCTGT
GCCCCCATCCTGGGTGCCAAGGTGCAGAGCTACGAGAAGGAGGAGGACCTGCTGCAGGCC
TGGTCCACCTTCATCCGTATCATGGACCCCGACGTGATCACCGGTTACAACATCCAGAAC
TTCGACCTTCCGTACCTCATCTCTCGGGCCCAGACCCTCAAGGTACAAACATTCCCTTTC
CTGGGCCGTGTGGCCGGCCTTTGCTCCAACATCCGGGACTCTTCATTCCAGTCCAAGCAG
ACGGGCCGGCGGGACACCAAGGTTGTCAGCATGGTGGGCCGCGTGCAGATGGACATGCTG
CAGGTGCTGCTGCGGGAGTACAAGCTCCGCTCCTACACGCTCAATGCCGTGAGCTTCCAC
TTCCTGGGCGAGCAGAAGGAGGACGTGCAGCACAGCATCATCACCGACCTGCAGAATGGG
AACGACCAGACCCGCCGCCGCCTGGCTGTGTACTGCCTGAAGGATGCCTACCTGCCACTG
CGGCTGCTGGAGCGGCTCATGGTGCTGGTGAACGCCGTGGAGATGGCGAGGGTCACTGGC
GTGCCCCTCAGCTACCTGCTCAGTCGTGGCCAGCAGGTCAAGGTCGTATCCCAGCTGTTG
CGGCAGGCCATGCACGAGGGGCTGCTGATGCCCGTGGTGAAGTCAGAGGGCGGCGAGGAC
TACACGGGAGCCACTGTCATCGAGCCCCTCAAAGGGTACTACGACGTCCCCATCGCCACC
CTGGACTTCTCCTCGCTGTACCCGTCCATCATGATGGCCCACAACCTGTGTTACACCACG
CTCCTTCGGCCCGGGACTGCACAGAAACTGGGCCTGACTGAGGATCAGTTCATCAGGACC
CCCACCGGGGACGAGTTTGTGAAGACCTCAGTGCGGAAGGGGCTGCTGCCCCAGATCCTG
GAGAACCTGCTCAGTGCCCGGAAGAGGGCCAAGGCCGAGCTGGCCAAGGAGACAGACCCC
CTCCGGCGCCAGGTCCTGGATGGACGGCAGCTGGCGCTGAAGGTGAGCGCCAACTCCGTA
TACGGCTTCACTGGCGCCCAGGTGGGCAAGTTGCCGTGCCTGGAGATCTCACAGAGCGTC
ACGGGGTTCGGACGTCAGATGATCGAGAAAACCAAGCAGCTGGTGGAGTCTAAGTACACA
GTGGAGAATGGCTACAGCACCAGTGCCAAGGTGGTGTATGGTGACACTGACTCCGTCATG
TGCCGATTCGGCGTGTCCTCGGTGGCTGAGGCGATGGCCCTGGGGCGGGAGGCCGCGGAC
TGGGTGTCAGGTCACTTCCCGTCGCCCATCCGGCTGGAGTTTGAGAAGGTCTACTTCCCA
TACCTGCTTATCAGCAAGAAGCGCTACGCGGGCCTGCTCTTCTCCTCCCGGCCCGACGCC
CACGACCGCATGGACTGCAAGGGCCTGGAGGCCGTGCGCAGGGACAACTGCCCCCTCGTG
GCCAACCTGGTCACTGCCTCACTGCGCCGCCTGCTCATCGACCGAGACCCTGAGGGCGCG
GTGGCTCACGCACAGGACGTCATCTCGGACCTGCTGTGCAACCGCATCGATATCTCCCAG
CTGGTCATCACCAAGGAGCTGACCCGCGCGGCCTCCGACTATGCCGGCAAGCAGGCCCAC
GTGGAGCTGGCCGAGAGGATGAGGAAGCGGGACCCCGGGAGTGCGCCCAGCCTGGGCGAC
CGCGTCCCCTACGTGATCATCAGTGCCGCCAAGGGTGTGGCCGCCTACATGAAGTCGGAG
GACCCGCTGTTCGTGCTGGAGCACAGCCTGCCCATTGACACGCAGTACTACCTGGAGCAG
CAGCTGGCCAAGCCCCTCCTGCGCATCTTCGAGCCCATCCTGGGCGAGGGCCGTGCCGAG
GCTGTGCTACTGCGGGGGGACCACACGCGCTGCAAGACGGTGCTCACGGGCAAGGTGGGC
GGCCTCCTGGCCTTCGCCAAACGCCGCAACTGCTGCATTGGCTGCCGCACAGTGCTCAGC
CACCAGGGAGCCGTGTGTGAGTTCTGCCAGCCCCGGGAGTCTGAGCTGTATCAGAAGGAG
GTATCCCATCTGAATGCCCTGGAGGAGCGCTTCTCGCGCCTCTGGACGCAGTGCCAGCGC
TGCCAGGGCAGCCTGCACGAGGACGTCATCTGCACCAGCCGGGACTGCCCCATCTTCTAC
ATGCGCAAGAAGGTGCGGAAGGACCTGGAAGACCAGGAGCAGCTCCTGCGGCGCTTCGGA
CCCCCTGGACCTGAGGCCTGGTGA
|
| Enzyme 11 GenBank Gene ID |
AY129569  |
| Enzyme 11 GeneCard ID |
POLD1  |
| Enzyme 11 GenAtlas ID |
POLD1  |
| Enzyme 11 HGNC ID |
HGNC:9175  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
19q13.3 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Chung DW, Zhang JA, Tan CK, Davie EW, So AG, Downey KM: Primary structure of the catalytic subunit of human DNA polymerase delta and chromosomal location of the gene. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11197-201. [PubMed
]
- Yang CL, Chang LS, Zhang P, Hao H, Zhu L, Toomey NL, Lee MY: Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase delta. Nucleic Acids Res. 1992 Feb 25;20(4):735-45. [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
]
- Tsurimoto T, Shinozaki A, Yano M, Seki M, Enomoto T: Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel modulator for DNA polymerase delta. Genes Cells. 2005 Jan;10(1):13-22. [PubMed
]
- Li H, Xie B, Zhou Y, Rahmeh A, Trusa S, Zhang S, Gao Y, Lee EY, Lee MY: Functional roles of p12, the fourth subunit of human DNA polymerase delta. J Biol Chem. 2006 May 26;281(21):14748-55. Epub 2006 Feb 28. [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
]
- 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 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6247 |
| Enzyme 12 Name |
DNA polymerase zeta catalytic subunit |
| Enzyme 12 Synonyms |
- Protein reversionless 3-like
- REV3-like
- hREV3
|
| Enzyme 12 Gene Name |
REV3L |
| Enzyme 12 Protein Sequence |
>DNA polymerase zeta catalytic subunit
MFSVRIVTADYYMASPLQGLDTCQSPLTQAPVKKVPVVRVFGATPAGQKTCLHLHGIFPY
LYVPYDGYGQQPESYLSQMAFSIDRALNVALGNPSSTAQHVFKVSLVSGMPFYGYHEKER
HFMKIYLYNPTMVKRICELLQSGAIMNKFYQPHEAHIPYLLQLFIDYNLYGMNLINLAAV
KFRKARRKSNTLHATGSCKNHLSGNSLADTLFRWEQDEIPSSLILEGVEPQSTCELEVDA
VAADILNRLDIEAQIGGNPGLQAIWEDEKQRRRNRNETSQMSQPESQDHRFVPATESEKK
FQKRLQEILKQNDFSVTLSGSVDYSDGSQEFSAELTLHSEVLSPEMLQCTPANMVEVHKD
KESSKGHTRHKVEEALINEEAILNLMENSQTFQPLTQRLSESPVFMDSSPDEALVHLLAG
LESDGYRGERNRMPSPCRSFGNNKYPQNSDDEENEPQIEKEEMELSLVMSQRWDSNIEEH
CAKKRSLCRNTHRSSTEDDDSSSGEEMEWSDNSLLLASLSIPQLDGTADENSDNPLNNEN
SRTHSSVIATSKLSVKPSIFHKDAATLEPSSSAKITFQCKHTSALSSHVLNKEDLIEDLS
QTNKNTEKGLDNSVTSFTNESTYSMKYPGSLSSTVHSENSHKENSKKEILPVSSCESSIF
DYEEDIPSVTRQVPSRKYTNIRKIEKDSPFIHMHRHPNENTLGKNSFNFSDLNHSKNKVS
SEGNEKGNSTALSSLFPSSFTENCELLSCSGENRTMVHSLNSTADESGLNKLKIRYEEFQ
EHKTEKPSLSQQAAHYMFFPSVVLSNCLTRPQKLSPVTYKLQPGNKPSRLKLNKRKLAGH
QETSTKSSETGSTKDNFIQNNPCNSNPEKDNALASDLTKTTRGAFENKTPTDGFIDCHFG
DGTLETEQSFGLYGNKYTLRAKRKVNYETEDSESSFVTHNSKISLPHPMEIGESLDGTLK
SRKRRKMSKKLPPVIIKYIIINRFRGRKNMLVKLGKIDSKEKQVILTEEKMELYKKLAPL
KDFWPKVPDSPATKYPIYPLTPKKSHRRKSKHKSAKKKTGKQQRTNNENIKRTLSFRKKR
SHAILSPPSPSYNAETEDCDLNYSDVMSKLGFLSERSTSPINSSPPRCWSPTDPRAEEIM
AAAEKEAMLFKGPNVYKKTVNSRIGKTSRARAQIKKSKAKLANPSIVTKKRNKRNQTNKL
VDDGKKKPRAKQKTNEKGTSRKHTTLKDEKIKSQSGAEVKFVLKHQNVSEFASSSGGSQL
LFKQKDMPLMGSAVDHPLSASLPTGINAQQKLSGCFSSFLESKKSVDLQTFPSSRDDLHP
SVVCNSIGPGVSKINVQRPHNQSAMFTLKESTLIQKNIFDLSNHLSQVAQNTQISSGMSS
KIEDNANNIQRNYLSSIGKLSEYRNSLESKLDQAYTPNFLHCKDSQQQIVCIAEQSKHSE
TCSPGNTASEESQMPNNCFVTSLRSPIKQIAWEQKQRGFILDMSNFKPERVKPRSLSEAI
SQTKALSQCKNRNVSTPSAFGEGQSGLAVLKELLQKRQQKAQNANTTQDPLSNKHQPNKN
ISGSLEHNKANKRTRSVTSPRKPRTPRSTKQKEKIPKLLKVDSLNLQNSSQLDNSVSDDS
PIFFSDPGFESCYSLEDSLSPEHNYNFDINTIGQTGFCSFYSGSQFVPADQNLPQKFLSD
AVQDLFPGQAIEKNEFLSHDNQKCDEDKHHTTDSASWIRSGTLSPEIFEKSTIDSNENRR
HNQWKNSFHPLTTRSNSIMDSFCVQQAEDCLSEKSRLNRSSVSKEVFLSLPQPNNSDWIQ
GHTRKEMGQSLDSANTSFTAILSSPDGELVDVACEDLELYVSRNNDMLTPTPDSSPRSTS
SPSQSKNGSFTPRTANILKPLMSPPSREEIMATLLDHDLSETIYQEPFCSNPSDVPEKPR
EIGGRLLMVETRLANDLAEFEGDFSLEGLRLWKTAFSAMTQNPRPGSPLRSGQGVVNKGS
SNSPKMVEDKKIVIMPCKCAPSRQLVQVWLQAKEEYERSKKLPKTKPTGVVKSAENFSSS
VNPDDKPVVPPKMDVSPCILPTTAHTKEDVDNSQIALQAPTTGCSQTASESQMLPPVASA
SDPEKDEDDDDNYYISYSSPDSPVIPPWQQPISPDSKALNGDDRPSSPVEELPSLAFENF
LKPIKDGIQKSPCSEPQEPLVISPINTRARTGKCESLCFHSTPIIQRKLLERLPEAPGLS
PLSTEPKTQKLSNKKGSNTDTLRRVLLTQAKNQFAAVNTPQKETSQIDGPSLNNTYGFKV
SIQNLQEAKALHEIQNLTLISVELHARTRRDLEPDPEFDPICALFYCISSDTPLPDTEKT
ELTGVIVIDKDKTVFSQDIRYQTPLLIRSGITGLEVTYAADEKALFHEIANIIKRYDPDI
LLGYEIQMHSWGYLLQRAAALSIDLCRMISRVPDDKIENRFAAERDEYGSYTMSEINIVG
RITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWKMVDHY
VSRVRGNLQMLEQLDLIGKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAKPMNYIPVT
PSVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHVENL
GKYDEFKFGCTSLRVPPDLLYQVRHDITVSPNGVAFVKPSVRKGVLPRMLEEILKTRFMV
KQSMKAYKQDRALSRMLDARQLGLKLIANVTFGYTSANFSGRMPCIEVGDSIVHKARETL
ERAIKLVNDTKKWGARVVYGDTDSMFVLLKGATKEQSFKIGQEIAEAVTATNPKPVKLKF
EKVYLPCVLQTKKRYVGYMYETLDQKDPVFDAKGIETVRRDSCPAVSKILERSLKLLFET
RDISLIKQYVQRQCMKLLEGKASIQDFIFAKEYRGSFSYKPGACVPALELTRKMLTYDRR
SEPQVGERVPYVIIYGTPGVPLIQLVRRPVEVLQDPTLRLNATYYITKQILPPLARIFSL
IGIDVFSWYHELPRIHKATSSSRSEPEGRKGTISQYFTTLHCPVCDDLTQHGICSKCRSQ
PQHVAVILNQEIRELERQQEQLVKICKNCTGCFDRHIPCVSLNCPVLFKLSRVNRELSKA
PYLRQLLDQF
|
| Enzyme 12 Number of Residues |
3130 |
| Enzyme 12 Molecular Weight |
352772.6 |
| Enzyme 12 Theoretical pI |
8.61 |
| Enzyme 12 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA replication
- cellular macromolecule metabolic process
- cellular nitrogen compound metabolic process
- macromolecule metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in nucleotide binding |
| Enzyme 12 Specific Function |
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1) |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
153792012  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
O60673  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
DPOLZ_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>9393 bp
ATGTTTTCAGTAAGGATAGTGACTGCAGACTACTACATGGCCAGCCCGCTGCAGGGGCTG
GATACCTGCCAATCCCCCCTCACCCAGGCCCCTGTCAAGAAGGTGCCGGTGGTGCGAGTC
TTCGGAGCGACCCCGGCAGGTCAGAAGACATGTCTTCATCTACATGGCATCTTTCCTTAC
CTCTATGTGCCATACGATGGTTATGGACAGCAGCCAGAAAGCTATCTTTCTCAGATGGCA
TTCAGTATCGACAGAGCACTTAATGTGGCTTTAGGCAATCCATCTTCCACTGCTCAGCAT
GTGTTCAAAGTGTCATTAGTATCAGGAATGCCTTTTTATGGTTATCATGAGAAGGAAAGA
CACTTTATGAAGATCTATCTTTACAATCCTACAATGGTGAAAAGGATATGTGAACTTTTG
CAAAGCGGAGCCATAATGAATAAATTTTACCAGCCTCATGAAGCGCATATTCCCTACCTC
CTACAGCTCTTCATTGACTACAATCTTTATGGCATGAATTTAATAAATCTGGCTGCTGTC
AAGTTCCGAAAAGCAAGAAGGAAAAGTAATACATTGCATGCAACTGGATCCTGCAAGAAT
CATTTATCAGGAAATTCTCTTGCTGATACTTTATTTCGGTGGGAACAAGATGAAATACCA
AGCTCTTTAATATTGGAAGGTGTTGAACCACAGAGTACATGTGAATTAGAAGTGGATGCT
GTAGCTGCTGATATCTTAAATCGTCTGGACATTGAAGCTCAAATTGGTGGAAACCCTGGT
CTACAGGCCATATGGGAAGATGAAAAGCAACGGCGAAGAAACAGAAATGAAACTTCTCAA
ATGAGCCAACCTGAGTCACAAGATCACAGGTTTGTGCCAGCAACAGAAAGTGAAAAAAAA
TTTCAGAAGAGACTTCAGGAAATTCTCAAACAGAATGATTTCTCTGTAACATTATCAGGA
TCTGTGGACTACAGCGATGGATCCCAGGAGTTCTCTGCTGAGTTAACATTGCACTCTGAG
GTTCTGTCTCCTGAAATGCTTCAGTGTACACCAGCCAATATGGTAGAAGTTCACAAAGAC
AAAGAGTCAAGCAAAGGTCACACTAGACACAAAGTGGAAGAAGCTCTTATTAATGAAGAA
GCAATTTTGAACCTTATGGAAAATAGTCAGACTTTTCAGCCTTTGACCCAAAGACTGAGT
GAGTCACCTGTTTTCATGGACAGTAGTCCTGATGAGGCTCTGGTACATCTTCTTGCTGGT
TTGGAAAGTGATGGATATCGGGGGGAAAGAAATAGGATGCCATCACCATGTCGCTCCTTT
GGAAATAATAAATATCCACAAAATAGTGATGATGAAGAAAATGAACCACAGATTGAAAAA
GAGGAAATGGAGCTTAGTTTGGTGATGTCCCAGAGATGGGACAGCAATATTGAAGAACAT
TGTGCCAAAAAGAGATCACTGTGCAGAAATACCCACAGAAGTTCAACTGAAGATGATGAC
TCATCTTCAGGAGAAGAAATGGAATGGAGTGATAACAGTTTGCTTCTAGCCAGTCTTTCT
ATACCTCAGTTAGATGGAACTGCAGATGAAAATAGTGACAATCCATTGAACAATGAAAAT
TCTAGAACCCACTCTTCTGTAATTGCAACAAGCAAGCTTTCAGTTAAACCCTCCATCTTT
CACAAAGATGCTGCTACATTAGAACCCTCATCTTCTGCTAAGATTACCTTTCAGTGTAAA
CACACAAGTGCCCTTTCTTCCCATGTTTTGAACAAGGAAGATTTAATTGAAGACCTTTCA
CAGACAAACAAAAATACAGAAAAAGGTCTAGATAACTCAGTCACTTCTTTTACAAACGAA
AGCACTTATTCTATGAAATACCCTGGATCTTTAAGCAGTACTGTTCATTCAGAAAATTCT
CATAAAGAGAATAGTAAGAAAGAGATCCTCCCAGTATCTTCCTGTGAAAGTAGTATTTTT
GATTATGAAGAAGATATTCCATCTGTTACAAGACAAGTACCAAGTAGAAAATATACAAAC
ATTAGAAAAATCGAAAAGGATTCCCCTTTTATACATATGCACCGTCACCCTAACGAGAAT
ACATTGGGCAAAAATTCTTTCAACTTTTCTGACTTAAATCATTCAAAAAATAAAGTATCC
TCTGAAGGAAATGAAAAAGGAAACAGCACAGCTCTGAGTAGTTTATTCCCTTCATCATTT
ACTGAAAATTGTGAATTACTGTCATGCTCAGGGGAGAATAGAACTATGGTGCATTCTCTT
AATAGCACTGCTGATGAAAGTGGACTAAATAAACTTAAAATTAGGTATGAAGAATTTCAA
GAACATAAAACAGAAAAGCCAAGCCTCAGCCAGCAAGCAGCACACTATATGTTTTTTCCC
AGTGTTGTTCTTTCTAACTGTCTTACTAGACCACAGAAACTATCTCCTGTCACATATAAA
TTACAACCTGGCAATAAACCATCCCGGTTAAAATTGAATAAAAGGAAACTTGCAGGTCAT
CAGGAGACTTCTACCAAAAGTAGTGAGACTGGATCCACAAAAGATAATTTTATACAAAAT
AATCCTTGTAATAGTAATCCTGAGAAGGATAATGCATTGGCTAGTGATTTAACTAAAACC
ACTCGTGGAGCTTTTGAAAATAAAACACCCACAGATGGTTTTATAGACTGTCACTTTGGA
GATGGAACGTTAGAAACTGAGCAGTCCTTTGGACTATATGGAAATAAATACACACTTAGA
GCCAAACGCAAGGTAAATTATGAGACTGAAGACAGTGAGTCAAGTTTTGTAACTCACAAC
TCAAAAATTAGTCTACCTCATCCCATGGAAATTGGTGAAAGTTTAGATGGAACTCTCAAA
TCCCGAAAACGAAGAAAAATGTCTAAAAAGCTGCCCCCTGTCATCATAAAGTATATTATT
ATTAATAGATTTAGAGGGAGAAAAAATATGCTTGTGAAGCTAGGAAAAATAGACTCTAAA
GAAAAACAAGTAATATTAACAGAAGAAAAAATGGAACTATATAAAAAGCTTGCACCTTTG
AAGGACTTTTGGCCAAAAGTTCCCGACTCCCCTGCAACCAAATATCCCATTTATCCACTA
ACACCAAAGAAAAGTCACAGAAGAAAGTCAAAACATAAATCTGCTAAGAAAAAAACTGGT
AAACAACAAAGGACAAATAATGAAAATATTAAAAGAACTTTGTCTTTCAGGAAAAAACGG
TCACATGCTATTCTTTCTCCTCCCTCACCATCTTACAATGCTGAAACCGAAGATTGTGAC
CTGAATTATAGTGATGTTATGTCTAAACTAGGTTTTCTTTCTGAGAGAAGCACAAGTCCC
ATAAATTCTTCTCCACCTCGCTGCTGGTCTCCCACAGATCCAAGAGCTGAAGAAATCATG
GCTGCTGCAGAAAAAGAGGCAATGCTTTTTAAGGGTCCTAATGTATATAAGAAGACTGTT
AATTCTCGTATAGGAAAAACTAGTCGCGCAAGAGCACAGATTAAGAAATCAAAAGCAAAG
CTTGCTAATCCCTCTATAGTTACTAAGAAAAGGAACAAACGAAATCAGACAAATAAACTA
GTAGATGATGGAAAAAAGAAACCAAGAGCAAAACAAAAAACAAATGAGAAAGGTACATCG
AGAAAGCATACAACACTTAAGGATGAAAAAATAAAATCTCAGTCTGGTGCTGAGGTTAAG
TTTGTACTGAAACACCAGAATGTGTCTGAATTTGCAAGTAGTTCTGGAGGCTCTCAACTA
CTTTTTAAACAGAAAGATATGCCACTAATGGGCTCTGCTGTAGATCATCCCCTTTCTGCT
TCCCTACCCACTGGAATTAATGCACAACAGAAGTTATCTGGCTGCTTTTCTTCTTTCTTA
GAAAGCAAGAAGTCTGTAGATTTGCAGACATTCCCCAGTTCACGAGATGATTTGCATCCA
TCAGTTGTTTGTAATTCTATAGGACCTGGAGTCTCAAAAATTAATGTTCAAAGGCCTCAT
AATCAAAGTGCTATGTTTACTCTAAAGGAATCAACGTTAATTCAAAAAAATATATTTGAC
CTTTCCAATCATTTATCTCAGGTAGCACAGAATACACAGATATCTTCTGGTATGTCCTCA
AAGATAGAAGATAATGCAAATAATATACAAAGAAACTATTTGTCATCAATCGGAAAGTTA
AGTGAATATCGCAATTCCCTAGAATCAAAGCTGGACCAAGCATATACCCCTAATTTTTTG
CATTGCAAAGACAGTCAGCAGCAGATTGTGTGCATAGCGGAACAGTCAAAGCACAGTGAA
ACTTGTTCTCCGGGAAATACAGCTTCAGAGGAAAGCCAAATGCCTAATAATTGCTTTGTA
ACTTCCTTGAGAAGTCCAATCAAACAAATAGCATGGGAGCAAAAGCAAAGGGGCTTTATT
TTAGATATGTCAAATTTTAAACCTGAAAGAGTAAAACCGAGGTCGTTATCAGAAGCAATT
TCACAAACCAAAGCACTTTCTCAGTGTAAAAATCGAAATGTGTCAACACCTTCAGCATTT
GGTGAAGGACAGTCTGGACTGGCAGTTCTAAAAGAATTGTTACAAAAAAGACAGCAGAAA
GCACAAAATGCAAATACTACACAAGACCCATTATCCAATAAACATCAACCAAATAAAAAT
ATTTCTGGTTCCCTTGAGCATAACAAAGCAAATAAACGGACACGATCGGTAACGTCCCCA
AGAAAACCTCGAACTCCCAGAAGTACAAAACAAAAAGAAAAAATCCCCAAACTTCTCAAA
GTAGACTCTTTAAATTTACAAAACTCTAGCCAGTTGGATAACTCTGTATCAGATGATAGT
CCCATCTTTTTTTCAGATCCAGGCTTTGAAAGTTGTTACTCACTTGAAGATAGTTTATCT
CCTGAACATAATTATAATTTTGATATTAACACAATAGGTCAGACTGGATTTTGTAGCTTT
TATTCTGGAAGTCAGTTTGTCCCAGCTGATCAGAATTTGCCTCAGAAGTTCCTAAGTGAT
GCTGTTCAGGATCTTTTTCCAGGACAAGCTATAGAAAAAAATGAGTTTTTAAGTCATGAC
AACCAGAAATGTGATGAAGACAAGCATCATACCACAGACTCAGCCTCATGGATTAGATCT
