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Human Metabolome Database Version 2.5

 

Showing metabocard for dATP (HMDB01532)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:50
Accession Number HMDB01532
Secondary Accession Numbers Not Available
Common Name dATP
Description Animals obtain their energy by oxidation of foods, plants do so by trapping the sunlight using chlorophyll. However, before the energy can be used, it is first transformed into a form which the organism can handle easily. This special carrier of energy is the molecule adenosine triphosphate, or ATP. The ATP molecule is composed of three components. At the centre is a sugar molecule, [[ribose] (the same sugar that forms the basis of DNA). Attached to one side of this is a base (a group consisting of linked rings of carbon and nitrogen atoms); in this case the base is adenine. The other side of the sugar is attached to a string of phosphate groups. These phosphates are the key to the activity of ATP. ATP consists of a base, in this case adenine (red), a ribose (magenta) and a phosphate chain (blue). ATP works by losing the endmost phosphate group when instructed to do so by an enzyme. This reaction releases a lot of energy, which the organism can then use to build proteins, contact muscles, etc.
Synonyms
  1. 2'-Deoxy-5'-ATP
  2. 2'-Deoxy-ATP
  3. 2'-Deoxyadenosine 5'-triphosphate
  4. 2'-deoxyadenosine triphosphate
  5. Deoxyadenosine 5'-triphosphate
  6. Deoxyadenosine triphosphate
  7. Deoxy-ATP
  8. deoxyadenosine-triphosphate
Chemical IUPAC Name [[[5-(6-aminopurin-9-yl)-3-hydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxyphosphonic acid
Chemical Formula C10H16N5O12P3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide triphosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • DNA component
Application
Source
  • Endogenous
Average Molecular Weight 491.182
Monoisotopic Molecular Weight 491.000824
Isomeric SMILES NC1=NC=NC2=C1N=CN2[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1
Canonical SMILES NC1=NC=NC2=C1N=CN2C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1
KEGG Compound ID C00131 Link Image
BioCyc ID DATP Link Image
BiGG ID 33969 Link Image
Wikipedia Link Deoxyadenosine triphosphate Link Image
NuGOwiki Link HMDB01532 Link Image
Metagene Link HMDB01532 Link Image
METLIN ID 6303 Link Image
PubChem Compound 15993 Link Image
PubChem Substance 836047 Link Image
ChEBI ID 16284 Link Image
CAS Registry Number 1927-31-7
InChI Identifier InChI=1/C10H16N5O12P3/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(25-7)2-24-29(20,21)27-30(22,23)26-28(17,18)19/h3-7,16H,1-2H2,(H,20,21)(H,22,23)(H2,11,12,13)(H2,17,18,19)/t5-,6+,7+/m0/s1
Synthesis Reference Munch-Petersen, Agnete. Formation in vitro of deoxyadenosine triphosphate from deoxyadenosine in Ehrlich ascites cells. Biochemical and Biophysical Research Communications (1960), 3 392-6.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.83 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.66 [Predicted by ALOGPS]; -4.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • mitochondria
  • nucleus
Biofluid Location Not Available
Tissue Location
Tissue References
Erythrocyte
Lymphocyte
T-Lymphocyte
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Nespoli L, Porta F, Locatelli F, Aversa F, Carotti A, Lanfranchi A, Gibardi A, Marchesi ME, Abate L, Martelli MF, et al.: Successful lectin-separated bone marrow transplantation in adenosine deaminase deficiency-related severe immunodeficiency. Haematologica. 1990 Nov-Dec;75(6):546-50. [PubMed Link Image]
  2. Hoffbrand AV, Ganeshaguru K, Hooton JW, Tattersall MH: Effect of iron deficiency and desferrioxamine on DNA synthesis in human cells. Br J Haematol. 1976 Aug;33(4):517-26. [PubMed Link Image]
  3. Waddell D, Ullman B: Characterization of a cultured human T-cell line with genetically altered ribonucleotide reductase activity. Model for immunodeficiency. J Biol Chem. 1983 Apr 10;258(7):4226-31. [PubMed Link Image]