GGTACTTTAAGTCCTGAAATTTTTGAGAAGTCAACCATAGATAGCAATGAGAATCGTCGC
CACAACCAGTGGAAAAATAGCTTTCATCCTCTAACAACTCGGTCTAACTCAATAATGGAT
TCTTTCTGTGTTCAGCAGGCAGAAGACTGTCTAAGTGAAAAATCTAGATTGAATAGGAGT
TCAGTAAGCAAAGAAGTGTTTCTTAGCCTCCCACAGCCAAACAATTCAGACTGGATTCAA
GGTCACACCAGAAAAGAAATGGGACAGTCTCTTGACTCAGCCAATACCTCTTTTACTGCA
ATACTCTCCTCCCCTGATGGTGAACTTGTAGACGTGGCCTGTGAAGATTTAGAACTGTAT
GTTTCAAGAAACAATGATATGTTGACACCAACTCCTGATAGTTCACCAAGATCTACTAGC
TCTCCTTCACAATCTAAAAATGGCAGCTTCACCCCTCGAACTGCTAACATTCTGAAACCA
CTTATGTCCCCCCCAAGTAGGGAAGAAATTATGGCAACTTTGTTGGATCATGACCTGTCT
GAGACTATTTACCAGGAACCATTTTGCAGTAATCCTTCTGATGTACCAGAAAAGCCCAGG
GAGATTGGTGGACGGCTCCTCATGGTAGAAACTCGACTTGCAAATGATCTGGCTGAGTTT
GAGGGAGACTTTTCCTTGGAAGGACTTCGTCTTTGGAAAACAGCATTCTCAGCAATGACT
CAGAATCCAAGGCCAGGGTCACCCCTTCGCAGTGGCCAAGGAGTTGTCAATAAAGGGTCA
AGTAATAGCCCTAAGATGGTTGAAGATAAAAAAATTGTGATTATGCCTTGCAAATGTGCC
CCAAGTCGACAACTGGTTCAAGTGTGGCTTCAAGCCAAAGAAGAATACGAACGTTCCAAG
AAACTGCCTAAAACCAAGCCAACTGGAGTTGTAAAATCTGCTGAGAACTTTAGCTCTTCA
GTTAACCCAGATGACAAACCTGTAGTGCCTCCAAAAATGGATGTAAGTCCATGTATACTC
CCCACTACAGCACATACCAAGGAGGATGTTGATAATTCTCAGATTGCTTTACAAGCACCA
ACCACGGGATGTAGTCAAACTGCAAGTGAAAGTCAGATGCTGCCACCAGTTGCCTCTGCA
AGTGATCCCGAAAAAGATGAAGATGATGATGATAACTATTACATTAGTTATAGCTCCCCT
GATTCTCCAGTAATTCCCCCTTGGCAACAACCAATATCCCCAGATTCCAAAGCATTAAAT
GGAGATGATAGACCCTCATCACCAGTAGAGGAGCTGCCTTCATTGGCTTTTGAGAACTTC
TTAAAGCCAATAAAAGATGGTATACAAAAAAGCCCCTGCAGTGAGCCTCAAGAGCCTCTA
GTGATATCTCCAATTAATACTAGGGCAAGAACTGGGAAATGTGAATCACTTTGCTTTCAT
AGTACACCAATCATACAGAGAAAACTTCTGGAAAGGCTTCCTGAAGCACCTGGCCTTAGC
CCATTATCAACAGAACCAAAAACACAGAAGTTGAGTAATAAGAAAGGAAGTAATACTGAC
ACTCTTAGAAGAGTACTGTTAACACAAGCAAAGAATCAATTTGCAGCAGTAAATACCCCA
CAGAAAGAAACTTCTCAGATTGATGGACCATCTTTAAACAATACTTACGGTTTCAAAGTC
AGCATACAAAACTTACAGGAGGCAAAAGCTTTACATGAGATACAAAATCTTACCCTAATC
AGTGTGGAGTTGCATGCTCGAACTAGACGAGACTTAGAACCGGATCCTGAATTTGACCCA
ATCTGTGCTCTGTTCTACTGCATCTCATCTGACACTCCACTGCCAGATACAGAAAAAACA
GAACTCACAGGTGTAATAGTGATTGATAAAGACAAGACAGTTTTCAGTCAAGATATCAGA
TATCAGACTCCATTACTTATTAGATCTGGAATTACAGGACTCGAAGTCACCTATGCTGCT
GATGAGAAGGCACTTTTTCATGAAATTGCAAATATAATAAAGAGGTATGATCCTGATATT
CTGCTAGGATATGAGATTCAGATGCATTCCTGGGGTTACCTCTTACAAAGGGCTGCCGCT
TTAAGTATTGACTTATGTCGGATGATCTCTCGGGTGCCAGATGACAAAATTGAGAACAGA
TTTGCAGCTGAAAGAGATGAGTATGGATCATATACAATGAGTGAGATAAATATTGTTGGC
CGAATTACACTAAATCTTTGGAGAATCATGAGAAATGAGGTGGCTCTAACTAACTACACC
TTTGAAAATGTGAGCTTTCATGTTCTTCATCAGCGTTTTCCCCTCTTTACCTTTCGAGTC
TTGTCAGACTGGTTTGATAACAAGACAGATCTATACAGATGGAAAATGGTTGATCATTAT
GTTAGCCGTGTCCGTGGAAATCTCCAAATGTTAGAACAGCTGGACCTGATTGGGAAAACC
AGTGAGATGGCTAGACTTTTTGGCATTCAGTTTTTACATGTACTGACAAGGGGTTCACAG
TACCGTGTGGAATCAATGATGTTGCGTATTGCTAAACCAATGAACTATATTCCTGTGACA
CCTAGTGTTCAGCAAAGATCCCAGATGAGAGCCCCACAGTGTGTTCCTCTAATTATGGAG
CCTGAATCCCGCTTCTATAGCAACTCTGTTCTCGTTTTGGATTTCCAATCACTTTATCCT
TCTATTGTGATTGCATATAACTACTGCTTTTCCACCTGCCTTGGCCATGTGGAGAACTTG
GGAAAGTATGATGAGTTCAAATTTGGCTGTACCTCTCTGAGAGTACCTCCAGATTTACTT
TACCAAGTTAGGCATGATATCACAGTGTCCCCCAATGGAGTAGCTTTTGTCAAGCCTTCA
GTAAGAAAAGGTGTACTACCAAGAATGCTTGAAGAAATTTTGAAGACTAGATTTATGGTG
AAGCAGTCAATGAAGGCTTACAAGCAAGACAGAGCCCTGTCACGAATGCTTGATGCGCGT
CAGTTGGGACTTAAGCTGATAGCAAATGTCACATTTGGCTATACATCTGCTAATTTTTCT
GGGAGAATGCCATGCATTGAGGTTGGCGATAGTATTGTTCACAAAGCCAGAGAGACCTTG
GAACGAGCTATTAAACTGGTGAATGATACCAAGAAATGGGGGGCTAGGGTTGTATATGGC
GATACTGACAGTATGTTTGTGCTACTGAAAGGAGCCACTAAGGAGCAGTCTTTTAAGATT
GGTCAGGAAATTGCCGAAGCTGTAACTGCTACCAATCCTAAACCAGTGAAATTGAAGTTT
GAAAAGGTATATTTGCCCTGTGTTTTACAAACAAAAAAGAGGTATGTGGGTTACATGTAT
GAAACACTGGATCAGAAGGACCCAGTATTTGATGCAAAAGGAATAGAAACAGTCAGAAGA
GATTCCTGCCCTGCTGTTTCTAAGATACTTGAGCGTTCTCTAAAGCTGCTATTTGAAACG
AGAGATATAAGTCTAATTAAACAGTATGTTCAGCGACAATGTATGAAGCTTCTGGAAGGA
AAGGCCAGCATACAAGACTTTATCTTTGCCAAGGAATACAGAGGAAGTTTTTCTTATAAA
CCAGGAGCTTGTGTGCCAGCCCTTGAACTTACAAGGAAAATGCTGACTTATGACCGGCGC
TCTGAGCCTCAGGTTGGGGAGCGAGTGCCATACGTCATCATTTATGGGACCCCCGGAGTA
CCACTTATCCAGCTTGTAAGGCGCCCAGTGGAAGTCCTGCAGGACCCAACTCTGAGACTG
AATGCTACTTACTATATTACCAAGCAAATCCTTCCACCCTTGGCAAGAATCTTCTCACTT
ATTGGTATTGATGTCTTCAGCTGGTATCATGAATTACCAAGGATCCATAAAGCTACCAGC
TCCTCGCGAAGTGAACCTGAAGGGCGGAAAGGCACTATTTCACAATATTTTACTACCTTA
CACTGTCCTGTGTGTGATGACCTAACTCAGCATGGCATCTGTAGTAAATGTCGGAGCCAA
CCTCAGCATGTTGCAGTCATCCTCAACCAAGAAATCCGGGAGTTGGAACGTCAACAGGAG
CAACTTGTAAAGATATGCAAGAACTGTACAGGTTGCTTTGATCGACACATCCCATGTGTT
TCTCTGAACTGCCCAGTACTTTTCAAACTCTCCCGAGTAAATAGAGAATTGTCCAAGGCA
CCATATCTCCGGCAGTTATTAGACCAGTTTTAA
|
| Enzyme 12 GenBank Gene ID |
NM_002912.3  |
| Enzyme 12 GeneCard ID |
REV3L  |
| Enzyme 12 GenAtlas ID |
REV3L  |
| Enzyme 12 HGNC ID |
HGNC:9968  |
| Enzyme 12 Chromosome Location |
6 |
| Enzyme 12 Locus |
6q21 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Gibbs PE, McGregor WG, Maher VM, Nisson P, Lawrence CW: A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase zeta. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6876-80. [PubMed
]
- Lin W, Wu X, Wang Z: A full-length cDNA of hREV3 is predicted to encode DNA polymerase zeta for damage-induced mutagenesis in humans. Mutat Res. 1999 Mar 10;433(2):89-98. [PubMed
]
- Morelli C, Mungall AJ, Negrini M, Barbanti-Brodano G, Croce CM: Alternative splicing, genomic structure, and fine chromosome localization of REV3L. Cytogenet Cell Genet. 1998;83(1-2):18-20. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Murakumo Y, Roth T, Ishii H, Rasio D, Numata S, Croce CM, Fishel R: A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2. J Biol Chem. 2000 Feb 11;275(6):4391-7. [PubMed
]
- Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R: Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. Nat Methods. 2005 Aug;2(8):591-8. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [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
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6249 |
| Enzyme 13 Name |
DNA polymerase epsilon catalytic subunit A |
| Enzyme 13 Synonyms |
- DNA polymerase II subunit A
|
| Enzyme 13 Gene Name |
POLE |
| Enzyme 13 Protein Sequence |
>DNA polymerase epsilon catalytic subunit A
MSLRSGGRRRADPGADGEASRDDGATSSVSALKRLERSQWTDKMDLRFGFERLKEPGEKT
GWLINMHPTEILDEDKRLGSAVDYYFIQDDGSRFKVALPYKPYFYIATRKGCEREVSSFL
SKKFQGKIAKVETVPKEDLDLPNHLVGLKRNYIRLSFHTVEDLVKVRKEISPAVKKNREQ
DHASDAYTALLSSVLQRGGVITDEEETSKKIADQLDNIVDMREYDVPYHIRLSIDLKIHV
AHWYNVRYRGNAFPVEITRRDDLVERPDPVVLAFDIETTKLPLKFPDAETDQIMMISYMI
DGQGYLITNREIVSEDIEDFEFTPKPEYEGPFCVFNEPDEAHLIQRWFEHVQETKPTIMV
TYNGDFFDWPFVEARAAVHGLSMQQEIGFQKDSQGEYKAPQCIHMDCLRWVKRDSYLPVG
SHNLKAAAKAKLGYDPVELDPEDMCRMATEQPQTLATYSVSDAVATYYLYMKYVHPFIFA
LCTIIPMEPDEVLRKGSGTLCEALLMVQAFHANIIFPNKQEQEFNKLTDDGHVLDSETYV
GGHVEALESGVFRSDIPCRFRMNPAAFDFLLQRVEKTLRHALEEEEKVPVEQVTNFEEVC
DEIKSKLASLKDVPSRIECPLIYHLDVGAMYPNIILTNRLQPSAMVDEATCAACDFNKPG
ANCQRKMAWQWRGEFMPASRSEYHRIQHQLESEKFPPLFPEGPARAFHELSREEQAKYEK
RRLADYCRKAYKKIHITKVEERLTTICQRENSFYVDTVRAFRDRRYEFKGLHKVWKKKLS
AAVEVGDAAEVKRCKNMEVLYDSLQLAHKCILNSFYGYVMRKGARWYSMEMAGIVCFTGA
NIITQARELIEQIGRPLELDTDGIWCVLPNSFPENFVFKTTNVKKPKVTISYPGAMLNIM
VKEGFTNDQYQELAEPSSLTYVTRSENSIFFEVDGPYLAMILPASKEEGKKLKKRYAVFN
EDGSLAELKGFEVKRRGELQLIKIFQSSVFEAFLKGSTLEEVYGSVAKVADYWLDVLYSK
AANMPDSELFELISENRSMSRKLEDYGEQKSTSISTAKRLAEFLGDQMVKDAGLSCRYII
SRKPEGSPVTERAIPLAIFQAEPTVRKHFLRKWLKSSSLQDFDIRAILDWDYYIERLGSA
IQKIITIPAALQQVKNPVPRVKHPDWLHKKLLEKNDVYKQKKISELFTLEGRRQVTMAEA
SEDSPRPSAPDMEDFGLVKLPHPAAPVTVKRKRVLWESQEESQDLTPTVPWQEILGQPPA
LGTSQEEWLVWLRFHKKKWQLQARQRLARRKRQRLESAEGVLRPGAIRDGPATGLGSFLR
RTARSILDLPWQIVQISETSQAGLFRLWALVGSDLHCIRLSIPRVFYVNQRVAKAEEGAS
YRKVNRVLPRSNMVYNLYEYSVPEDMYQEHINEINAELSAPDIEGVYETQVPLLFRALVH
LGCVCVVNKQLVRHLSGWEAETFALEHLEMRSLAQFSYLEPGSIRHIYLYHHAQAHKALF
GIFIPSQRRASVFVLDTVRSNQMPSLGALYSAEHGLLLEKVGPELLPPPKHTFEVRAETD
LKTICRAIQRFLLAYKEERRGPTLIAVQSSWELKRLASEIPVLEEFPLVPICVADKINYG
VLDWQRHGARRMIRHYLNLDTCLSQAFEMSRYFHIPIGNLPEDISTFGSDLFFARHLQRH
NHLLWLSPTARPDLGGKEADDNCLVMEFDDQATVEINSSGCYSTVCVELDLQNLAVNTIL
QSHHVNDMEGADSMGISFDVIQQASLEDMITGGQAASAPASYDETALCSNTFRILKSMVV
GWVKEITQYHNIYADNQVMHFYRWLRSPSSLLHDPALHRTLHNMMKKLFLQLIAEFKRLG
SSVIYANFNRIILCTKKRRVEDAIAYVEYITSSIHSKETFHSLTISFSRCWEFLLWMDPS
NYGGIKGKVSSRIHCGLQDSQKAGGAEDEQENEDDEEERDGEEEEEAEESNVEDLLENNW
NILQFLPQAASCQNYFLMIVSAYIVAVYHCMKDGLRRSAPGSTPVRRRGASQLSQEAEGA
VGALPGMITFSQDYVANELTQSFFTITQKIQKKVTGSRNSTELSEMFPVLPGSHLLLNNP
ALEFIKYVCKVLSLDTNITNQVNKLNRDLLRLVDVGEFSEEAQFRDPCRSYVLPEVICRS
CNFCRDLDLCKDSSFSEDGAVLPQWLCSNCQAPYDSSAIEMTLVEVLQKKLMAFTLQDLV
CLKCRGVKETSMPVYCSCAGDFALTIHTQVFMEQIGIFRNIAQHYGMSYLLETLEWLLQK
NPQLGH
|
| Enzyme 13 Number of Residues |
2286 |
| Enzyme 13 Molecular Weight |
261515.5 |
| Enzyme 13 Theoretical pI |
6.35 |
| Enzyme 13 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- DNA metabolic process
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 13 General Function |
Involved in nucleotide binding |
| Enzyme 13 Specific Function |
Participates in DNA repair and in chromosomal DNA replication |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
62198237  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q07864  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
DPOE1_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>6861 bp
ATGTCTCTGAGGAGCGGCGGGCGGCGGCGCGCGGACCCAGGCGCGGATGGCGAGGCCAGC
AGGGATGATGGCGCCACTTCCTCAGTTTCGGCACTCAAGCGCCTGGAACGGAGTCAGTGG
ACGGATAAGATGGATTTGCGGTTTGGTTTTGAGCGGCTGAAGGAGCCTGGTGAGAAGACA
GGCTGGCTCATTAACATGCATCCTACCGAGATTTTAGATGAAGATAAGCGCTTAGGCAGT
GCAGTGGATTACTACTTTATTCAAGATGACGGAAGCAGATTTAAGGTGGCTTTGCCCTAT
AAACCGTATTTCTACATTGCGACCAGAAAGGGTTGTGAGCGAGAAGTTTCATCTTTTCTC
TCCAAGAAGTTTCAGGGCAAAATTGCAAAAGTGGAGACTGTCCCCAAAGAGGATCTGGAC
TTGCCAAATCACTTGGTGGGTTTGAAGCGAAATTACATCAGGCTGTCCTTCCACACTGTG
GAGGATCTTGTCAAAGTGAGGAAGGAGATCTCCCCTGCCGTGAAGAAGAACAGGGAGCAG
GATCACGCCAGCGACGCGTACACAGCTCTGCTTTCCAGTGTTCTGCAGAGGGGCGGTGTC
ATTACTGATGAAGAGGAAACCTCTAAGAAGATAGCTGACCAGTTGGACAACATTGTGGAC
ATGCGCGAGTACGATGTTCCCTACCACATCCGCCTCTCCATTGACCTGAAGATCCACGTG
GCTCATTGGTACAATGTCAGATACCGAGGAAATGCTTTTCCGGTAGAAATCACCCGCCGA
GATGACCTTGTTGAACGACCTGACCCTGTGGTTTTGGCATTTGACATTGAGACGACCAAA
CTGCCCCTCAAGTTTCCTGATGCTGAGACAGACCAGATTATGATGATTTCCTACATGATC
GATGGCCAGGGCTACCTCATCACCAACAGGGAGATTGTTTCAGAAGATATTGAAGATTTT
GAGTTCACCCCCAAGCCAGAATATGAAGGCCCCTTTTGTGTCTTCAATGAACCCGATGAG
GCTCATCTGATCCAAAGGTGGTTTGAACACGTCCAGGAGACCAAACCCACCATCATGGTC
ACCTACAACGGGGACTTTTTTGACTGGCCATTTGTGGAGGCCCGGGCAGCAGTCCACGGT
CTGAGCATGCAGCAGGAGATAGGCTTCCAGAAGGACAGCCAGGGGGAGTACAAGGCGCCC
CAGTGCATCCACATGGACTGCCTCAGGTGGGTGAAGAGGGACAGTTACCTTCCTGTGGGC
AGTCATAATCTCAAGGCGGCCGCCAAGGCCAAGCTAGGCTATGATCCCGTGGAGCTAGAC
CCGGAGGACATGTGCCGGATGGCCACGGAGCAGCCCCAGACTCTGGCCACGTATTCTGTG
TCAGATGCTGTCGCCACTTACTACCTGTACATGAAGTACGTCCACCCATTCATCTTTGCT
CTGTGCACCATTATTCCCATGGAGCCCGACGAGGTGCTGCGGAAGGGCTCTGGCACTCTG
TGTGAGGCCTTGCTGATGGTGCAGGCCTTCCACGCCAACATCATCTTCCCCAACAAGCAA
GAGCAGGAGTTCAATAAGCTGACGGACGACGGACACGTGCTGGACTCTGAGACCTACGTC
GGGGGCCACGTGGAGGCCCTCGAGTCTGGGGTTTTCCGCAGCGATATCCCTTGCCGGTTT
AGGATGAATCCTGCCGCCTTTGACTTCCTGCTGCAGCGGGTTGAGAAGACCTTGCGCCAC
GCCCTTGAGGAAGAGGAGAAAGTGCCTGTGGAGCAAGTCACCAACTTTGAAGAGGTGTGT
GATGAGATTAAGAGCAAGCTTGCCTCCCTGAAGGACGTTCCCAGCCGCATCGAGTGTCCA
CTCATCTACCACCTGGACGTGGGGGCCATGTACCCCAACATCATCCTGACCAACCGCCTG
CAGCCCTCTGCCATGGTGGACGAAGCCACCTGTGCTGCCTGTGACTTCAATAAGCCTGGA
GCAAACTGCCAGCGGAAGATGGCCTGGCAGTGGAGGGGCGAGTTCATGCCAGCCAGTCGC
AGCGAATACCATCGGATCCAGCACCAGCTGGAGTCAGAGAAGTTCCCCCCCTTGTTCCCA
GAGGGGCCAGCTCGGGCCTTTCATGAACTGTCCCGCGAGGAACAGGCGAAATACGAGAAG
AGAAGGCTGGCGGATTACTGCCGGAAAGCCTACAAGAAGATCCACATCACCAAGGTGGAA
GAGCGTCTCACCACCATCTGCCAGCGGGAAAACTCCTTCTACGTGGACACCGTGCGTGCC
TTCCGGGACAGGCGTTACGAGTTCAAAGGGCTCCACAAGGTGTGGAAAAAGAAGCTCTCG
GCGGCCGTGGAGGTGGGCGACGCGGCTGAGGTGAAGCGCTGCAAGAACATGGAGGTGCTG
TATGACTCGCTGCAGCTGGCCCACAAGTGCATCCTGAACTCCTTCTATGGCTATGTCATG
CGCAAGGGGGCTCGCTGGTACTCCATGGAGATGGCTGGCATCGTCTGCTTCACAGGGGCC
AACATCATCACCCAGGCACGGGAGCTGATCGAGCAGATTGGGAGGCCCTTAGAGCTGGAC
ACAGATGGTATATGGTGCGTCCTGCCCAACAGCTTCCCAGAAAATTTTGTCTTCAAGACG
ACCAATGTGAAGAAGCCCAAAGTGACCATCTCCTACCCAGGCGCCATGTTGAACATCATG
GTCAAGGAAGGCTTCACCAATGACCAGTACCAGGAGCTGGCTGAGCCGTCCTCACTCACC
TACGTCACCCGCTCAGAGAACAGCATCTTTTTTGAGGTTGATGGGCCCTACCTTGCCATG
ATTCTTCCAGCCTCCAAGGAAGAAGGCAAGAAATTGAAGAAGAGGTATGCTGTGTTCAAT
GAAGACGGTTCTCTGGCTGAGCTCAAGGGCTTTGAGGTCAAACGCCGCGGGGAACTGCAG
CTGATTAAGATCTTCCAATCCTCGGTGTTTGAGGCCTTCCTCAAGGGCAGCACGCTGGAA
GAGGTGTATGGCTCTGTAGCCAAGGTGGCTGACTACTGGCTGGACGTGCTGTACAGCAAG
GCAGCCAACATGCCTGACTCTGAGCTATTCGAGCTCATCTCTGAGAACCGTTCCATGTCT
CGGAAGCTGGAAGATTACGGGGAGCAGAAGTCTACGTCCATCAGCACAGCAAAGCGCCTG
GCCGAGTTCCTGGGAGACCAGATGGTCAAGGATGCAGGGCTGAGTTGCCGCTACATCATC
TCCCGCAAGCCCGAGGGCTCCCCTGTCACGGAGAGGGCCATCCCACTTGCCATTTTCCAA
GCAGAGCCCACGGTGAGGAAGCACTTTCTCCGGAAATGGCTCAAGAGCTCTTCCCTTCAA
GACTTTGATATTCGAGCAATTCTGGATTGGGACTACTACATTGAGCGGCTGGGAAGCGCC
ATCCAGAAGATCATCACCATCCCTGCGGCCCTGCAGCAGGTAAAGAACCCAGTGCCACGT
GTCAAACACCCCGACTGGCTGCACAAAAAACTGCTGGAGAAGAATGATGTCTACAAGCAG
AAGAAGATCAGTGAGCTCTTCACCCTGGAGGGCAGGAGACAGGTCACGATGGCCGAGGCC
TCAGAAGACAGTCCGAGGCCAAGTGCTCCTGACATGGAGGACTTCGGCCTCGTAAAGCTG
CCTCACCCAGCAGCCCCTGTCACTGTGAAGAGGAAGCGAGTTCTTTGGGAGAGCCAGGAG
GAGTCCCAGGACCTCACGCCGACTGTGCCCTGGCAGGAAATCTTGGGGCAGCCTCCCGCC
CTGGGAACCAGCCAGGAGGAATGGCTTGTCTGGCTCCGGTTCCACAAGAAGAAGTGGCAG
CTGCAGGCCCGGCAGCGCCTCGCCCGCAGGAAGAGGCAGCGTCTGGAGTCGGCAGAGGGT
GTGCTCAGGCCCGGGGCCATCCGGGATGGTCCTGCCACGGGGCTGGGGAGCTTCTTGCGA
AGAACTGCCCGCAGCATCCTGGACCTTCCGTGGCAGATTGTGCAGATCAGCGAGACCAGC