  4. Bory C, Boulieu R, Souillet G, Chantin C, Guibaud P, Hershfield MS: Effect of polyethylene glycol-modified adenosine deaminase (PEG-ADA) therapy in two ADA-deficient children: measurement of erythrocyte deoxyadenosine triphosphate as a useful tool. Adv Exp Med Biol. 1991;309A:173-6. [PubMed Link Image]
  5. Dang-Vu AP, Olsen EA, Vollmer RT, Greenberg ML, Hershfield MS: Treatment of cutaneous T cell lymphoma with 2'-deoxycoformycin (pentostatin). J Am Acad Dermatol. 1988 Oct;19(4):692-8. [PubMed Link Image]
  6. Donofrio J, Coleman MS, Hutton JJ, Daoud A, Lampkin B, Dyminski J: Overproduction of adenine deoxynucleosides and deoxynucletides in adenosine deaminase deficiency with severe combined immunodeficiency disease. J Clin Invest. 1978 Oct;62(4):884-7. [PubMed Link Image]
  7. Cowan MJ, Shannon KM, Wara DW, Ammann AJ: Rejection of bone marrow transplant and resistance of alloantigen reactive cells to in vivo deoxyadenosine in adenosine deaminase deficiency. Clin Immunol Immunopathol. 1988 Nov;49(2):242-50. [PubMed Link Image]
  8. Grever MR, Siaw MF, Jacob WF, Neidhart JA, Miser JS, Coleman MS, Hutton JJ, Balcerzak SP: The biochemical and clinical consequences of 2'-deoxycoformycin in refractory lymphoproliferative malignancy. Blood. 1981 Mar;57(3):406-17. [PubMed Link Image]
  9. Simmonds HA, Fairbanks LD, Morris GS, Webster DR, Harley EH: Altered erythrocyte nucleotide patterns are characteristic of inherited disorders of purine or pyrimidine metabolism. Clin Chim Acta. 1988 Feb 15;171(2-3):197-210. [PubMed Link Image]
  10. Hirschhorn R, Roegner V, Rubinstein A, Papageorgiou P: Plasma deoxyadenosine, adenosine, and erythrocyte deoxyATP are elevated at birth in an adenosine deaminase-deficient child. J Clin Invest. 1980 Mar;65(3):768-71. [PubMed Link Image]
  11. Schmalstieg FC, Mills GC, Tsuda H, Goldman AS: Severe combined immunodeficiency in a child with a healthy adenosine deaminase deficient mother. Pediatr Res. 1983 Dec;17(12):935-40. [PubMed Link Image]
  12. Simmonds HA, Webster DR, Perrett D, Reiter S, Levinsky RJ: Formation and degradation of deoxyadenosine nucleotides in inherited adenosine deaminase deficiency. Biosci Rep. 1982 May;2(5):303-14. [PubMed Link Image]
  13. Simmonds HA, Sahota A, Potter CF, Perrett D, Hugh-Jones K, Watson JG: Purine metabolism in adenosine deaminase deficiency. Ciba Found Symp. 1978;(68):255-62. [PubMed Link Image]
  14. Hirschhorn R, Roegner-Maniscalco V, Kuritsky L, Rosen FS: Bone marrow transplantation only partially restores purine metabolites to normal in adenosine deaminase-deficient patients. J Clin Invest. 1981 Dec;68(6):1387-93. [PubMed Link Image]
  15. Goday A, Simmonds HA, Webster DR, Levinsky RJ, Watson AR, Hoffbrand AV: Importance of platelet-free preparations for evaluating lymphocyte nucleotide levels in inherited or acquired immunodeficiency syndromes. Clin Sci (Lond). 1983 Dec;65(6):635-43. [PubMed Link Image]
  16. Chen SH, Ochs HD, Scott CR, Giblett ER, Tingle AJ: Adenosine deaminase deficiency: disappearance of adenine deoxynucleotides from a patient's erythrocytes after successful marrow transplantation. J Clin Invest. 1978 Dec;62(6):1386-9. [PubMed Link Image]
  17. Gruber HE, Cohen AH, Firestein GS, Redelman D, Bluestein HG: Deoxy-ATP accumulation in adenosine deaminase-inhibited human B and T lymphocytes. Adv Exp Med Biol. 1986;195 Pt A:503-7. [PubMed Link Image]
  18. Bory C, Boulieu R, Souillet G, Chantin C, Rolland MO, Mathieu M, Hershfield M: Comparison of red cell transfusion and polyethylene glycol-modified adenosine deaminase therapy in an adenosine deaminase-deficient child: measurement of erythrocyte deoxyadenosine triphosphate as a useful tool. Pediatr Res. 1990 Aug;28(2):127-30. [PubMed Link Image]
  19. Peters GJ, De Abreu RA, Oosterhof A, Veerkamp JH: Concentration of nucleotides and deoxynucleotides in peripheral and phytohemagglutinin-stimulated mammalian lymphocytes. Effects of adenosine and deoxyadenosine. Biochim Biophys Acta. 1983 Aug 23;759(1-2):7-15. [PubMed Link Image]