CAGGCCGGCCTGTTCAGGCTGTGGGCGCTCGTTGGCAGTGACTTGCACTGCATCAGGCTG
AGCATCCCCCGTGTGTTCTACGTGAACCAGCGAGTCGCTAAAGCGGAGGAGGGTGCTTCG
TATCGCAAGGTAAATCGGGTCCTTCCTCGCTCCAACATGGTCTACAATCTCTATGAGTAT
TCAGTGCCAGAGGACATGTACCAGGAACACATCAACGAGATCAACGCTGAGCTGTCAGCG
CCAGACATCGAGGGCGTATATGAGACTCAGGTTCCGTTACTGTTCCGGGCCCTGGTGCAC
CTGGGCTGTGTGTGTGTGGTCAATAAACAGCTGGTGAGGCACCTTTCAGGCTGGGAAGCA
GAGACCTTTGCTCTTGAGCACCTGGAGATGCGCTCTCTGGCCCAGTTCAGCTACCTGGAA
CCAGGGAGTATCCGCCATATCTACCTGTACCACCACGCACAGGCCCACAAAGCGCTCTTC
GGGATCTTCATCCCCTCACAGCGCAGGGCATCCGTCTTTGTGCTGGACACTGTGCGCAGC
AACCAGATGCCCAGCCTTGGCGCCCTGTACTCAGCAGAGCACGGCCTCCTCCTGGAGAAG
GTGGGCCCTGAGCTCCTGCCACCCCCCAAACACACCTTCGAAGTTCGGGCAGAAACTGAC
CTGAAGACCATCTGCAGAGCCATCCAGCGATTCCTGCTCGCCTACAAGGAGGAGCGCCGG
GGGCCCACACTCATCGCTGTTCAGTCCAGCTGGGAGCTGAAGAGGCTGGCCAGTGAAATT
CCTGTCTTGGAGGAATTCCCACTGGTGCCTATCTGTGTGGCTGACAAGATCAACTATGGG
GTCCTGGACTGGCAGCGCCATGGAGCCCGGCGCATGATCCGTCACTACCTCAACCTGGAC
ACCTGCCTGTCGCAGGCCTTCGAGATGAGCAGGTACTTTCACATTCCCATTGGGAACCTA
CCAGAGGACATCTCCACATTCGGCTCCGACCTCTTCTTTGCCCGCCACCTCCAGCGCCAC
AACCACCTGCTCTGGCTGTCCCCTACAGCCCGCCCTGACCTGGGTGGAAAGGAGGCTGAT
GACAACTGTCTTGTCATGGAGTTCGATGACCAAGCCACTGTTGAGATCAACAGTTCAGGC
TGTTACTCCACAGTGTGTGTGGAGCTGGACCTTCAGAACCTGGCCGTCAACACCATTCTC
CAGTCTCACCATGTCAACGACATGGAGGGGGCCGACAGCATGGGGATCAGCTTCGACGTG
ATCCAGCAGGCCTCCCTGGAGGACATGATCACGGGTGGTCAGGCTGCCAGTGCCCCGGCC
AGCTACGATGAGACAGCCCTGTGCTCTAACACCTTCAGGATCCTGAAGAGCATGGTCGTG
GGCTGGGTGAAGGAGATCACCCAGTACCACAACATCTATGCAGACAACCAGGTGATGCAC
TTCTACCGCTGGCTTCGGTCGCCATCCTCTCTGCTTCATGACCCTGCCCTGCACCGCACA
CTCCACAACATGATGAAGAAGCTCTTCCTGCAGCTCATCGCTGAGTTCAAGCGCCTGGGG
TCATCAGTCATCTACGCCAACTTCAACCGCATCATCCTCTGTACAAAGAAGCGCCGTGTG
GAAGATGCCATCGCTTACGTGGAGTACATCACCAGCAGCATCCATTCAAAGGAGACCTTC
CATTCTCTGACAATTTCTTTCTCTCGATGCTGGGAATTTCTTCTCTGGATGGATCCATCT
AACTATGGCGGAATCAAAGGAAAAGTTTCATCTCGTATTCACTGTGGACTGCAAGACTCC
CAGAAAGCAGGGGGAGCAGAGGATGAGCAGGAAAATGAGGACGATGAGGAGGAAAGAGAT
GGGGAGGAGGAGGAAGAGGCGGAGGAATCCAACGTGGAGGATTTACTGGAAAACAACTGG
AACATTTTGCAGTTTTTGCCACAGGCAGCCTCCTGCCAGAACTACTTCCTCATGATTGTT
TCAGCGTACATCGTGGCCGTGTACCACTGCATGAAGGACGGGCTGAGGCGCAGTGCTCCA
GGGAGCACCCCCGTGAGGAGGAGGGGGGCCAGCCAGCTCTCCCAGGAGGCCGAGGGGGCG
GTCGGAGCCCTTCCCGGAATGATCACCTTCTCTCAGGATTATGTCGCAAATGAGCTCACT
CAGAGCTTCTTCACCATCACTCAGAAGATTCAGAAGAAAGTCACAGGCTCTCGGAACTCC
ACTGAGCTCTCAGAGATGTTTCCTGTCCTCCCCGGTTCCCACTTGCTGCTCAATAACCCT
GCCCTGGAGTTCATCAAATACGTGTGCAAGGTGCTGTCCCTGGACACCAACATCACAAAC
CAGGTGAATAAGCTGAACCGAGACCTGCTTCGCCTGGTGGATGTCGGCGAGTTCTCCGAG
GAGGCCCAGTTCCGAGACCCCTGCCGCTCCTACGTGCTTCCTGAGGTCATCTGCCGCAGC
TGTAACTTCTGCCGCGACCTGGACCTGTGTAAAGACTCTTCCTTCTCAGAGGATGGGGCG
GTCCTGCCTCAGTGGCTCTGCTCCAACTGTCAGGCGCCCTACGACTCCTCTGCCATCGAG
ATGACGCTGGTGGAAGTTCTACAGAAGAAGCTGATGGCCTTCACCCTGCAGGACCTGGTC
TGCCTGAAGTGCCGCGGGGTGAAGGAGACCAGCATGCCTGTGTACTGCAGCTGCGCGGGA
GACTTCGCCCTCACCATCCACACCCAGGTCTTCATGGAACAGATCGGAATATTCCGGAAC
ATTGCCCAGCACTACGGCATGTCGTACCTCCTGGAGACCCTGGAGTGGCTGCTGCAGAAG
AACCCACAGCTGGGCCATTAG
|
| Enzyme 13 GenBank Gene ID |
NM_006231.2  |
| Enzyme 13 GeneCard ID |
POLE  |
| Enzyme 13 GenAtlas ID |
POLE  |
| Enzyme 13 HGNC ID |
HGNC:9177  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
12q24.3 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Kesti T, Frantti H, Syvaoja JE: Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase epsilon. J Biol Chem. 1993 May 15;268(14):10238-45. [PubMed
]
- Makiniemi M, Hillukkala T, Tuusa J, Reini K, Vaara M, Huang D, Pospiech H, Majuri I, Westerling T, Makela TP, Syvaoja JE: BRCT domain-containing protein TopBP1 functions in DNA replication and damage response. J Biol Chem. 2001 Aug 10;276(32):30399-406. Epub 2001 Jun 6. [PubMed
]
- Post SM, Tomkinson AE, Lee EY: The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon. Nucleic Acids Res. 2003 Oct 1;31(19):5568-75. [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
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6252 |
| Enzyme 14 Name |
DNA polymerase mu |
| Enzyme 14 Synonyms |
- Pol Mu
|
| Enzyme 14 Gene Name |
POLM |
| Enzyme 14 Protein Sequence |
>DNA polymerase mu
MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLD
ACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECR
HRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFC
RAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKLF
TQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQKAGLQHHQDLSTPVLRSDVDALQQ
VVEEAVGQALPGATVTLTGGFRRGKLQGHDVDFLITHPKEGQEAGLLPRVMCRLQDQGLI
LYHQHQHSCCESPTRLAQQSHMDAFERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLV
VAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFDPEQKTFFQAASEEDIFR
HLGLEYLPPEQRNA
|
| Enzyme 14 Number of Residues |
494 |
| Enzyme 14 Molecular Weight |
54815.1 |
| Enzyme 14 Theoretical pI |
8.50 |
| Enzyme 14 GO Classification |
| Function |
- DNA binding
- DNA nucleotidylexotransferase activity
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
|
|
| Enzyme 14 General Function |
Involved in DNA binding |
| Enzyme 14 Specific Function |
Seems to act as an Ig mutase which is responsible for immunoglobulin (Ig) gene hypermutation |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
6715109  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q9NP87  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
DPOLM_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1485 bp
ATGCTCCCCAAACGGCGGCGAGCGCGGGTCGGGTCCCCTAGCGGCGATGCCGCTTCCTCC
ACGCCGCCCTCGACGCGCTTCCCGGGAGTCGCCATCTACCTGGTCGAGCCTCGCATGGGT
CGCAGCCGCCGGGCCTTCCTCACAGGCCTGGCGCGCTCCAAAGGCTTCCGCGTCCTTGAC
GCCTGCAGCTCCGAAGCGACACATGTTGTGATGGAAGAGACCTCAGCAGAGGAGGCCGTC
AGCTGGCAGGAGCGCAGGATGGCAGCTGCTCCCCCGGGTTGCACCCCCCCAGCTCTGCTG
GACATAAGCTGGTTAACAGAGAGCCTGGGAGCTGGGCAGCCTGTACCTGTGGAGTGCCGG
CACCGCCTGGAGGTGGCTGGGCCAAGGAAGGGGCCTCTGAGCCCAGCATGGATGCCTGCC
TATGCCTGCCAGCGCCCTACGCCCCTCACACACCACAACACTGGCCTCTCCGAGGCTCTG
GAGATACTGGCCGAGGCAGCAGGCTTTGAAGGCAGTGAGGGCCGCCTCCTCACCTTCTGC
AGAGCAGCCTCGGTGCTCAAGGCCCTTCCCAGCCCTGTCACAACCCTGAGCCAGCTGCAG
GGGCTTCCCCACTTTGGAGAACACTCCTCTAGGGTTGTCCAGGAGCTGCTGGAGCATGGA
GTGTGTGAGGAGGTGGAGAGAGTTCGGCGCTCAGAGAGGTACCAGACCATGAAGCTCTTC
ACCCAGATCTTCGGGGTCGGTGTGAAGACTGCTGACCGGTGGTACCGGGAAGGACTGCGA
ACCTTAGATGACCTCCGAGAGCAGCCCCAGAAACTAACCCAACAGCAGAAAGCGGGGCTC
CAGCACCACCAGGACCTGAGCACCCCAGTCCTGCGGTCCGATGTAGATGCCCTGCAGCAG
GTGGTGGAGGAAGCTGTGGGGCAGGCCCTGCCTGGGGCCACCGTCACGCTGACCGGCGGC
TTCCGCAGGGGGAAGTTGCAGGGCCATGACGTGGACTTCCTCATCACCCACCCCAAGGAG
GGTCAGGAGGCGGGGCTGCTGCCTAGAGTGATGTGCCGCCTGCAGGACCAGGGCCTCATC
CTGTACCACCAGCACCAGCACAGCTGCTGTGAGTCCCCTACCCGCCTGGCCCAACAGAGC
CACATGGACGCTTTTGAGAGAAGTTTCTGCATTTTCCGCCTACCACAACCTCCAGGGGCT
GCTGTGGGGGGATCCACGAGGCCCTGCCCATCCTGGAAGGCCGTGAGAGTGGACTTGGTA
GTTGCACCCGTCAGCCAGTTCCCTTTCGCCCTGCTCGGTTGGACTGGCTCCAAGCTTTTC
CAGCGGGAGCTGCGCCGCTTCAGCCGGAAGGAGAAGGGCCTGTGGCTGAACAGCCATGGG
CTGTTTGACCCGGAGCAGAAGACATTTTTCCAAGCGGCTTCAGAGGAAGACATCTTCAGA
CACCTGGGCCTTGAGTACCTTCCTCCAGAGCAGAGAAACGCCTGA
|
| Enzyme 14 GenBank Gene ID |
AF176097  |
| Enzyme 14 GeneCard ID |
POLM  |
| Enzyme 14 GenAtlas ID |
POLM  |
| Enzyme 14 HGNC ID |
HGNC:9185  |
| Enzyme 14 Chromosome Location |
7 |
| Enzyme 14 Locus |
7p13 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Dominguez O, Ruiz JF, Lain de Lera T, Garcia-Diaz M, Gonzalez MA, Kirchhoff T, Martinez-A C, Bernad A, Blanco L: DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA mutator in eukaryotic cells. EMBO J. 2000 Apr 3;19(7):1731-42. [PubMed
]
- Aoufouchi S, Flatter E, Dahan A, Faili A, Bertocci B, Storck S, Delbos F, Cocea L, Gupta N, Weill JC, Reynaud CA: Two novel human and mouse DNA polymerases of the polX family. Nucleic Acids Res. 2000 Sep 15;28(18):3684-93. [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
]
- 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
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6253 |
| Enzyme 15 Name |
DNA polymerase kappa |
| Enzyme 15 Synonyms |
- DINB protein
- DINP
|
| Enzyme 15 Gene Name |
POLK |
| Enzyme 15 Protein Sequence |
>DNA polymerase kappa
MDSTKEKCDSYKDDLLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQV
NQRIENMMQQKAQITSQQLRKAQLQVDRFAMELEQSRNLSNTIVHIDMDAFYAAVEMRDN
PELKDKPIAVGSMSMLSTSNYHARRFGVRAAMPGFIAKRLCPQLIIVPPNFDKYRAVSKE
VKEILADYDPNFMAMSLDEAYLNITKHLEERQNWPEDKRRYFIKMGSSVENDNPGKEVNK
LSEHERSISPLLFEESPSDVQPPGDPFQVNFEEQNNPQILQNSVVFGTSAQEVVKEIRFR
IEQKTTLTASAGIAPNTMLAKVCSDKNKPNGQYQILPNRQAVMDFIKDLPIRKVSGIGKV
TEKMLKALGIITCTELYQQRALLSLLFSETSWHYFLHISLGLGSTHLTRDGERKSMSVER
TFSEINKAEEQYSLCQELCSELAQDLQKERLKGRTVTIKLKNVNFEVKTRASTVSSVVST
AEEIFAIAKELLKTEIDADFPHPLRLRLMGVRISSFPNEEDRKHQQRSIIGFLQAGNQAL
SATECTLEKTDKDKFVKPLEMSHKKSFFDKKRSERKWSHQDTFKCEAVNKQSFQTSQPFQ
VLKKKMNENLEISENSDDCQILTCPVCFRAQGCISLEALNKHVDECLDGPSISENFKMFS
CSHVSATKVNKKENVPASSLCEKQDYEAHPKIKEISSVDCIALVDTIDNSSKAESIDALS
NKHSKEECSSLPSKSFNIEHCHQNSSSTVSLENEDVGSFRQEYRQPYLCEVKTGQALVCP
VCNVEQKTSDLTLFNVHVDVCLNKSFIQELRKDKFNPVNQPKESSRSTGSSSGVQKAVTR
TKRPGLMTKYSTSKKIKPNNPKHTLDIFFK
|
| Enzyme 15 Number of Residues |
870 |
| Enzyme 15 Molecular Weight |
98807.8 |
| Enzyme 15 Theoretical pI |
8.22 |
| Enzyme 15 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- damaged DNA binding
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA repair
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in damaged DNA binding |
| Enzyme 15 Specific Function |
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| 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 |
Q9UBT6  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
POLK_HUMAN  |
| Enzyme 15 PDB ID |
1T94  |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>2613 bp
ATGGATAGCACAAAGGAGAAGTGTGACAGTTACAAAGATGATCTTCTGCTTAGGATGGGA
CTTAATGATAATAAAGCAGGAATGGAAGGATTAGATAAAGAGAAAATTAACAAAATTATA
ATGGAAGCCACGAAGGGGTCCAGATTTTATGGAAATGAGCTCAAGAAAGAAAAGCAAGTC
AACCAACGAATTGAAAATATGATGCAACAAAAAGCTCAAATCACCAGCCAACAGCTAAGA
AAAGCACAATTACAGGTTGACAGATTTGCAATGGAATTAGAACAAAGCCGAAATTTGAGC
AATACCATAGTGCACATTGACATGGATGCTTTCTATGCAGCTGTAGAAATGAGGGACAAT
CCAGAATTGAAGGATAAACCCATTGCTGTAGGATCAATGAGTATGCTGTCTACTTCAAAT
TACCATGCAAGGAGATTTGGTGTTCGTGCAGCCATGCCAGGATTTATTGCTAAGAGGCTG
TGCCCACAACTTATAATAGTGCCCCCCAACTTTGACAAATACCGAGCTGTGAGTAAAGAG
GTTAAGGAAATACTTGCTGATTATGATCCCAATTTTATGGCCATGAGTCTTGATGAAGCC
TACTTGAATATAACAAAGCACTTAGAAGAAAGACAAAATTGGCCTGAGGATAAAAGAAGG
TATTTCATCAAAATGGGAAGCTCTGTAGAAAATGATAATCCAGGAAAGGAAGTTAATAAA
CTGAGTGAGCATGAACGATCCATCTCTCCACTACTTTTTGAAGAGAGTCCTTCTGATGTG
CAGCCCCCAGGAGATCCTTTCCAAGTGAACTTTGAAGAACAAAACAATCCTCAAATACTC
CAAAACTCAGTTGTTTTTGGAACATCAGCCCAGGAAGTGGTAAAGGAAATTCGTTTCAGA
ATTGAGCAGAAAACAACACTGACAGCTAGTGCAGGCATTGCCCCAAATACAATGTTAGCA
AAAGTATGCAGTGATAAGAATAAACCAAATGGACAATACCAAATTCTTCCCAATAGACAA
GCTGTGATGGACTTCATCAAGGATTTACCCATTAGAAAGGTTTCTGGAATAGGAAAAGTT
ACAGAGAAAATGTTAAAGGCCCTTGGAATTATTACATGTACAGAACTTTACCAACAGAGG
GCATTGCTTTCTCTCCTTTTCTCTGAAACATCTTGGCATTATTTCCTTCATATCTCCTTG
GGTCTAGGTTCAACACACCTGACGAGGGATGGAGAGAGGAAAAGTATGAGCGTTGAGAGG
ACATTCAGTGAGATAAATAAAGCGGAAGAGCAATACAGCCTATGTCAAGAACTTTGCAGT
GAGCTTGCTCAGGATCTACAGAAAGAAAGACTTAAGGGTAGAACTGTTACCATTAAGTTG
AAGAATGTGAATTTTGAAGTAAAAACTCGTGCATCTACAGTTTCATCTGTTGTTTCTACT
GCAGAAGAAATATTTGCCATTGCTAAGGAATTGCTAAAAACAGAAATTGATGCTGATTTT
CCACATCCCTTGAGATTAAGGCTTATGGGTGTTCGGATATCTAGTTTTCCCAATGAAGAG
GACAGGAAACACCAACAAAGGAGCATTATTGGCTTTTTACAGGCTGGAAACCAAGCCCTG
TCAGCCACTGAGTGTACATTAGAGAAAACTGACAAAGATAAGTTTGTAAAACCTCTAGAA
ATGTCTCATAAGAAGAGTTTCTTTGATAAAAAACGATCAGAAAGGAAATGGAGTCACCAA
GATACATTTAAATGTGAAGCCGTGAATAAACAAAGTTTCCAGACATCACAACCATTCCAA
GTTTTAAAGAAGAAGATGAATGAGAATTTGGAAATATCAGAGAATTCAGATGACTGTCAG
ATACTTACCTGTCCTGTTTGCTTTAGGGCTCAAGGGTGCATCAGTCTGGAAGCCTTGAAT
AAACATGTAGATGAATGTCTTGATGGACCTTCAATCAGTGAAAACTTTAAAATGTTCTCG
TGTTCACATGTTTCTGCTACCAAAGTTAACAAGAAAGAAAATGTTCCTGCTTCTTCACTT
TGTGAGAAGCAAGATTATGAAGCCCATCCAAAAATTAAAGAAATATCTTCAGTAGATTGT
ATAGCTTTAGTAGATACTATAGATAACTCATCTAAAGCAGAAAGCATAGATGCTTTAAGT
AATAAGCATAGCAAGGAAGAATGTTCTAGTCTCCCAAGCAAGTCTTTTAATATTGAACAC
TGTCATCAGAATTCTTCTTCTACTGTTTCATTGGAAAACGAAGATGTTGGATCATTTAGA
CAAGAATACCGCCAGCCTTACTTATGTGAAGTGAAAACAGGCCAAGCTCTAGTTTGTCCT
GTTTGTAACGTAGAACAAAAGACTTCAGATCTAACCCTGTTCAATGTGCATGTGGATGTT
TGCTTAAATAAAAGTTTTATCCAAGAATTAAGAAAGGATAAATTTAACCCAGTTAATCAA
CCCAAAGAAAGCTCCAGAAGTACTGGTAGCTCAAGTGGAGTACAGAAGGCTGTAACAAGA
ACAAAAAGGCCAGGATTGATGACAAAGTACTCAACATCAAAGAAAATAAAACCAAACAAT
CCCAAACATACCCTTGATATATTTTTTAAGTAA
|
| Enzyme 15 GenBank Gene ID |
AB027564  |
| Enzyme 15 GeneCard ID |
POLK  |
| Enzyme 15 GenAtlas ID |
POLK  |
| Enzyme 15 HGNC ID |
HGNC:9183  |
| Enzyme 15 Chromosome Location |
5 |
| Enzyme 15 Locus |
5q13 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Ogi T, Kato T Jr, Kato T, Ohmori H: Mutation enhancement by DINB1, a mammalian homologue of the Escherichia coli mutagenesis protein dinB. Genes Cells. 1999 Nov;4(11):607-18. [PubMed
]
- Gerlach VL, Aravind L, Gotway G, Schultz RA, Koonin EV, Friedberg EC: Human and mouse homologs of Escherichia coli DinB (DNA polymerase IV), members of the UmuC/DinB superfamily. Proc Natl Acad Sci U S A. 1999 Oct 12;96(21):11922-7. [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
]
- Gerlach VL, Feaver WJ, Fischhaber PL, Friedberg EC: Purification and characterization of pol kappa, a DNA polymerase encoded by the human DINB1 gene. J Biol Chem. 2001 Jan 5;276(1):92-8. [PubMed
]
- Fischhaber PL, Gerlach VL, Feaver WJ, Hatahet Z, Wallace SS, Friedberg EC: Human DNA polymerase kappa bypasses and extends beyond thymine glycols during translesion synthesis in vitro, preferentially incorporating correct nucleotides. J Biol Chem. 2002 Oct 4;277(40):37604-11. Epub 2002 Jul 26. [PubMed
]
- Bergoglio V, Bavoux C, Verbiest V, Hoffmann JS, Cazaux C: Localisation of human DNA polymerase kappa to replication foci. J Cell Sci. 2002 Dec 1;115(Pt 23):4413-8. [PubMed
]
- Haracska L, Unk I, Johnson RE, Phillips BB, Hurwitz J, Prakash L, Prakash S: Stimulation of DNA synthesis activity of human DNA polymerase kappa by PCNA. Mol Cell Biol. 2002 Feb;22(3):784-91. [PubMed
]
- Haracska L, Prakash L, Prakash S: Role of human DNA polymerase kappa as an extender in translesion synthesis. Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16000-5. Epub 2002 Nov 20. [PubMed
]
- Wolfle WT, Washington MT, Prakash L, Prakash S: Human DNA polymerase kappa uses template-primer misalignment as a novel means for extending mispaired termini and for generating single-base deletions. Genes Dev. 2003 Sep 1;17(17):2191-9. [PubMed
]
- Haracska L, Prakash L, Prakash S: A mechanism for the exclusion of low-fidelity human Y-family DNA polymerases from base excision repair. Genes Dev. 2003 Nov 15;17(22):2777-85. [PubMed
]
- Yasui M, Suzuki N, Miller H, Matsuda T, Matsui S, Shibutani S: Translesion synthesis past 2'-deoxyxanthosine, a nitric oxide-derived DNA adduct, by mammalian DNA polymerases. J Mol Biol. 2004 Nov 26;344(3):665-74. [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
]
- Uljon SN, Johnson RE, Edwards TA, Prakash S, Prakash L, Aggarwal AK: Crystal structure of the catalytic core of human DNA polymerase kappa. Structure. 2004 Aug;12(8):1395-404. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6254 |
| Enzyme 16 Name |
DNA polymerase epsilon subunit 3 |
| Enzyme 16 Synonyms |
- Arsenic-transactivated protein
- AsTP
- Chromatin accessibility complex 17 kDa protein
- CHRAC-17
- HuCHRAC17
- DNA polymerase II subunit 3
- DNA polymerase epsilon subunit p17
|
| Enzyme 16 Gene Name |
POLE3 |
| Enzyme 16 Protein Sequence |
>DNA polymerase epsilon subunit 3
MAERPEDLNLPNAVITRIIKEALPDGVNISKEARSAISRAASVFVLYATSCANNFAMKGK
RKTLNASDVLSAMEEMEFQRFVTPLKEALEAYRREQKGKKEASEQKKKDKDKKTDSEEQD
KSRDEDNDEDEERLEEEEQNEEEEVDN
|
| Enzyme 16 Number of Residues |
147 |
| Enzyme 16 Molecular Weight |
16859.4 |
| Enzyme 16 Theoretical pI |
4.38 |
| Enzyme 16 GO Classification |
| Function |
- DNA binding
- binding
- nucleic acid binding
- sequence-specific DNA binding
|
| Process |
| — |
| Component |
|
|
| Enzyme 16 General Function |
Involved in sequence-specific DNA binding |
| Enzyme 16 Specific Function |
Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1 |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
8100806  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q9NRF9  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
DPOE3_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>444 bp
ATGGCGGAGAGGCCCGAGGACCTAAACCTGCCCAATGCCGTGATCACCAGGATCATCAAG
GAGGCGCTCCCGGACGGTGTCAACATCTCCAAGGAGGCCCGGAGCGCCATCTCCCGCGCC
GCCAGCGTCTTCGTGCTGTACGCCACATCCTGTGCTAACAACTTTGCAATGAAAGGAAAG
CGGAAGACGCTGAATGCCAGTGATGTGCTCTCAGCCATGGAAGAGATGGAGTTCCAGCGG
TTCGTTACCCCATTGAAAGAAGCTCTGGAAGCATATAGGCGGGAGCAGAAAGGCAAGAAG
GAGGCCTCAGAGCAAAAGAAGAAGGACAAAGACAAAAAAACAGACTCGGAAGAGCAAGAC
AAGAGCAGGGATGAGGACAATGATGAAGACGAAGAAAGGCTGGAAGAAGAAGAACAGAAT
GAAGAGGAAGAAGTAGACAACTGA
|
| Enzyme 16 GenBank Gene ID |
AF226077  |
| Enzyme 16 GeneCard ID |
POLE3  |
| Enzyme 16 GenAtlas ID |
POLE3  |
| Enzyme 16 HGNC ID |
HGNC:13546  |
| Enzyme 16 Chromosome Location |
9 |
| Enzyme 16 Locus |
9q33 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Poot RA, Dellaire G, Hulsmann BB, Grimaldi MA, Corona DF, Becker PB, Bickmore WA, Varga-Weisz PD: HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two novel histone-fold proteins. EMBO J. 2000 Jul 3;19(13):3377-87. [PubMed
]
- Li Y, Pursell ZF, Linn S: Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon. J Biol Chem. 2000 Jul 28;275(30):23247-52. [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
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [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
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [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
]
- 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
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6256 |
| Enzyme 17 Name |
DNA polymerase subunit gamma-1 |
| Enzyme 17 Synonyms |
- Mitochondrial DNA polymerase catalytic subunit
- PolG-alpha
|
| Enzyme 17 Gene Name |
POLG |
| Enzyme 17 Protein Sequence |
>DNA polymerase subunit gamma-1
MSRLLWRKVAGATVGPGPVPAPGRWVSSSVPASDPSDGQRRRQQQQQQQQQQQQQPQQPQ
VLSSEGGQLRHNPLDIQMLSRGLHEQIFGQGGEMPGEAAVRRSVEHLQKHGLWGQPAVPL
PDVELRLPPLYGDNLDQHFRLLAQKQSLPYLEAANLLLQAQLPPKPPAWAWAEGWTRYGP
EGEAVPVAIPEERALVFDVEVCLAEGTCPTLAVAISPSAWYSWCSQRLVEERYSWTSQLS
PADLIPLEVPTGASSPTQRDWQEQLVVGHNVSFDRAHIREQYLIQGSRMRFLDTMSMHMA
ISGLSSFQRSLWIAAKQGKHKVQPPTKQGQKSQRKARRGPAISSWDWLDISSVNSLAEVH
RLYVGGPPLEKEPRELFVKGTMKDIRENFQDLMQYCAQDVWATHEVFQQQLPLFLERCPH
PVTLAGMLEMGVSYLPVNQNWERYLAEAQGTYEELQREMKKSLMDLANDACQLLSGERYK
EDPWLWDLEWDLQEFKQKKAKKVKKEPATASKLPIEGAGAPGDPMDQEDLGPCSEEEEFQ
QDVMARACLQKLKGTTELLPKRPQHLPGHPGWYRKLCPRLDDPAWTPGPSLLSLQMRVTP
KLMALTWDGFPLHYSERHGWGYLVPGRRDNLAKLPTGTTLESAGVVCPYRAIESLYRKHC
LEQGKQQLMPQEAGLAEEFLLTDNSAIWQTVEELDYLEVEAEAKMENLRAAVPGQPLALT
ARGGPKDTQPSYHHGNGPYNDVDIPGCWFFKLPHKDGNSCNVGSPFAKDFLPKMEDGTLQ
AGPGGASGPRALEINKMISFWRNAHKRISSQMVVWLPRSALPRAVIRHPDYDEEGLYGAI
LPQVVTAGTITRRAVEPTWLTASNARPDRVGSELKAMVQAPPGYTLVGADVDSQELWIAA
VLGDAHFAGMHGCTAFGWMTLQGRKSRGTDLHSKTATTVGISREHAKIFNYGRIYGAGQP
FAERLLMQFNHRLTQQEAAEKAQQMYAATKGLRWYRLSDEGEWLVRELNLPVDRTEGGWI
SLQDLRKVQRETARKSQWKKWEVVAERAWKGGTESEMFNKLESIATSDIPRTPVLGCCIS
RALEPSAVQEEFMTSRVNWVVQSSAVDYLHLMLVAMKWLFEEFAIDGRFCISIHDEVRYL
VREEDRYRAALALQITNLLTRCMFAYKLGLNDLPQSVAFFSAVDIDRCLRKEVTMDCKTP
SNPTGMERRYGIPQGEALDIYQIIELTKGSLEKRSQPGP
|
| Enzyme 17 Number of Residues |
1239 |
| Enzyme 17 Molecular Weight |
139561.1 |
| Enzyme 17 Theoretical pI |
6.89 |
| Enzyme 17 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA replication
- DNA-dependent DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
- DNA polymerase complex
- gamma DNA polymerase complex
- macromolecular complex
- protein complex
|
|
| Enzyme 17 General Function |
Involved in DNA binding |
| Enzyme 17 Specific Function |
Involved in the replication of mitochondrial DNA |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
Not Available |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P54098  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
DPOG1_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>3720 bp
ATGAGCCGCCTGCTCTGGAGGAAGGTGGCCGGCGCCACCGTCGGGCCAGGGCCGGTTCCA
GCTCCGGGGCGCTGGGTCTCCAGCTCCGTCCCCGCGTCCGACCCCAGCGACGGGCAGCGG
CGGCGGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAACAGCAGCCTCAGCAGCCGCAA
GTGCTATCCTCGGAGGGCGGGCAGCTGCGGCACAACCCATTGGACATCCAGATGCTCTCG
AGAGGGCTGCACGAGCAAATCTTCGGGCAAGGAGGGGAGATGCCTGGCGAGGCCGCGGTG
CGCCGCAGCGTCGAGCACCTGCAGAAGCACGGGCTCTGGGGGCAGCCAGCCGTGCCCTTG
CCCGACGTGGAGCTGCGCCTGCCGCCCCTCTACGGGGACAACCTGGACCAGCACTTCCGC
CTCCTGGCCCAGAAGCAGAGCCTGCCCTACCTGGAGGCGGCCAACTTGCTGTTGCAGGCC
CAGCTGCCCCCGAAGCCCCCGGCTTGGGCCTGGGCGGAGGGCTGGACCCGGTACGGCCCC
GAGGGGGAGGCCGTACCCGTGGCCATCCCCGAGGAGCGGGCCCTGGTGTTCGACGTGGAG
GTCTGCTTGGCAGAGGGAACTTGCCCCACATTGGCGGTGGCCATATCCCCCTCGGCCTGG
TATTCCTGGTGCAGCCAGCGGCTGGTGGAAGAGCGTTACTCTTGGACCAGCCAGCTGTCG
CCGGCTGACCTCATCCCCCTGGAGGTCCCTACTGGTGCCAGCAGCCCCACCCAGAGAGAC
TGGCAGGAGCAGTTAGTGGTGGGGCACAATGTTTCCTTTGACCGAGCTCATATCAGGGAG
CAGTACCTGATCCAGGGTTCCCGCATGCGTTTCCTGGACACCATGAGCATGCACATGGCC
ATCTCAGGGCTAAGCAGCTTCCAGCGCAGTCTGTGGATAGCAGCCAAGCAGGGCAAACAC
AAGGTCCAGCCCCCCACAAAGCAAGGCCAGAAGTCCCAGAGGAAAGCCAGAAGAGGCCCA
GCGATCTCATCCTGGGACTGGCTGGACATCAGCAGTGTCAACAGTCTGGCAGAGGTGCAC
AGACTTTATGTAGGGGGGCCTCCCTTAGAGAAGGAGCCTCGAGAACTGTTTGTGAAGGGC
ACCATGAAGGACATTCGTGAGAACTTCCAGGACCTGATGCAGTACTGTGCCCAGGACGTG
TGGGCCACCCATGAGGTTTTCCAGCAGCAGCTACCGCTCTTCTTGGAGAGGTGTCCCCAC
CCAGTGACTCTGGCCGGCATGCTGGAGATGGGTGTCTCCTACCTGCCTGTCAACCAGAAC
TGGGAGCGTTACCTGGCAGAGGCACAGGGCACTTATGAGGAGCTCCAGCGGGAGATGAAG
AAGTCGTTGATGGATCTGGCCAATGATGCCTGCCAGCTGCTCTCAGGAGAGAGGTACAAA
GAAGACCCCTGGCTCTGGGACCTGGAGTGGGACCTGCAAGAATTTAAGCAGAAGAAAGCT
AAGAAGGTGAAGAAGGAACCAGCCACAGCCAGCAAGTTGCCCATCGAGGGGGCTGGGGCC
CCTGGTGATCCCATGGATCAGGAAGACCTCGGCCCCTGCAGTGAGGAGGAGGAGTTTCAA
CAAGATGTCATGGCCCGCGCCTGCTTGCAGAAGCTGAAGGGGACCACAGAGCTCCTGCCC
AAGCGGCCCCAGCACCTTCCTGGACACCCTGGATGGTACCGGAAGCTCTGCCCCCGGCTA
GACGACCCTGCATGGACCCCGGGCCCCAGCCTCCTCAGCCTGCAGATGCGGGTCACACCT
AAACTCATGGCACTTACCTGGGATGGCTTCCCTCTGCACTACTCAGAGCGTCATGGCTGG
GGCTACTTGGTGCCTGGGCGGCGGGACAACCTGGCCAAGCTGCCGACAGGTACCACCCTG
GAGTCAGCTGGGGTGGTCTGCCCCTACAGAGCCATCGAGTCCCTGTACAGGAAGCACTGT
CTCGAACAGGGGAAGCAGCAGCTGATGCCCCAGGAGGCCGGCCTGGCGGAGGAGTTCCTG
CTCACTGACAATAGTGCCATATGGCAAACGGTAGAAGAACTGGATTACTTAGAAGTGGAG
GCTGAGGCCAAGATGGAGAACTTGCGAGCTGCAGTGCCAGGTCAACCCCTAGCTCTGACT
GCCCGTGGTGGCCCCAAGGACACCCAGCCCAGCTATCACCATGGCAATGGACCTTACAAC
GACGTGGACATCCCTGGCTGCTGGTTTTTCAAGCTGCCTCACAAGGATGGTAATAGCTGT
AATGTGGGAAGCCCCTTTGCCAAGGACTTCCTGCCCAAGATGGAGGATGGCACCCTGCAG
GCTGGCCCAGGAGGTGCCAGTGGGCCCCGTGCTCTGGAAATCAACAAAATGATTTCTTTC
TGGAGGAACGCCCATAAACGTATCAGCTCCCAGATGGTGGTGTGGCTGCCCAGGTCAGCT
CTGCCCCGTGCTGTGATCAGGCACCCCGACTATGATGAGGAAGGCCTCTATGGGGCCATC
CTGCCCCAAGTGGTGACTGCCGGCACCATCACTCGCCGGGCTGTGGAGCCCACATGGCTC
ACCGCCAGCAATGCCCGGCCTGACCGAGTAGGCAGTGAGTTGAAAGCCATGGTGCAGGCC
CCACCTGGCTACACCCTTGTGGGTGCTGATGTGGACTCCCAAGAGCTGTGGATTGCAGCT
GTGCTTGGAGACGCCCACTTTGCCGGCATGCATGGCTGCACAGCCTTTGGGTGGATGACA
CTGCAGGGCAGGAAGAGCAGGGGCACTGATCTACACAGTAAGACAGCCACTACTGTGGGC
ATCAGCCGTGAGCATGCCAAAATCTTCAACTACGGCCGCATCTATGGTGCTGGGCAGCCC
TTTGCTGAGCGCTTACTAATGCAGTTTAACCACCGGCTCACACAGCAGGAGGCAGCTGAG
AAGGCCCAGCAGATGTACGCTGCCACCAAGGGCCTCCGCTGGTATCGGCTGTCGGATGAG
GGCGAGTGGCTGGTGAGGGAGTTGAACCTCCCAGTGGACAGGACTGAGGGTGGCTGGATT
TCCCTGCAGGATCTGCGCAAGGTCCAGAGAGAAACTGCAAGGAAGTCACAGTGGAAGAAG
TGGGAGGTGGTTGCTGAACGGGCATGGAAGGGGGGCACAGAGTCAGAAATGTTCAATAAG
CTTGAGAGCATTGCTACGTCTGACATACCACGTACCCCGGTGCTGGGCTGCTGCATCAGC
CGAGCCCTGGAGCCCTCGGCTGTCCAGGAAGAGTTTATGACCAGCCGTGTGAATTGGGTG
GTACAGAGCTCTGCTGTTGACTACTTACACCTCATGCTTGTGGCCATGAAGTGGCTGTTT
GAAGAGTTTGCCATAGATGGGCGCTTCTGCATCAGCATCCATGACGAGGTTCGCTACCTG
GTGCGGGAGGAGGACCGCTACCGCGCTGCCCTGGCCTTGCAGATCACCAACCTCTTGACC
AGGTGCATGTTTGCCTACAAGCTGGGTCTGAATGACTTGCCCCAGTCAGTCGCCTTTTTC
AGTGCAGTCGATATTGACCGGTGCCTCAGGAAGGAAGTGACCATGGATTGTAAAACCCCT
TCCAACCCAACTGGGATGGAAAGGAGATACGGGATTCCCCAGGGTGAAGCGCTGGATATT
TACCAGATAATTGAACTCACCAAAGGCTCCTTGGAAAAACGAAGCCAGCCTGGACCATAG
|
| Enzyme 17 GenBank Gene ID |
U60325  |
| Enzyme 17 GeneCard ID |
POLG  |
| Enzyme 17 GenAtlas ID |
POLG  |
| Enzyme 17 HGNC ID |
HGNC:9179  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
15q25 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Ropp PA, Copeland WC: Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma. Genomics. 1996 Sep 15;36(3):449-58. [PubMed
]
- Lecrenier N, Van Der Bruggen P, Foury F: Mitochondrial DNA polymerases from yeast to man: a new family of polymerases. Gene. 1997 Jan 31;185(1):147-52. [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
]
- Van Goethem G, Dermaut B, Lofgren A, Martin JJ, Van Broeckhoven C: Mutation of POLG is associated with progressive external ophthalmoplegia characterized by mtDNA deletions. Nat Genet. 2001 Jul;28(3):211-2. [PubMed
]
- Lamantea E, Tiranti V, Bordoni A, Toscano A, Bono F, Servidei S, Papadimitriou A, Spelbrink H, Silvestri L, Casari G, Comi GP, Zeviani M: Mutations of mitochondrial DNA polymerase gammaA are a frequent cause of autosomal dominant or recessive progressive external ophthalmoplegia. Ann Neurol. 2002 Aug;52(2):211-9. [PubMed
]
- Ponamarev MV, Longley MJ, Nguyen D, Kunkel TA, Copeland WC: Active site mutation in DNA polymerase gamma associated with progressive external ophthalmoplegia causes error-prone DNA synthesis. J Biol Chem. 2002 May 3;277(18):15225-8. Epub 2002 Mar 15. [PubMed
]
- Filosto M, Mancuso M, Nishigaki Y, Pancrudo J, Harati Y, Gooch C, Mankodi A, Bayne L, Bonilla E, Shanske S, Hirano M, DiMauro S: Clinical and genetic heterogeneity in progressive external ophthalmoplegia due to mutations in polymerase gamma. Arch Neurol. 2003 Sep;60(9):1279-84. [PubMed
]
- Van Goethem G, Schwartz M, Lofgren A, Dermaut B, Van Broeckhoven C, Vissing J: Novel POLG mutations in progressive external ophthalmoplegia mimicking mitochondrial neurogastrointestinal encephalomyopathy. Eur J Hum Genet. 2003 Jul;11(7):547-9. [PubMed
]
- Van Goethem G, Lofgren A, Dermaut B, Ceuterick C, Martin JJ, Van Broeckhoven C: Digenic progressive external ophthalmoplegia in a sporadic patient: recessive mutations in POLG and C10orf2/Twinkle. Hum Mutat. 2003 Aug;22(2):175-6. [PubMed
]
- Di Fonzo A, Bordoni A, Crimi M, Sara G, Del Bo R, Bresolin N, Comi GP: POLG mutations in sporadic mitochondrial disorders with multiple mtDNA deletions. Hum Mutat. 2003 Dec;22(6):498-9. [PubMed
]