  20. Morgan G, Levinsky RJ, Hugh-Jones K, Fairbanks LD, Morris GS, Simmonds HA: Heterogeneity of biochemical, clinical and immunological parameters in severe combined immunodeficiency due to adenosine deaminase deficiency. Clin Exp Immunol. 1987 Dec;70(3):491-9. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Nucleoside diphosphate kinase, mitochondrial precursor
  2. Nucleoside diphosphate kinase A
  3. Nucleoside diphosphate kinase B
  4. Nucleoside diphosphate kinase 6
  5. Glucokinase
  6. Hexokinase-3
  7. Hexokinase-2
  8. Pyruvate kinase isozymes R/L
  9. DNA polymerase beta
  10. DNA polymerase alpha catalytic subunit
  11. DNA polymerase subunit delta 3
  12. DNA polymerase lambda
  13. DNA polymerase epsilon subunit 4
  14. DNA polymerase eta
  15. DNA polymerase delta catalytic subunit
  16. DNA polymerase zeta catalytic subunit
  17. DNA polymerase epsilon, catalytic subunit A
  18. DNA polymerase mu
  19. DNA polymerase epsilon subunit 3
  20. DNA polymerase subunit gamma 1
  21. DNA polymerase iota
  22. DNA polymerase epsilon subunit 2
  23. Apoptotic protease-activating factor 1
  24. Uridine-cytidine kinase 2
  25. Uridine/cytidine kinase-like 1
  26. 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)
  27. Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
  28. cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
  29. Myb-binding protein 1A
  30. DNA polymerase theta
  31. cDNA FLJ76751, highly similar to Homo sapiens polymerase (DNA directed) sigma (POLS), mRNA (Polymerase (DNA directed) sigma)
  32. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
  33. Polymerase (DNA directed) kappa, isoform CRA_b
Enzyme 1 [top]
Enzyme 1 ID 5338
Enzyme 1 Name Nucleoside diphosphate kinase, mitochondrial precursor
Enzyme 1 Synonyms
  1. NDP kinase, mitochondrial
  2. NDK
  3. nm23-H4
  4. Nucleoside diphosphate kinase D
  5. NDPKD
Enzyme 1 Gene Name NME4
Enzyme 1 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial precursor
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 1 Number of Residues 187
Enzyme 1 Molecular Weight 20659
Enzyme 1 Theoretical pI 10.75
Enzyme 1 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 1 General Function Nucleotide transport and metabolism
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
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-15
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1945762 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 1 PDB ID 1EHW Link Image
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
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 1 GenBank Gene ID Y07604 Link Image
Enzyme 1 GeneCard ID NME4 Link Image
Enzyme 1 GenAtlas ID NME4 Link Image
Enzyme 1 HGNC ID HGNC:7852 Link Image
Enzyme 1 Chromosome Location 16
Enzyme 1 Locus 16p13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5341
Enzyme 2 Name Nucleoside diphosphate kinase A
Enzyme 2 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Tumor metastatic process-associated protein
  4. Metastasis inhibition factor nm23
  5. nm23-H1
  6. Granzyme A-activated DNase
  7. GAAD
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 17149
Enzyme 2 Theoretical pI 6.11
Enzyme 2 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 2 General Function Nucleotide transport and metabolism
Enzyme 2 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 35068 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 2 PDB ID 1JXV Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >543 bp
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
Enzyme 2 GenBank Gene ID X17620 Link Image
Enzyme 2 GeneCard ID NME1 Link Image
Enzyme 2 GenAtlas ID NME1 Link Image
Enzyme 2 HGNC ID HGNC:7849 Link Image
Enzyme 2 Chromosome Location 17
Enzyme 2 Locus 17q21.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5344
Enzyme 3 Name Nucleoside diphosphate kinase B
Enzyme 3 Synonyms
  1. NDK B
  2. NDP kinase B
  3. nm23-H2
  4. C-myc purine-binding transcription factor PUF
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 17298
Enzyme 3 Theoretical pI 8.69
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 3 General Function Nucleotide transport and metabolism