- Agostino A, Valletta L, Chinnery PF, Ferrari G, Carrara F, Taylor RW, Schaefer AM, Turnbull DM, Tiranti V, Zeviani M: Mutations of ANT1, Twinkle, and POLG1 in sporadic progressive external ophthalmoplegia (PEO). Neurology. 2003 Apr 22;60(8):1354-6. [PubMed
]
- Van Goethem G, Mercelis R, Lofgren A, Seneca S, Ceuterick C, Martin JJ, Van Broeckhoven C: Patient homozygous for a recessive POLG mutation presents with features of MERRF. Neurology. 2003 Dec 23;61(12):1811-3. [PubMed
]
- Van Goethem G, Martin JJ, Dermaut B, Lofgren A, Wibail A, Ververken D, Tack P, Dehaene I, Van Zandijcke M, Moonen M, Ceuterick C, De Jonghe P, Van Broeckhoven C: Recessive POLG mutations presenting with sensory and ataxic neuropathy in compound heterozygote patients with progressive external ophthalmoplegia. Neuromuscul Disord. 2003 Feb;13(2):133-42. [PubMed
]
- Naviaux RK, Nguyen KV: POLG mutations associated with Alpers' syndrome and mitochondrial DNA depletion. Ann Neurol. 2004 May;55(5):706-12. [PubMed
]
- Lamantea E, Zeviani M: Sequence analysis of familial PEO shows additional mutations associated with the 752C-->T and 3527C-->T changes in the POLG1 gene. Ann Neurol. 2004 Sep;56(3):454-5. [PubMed
]
- Mancuso M, Filosto M, Oh SJ, DiMauro S: A novel polymerase gamma mutation in a family with ophthalmoplegia, neuropathy, and Parkinsonism. Arch Neurol. 2004 Nov;61(11):1777-9. [PubMed
]
- Luoma P, Melberg A, Rinne JO, Kaukonen JA, Nupponen NN, Chalmers RM, Oldfors A, Rautakorpi I, Peltonen L, Majamaa K, Somer H, Suomalainen A: Parkinsonism, premature menopause, and mitochondrial DNA polymerase gamma mutations: clinical and molecular genetic study. Lancet. 2004 Sep 4-10;364(9437):875-82. [PubMed
]
- Mancuso M, Filosto M, Bellan M, Liguori R, Montagna P, Baruzzi A, DiMauro S, Carelli V: POLG mutations causing ophthalmoplegia, sensorimotor polyneuropathy, ataxia, and deafness. Neurology. 2004 Jan 27;62(2):316-8. [PubMed
]
- Van Goethem G, Luoma P, Rantamaki M, Al Memar A, Kaakkola S, Hackman P, Krahe R, Lofgren A, Martin JJ, De Jonghe P, Suomalainen A, Udd B, Van Broeckhoven C: POLG mutations in neurodegenerative disorders with ataxia but no muscle involvement. Neurology. 2004 Oct 12;63(7):1251-7. [PubMed
]
- Hakonen AH, Heiskanen S, Juvonen V, Lappalainen I, Luoma PT, Rantamaki M, Goethem GV, Lofgren A, Hackman P, Paetau A, Kaakkola S, Majamaa K, Varilo T, Udd B, Kaariainen H, Bindoff LA, Suomalainen A: Mitochondrial DNA polymerase W748S mutation: a common cause of autosomal recessive ataxia with ancient European origin. Am J Hum Genet. 2005 Sep;77(3):430-41. Epub 2005 Jul 27. [PubMed
]
- Davidzon G, Mancuso M, Ferraris S, Quinzii C, Hirano M, Peters HL, Kirby D, Thorburn DR, DiMauro S: POLG mutations and Alpers syndrome. Ann Neurol. 2005 Jun;57(6):921-3. [PubMed
]
- Ferrari G, Lamantea E, Donati A, Filosto M, Briem E, Carrara F, Parini R, Simonati A, Santer R, Zeviani M: Infantile hepatocerebral syndromes associated with mutations in the mitochondrial DNA polymerase-gammaA. Brain. 2005 Apr;128(Pt 4):723-31. Epub 2005 Feb 2. [PubMed
]
- Luoma PT, Luo N, Loscher WN, Farr CL, Horvath R, Wanschitz J, Kiechl S, Kaguni LS, Suomalainen A: Functional defects due to spacer-region mutations of human mitochondrial DNA polymerase in a family with an ataxia-myopathy syndrome. Hum Mol Genet. 2005 Jul 15;14(14):1907-20. Epub 2005 May 25. [PubMed
]
- Winterthun S, Ferrari G, He L, Taylor RW, Zeviani M, Turnbull DM, Engelsen BA, Moen G, Bindoff LA: Autosomal recessive mitochondrial ataxic syndrome due to mitochondrial polymerase gamma mutations. Neurology. 2005 Apr 12;64(7):1204-8. [PubMed
]
- Davidzon G, Greene P, Mancuso M, Klos KJ, Ahlskog JE, Hirano M, DiMauro S: Early-onset familial parkinsonism due to POLG mutations. Ann Neurol. 2006 May;59(5):859-62. [PubMed
]
- Gonzalez-Vioque E, Blazquez A, Fernandez-Moreira D, Bornstein B, Bautista J, Arpa J, Navarro C, Campos Y, Fernandez-Moreno MA, Garesse R, Arenas J, Martin MA: Association of novel POLG mutations and multiple mitochondrial DNA deletions with variable clinical phenotypes in a Spanish population. Arch Neurol. 2006 Jan;63(1):107-11. [PubMed
]
- Horvath R, Hudson G, Ferrari G, Futterer N, Ahola S, Lamantea E, Prokisch H, Lochmuller H, McFarland R, Ramesh V, Klopstock T, Freisinger P, Salvi F, Mayr JA, Santer R, Tesarova M, Zeman J, Udd B, Taylor RW, Turnbull D, Hanna M, Fialho D, Suomalainen A, Zeviani M, Chinnery PF: Phenotypic spectrum associated with mutations of the mitochondrial polymerase gamma gene. Brain. 2006 Jul;129(Pt 7):1674-84. Epub 2006 Apr 18. [PubMed
]
- Naimi M, Bannwarth S, Procaccio V, Pouget J, Desnuelle C, Pellissier JF, Rotig A, Munnich A, Calvas P, Richelme C, Jonveaux P, Castelnovo G, Simon M, Clanet M, Wallace D, Paquis-Flucklinger V: Molecular analysis of ANT1, TWINKLE and POLG in patients with multiple deletions or depletion of mitochondrial DNA by a dHPLC-based assay. Eur J Hum Genet. 2006 Aug;14(8):917-22. Epub 2006 Apr 26. [PubMed
]
- Gago MF, Rosas MJ, Guimaraes J, Ferreira M, Vilarinho L, Castro L, Carpenter S: SANDO: two novel mutations in POLG1 gene. Neuromuscul Disord. 2006 Aug;16(8):507-9. Epub 2006 Aug 21. [PubMed
]
- Hudson G, Schaefer AM, Taylor RW, Tiangyou W, Gibson A, Venables G, Griffiths P, Burn DJ, Turnbull DM, Chinnery PF: Mutation of the linker region of the polymerase gamma-1 (POLG1) gene associated with progressive external ophthalmoplegia and Parkinsonism. Arch Neurol. 2007 Apr;64(4):553-7. [PubMed
]
- Taanman JW, Rahman S, Pagnamenta AT, Morris AA, Bitner-Glindzicz M, Wolf NI, Leonard JV, Clayton PT, Schapira AH: Analysis of mutant DNA polymerase gamma in patients with mitochondrial DNA depletion. Hum Mutat. 2009 Feb;30(2):248-54. [PubMed
]
- Giordano C, Powell H, Leopizzi M, De Curtis M, Travaglini C, Sebastiani M, Gallo P, Taylor RW, d'Amati G: Fatal congenital myopathy and gastrointestinal pseudo-obstruction due to POLG1 mutations. Neurology. 2009 Mar 24;72(12):1103-5. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
6257 |
| Enzyme 18 Name |
DNA polymerase iota |
| Enzyme 18 Synonyms |
- Eta2
- RAD30 homolog B
|
| Enzyme 18 Gene Name |
POLI |
| Enzyme 18 Protein Sequence |
>DNA polymerase iota
MELADVGAAASSQGVHDQVLPTPNASSRVIVHVDLDCFYAQVEMISNPELKDKPLGVQQK
YLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTRYREMSYKVTELLEEFSPVV
ERLGFDENFVDLTEMVEKRLQQLQSDELSAVTVSGHVYNNQSINLLDVLHIRLLVGSQIA
AEMREAMYNQLGLTGCAGVASNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNHIKEIP
GIGYKTAKCLEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQ
SFSEEDSFKKCSSEVEAKNKIEELLASLLNRVCQDGRKPHTVRLIIRRYSSEKHYGRESR
QCPIPSHVIQKLGTGNYDVMTPMVDILMKLFRNMVNVKMPFHLTLLSVCFCNLKALNTAK
KGLIDYYLMPSLSTTSRSGKHSFKMKDTHMEDFPKDKETNRDFLPSGRIESTRTRESPLD
TTNFSKEKDINEFPLCSLPEGVDQEVFKQLPVDIQEEILSGKSREKFQGKGSVSCPLHAS
RGVLSFFSKKQMQDIPINPRDHLSSSKQVSSVSPCEPGTSGFNSSSSSYMSSQKDYSYYL
DNRLKDERISQGPKEPQGFHFTNSNPAVSAFHSFPNLQSEQLFSRNHTTDSHKQTVATDS
HEGLTENREPDSVDEKITFPSDIDPQVFYELPEAVQKELLAEWKRTGSDFHIGHK
|
| Enzyme 18 Number of Residues |
715 |
| Enzyme 18 Molecular Weight |
80345.7 |
| Enzyme 18 Theoretical pI |
6.82 |
| Enzyme 18 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- damaged DNA binding
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA repair
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Involved in damaged DNA binding |
| Enzyme 18 Specific Function |
Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
5739208  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q9UNA4  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
POLI_HUMAN  |
| Enzyme 18 PDB ID |
1T3N  |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>2148 bp
ATGGAACTGGCGGACGTGGGGGCGGCAGCCAGCTCGCAGGGAGTTCATGATCAAGTGTTG
CCCACACCAAATGCTTCATCCAGAGTCATAGTACATGTGGATCTGGATTGCTTTTATGCA
CAAGTAGAAATGATCTCAAATCCAGAGCTAAAAGACAAACCTTTAGGGGTTCAACAGAAA
TATTTGGTGGTTACCTGCAACTATGAAGCTAGGAAACTTGGAGTTAAGAAACTTATGAAT
GTCAGAGATGCAAAAGAAAAGTGTCCACAGTTGGTATTAGTTAATGGAGAAGACCTGACC
CGCTACAGAGAAATGTCTTATAAGGTTACAGAATTACTGGAAGAATTTAGTCCAGTTGTT
GAGAGACTTGGATTTGATGAAAATTTTGTGGATCTAACAGAAATGGTTGAGAAGAGACTA
CAGCAGCTGCAAAGTGATGAACTTTCTGCGGTGACTGTGTCGGGTCATGTATACAATAAT
CAGTCTATAAACCTGCTTGACGTCTTGCACATCAGACTACTTGTTGGATCTCAGATTGCA
GCAGAGATGCGGGAAGCCATGTATAATCAGTTGGGGCTCACTGGCTGTGCTGGAGTGGCT
TCTAATAAACTGTTGGCAAAATTAGTTTCTGGTGTCTTTAAACCAAATCAACAAACAGTC
TTATTACCTGAAAGTTGTCAACATCTTATTCATAGTTTGAATCACATAAAGGAAATACCT
GGTATTGGCTATAAAACTGCCAAATGTCTTGAAGCACTGGGTATCAATAGTGTGCGTGAT
CTCCAAACCTTTTCACCCAAAATTTTAGAAAAAGAATTAGGAATTTCAGTTGCTCAGCGT
ATCCAAAAGCTCAGTTTTGGAGAGGATAACTCCCCTGTGATACTCTCAGGACCACCTCAG
TCCTTTAGTGAAGAAGATTCATTTAAAAAATGTTCATCTGAAGTTGAAGCTAAAAATAAG
ATTGAAGAACTACTTGCTAGTCTTTTAAACAGAGTATGCCAAGATGGAAGGAAGCCTCAT
ACAGTGAGATTAATAATCCGTCGGTATTCCTCTGAGAAGCACTATGGTCGTGAGAGTCGT
CAGTGCCCTATTCCTTCACATGTAATTCAGAAATTAGGGACAGGAAATTATGATGTGATG
ACCCCAATGGTTGATATACTTATGAAACTTTTTCGAAATATGGTGAATGTGAAGATGCCA
TTTCACCTTACCCTTCTAAGTGTGTGCTTCTGCAACCTTAAAGCACTAAATACTGCTAAG
AAAGGGCTTATTGATTATTATTTAATGCCATCATTATCAACTACTTCACGCTCTGGCAAG
CACAGTTTTAAAATGAAAGACACTCATATGGAAGATTTTCCCAAAGACAAAGAAACAAAC
CGGGATTTCCTACCAAGTGGAAGAATTGAAAGTACAAGAACTAGGGAGTCTCCACTAGAT
ACCACAAATTTTTCTAAAGAAAAAGACATTAATGAATTCCCACTCTGTTCACTTCCTGAA
GGTGTTGACCAAGAAGTCTTCAAGCAGCTTCCAGTAGATATTCAAGAAGAAATCCTTTCT
GGAAAATCTAGGGAAAAATTTCAAGGGAAAGGAAGTGTGAGTTGTCCATTACATGCCTCT
AGAGGAGTATTATCTTTCTTTTCTAAAAAACAAATGCAAGATATTCCCATAAATCCTAGA
GATCATTTATCCAGTAGCAAACAGGTATCCTCTGTATCTCCTTGTGAACCGGGAACATCA
GGCTTTAATAGCAGTAGTTCTTCTTACATGTCTAGCCAAAAGGATTATTCATATTATTTA
GATAATAGATTAAAAGATGAACGAATAAGTCAAGGACCTAAAGAACCTCAAGGATTCCAC
TTTACAAATTCAAACCCTGCTGTGTCTGCTTTTCATTCATTTCCAAACTTGCAGAGTGAG
CAACTTTTCTCCAGAAACCACACTACAGATAGCCATAAGCAAACAGTAGCAACAGACTCT
CATGAAGGACTTACAGAAAATAGAGAGCCAGATTCTGTTGATGAGAAAATTACTTTCCCT
TCTGACATTGATCCTCAAGTTTTCTATGAACTACCAGAAGCAGTACAAAAGGAACTGCTG
GCAGAGTGGAAGAGAACAGGATCAGATTTCCACATTGGACATAAATAA
|
| Enzyme 18 GenBank Gene ID |
AF140501  |
| Enzyme 18 GeneCard ID |
POLI  |
| Enzyme 18 GenAtlas ID |
POLI  |
| Enzyme 18 HGNC ID |
HGNC:9182  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
18q21.1 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- McDonald JP, Rapic-Otrin V, Epstein JA, Broughton BC, Wang X, Lehmann AR, Wolgemuth DJ, Woodgate R: Novel human and mouse homologs of Saccharomyces cerevisiae DNA polymerase eta. Genomics. 1999 Aug 15;60(1):20-30. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [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
]
- Tissier A, Frank EG, McDonald JP, Iwai S, Hanaoka F, Woodgate R: Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase iota. EMBO J. 2000 Oct 2;19(19):5259-66. [PubMed
]
- Bebenek K, Tissier A, Frank EG, McDonald JP, Prasad R, Wilson SH, Woodgate R, Kunkel TA: 5'-Deoxyribose phosphate lyase activity of human DNA polymerase iota in vitro. Science. 2001 Mar 16;291(5511):2156-9. [PubMed
]
- Frank EG, Tissier A, McDonald JP, Rapic-Otrin V, Zeng X, Gearhart PJ, Woodgate R: Altered nucleotide misinsertion fidelity associated with poliota-dependent replication at the end of a DNA template. EMBO J. 2001 Jun 1;20(11):2914-22. [PubMed
]
- Faili A, Aoufouchi S, Flatter E, Gueranger Q, Reynaud CA, Weill JC: Induction of somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase iota. Nature. 2002 Oct 31;419(6910):944-7. [PubMed
]
- Kannouche P, Fernandez de Henestrosa AR, Coull B, Vidal AE, Gray C, Zicha D, Woodgate R, Lehmann AR: Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells. EMBO J. 2003 Mar 3;22(5):1223-33. [PubMed
]
- Haracska L, Prakash L, Prakash S: A mechanism for the exclusion of low-fidelity human Y-family DNA polymerases from base excision repair. Genes Dev. 2003 Nov 15;17(22):2777-85. [PubMed
]
- Washington MT, Minko IG, Johnson RE, Wolfle WT, Harris TM, Lloyd RS, Prakash S, Prakash L: Efficient and error-free replication past a minor-groove DNA adduct by the sequential action of human DNA polymerases iota and kappa. Mol Cell Biol. 2004 Jul;24(13):5687-93. [PubMed
]
- Nair DT, Johnson RE, Prakash S, Prakash L, Aggarwal AK: Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing. Nature. 2004 Jul 15;430(6997):377-80. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
6258 |
| Enzyme 19 Name |
DNA polymerase epsilon subunit 2 |
| Enzyme 19 Synonyms |
- DNA polymerase II subunit 2
- DNA polymerase epsilon subunit B
|
| Enzyme 19 Gene Name |
POLE2 |
| Enzyme 19 Protein Sequence |
>DNA polymerase epsilon subunit 2
MAPERLRSRALSAFKLRGLLLRGEAIKYLTEALQSISELELEDKLEKIINAVEKQPLSSN
MIERSVVEAAVQECSQSVDETIEHVFNIIGAFDIPRFVYNSERKKFLPLLMTNHPAPNLF
GTPRDKAEMFRERYTILHQRTHRHELFTPPVIGSHPDESGSKFQLKTIETLLGSTTKIGD
AIVLGMITQLKEGKFFLEDPTGTVQLDLSKAQFHSGLYTEACFVLAEGWFEDQVFHVNAF
GFPPTEPSSTTRAYYGNINFFGGPSNTSVKTSAKLKQLEEENKDAMFVFLSDVWLDQVEV
LEKLRIMFAGYSPAPPTCFILCGNFSSAPYGKNQVQALKDSLKTLADIICEYPDIHQSSR
FVFVPGPEDPGFGSILPRPPLAESITNEFRQRVPFSVFTTNPCRIQYCTQEITVFREDLV
NKMCRNCVRFPSSNLAIPNHFVKTILSQGHLTPLPLYVCPVYWAYDYALRVYPVPDLLVI
ADKYDPFTTTNTECLCINPGSFPRSGFSFKVFYPSNKTVEDSKLQGF
|
| Enzyme 19 Number of Residues |
527 |
| Enzyme 19 Molecular Weight |
59536.6 |
| Enzyme 19 Theoretical pI |
6.30 |
| Enzyme 19 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA replication
- DNA-dependent DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 19 General Function |
Involved in DNA binding |
| Enzyme 19 Specific Function |
Participates in DNA repair and in chromosomal DNA replication |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1 [RN:R00379]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
32189369  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
P56282  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
DPOE2_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>1584 bp
ATGGCGCCGGAGCGGCTGCGGAGCCGGGCGCTCTCCGCCTTCAAGTTGCGGGGCTTGCTG
CTCCGTGGTGAAGCTATTAAGTACCTCACAGAAGCTCTTCAGTCTATCAGTGAATTAGAG
CTTGAAGATAAACTGGAAAAGATAATTAATGCAGTTGAGAAGCAACCCTTGTCATCAAAC
ATGATTGAACGATCTGTGGTGGAAGCAGCAGTCCAGGAATGCAGTCAGTCTGTTGATGAA
ACTATAGAGCACGTTTTCAATATCATAGGAGCATTTGATATTCCACGCTTTGTGTACAAT
TCAGAAAGAAAAAAATTTCTTCCTCTGTTAATGACCAACCACCCTGCACCAAATTTATTT
GGAACACCAAGAGATAAAGCAGAGATGTTTCGTGAGCGATATACCATTTTGCACCAGAGG
ACCCACAGGCATGAATTATTTACTCCTCCGGTGATAGGTTCTCACCCTGATGAAAGCGGA
AGCAAATTCCAGCTTAAAACAATAGAAACCTTATTGGGTAGTACAACCAAAATCGGAGAT
GCGATTGTTCTTGGAATGATAACGCAGTTAAAAGAGGGAAAATTTTTTCTGGAAGATCCT
ACTGGAACAGTCCAACTAGACCTTAGTAAAGCTCAGTTCCATAGTGGTTTATACACAGAG
GCATGCTTTGTCTTAGCAGAAGGTTGGTTTGAAGATCAAGTGTTTCATGTCAATGCCTTT
GGATTTCCACCCACTGAGCCCTCTAGTACTACTAGGGCATACTATGGAAATATTAATTTT
TTTGGAGGTCCTTCTAATACATCTGTGAAGACTTCTGCAAAACTAAAACAGCTAGAAGAG
GAGAATAAAGATGCTATGTTTGTGTTTTTATCTGATGTTTGGTTGGACCAGGTGGAAGTA
TTGGAAAAACTTCGCATAATGTTTGCTGGTTATTCACCAGCACCTCCAACCTGCTTTATT
CTGTGTGGTAATTTTTCATCTGCACCATATGGAAAAAATCAAGTTCAAGCTTTGAAAGAT
TCCCTAAAAACTTTGGCAGATATAATATGTGAATACCCAGATATTCACCAAAGTAGTCGT
TTTGTGTTTGTACCTGGTCCAGAGGATCCTGGATTTGGTTCCATCTTACCAAGGCCACCA
CTTGCTGAAAGCATCACTAATGAATTCAGACAAAGGGTACCATTTTCAGTTTTTACTACT
AATCCTTGCAGAATTCAGTACTGTACACAGGAAATTACTGTCTTCCGTGAAGACTTAGTA
AATAAAATGTGCAGAAACTGCGTCCGTTTTCCTAGCAGCAATTTGGCTATTCCTAATCAC
TTTGTAAAGACTATCTTATCCCAAGGACATCTGACTCCCCTACCTCTTTATGTCTGCCCA
GTGTATTGGGCATATGACTATGCTTTGAGAGTGTATCCTGTGCCCGATCTACTTGTCATT
GCAGACAAATATGATCCTTTCACTACGACAAATACCGAATGCCTCTGCATAAACCCTGGC
TCTTTTCCAAGAAGTGGATTTTCATTCAAAGTTTTTTATCCTTCTAATAAGACAGTAGAA
GATAGCAAACTTCAAGGCTTTTGA
|
| Enzyme 19 GenBank Gene ID |
NM_002692.3  |
| Enzyme 19 GeneCard ID |
POLE2  |
| Enzyme 19 GenAtlas ID |
POLE2  |
| Enzyme 19 HGNC ID |
HGNC:9178  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
14q21-q22 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Li Y, Asahara H, Patel VS, Zhou S, Linn S: Purification, cDNA cloning, and gene mapping of the small subunit of human DNA polymerase epsilon. J Biol Chem. 1997 Dec 19;272(51):32337-44. [PubMed
]
- Jokela M, Makiniemi M, Lehtonen S, Szpirer C, Hellman U, Syvaoja JE: The small subunits of human and mouse DNA polymerase epsilon are homologous to the second largest subunit of the yeast Saccharomyces cerevisiae DNA polymerase epsilon. Nucleic Acids Res. 1998 Feb 1;26(3):730-4. [PubMed
]
- Huang D, Jokela M, Tuusa J, Skog S, Poikonen K, Syvaoja JE: E2F mediates induction of the Sp1-controlled promoter of the human DNA polymerase epsilon B-subunit gene POLE2. Nucleic Acids Res. 2001 Jul 1;29(13):2810-21. [PubMed
]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [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
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
8075 |
| Enzyme 20 Name |
Uridine-cytidine kinase 2 |
| Enzyme 20 Synonyms |
- UCK 2
- Cytidine monophosphokinase 2
- Testis-specific protein TSA903
- Uridine monophosphokinase 2
|
| Enzyme 20 Gene Name |
UCK2 |
| Enzyme 20 Protein Sequence |
>Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
|
| Enzyme 20 Number of Residues |
261 |
| Enzyme 20 Molecular Weight |
29298.9 |
| Enzyme 20 Theoretical pI |
6.68 |
| Enzyme 20 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 20 General Function |
Involved in ATP binding |
| Enzyme 20 Specific Function |
Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- ATP + uridine = ADP + UMP [RN:R00964]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
18699734  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q9BZX2  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
UCK2_HUMAN  |
| Enzyme 20 PDB ID |
1XRJ  |
| Enzyme 20 PDB File |
Show |
| Enzyme 20 3D Structure |
|
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>786 bp
ATGGCCGGGGACAGCGAGCAGACCCTGCAGAACCACCAGCAGCCCAACGGCGGCGAGCCC
TTCCTTATAGGCGTCAGCGGGGGAACAGCTAGCGGCAAGTCTTCCGTGTGTGCTAAGATC
GTGCAGCTCCTGGGGCAGAATGAGGTGGACTATCGCCAGAAGCAGGTGGTCATCCTGAGC
CAGGATAGCTTCTACCGTGTCCTTACCTCGGAGCAGAAGGCCAAAGCCCTGAAGGGCCAG
TTCAACTTTGACCACCCGGATGCCTTTGACAATGAACTCATTCTCAAAACACTCAAAGAA
ATCACTGAAGGGAAAACAGTCCAGATCCCCGTGTATGACTTTGTCTCCCATTCCCGGAAG
GAGGAGACAGTTACTGTCTATCCCGCAGACGTGGTGCTCTTTGAAGGGATCCTGGCCTTC
TACTCCCAGGAGGTACGAGACCTGTTCCAGATGAAGCTTTTTGTGGATACAGATGCGGAC
ACCCGGCTCTCACGCAGAGTATTAAGGGACATCAGCGAGAGAGGCAGGGATCTTGAGCAG
ATTTTATCTCAGTACATTACGTTCGTCAAGCCTGCCTTTGAGGAATTCTGCTTGCCAACA
AAGAAGTATGCTGATGTGATCATCCCTAGAGGTGCAGATAATCTGGTGGCCATCAACCTC
ATCGTGCAGCACATCCAGGACATCCTGAATGGAGGGCCCTCCAAACGGCAGACCAATGGC
TGTCTCAACGGCTACACCCCTTCACGCAAGAGGCAGGCATCGGAGTCCAGCAGCAGGCCG
CATTGA
|
| Enzyme 20 GenBank Gene ID |
NM_012474.3  |
| Enzyme 20 GeneCard ID |
UCK2  |
| Enzyme 20 GenAtlas ID |
UCK2  |
| Enzyme 20 HGNC ID |
HGNC:12562  |
| Enzyme 20 Chromosome Location |
1 |
| Enzyme 20 Locus |
1q23 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Ozaki K, Kuroki T, Hayashi S, Nakamura Y: Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method. Genomics. 1996 Sep 1;36(2):316-9. [PubMed
]
- Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [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
]
- Koizumi K, Shimamoto Y, Azuma A, Wataya Y, Matsuda A, Sasaki T, Fukushima M: Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells. Int J Mol Med. 2001 Sep;8(3):273-8. [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
]
- 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
]
- Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F: Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase. Structure. 2004 May;12(5):751-64. [PubMed
]
- Appleby TC, Larson G, Cheney IW, Walker H, Wu JZ, Zhong W, Hong Z, Yao N: Structure of human uridine-cytidine kinase 2 determined by SIRAS using a rotating-anode X-ray generator and a single samarium derivative. Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):278-84. Epub 2005 Feb 24. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
13098 |
| Enzyme 21 Name |
Uridine-cytidine kinase-like 1 |
| Enzyme 21 Synonyms |
Not Available |
| Enzyme 21 Gene Name |
UCKL1 |
| Enzyme 21 Protein Sequence |
>Uridine-cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
|
| Enzyme 21 Number of Residues |
548 |
| Enzyme 21 Molecular Weight |
61140.4 |
| Enzyme 21 Theoretical pI |
7.40 |
| Enzyme 21 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 21 General Function |
Involved in ATP binding |
| Enzyme 21 Specific Function |
May contribute to UTP accumulation needed for blast transformation and proliferation |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- ATP + uridine = ADP + UMP [RN:R00964]
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
57863312  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9NWZ5  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
UCKL1_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1647 bp
ATGGCTGCGCCCCCGGCCCGCGCGGACGCTGATCCTTCGCCCACGTCGCCACCTACGGCC
CGAGACACACCAGGCCGGCAGGCTGAGAAAAGCGAGACCGCGTGCGAGGACCGCAGCAAT
GCAGAGTCCCTGGACAGGCTCCTGCCACCTGTGGGCACTGGGCGCTCTCCCCGGAAGCGG
ACCACCAGCCAGTGCAAGTCAGAGCCTCCCCTGCTGCGTACAAGCAAGCGTACCATCTAC
ACCGCCGGGCGGCCGCCCTGGTACAATGAACACGGCACGCAATCCAAAGAGGCCTTCGCC
ATCGGCTTGGGAGGCGGCAGTGCCTCTGGGAAGACCACTGTGGCCAGAATGATCATCGAG
GCCCTGGATGTGCCCTGGGTGGTCTTGCTGTCCATGGACTCCTTCTACAAGGTGCTGACT
GAGCAGCAGCAGGAACAGGCCGCACACAACAACTTCAACTTCGACCACCCAGATGCCTTT
GACTTCGACCTCATCATTTCCACCCTCAAGAAGCTGAAGCAGGGGAAGAGTGTCAAGGTG
CCCATTTATGACTTCACCACGCACAGCCGGAAGAAGGACTGGAAAACACTGTATGGTGCA
AACGTCATCATCTTTGAGGGCATCATGGCCTTTGCTGACAAGACACTGTTGGAGCTCCTG
GACATGAAGATCTTTGTGGACACAGACTCCGACATCCGCCTGGTACGGCGGCTGCGCCGG
GACATCAGTGAGCGCGGCCGGGACATCGAGGGTGTCATCAAGCAGTACAACAAGTTTGTC
AAGCCCTCCTTCGACCAGTACATCCAGCCCACCATGCGCCTGGCAGACATCGTGGTCCCC
AGAGGGAGCGGCAACACGGTGGCCATCGACCTGATTGTGCAGCACGTGCACAGCCAGCTG
GAGGAGCGTGAACTCAGCGTCAGGGCTGCGCTGGCCTCGGCACACCAGTGCCACCCGCTG
CCCCGGACGCTGAGCGTCCTGAAGAGCACGCCGCAGGTACGGGGCATGCACACCATCATC
AGGGACAAGGAGACCAGTCGCGACGAGTTCATCTTCTACTCCAAGAGACTGATGCGGCTG
CTCATCGAGCACGCGCTCTCCTTCCTGCCCTTTCAGGACTGCGTCGTACAGACCCCGCAG
GGGCAGGACTATGCGGGCAAGTGCTATGCGGGGAAGCAGATCACCGGTGTGTCCATTCTG
CGCGCCGGTGAAACCATGGAGCCCGCGCTGCGCGCTGTGTGCAAAGACGTGCGCATCGGC
ACCATCCTCATCCAGACCAACCAGCTTACCGGGGAGCCCGAGCTCCACTACCTGAGGCTG
CCCAAGGACATCAGCGATGACCACGTGATCCTCATGGACTGCACCGTGTCCACGGGCGCG
GCGGCCATGATGGCAGTGCGCGTGCTCCTGGACCACGACGTGCCTGAGGACAAGATCTTT
TTGCTGTCGCTGCTCATGGCAGAGATGGGCGTGCACTCAGTGGCCTATGCATTTCCGCGA
GTGAGAATCATCACCACGGCGGTGGACAAGCGGGTCAATGACCTTTTCCGCATCATCCCA
GGCATTGGGAACTTTGGCGACCGCTACTTTGGGACAGACGCGGTCCCCGATGGCAGTGAC
GAGGAGGAAGTGGCCTACACGGGTTAG
|
| Enzyme 21 GenBank Gene ID |
NM_017859.3  |
| Enzyme 21 GeneCard ID |
UCKL1  |
| Enzyme 21 GenAtlas ID |
UCKL1  |
| Enzyme 21 HGNC ID |
HGNC:15938  |
| Enzyme 21 Chromosome Location |
2 |
| Enzyme 21 Locus |
20q13.33 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Kashuba E, Kashuba V, Sandalova T, Klein G, Szekely L: Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase. BMC Cell Biol. 2002 Aug 29;3:23. Epub 2002 Aug 29. [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
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [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
]
- Fortier JM, Kornbluth J: NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase. J Immunol. 2006 Jun 1;176(11):6454-63. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [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
]
- 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
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
15191 |
| Enzyme 22 Name |
cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a) |
| Enzyme 22 Synonyms |
Not Available |
| Enzyme 22 Gene Name |
NME7 |
| Enzyme 22 Protein Sequence |
>cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a)
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
|
| Enzyme 22 Number of Residues |
376 |
| Enzyme 22 Molecular Weight |
42492 |
| Enzyme 22 Theoretical pI |
6.44 |
| Enzyme 22 GO Classification |
Not Available |
| Enzyme 22 General Function |
Nucleotide transport and metabolism |
| Enzyme 22 Specific Function |
Not Available |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
Not Available |
| Enzyme 22 Pfam Domain Function |
Not Available |
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
158254838  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
A8K3T6  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
A8K3T6_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
|
| Enzyme 22 GenBank Gene ID |
AK290701  |
| Enzyme 22 GeneCard ID |
A8K3T6  |
| Enzyme 22 GenAtlas ID |
Not Available |
| Enzyme 22 HGNC ID |
Not Available |
| Enzyme 22 Chromosome Location |
Not Available |
| Enzyme 22 Locus |
Not Available |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
Not Available |
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
15200 |
| Enzyme 23 Name |
Uridine kinase |
| Enzyme 23 Synonyms |
Not Available |
| Enzyme 23 Gene Name |
UCK1 |
| Enzyme 23 Protein Sequence |
>Uridine kinase
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
|
| Enzyme 23 Number of Residues |
201 |
| Enzyme 23 Molecular Weight |
22760.4 |
| Enzyme 23 Theoretical pI |
6.23 |
| Enzyme 23 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 23 General Function |
Involved in ATP binding |
| Enzyme 23 Specific Function |
ATP + cytidine = ADP + CMP |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
- ATP + uridine = ADP + UMP [RN:R00964]
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
57162374  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q5JT13  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
Q5JT13_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>606 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGGTGAGCGGCGGCACTGCCAGCGGGAAGTCGACCGTGTGT
GAGAAGATCATGGAGTTGCTGGGACAGAACGAGGTGGAACAGCGGCAGCGGAAGGTGGTC
ATCCTGAGCCAGGACAGGTTCTACAAGGTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTG
AAAGGACAGTACAATTTTGACCATCCAGATGCCTTTGATAATGATTTGATGCACAGGACT
CTGAAGAACATCGTGGAGGGCAAAACGGTGGAGGTGCCGACCTATGATTTTGTGACACAC
TCAAGGTTACCAGAGACCACGGTGGTCTACCCTGCGGACGTGGTTCTGTTTGAGGGCATC
TTGGTGTTCTACAGCCAGGAGATCCGGGACATGTTCCACCTGCGCCTCTTCGTGGACACC
GACTCCGACGTCAGGCTGTCTCGAAGAGACAAAGAAGTATGCCGATGTGATCATCCCGCG
AGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGACATTCTGAA
TGGTGA
|
| Enzyme 23 GenBank Gene ID |
AL358781  |
| Enzyme 23 GeneCard ID |
UCK1  |
| Enzyme 23 GenAtlas ID |
UCK1  |
| Enzyme 23 HGNC ID |
HGNC:14859  |
| Enzyme 23 Chromosome Location |
9 |
| Enzyme 23 Locus |
9q34.13 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
Not Available |
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
15252 |
| Enzyme 24 Name |
Myb-binding protein 1A |
| Enzyme 24 Synonyms |
Not Available |
| Enzyme 24 Gene Name |
MYBBP1A |
| Enzyme 24 Protein Sequence |
>Myb-binding protein 1A
MESRDPAQPMSPGEATQSGARPADRYGLLKHSREFLDFFWDIAKPEQETRLAATEKLLEY
LRGRPKGSEMKYALKRLITGLGVGRETARPCYSLALAQLLQSFEDLPLCSILQQIQEKYD
LHQVKKAMLRPALFANLFGVLALFQSGRLVKDQEALMKSVKLLQALAQYQNHLQEQPRKA
LVDILSEVSKATLQEILPEVLKADLNIILSSPEQLELFLLAQQKVPSKLKKLVGSVNLFS
DENVPRLVNVLKMAASSVKKDRKLPAIALDLLRLALKEDKFPRFWKEVVEQGLLKMQFWP
ASYLCFRLLGAALPLLTKEQLHLVMQGDVIRHYGEHVCTAKLPKQFKFAPEMDDYVGTFL
EGCQDDPERQLAVLVAFSSVTNQGLPVTPTFWRVVRFLSPPALQGYVAWLRAMFLQPDLD
SLVDFSTNNQKKAQDSSLHMPERAVFRLRKWIIFRLVSIVDSLHLEMEEALTEQVARFCL
FHSFFVTKKPTSQIPETKHPFSFPLENQAREAVSSAFFSLLQTLSTQFKQAPGQTQGGQP
WTYHLVQFADLLLNHSHNVTTVTPFTAQQRQAWDRMLQTLKELEAHSAEARAAAFQHLLL
LVGIHLLKSPAESCDLLGDIQTCIRKSLGEKPRRSRTKTIDPQEPPWVEVLVEILLALLA
QPSHLMRQVARSVFGHICSHLTPRALQLILDVLNPETSEDENDRVVVTDDSDERRLKGAE
DKSEEGEDNRSSESEEESEGEESEEEERDGDVDQGFREQLMTVLQAGKALGGEDSENEEE
LGDEAMMALDQSLASLFAEQKLRIQARRDEKNKLQKEKALRRDFQIRVLDLVEVLVTKQP
ENALVLELLEPLLSIIRRSLRSSSSKQEQDLLHKTARIFTHHLCRARRYCHDLGERAGAL
HAQVERLVQQAGRQPDSPTALYHFNASLYLLRVLKGNTAEGCVHETQEKQKAGTDPSHMP
TGPQAASCLDLNLVTRVYSTALSSFLTKRNSPLTVPMFLSLFSRHPVLCQSLLPILVQHI
TGPVRPRHQACLLLQKTLSMREVRSCFEDPEWKQLMGQVLAKVTENLRVLGEAQTKAQHQ
QALSSLELLNVLFRTCKHEKLTLDLTVLLGVLQGQQQSLQQGAHSTGSSRLHDLYWQAMK
TLGVQRPKLEKKDAKEIPSATQSPISKKRKKKGFLPETKKRKKRKSEDGTPAEDGTPAAT
GGSQPPSMGRKKRNRTKAKVPAQANGTPTTKSPAPGAPTRSPSTPAKSPKLQKKNQKPSQ
VNGAPGSPTEPAGQKQHQKALPKKGVLGKSPLSALARKKARLSLVIRSPSLLQSGAKKKA
QVRKAGKP
|
| Enzyme 24 Number of Residues |
1328 |
| Enzyme 24 Molecular Weight |
148853.2 |
| Enzyme 24 Theoretical pI |
9.87 |
| Enzyme 24 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- cellular macromolecule biosynthetic process
- macromolecule biosynthetic process
- metabolic process
- transcription
|
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in binding |
| Enzyme 24 Specific Function |
May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity) |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
6959304  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q9BQG0  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
MBB1A_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>3987 bp
ATGGAGAGCCGGGATCCCGCCCAGCCGATGTCGCCTGGAGAAGCGACGCAGAGTGGCGCC
CGGCCTGCCGACCGCTATGGCCTATTGAAGCACAGTCGCGAGTTCTTGGACTTCTTCTGG
GACATTGCGAAGCCTGAGCAGGAGACGCGACTTGCGGCCACGGAGAAGCTGCTGGAGTAT
CTGCGTGGCAGGCCGAAGGGGTCCGAGATGAAATATGCCCTGAAGCGTCTAATCACGGGA
CTCGGGGTCGGGCGAGAAACAGCCCGGCCCTGCTACAGTTTGGCCCTGGCACAGCTGTTA
CAGTCTTTTGAAGACCTCCCCTTGTGCAGCATCCTGCAGCAGATACAAGAAAAATATGAC
CTGCATCAGGTGAAGAAGGCAATGCTGAGACCTGCTCTCTTTGCAAACCTGTTTGGAGTG
CTCGCCCTCTTTCAGTCAGGTCGGCTGGTGAAGGACCAGGAGGCACTGATGAAGTCGGTG
AAGCTGCTGCAGGCCCTGGCCCAGTACCAAAACCACTTGCAGGAGCAGCCCCGGAAGGCC
CTGGTGGACATCCTCTCCGAGGTCTCGAAGGCCACATTGCAGGAGATCCTGCCGGAGGTC
CTCAAAGCCGACTTGAATATAATACTCAGCTCCCCTGAACAGCTAGAGCTCTTCCTCCTG
GCCCAGCAGAAGGTGCCCTCCAAGCTCAAGAAGCTGGTGGGATCCGTGAACCTATTCTCA
GATGAGAATGTCCCCAGGCTGGTGAATGTGCTGAAGATGGCCGCCTCCTCTGTGAAGAAG
GACCGCAAGCTGCCCGCCATTGCTCTGGACCTGCTCCGCCTGGCGCTCAAGGAAGACAAG
TTCCCACGGTTCTGGAAGGAGGTGGTGGAACAAGGGCTGCTGAAGATGCAGTTCTGGCCA
GCCAGCTACCTGTGTTTCCACCTGCTGGGCGCGGCCCTGCCCCTGCTGACCAAGGAGCAG
CTGCACCTGGTGATGCAGGGAGACGTGATCCGCCATTACGGGGAGCACGTGTGCACTGCT
AAGCTCCCAAAGCAGTTCAAGTTTGCCCCAGAGATGGACGATTACGTGGGCACCTTCCTA
GAGGGGTGCCAGGATGACCCTGAGCGGCAGCTGGCCGTGCTAGTGGCCTTCTCATCTGTC
ACCAACCAAGGCCTCCCTGTCACGCCTACTTTCTGGCGGGTCGTGCGGTTCCTGAGCCCT
CCGGCCCTGCAGGGCTATGTGGCCTGGCTGCGGGCCATGTTTCTCCAGCCAGACCTGGAC
TCCTTGGTTGACTTCAGCACCAACAACCAGAAGAAAGCCCAGGATTCATCGCTCCACATG
CCTGAGCGAGCTGTGTTCCGGCTGAGGAAATGGATCATCTTTCGATTGGTGAGCATTGTG
GACAGCCTGCACCTGGAGATGGAGGAGGCCTTGACTGAGCAGGTGGCCAGGTTTTGTTTG
TTCCACTCGTTCTTTGTCACAAAGAAGCCCACATCCCAGATCCCTGAGACAAAGCACCCG
TTCTCCTTCCCTTTGGAAAACCAGGCCCGAGAGGCTGTCAGCAGTGCCTTCTTCAGTCTG
TTGCAGACCCTCAGCACGCAGTTCAAGCAGGCACCGGGCCAGACCCAGGGTGGGCAGCCC
TGGACCTACCACCTGGTGCAATTCGCAGACCTCCTGTTGAATCACAGCCACAACGTGACC
ACCGTGACACCCTTCACTGCGCAGCAGCACCAGGCCTGGGACCGGATGCTGCAGACTCTG
AAGGAGCTGGAGGCCCACTCCGCAGAGGCCAGGGCTGCTGCCTTCCAGCACCTTCTGCTC
TTCGTGGGCATCCACCTCCTCAAGTCCCCTGCAGAGAGCTGTGACCTGCTGGGTGACATC
CAGACCTGCATCAGGAAAAGTCTGGGAGAGAAGCCCCGCCGGAGCCGCACCAAGACCATC
GACCCCCAGGAACCCCCGTGGGTAGAGGTGCTGGTGGAGATCTTGCTGGCCCTGTTGGCC
CAGCCCAGCCACCTCATGCGCCAGGTGGCCCGGAGCGTGTTTGGCCACATCTGCTCCCAC
CTGACCCCGCGTGCCCTGCAGCTAATTCTGGATGTGCTGAACCCCGAGACCAGTGAGGAT
GAGAATGACCGTGTGGTGGTGACGGACGATTCTGATGAGCGGCGGCTGAAGGGTGCAGAG
GACAAGAGCGAGGAAGGTGAGGACAACAGAAGCTCAGAGAGTGAAGAGGAGAGCGAGGGG
GAGGAGAGCGAGGAGGAGGAGCGCGACGGGGACGTGGATCAGGGCTTCCGGGAACAGCTG
ATGACCGTGCTGCAGGCTGGGAAGGCGCTGGGTGGAGAGGACAGTGAGAACGAGGAGGAG
CTGGGGGATGAGGCCATGATGGCCCTGGACCAGAGCCTCGCCAGCCTCTTTGCCGAGCAG
AAGCTGCGTATCCAGGCCCGGCGAGACGAGAAGAACAAGCTGCAGAAGGAGAAGGCTCTG
CGGCGCGACTTCCAGATCCGGGTGCTGGACCTGGTGGAGGTGCTAGTGACCAAGCAGCCC
GAGAATGCCCTGGTCCTGGAGCTGCTGGAGCCGCTGCTGAGCATCATCCGGCGCAGCCTG
CGCAGCAGCAGCTCCAAACAGGAGCAGGACCTTCTGCACAAGACGGCGCGCATCTTCACG
CATCACCTGTGCCGTGCCCGGCGCTACTGCCACGACTTGGGTGAGCGCGCAGGGGCCCTG
CACGCCCAGGTGGAGCGGTTGGTGCAGCAGGCTGGCCGCCAGCCCGACTCCCCCACCGCC
CTCTACCACTTCAACGCCTCTCTCTACCTGCTCCGGGTCTTGAAGGGCAACACTGCTGAG
GGCTGCGTGCATGAGACACAGGAGAAGCAGAAAGCTGGCACTGACCCCAGCCACATGCCC
ACGGGCCCGCAGGCTGCCAGCTGCTTGGACTTGAACCTGGTGACCCGGGTGTACTCGACA
GCACTGAGCTCCTTCCTGACCAAGCGCAACAGCCCCCTCACAGTTCCCATGTTCCTCAGC
CTCTTCTCCCGGCACCCGGTGCTCTGTCAGAGCCTGCTCCCCATCCTGGTCCAGCATATC
ACGGGCCCGGTGCGGCCCCGTCATCAGGCCTGCCTGCTGCTCCAGAAGACCCTGTCCATG
CGGGAGGTGAGGTCGTGCTTTGAGGACCCCGAGTGGAAGCAGCTGATGGGCCAGGTCCTA
GCAAAGGTCACCGAGAACTTGCGCGTGCTGGGGGAGGCGCAGACCAAGGCGCAGCATCAG
CAGGCACTGTCCTCCCTGGAGCTGCTCAACGTTCTCTTCAGGACCTGCAAACATGAGAAG
CTGACCTTGGACCTGACGGTGCTCCTGGGTGTGCTGCAGGGGCAACAGCAGAGCCTACAG
CAGGGGGCACACTCCACCGGCTCCAGCCGCCTGCACGACCTCTACTGGCAGGCCATGAAA
ACCCTGGGAGTCCAGCGCCCCAAGTTGGAGAAGAAGGATGCCAAGGAGATCCCCAGTGCC
ACCCAGAGCCCCATCAGTAAGAAGCGGAAGAAAAAGGGATTCTTGCCAGAGACGAAGAAG
CGCAAGAAACGCAAGTCAGAGGATGGCACGCCAGCGGAGGATGGCACACCTGCAGCCACC
GGCGGGAGCCAGCCCCCCAGCATGGGCAGGAAGAAGAGGAACAGGACAAAGGCTAAGGTC
CCAGCCCAGGCAAACGGGACGCCAACCACCAAGAGTCCAGCCCCTGGCGCCCCCACCCGG
AGCCCCAGCACCCCTGCCAAATCCCCAAAACTGCAGAAGAAAAACCAGAAGCCGTCCCAG
GTGAATGGAGCTCCCGGGTCCCCCACGGAACCTGCAGGCCAAAAGCAGCATCAGAAGGCT
CTTCCCAAAAAGGGGGTCTTGGGCAAATCACCACTGTCCGCGCTGGCACGGAAAAAGGCA
AGGCTGTCTTTGGTCATCAGGAGTCCCAGCCTGCTTCAGAGTGGGGCCAAGAAGAAAGCA
CAGGTGAGGAAGGCAGGGAAGCCCTGA
|
| Enzyme 24 GenBank Gene ID |
AF147709  |
| Enzyme 24 GeneCard ID |
MYBBP1A  |
| Enzyme 24 GenAtlas ID |
MYBBP1A  |
| Enzyme 24 HGNC ID |
HGNC:7546  |
| Enzyme 24 Chromosome Location |
1 |
| Enzyme 24 Locus |
17p13.3 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Keough R, Woollatt E, Crawford J, Sutherland GR, Plummer S, Casey G, Gonda TJ: Molecular cloning and chromosomal mapping of the human homologue of MYB binding protein (P160) 1A (MYBBP1A) to 17p13.3. Genomics. 1999 Dec 15;62(3):483-9. [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
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [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
]
- Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ: Functional proteomic analysis of human nucleolus. Mol Biol Cell. 2002 Nov;13(11):4100-9. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Cavellan E, Asp P, Percipalle P, Farrants AK: The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription. J Biol Chem. 2006 Jun 16;281(24):16264-71. Epub 2006 Apr 9. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [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
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [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
]
- 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
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [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
]
- 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 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
15253 |
| Enzyme 25 Name |
DNA polymerase theta |
| Enzyme 25 Synonyms |
Not Available |
| Enzyme 25 Gene Name |
POLQ |
| Enzyme 25 Protein Sequence |
>DNA polymerase theta
MNLLRRSGKRRRSESGSDSFSGSGGDSSASPQFLSGSVLSPPPGLGRCLKAAAAGECKPT
VPDYEIDKLLLANWGLPKAVLEKYHSFGVKKMFEWQAECLLLGQVLEGKNLVYSAPTSAG
KTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPSRH
FSSLDIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYI
TRKSASCQADLASSLSNAVQIVGMSATLPNLELVASWLNAELYHTDFRPVPLLESVKVGN
SIYDSSMKLVREFEPMLQVKGDEDHVVSLCYETICDNHSVLLFCPSKKWCEKLADIIARE
FYNLHHQAEGLVKPSECPPVILEQKELLEVMDQLRRLPSGLDSVLQKTVPWGVAFHHAGL
TFEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPIFGGRPLDILTYKQMVGR
AGRKGVDTVGESILICKNSEKSKGIALLQGSLKPVRSCLQRREGEEVTGSMIRAILEIIV
GGVASTSQDMHTYAACTFLAASMKEGKQGIQRNQESVQLGAIEACVMWLLENEFIQSTEA
SDGTEGKVYHPTHLGSATLSSSLSPADTLDIFADLQRAMKGFVLENDLHILYLVTPMFED
WTTIDWYRFFCLWEKLPTSMKRVAELVGVEEGFLARCVKGKVVARTERQHRQMAIHKRFF
TSLVLLDLISEVPLREINQKYGCNRGQIQSLQQSAAVYAGMITVFSNRLGWHNMELLLSQ
FQKRLTFGIQRELCDLVRVSLLNAQRARVLYASGFHTVADLARANIVEVEVILKNAVPFK
SARKAVDEEEEAVEERRNMRTIWVTGRKGLTEREAAALIVEEARMILQQDLVEMGVQWNP
CALLHSSTCSLTHSESEVKEHTFISQTKSSYKKLTSKNKSNTIFSDSYIKHSPNIVQDLN
KSREHTSSFNCNFQNGNQEHQRCSIFRARKRASLDINKEKPGASQNEGKTSDKKVVQTFS
QKTKKAPLNFNSEKMSRSFRSWKRRKHLKRSRDSSPLKDSGACRIHLQGQTLSNPSLCED
PFTLDEKKTEFRNSGPFAKNVSLSGKEKDNKTSFPLQIKQNCSWNITLTNDNFVEHIVTG
SQSKNVTCQATSVVSEKGRGVAVEAEKINEVLIQNGSKNQNVYMKHHDIHPINQYLRKQS
HEQTSTITKQKNIIERQMPCEAVSSYINRDSNVTINCERIKLNTEENKPSHFQALGDDIS
RTVIPSEVLPSAGAFSKSEGQHENFLNISRLQEKTGTYTTNKTKNNHVSDLGLVLCDFED
SFYLDTQSEKIIQQMATENAKLGAKDTNLAAGIMQKSLVQQNSMNSFQKECHIPFPAEQH
PLGATKIDHLDLKTVGTMKQSSDSHGVDILTPESPIFHSPILLEENGLFLKKNEVSVTDS
QLNSFLQGYQTQETVKPVILLIPQKRTPTGVEGECLPVPETSLNMSDSLLFDSFSDDYLV
KEQLPDMQMKEPLPSEVTSNHFSDSLCLQEDLIKKSNVNENQDTHQQLTCSNDESIIFSE
MDSVQMVEALDNVDIFPVQEKNHTVVSPRALELSDPVLDEHHQGDQDGGDQDERAEKSKL
TGTRQNHSFIWSGASFDLSPGLQRILDKVSSPLENEKLKSMTINFSSLNRKNTELNEEQE
VISNLETKQVQGISFSSNNEVKSKIEMLENNANHDETSSLLPRKESNIVDDNGLIPPTPI
PTSASKLTFPGILETPVNPWKTNNVLQPGESYLFGSPSDIKNHDLSPGSRNGFKDNSPIS
DTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIR
SLTSSKTATIGSRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKE
QKHSEISASLVPPSLDPSLTLKDRMWYLQSCLRKESDKECSVVIYDFIQSYKILLLSCGI
SLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQSLGLNAGSEH
SGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECE
SQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGS
TRRGIDNGRKLRLGRQFSTSKDVLNKLKALHPLPGLILEWRRITNAITKVVFPLQREKCL
NPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQAVGKGLLPM
GRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILA
HLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGE
QMGIKENDAACYIDSFKSRYTGINQFMTETVKNCKRDGFVQTILGRRRYLPGIKDNNPYR
KAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQSDRTGLSRKR
KLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGA
SWGELKDFDV
|
| Enzyme 25 Number of Residues |
2590 |
| Enzyme 25 Molecular Weight |
289656.8 |
| Enzyme 25 Theoretical pI |
7.42 |
| Enzyme 25 GO Classification |
| Function |
- ATP binding
- ATP-dependent helicase activity
- ATPase activity
- ATPase activity, coupled
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- helicase activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
- nucleic acid binding
- nucleoside binding
- nucleoside-triphosphatase activity
- nucleotidyltransferase activity
- purine nucleoside binding
- pyrophosphatase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 25 General Function |
Involved in DNA binding |
| Enzyme 25 Specific Function |
Not Available |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
76364226  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q6VMB5  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
Q6VMB5_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>7773 bp
ATGAATCTTCTGCGTCGGAGTGGGAAACGGCGGCGTTCAGAATCAGGCTCAGATTCGTTC
TCGGGAAGCGGCGGTGACAGCAGTGCCAGCCCCCAGTTCCTCTCCGGGTCCGTGCTGAGC
CCGCCGCCCGGCCTTGGTCGCTGCCTGAAGGCCGCAGCTGCAGGAGAATGCAAGCCTACA
GTTCCTGACTACGAAATAGACAAGCTACTATTGGCAAACTGGGGACTTCCTAAAGCAGTT
CTGGAAAAATACCACAGTTTTGGTGTAAAAAAGATGTTTGAATGGCAGGCAGAGTGCCTT
TTGCTTGGACAAGTCCTGGAAGGAAAGAATTTAGTTTATTCAGCTCCTACAAGTGCTGGG
AAGACTCTTGTGGCAGAATTACTTATTTTGAAGCGGGTTTTGGAAATGCGGAAGAAAGCT
TTGTTTATTCTTCCCTTTGTTTCTGTGGCTAAAGAGAAGAAATACTACCTCCAGAGTCTG
TTTCAGGAAGTAGGAATAAAAGTAGACGGTTATATGGGCAGCACCTCTCCATCAAGGCAT
TTCTCTTCATTGGATATTGCAGTCTGCACAATTGAGAGAGCCAATGGTCTGATCAATCGC
CTCATAGAGGAAAATAAGATGGATCTGTTAGGAATGGTGGTTGTGGATGAATTACATATG
CTGGGAGACTCTCACCGAGGGTATCTGCTGGAACTTTTGCTGACCAAGATTTGCTATATT
ACTCGGAAATCAGCATCTTGTCAGGCAGATCTAGCCAGTTCTCTGTCTAATGCTGTGCAA
ATCGTTGGCATGAGTGCTACCCTTCCTAATTTGGAGCTTGTGGCTTCCTGGTTGAATGCT
GAACTCTACCATACCGACTTTCGCCCTGTACCGCTTTTGGAGTCAGTAAAAGTTGGAAAT
TCCATATATGACTCTTCAATGAAACTTGTGAGGGAATTTGAGCCCATGCTTCAAGTGAAG
GGAGATGAGGACCATGTTGTTAGCTTATGTTATGAGACGATTTGTGATAACCATTCAGTA
TTACTTTTTTGTCCATCAAAGAAATGGTGTGAGAAGCTGGCAGATATCATTGCTCGAGAG
TTTTATAATCTACATCATCAAGCTGAGGGTTTGGTGAAACCCTCTGAATGCCCACCAGTA
ATTCTGGAACAAAAAGAACTCCTGGAAGTGATGGATCAGTTAAGACGTTTGCCTTCAGGA
CTGGACTCTGTATTACAGAAAACTGTACCATGGGGAGTAGCATTTCATCATGCAGGTCTT
ACTTTTGAGGAGAGGGATATCATTGAAGGAGCCTTTCGTCAAGGTCTCATTCGGGTCTTG
GCGGCAACTTCTACTCTTTCTTCTGGGGTGAATTTACCTGCACGTCGTGTGATTATTCGA
ACCCCTATTTTTGGTGGTCGACCTCTAGATATTCTTACTTATAAGCAGATGGTTGGTCGT
GCTGGCAGGAAAGGAGTGGACACAGTAGGCGAGAGTATCTTAATTTGTAAGAACTCTGAG
AAATCAAAAGGCATAGCTCTCCTTCAGGGTTCTCTAAAGCCTGTTCGCAGCTGTCTGCAA
AGACGAGAAGGAGAAGAAGTAACTGGCAGCATGATACGAGCTATTCTGGAGATAATAGTT
GGTGGAGTGGCAAGTACATCACAAGATATGCATACTTATGCTGCCTGCACATTTTTGGCT
GCAAGTATGAAAGAAGGGAAGCAAGGAATTCAGAGAAATCAAGAGTCTGTTCAGCTTGGA
GCGATTGAGGCCTGTGTGATGTGGCTACTAGAAAATGAATTCATCCAGAGTACAGAAGCC
AGTGATGGAACAGAAGGAAAGGTGTATCATCCAACACATCTTGGTTCGGCCACTCTTTCT
TCTTCACTTTCTCCAGCTGATACTTTAGATATTTTTGCTGACCTGCAAAGAGCAATGAAG
GGCTTTGTTTTAGAGAATGATCTTCATATTCTCTATCTGGTTACACCTATGTTTGAGGAT
TGGACTACTATTGATTGGTATCGATTTTTCTGTTTATGGGAGAAGTTGCCAACTTCAATG
AAAAGGGTGGCAGAGCTAGTGGGAGTTGAAGAGGGGTTCTTGGCCCGTTGTGTGAAAGGA
AAAGTAGTAGCCAGAACTGAGAGACAGCATCGACAAATGGCCATCCATAAAAGGTTTTTC
ACCAGTCTTGTGCTATTAGATTTAATCAGTGAAGTTCCCTTAAGGGAAATAAATCAGAAA
TATGGATGCAATCGTGGGCAGATTCAATCTTTGCAACAGTCAGCTGCTGTTTATGCAGGG
ATGATTACAGTATTTTCCAACCGTCTGGGCTGGCACAACATGGAACTACTACTTTCCCAA
TTTCAGAAGCGTCTTACGTTTGGCATCCAGAGGGAGCTGTGTGACCTGGTTCGGGTATCC
TTACTAAATGCTCAGAGAGCCAGGGTTCTCTATGCTTCTGGCTTTCATACTGTGGCAGAC
CTTGCTAGAGCAAATATTGTGGAGGTGGAGGTGATTCTGAAAAATGCTGTGCCTTTCAAA
AGTGCCCGGAAGGCAGTGGATGAGGAAGAGGAAGCAGTTGAAGAACGTCGCAATATGCGA
ACTATCTGGGTGACTGGCAGAAAAGGTTTAACTGAAAGGGAAGCAGCAGCCCTTATAGTG
GAAGAAGCCAGAATGATTCTGCAGCAGGACTTAGTTGAAATGGGAGTGCAATGGAATCCA
TGTGCCCTGTTACATTCTAGTACATGCTCATTGACTCATAGTGAGTCCGAAGTAAAGGAA
CACACATTTATATCCCAAACTAAGAGTTCTTATAAAAAATTAACATCAAAGAACAAAAGT
AACACAATATTTAGTGATTCTTATATTAAGCATTCACCAAATATAGTGCAAGACTTAAAT
AAAAGTAGAGAGCATACAAGTTCCTTTAATTGTAATTTCCAGAATGGGAATCAAGAACAT
CAGAGATGTTCCATTTTCAGAGCAAGAAAACGGGCCTCTTTAGATATAAATAAAGAGAAG
CCAGGAGCCTCTCAGAATGAGGGGAAAACAAGTGATAAGAAAGTTGTTCAGACTTTTTCA
CAGAAAACAAAAAAGGCACCTTTGAATTTCAATTCAGAAAAGATGAGCAGAAGTTTTCGA
TCTTGGAAACGTAGAAAGCATCTAAAGCGATCTAGGGACAGCAGCCCCCTGAAAGACTCT
GGAGCGTGTAGAATCCATTTACAAGGACAGACTCTGTCTAATCCTAGTCTTTGTGAAGAC
CCGTTTACCTTAGATGAGAAGAAAACGGAATTTAGAAATTCAGGGCCATTTGCTAAAAAT
GTATCTTTGAGTGGTAAGGAAAAAGATAATAAAACATCATTCCCATTACAAATAAAGCAA
AATTGTTCATGGAACATAACACTAACTAATGATAATTTTGTGGAGCATATTGTCACAGGA
TCTCAGAGTAAAAATGTGACTTGTCAGGCCACTAGTGTGGTTAGTGAAAAGGGCAGAGGA
GTAGCTGTTGAGGCAGAAAAAATAAATGAAGTGCTGATACAAAATGGTTCAAAAAACCAG
AATGTTTATATGAAACACCATGACATCCATCCAATTAACCAGTACCTGCGAAAGCAATCT
CATGAACAGACAAGCACTATTACCAAACAGAAAAATATAATAGAGAGACAAATGCCCTGT
GAAGCAGTCAGTAGTTACATAAATAGAGACTCAAATGTTACTATCAATTGTGAAAGGATA
AAGCTTAATACAGAGGAAAATAAACCAAGTCATTTTCAGGCATTAGGAGATGATATAAGC
AGAACTGTGATACCCAGTGAAGTACTTCCATCAGCTGGAGCATTTAGCAAATCAGAAGGC
CAGCATGAGAATTTTCTAAATATTTCTAGACTACAAGAAAAAACAGGTACTTATACAACA
AACAAAACTAAAAATAATCATGTTTCTGACTTAGGTTTAGTCCTCTGTGATTTTGAAGAT
AGTTTCTATCTGGATACTCAGTCAGAGAAAATAATACAACAGATGGCAACTGAAAATGCC
AAACTAGGAGCAAAGGACACCAACCTGGCAGCAGGGATAATGCAGAAGAGCTTAGTCCAA
CAGAACTCAATGAACTCTTTTCAGAAGGAGTGTCACATTCCTTTTCCTGCTGAACAGCAC
CCTCTAGGAGCGACTAAGATAGATCATTTGGACCTTAAGACTGTAGGTACTATGAAACAA
AGCAGTGATTCACATGGGGTTGATATCCTGACTCCAGAAAGCCCGATTTTCCATTCTCCA
ATACTATTGGAGGAAAATGGTCTTTTTTTAAAAAAGAATGAAGTTTCTGTTACTGATTCA
CAATTAAATAGTTTTCTTCAAGGTTATCAAACACAAGAAACTGTGAAACCAGTTATACTT
CTGATTCCTCAAAAGAGAACTCCCACTGGTGTAGAAGGAGAATGTCTTCCAGTTCCTGAA
ACAAGTTTGAATATGAGTGATAGTTTACTATTTGATAGCTTCAGTGATGACTATCTAGTA
AAAGAACAATTACCTGATATGCAAATGAAAGAACCCCTTCCTTCAGAAGTAACATCAAAC
CATTTTAGTGATTCTCTGTGTCTACAAGAAGACCTAATTAAAAAATCAAATGTAAATGAG
AATCAAGATACCCACCAGCAGTTGACTTGTTCCAATGATGAATCTATTATATTTTCAGAA
ATGGATTCTGTTCAGATGGTTGAAGCTTTGGACAATGTGGATATATTTCCTGTCCAAGAG
AAGAATCATACTGTAGTATCTCCTAGAGCATTAGAACTAAGTGATCCAGTACTTGATGAG
CACCACCAAGGTGATCAAGATGGAGGAGATCAAGATGAAAGGGCTGAAAAATCAAAATTA
ACTGGGACCAGGCAAAATCATTCATTCATATGGTCAGGGGCATCATTTGATCTAAGTCCA
GGACTGCAAAGGATTTTAGATAAAGTATCCAGTCCTCTAGAAAATGAAAAGCTAAAATCA
ATGACTATAAACTTTTCCAGTTTGAATAGAAAAAATACAGAGTTAAATGAAGAACAAGAA
GTTATTTCAAACTTGGAGACAAAACAAGTGCAGGGAATTTCATTTTCTTCTAATAATGAA
GTAAAAAGCAAGATTGAGATGCTAGAAAACAATGCCAATCATGATGAAACCTCATCCCTC
TTACCTCGTAAAGAAAGTAATATAGTTGATGATAATGGTCTCATTCCTCCTACACCCATT
CCAACATCTGCTTCTAAGCTGACATTTCCAGGGATTCTTGAAACACCTGTAAACCCTTGG
AAAACTAATAATGTTTTACAACCTGGTGAAAGTTATTTATTTGGCTCACCTTCAGATATT
AAAAACCACGATTTAAGTCCAGGGAGTAGAAATGGGTTCAAAGACAACAGCCCTATTAGT
GACACAAGCTTTTCACTTCAGTTATCACAGGATGGATTACAGTTAACTCCAGCCTCAAGC
AGTTCAGAAAGTTTGTCCATAATTGATGTAGCAAGTGACCAAAATCTTTTCCAAACATTC
ATTAAGGAGTGGCGGTGCAAAAAGCGATTTTCCATCTCACTGGCTTGTGAAAAGATTAGA
AGTTTGACATCTTCTAAAACTGCTACTATTGGCAGTAGGTTTAAGCAAGCTAGCTCACCT
CAGGAAATTCCTATTAGAGATGATGGATTTCCCATTAAAGGTTGTGATGACACCTTGGTG
GTTGGACTGGCAGTATGCTGGGGTGGAAGGGATGCCTATTATTTTTCACTGCAGAAGGAA
CAAAAGCATTCTGAAATTAGTGCCAGTTTGGTTCCACCTTCTTTAGATCCAAGCCTGACT
TTGAAAGACAGGATGTGGTACCTTCAATCTTGCTTGCGAAAGGAATCTGATAAAGAATGT
TCTGTTGTCATCTATGACTTCATCCAGAGCTATAAAATTCTTCTTCTTTCTTGTGGCATC
TCCTTGGAGCAAAGTTATGAAGATCCTAAGGTGGCATGCTGGTTACTAGATCCAGATTCT
CAGGAGCCGACTCTTCATAGCATAGTTACCAGTTTTCTTCCTCATGAGCTTCCACTCCTA
GAAGGGATGGAGACCAGCCAAGGGATTCAAAGCCTGGGGCTAAATGCTGGCAGTGAGCAT
TCTGGGCGATACAGAGCATCTGTGGAGTCCATTCTCATCTTCAACTCTATGAATCAGCTC
AACTCTTTGTTGCAGAAGGAAAACCTTCAAGATGTTTTCCGTAAGGTGGAAATGCCCTCT
CAGTACTGCTTGGCCTTGCTAGAACTAAATGGAATTGGCTTTAGTACTGCAGAATGTGAA
AGTCAGAAACATATAATGCAAGCCAAGCTGGATGCAATTGAGACCCAGGCCTATCAACTA
GCTGGCCACAGTTTTTCTTTCACCAGTTCAGATGACATCGCTGAGGTTTTATTTTTGGAA
TTGAAGTTGCCCCCAAATAGAGAGATGAAAAACCAAGGCAGCAAGAAAACTCTGGGTTCT
ACCAGAAGAGGGATTGACAATGGACGCAAGCTAAGGCTGGGAAGACAGTTCAGCACTAGT
AAGGACGTTTTAAATAAATTAAAGGCATTACATCCTTTACCAGGCTTGATATTAGAATGG
AGAAGAATCACTAATGCTATTACCAAAGTGGTCTTTCCCCTTCAGCGGGAAAAGTGTCTT
AATCCTTTTCTTGGAATGGAAAGAATCTATCCTGTATCACAGTCGCACACTGCTACAGGA
CGAATAACCTTTACAGAACCAAATATTCAGAATGTGCCAAGAGATTTTGAAATCAAAATG
CCAACACTAGTAGGAGAAAGCCCACCTTCTCAAGCTGTAGGCAAAGGCCTACTTCCCATG
GGCAGAGGAAAATATAAGAAGGGTTTCAGCGTGAATCCTAGATGCCAGGCACAGATGGAG
GAGAGAGCTGCAGACAGAGGAATGCCATTTTCAATTAGCATGCGACATGCCTTTGTGCCT
TTCCCAGGTGGTTCAATACTGGCTGCTGACTACTCTCAGCTTGAACTGAGGATCTTGGCT
CATTTATCCCATGATCGTCGTCTCATTCAAGTGTTAAACACTGGAGCTGATGTTTTCAGG
AGCATTGCAGCAGAGTGGAAGATGATTGAGCCAGAGTCTGTTGGGGATGATCTGAGGCAG
CAGGCAAAACAGATTTGCTATGGGATCATTTATGGAATGGGAGCTAAATCTTTGGGAGAG
CAGATGGGCATTAAAGAAAATGATGCTGCATGCTATATTGACTCCTTCAAATCCAGATAC
ACAGGGATTAATCAATTCATGACAGAGACAGTGAAGAATTGTAAAAGAGACGGATTTGTT
CAGACCATTTTGGGAAGGCGTAGATATTTGCCAGGAATCAAAGACAACAACCCTTATCGT
AAAGCTCACGCTGAGCGTCAAGCTATCAACACAATAGTCCAAGGATCAGCAGCTGATATT
GTCAAAATAGCCACAGTTAACATTCAGAAGCAATTAGAGACCTTCCACTCAACCTTCAAA
TCCCATGGTCATCGAGAGGGTATGCTCCAAAGTGACCGAACAGGATTGTCACGAAAGAGA
AAACTGCAAGGGATGTTCTGCCCAATCAGAGGAGGCTTCTTCATCCTTCAACTCCATGAT
GAACTCCTATATGAAGTGGCAGAAGAAGATGTTGTTCAGGTAGCTCAGATTGTCAAGAAT
GAAATGGAAAGTGCTGTAAAACTGTCTGTGAAATTGAAAGTGAAAGTGAAAATAGGCGCC
AGCTGGGGAGAGCTAAAGGACTTTGATGTGTAA
|
| Enzyme 25 GenBank Gene ID |
AY338826  |
| Enzyme 25 GeneCard ID |
POLQ  |
| Enzyme 25 GenAtlas ID |
POLQ  |
| Enzyme 25 HGNC ID |
HGNC:9186  |
| Enzyme 25 Chromosome Location |
3 |
| Enzyme 25 Locus |
3q13.33 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Seki M, Marini F, Wood RD: POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells. Nucleic Acids Res. 2003 Nov 1;31(21):6117-26. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
15254 |
| Enzyme 26 Name |
cDNA FLJ76751, highly similar to Homo sapiens polymerase (DNA directed) sigma (POLS), mRNA (Polymerase (DNA directed) sigma) |
| Enzyme 26 Synonyms |
Not Available |
| Enzyme 26 Gene Name |
POLS |
| Enzyme 26 Protein Sequence |
>cDNA FLJ76751, highly similar to Homo sapiens polymerase (DNA directed) sigma (POLS), mRNA (Polymerase (DNA directed) sigma)
MSPCPEEAAMRREVVKRIETVVKDLWPTADVQIFGSFSTGLYLPTSDIDLVVFGKWERPP
LQLLEQALRKHNVAEPCSIKVLDKATVPIIKLTDQETEVKVDISFNMETGVRAAEFIKNY
MKKYSLLPYLILVLKQFLLQRDLNEVFTGGISSYSLILMAISFLQLHPRIDARRADENLG
MLLVEFFELYGRNFNYLKTGIRIKEGGAYIAKEEIMKAMTSGYRPSMLCIEDPLLPGNDV
GRSSYGAMQVKQVFDYAYIVLSHAVSPLARSYPNRDAESTLGRIIKVTQEVIDYRRWIKE
KWGSKAHPSPGMDSRIKIKERIATCNGEQTQNREPESPYGQRLTLSLSSPQLLSSGSSAS
SVSSLSGSDVDSDTPPCTTPSVYQFSLQAPAPLMAGLPTALPMPSGKPQPTTSRTLIMTT
NNQTRFTIPPPTLGVAPVPCRQAGVEGTASLKAVHHMSSPAIPSASPNPLSSPHLYHKQH
NGMKLSMKGSHGHTQGGGYSSVGSGGVRPPVGNRGHHQYNRTGWRRKKHTHTRDSLPVSL
SR
|
| Enzyme 26 Number of Residues |
542 |
| Enzyme 26 Molecular Weight |
59874 |
| Enzyme 26 Theoretical pI |
9.81 |
| Enzyme 26 GO Classification |
Not Available |
| Enzyme 26 General Function |
Not Available |
| Enzyme 26 Specific Function |
Not Available |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
Not Available |
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
158260737  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
A8K1E2  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
A8K1E2_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1629 bp
ATGTCCCCTTGTCCTGAAGAAGCAGCTATGAGAAGAGAGGTGGTGAAACGGATCGAAACT
GTGGTGAAAGACCTTTGGCCGACGGCTGATGTACAGATATTTGGCAGCTTTAGTACAGGT
CTTTATCTTCCAACTAGCGACATAGACCTGGTGGTCTTCGGGAAATGGGAGCGTCCTCCT
TTACAGCTGCTGGAGCAAGCCCTGCGGAAGCACAACGTGGCTGAGCCGTGTTCCATCAAA
GTCCTTGACAAGGCTACGGTACCAATAATAAAGCTCACAGATCAGGAGACTGAAGTGAAA
GTTGACATCAGCTTTAACATGGAGACGGGCGTCCGGGCAGCGGAGTTCATCAAGAATTAC
ATGAAGAAATATTCATTGCTGCCTTACTTGATTTTAGTATTGAAACAGTTCCTTCTGCAG
AGGGACCTGAATGAAGTTTTTACAGGTGGAATTAGCTCATACAGCCTAATTTTAATGGCC
ATTAGCTTTCTACAGTTGCATCCAAGAATTGATGCCCGGAGAGCTGATGAAAACCTTGGA
ATGCTTCTTGTAGAATTTTTTGAACTCTATGGGAGAAATTTTAATTACTTGAAAACCGGT
ATTAGAATCAAAGAAGGAGGTGCCTATATCGCCAAAGAGGAGATCATGAAAGCCATGACC
AGCGGGTACAGACCGTCGATGCTGTGCATTGAGGACCCCCTGCTGCCAGGGAATGACGTT
GGCCGGAGCTCCTATGGCGCCATGCAGGTGAAGCAGGTCTTCGATTATGCCTACATAGTG
CTCAGCCATGCTGTGTCACCGCTGGCCAGGTCCTATCCAAACAGAGACGCCGAAAGTACT
TTAGGAAGAATCATCAAAGTAACTCAGGAGGTGATTGACTACCGGAGGTGGATCAAAGAG
AAGTGGGGCAGCAAAGCCCACCCGTCGCCAGGCATGGACAGCAGGATCAAGATCAAAGAG
CGAATAGCCACATGCAATGGGGAGCAGACGCAGAACCGAGAGCCCGAGTCTCCCTATGGC
CAGCGCTTGACTTTGTCGCTGTCCAGCCCCCAGCTCCTGTCTTCAGGCTCCTCGGCCTCT
TCTGTGTCTTCACTTTCTGGGAGTGACGTTGATTCAGACACACCGCCCTGCACAACGCCC
AGTGTTTACCAGTTCAGTCTGCAAGCGCCAGCTCCTCTCATGGCCGGCTTACCCACCGCC
TTGCCAATGCCCAGTGGCAAACCTCAGCCCACCACTTCCAGAACACTGATCATGACAACC
AACAATCAGACCAGGTTTACTATACCTCCACCGACCCTAGGGGTTGCTCCTGTTCCTTGC
AGACAAGCTGGTGTAGAAGGAACTGCGTCTTTGAAAGCCGTCCACCACATGTCTTCCCCG
GCCATTCCCTCAGCGTCCCCCAACCCGCTCTCGAGCCCTCATCTGTATCATAAGCAGCAC
AACGGCATGAAACTGTCCATGAAGGGCTCTCACGGCCACACCCAAGGCGGCGGCTACAGC
TCTGTGGGTAGCGGAGGTGTGCGGCCCCCTGTGGGCAACAGGGGACACCACCAGTATAAC
CGCACCGGCTGGAGGAGGAAAAAACACACACACACACGGGACAGTCTGCCCGTGAGCCTC
AGCAGATAA
|
| Enzyme 26 GenBank Gene ID |
AK289857  |
| Enzyme 26 GeneCard ID |
A8K1E2  |
| Enzyme 26 GenAtlas ID |
Not Available |
| Enzyme 26 HGNC ID |
Not Available |
| Enzyme 26 Chromosome Location |
Not Available |
| Enzyme 26 Locus |
Not Available |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
Not Available |
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
16536 |
| Enzyme 27 Name |
Polymerase (DNA directed) kappa, isoform CRA_b |
| Enzyme 27 Synonyms |
- SubName: cDNA, FLJ95449, Homo sapiens polymerase (DNA directed) kappa (POLK), mRNA
|
| Enzyme 27 Gene Name |
POLK |
| Enzyme 27 Protein Sequence |
>Polymerase (DNA directed) kappa, isoform CRA_b
MDSTKEKCDSYKDDLLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQV
NQRIENMMQQKAQITSQQLRKAQLQVDRFAMELEQSRNLSNTIVHIDMDAFYAAVEMRDN
PELKDKPIAVGSMSMLSTSNYHARRFGVRAAMPGFIAKRLCPQLIIVPPNFDKYRAVSKE
VKEILADYDPNFMAMSLDEAYLNITKHLEERQNWPEDKRRYFIKMGSSVENDNPGKEVNK
LSEHERSISPLLFEESPSDVQPPGDPFQVNFEEQNNPQILQNSVVFGTSAQEVVKEIRFR
IEQKTTLTASAGIAPNTMLAKVCSDKNKPNGQYQILPNRQAVMDFIKDLPIRKVSGIGKV
TEKMLKALGIITCTELYQQRALLSLLFSETSWHYFLHISLGLGSTHLTRDGERKSMSVER
TFSEINKAEEQYSLCQELCSELAQDLQKERLKGRTVTIKLKNVNFEVKTRASTVSSVVST
AEEIFAIAKELLKTEIDADFPHPLRLRLMGVRISSFPNEEDRKHQQRSIIGFLQAGNQAL
SATECTLEKTDKDKFVKPLEMSHKKSFFDKKRSERKWSHQDTFKCEAVNKQSFQTSQPFQ
VLKKKMNENLEISENSDDCQILTCPVCFRAQGCISLEALNKHVDECLDGPSISENFKMFS
CSHVSATKVNKKENVPASSLCEKQDYEAHPKIKEISSVDCIALVDTIDNSSKAESIDALS
NKHSKEECSSLPSKSFNIEHCHQNSSSTVSLENEDVGSFRQEYRQPYLCEVKTGQALVCP
VCNVEQKTSDLTLFNVHVDVCLNKSFIQELRKDKFNPVNQPKESSRSTGSSSGVQKAVTR
TKRPGLMTKYSTSKKIKPNNPKHTLDIFFK
|
| Enzyme 27 Number of Residues |
870 |
| Enzyme 27 Molecular Weight |
98810 |
| Enzyme 27 Theoretical pI |
8.22 |
| Enzyme 27 GO Classification |
| Function |
- DNA binding
- binding
- nucleic acid binding
|
| Process |
- DNA metabolism
- DNA repair
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 27 General Function |
Replication, recombination and repair |
| Enzyme 27 Specific Function |
Not Available |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
Not Available |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
B2RBD2  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
B2RBD2_HUMAN  |
| Enzyme 27 PDB ID |
1T94  |
| Enzyme 27 PDB File |
Show |
| Enzyme 27 3D Structure |
|
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
Not Available |
| Enzyme 27 GenBank Gene ID |
AK314610  |
| Enzyme 27 GeneCard ID |
B2RBD2  |
| Enzyme 27 GenAtlas ID |
Not Available |
| Enzyme 27 HGNC ID |
Not Available |
| Enzyme 27 Chromosome Location |
Not Available |
| Enzyme 27 Locus |
Not Available |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
Not Available |
| Enzyme 27 Metabolite References |
Not Available |