Enzyme 3 Specific Function Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 4467843 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 3 PDB ID 1NSK Link Image
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 Link Image
Enzyme 3 GeneCard ID NME2 Link Image
Enzyme 3 GenAtlas ID NME2 Link Image
Enzyme 3 HGNC ID HGNC:7850 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5346
Enzyme 4 Name Nucleoside diphosphate kinase 6
Enzyme 4 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. nm23-H6
  4. Inhibitor of p53-induced apoptosis-alpha
  5. IPIA-alpha
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
Enzyme 4 Theoretical pI 8.49
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 4 General Function Nucleotide transport and metabolism
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
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-24
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 3228530 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
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 Link Image
Enzyme 4 GeneCard ID NME6 Link Image
Enzyme 4 GenAtlas ID NME6 Link Image
Enzyme 4 HGNC ID HGNC:20567 Link Image
Enzyme 4 Chromosome Location 3
Enzyme 4 Locus 3p21
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5442
Enzyme 5 Name Glucokinase
Enzyme 5 Synonyms
  1. Hexokinase-4
  2. Hexokinase type IV
  3. HK IV
  4. HK4
  5. Hexokinase-D
Enzyme 5 Gene Name GCK
Enzyme 5 Protein Sequence >Glucokinase
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
Enzyme 5 Number of Residues 465
Enzyme 5 Molecular Weight 52192
Enzyme 5 Theoretical pI 4.85
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + D-glucose = ADP + D-glucose 6-phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 179427 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P35557 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name HXK4_HUMAN Link Image
Enzyme 5 PDB ID 1V4T Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1398 bp
ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA
Enzyme 5 GenBank Gene ID M88011 Link Image
Enzyme 5 GeneCard ID GCK Link Image
Enzyme 5 GenAtlas ID GCK Link Image
Enzyme 5 HGNC ID HGNC:4195 Link Image
Enzyme 5 Chromosome Location 7
Enzyme 5 Locus 7p15.3-p15.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed Link Image]
  2. Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed Link Image]
  3. Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed Link Image]
  4. Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed Link Image]
  5. Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed Link Image]
  6. Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [PubMed Link Image]
  7. St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed Link Image]
  8. Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed Link Image]
  9. Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed Link Image]
  10. Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed Link Image]
  11. Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed Link Image]
  12. Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed Link Image]
  13. Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed Link Image]
  14. Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed Link Image]
  15. Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed Link Image]
  16. Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed Link Image]
  17. Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed Link Image]
  18. Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed Link Image]
  19. Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5444
Enzyme 6 Name Hexokinase-3
Enzyme 6 Synonyms
  1. Hexokinase type III
  2. HK III
Enzyme 6 Gene Name HK3
Enzyme 6 Protein Sequence >Hexokinase-3
MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSLSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRGNRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV
Enzyme 6 Number of Residues 923
Enzyme 6 Molecular Weight 98921
Enzyme 6 Theoretical pI 5.11
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1255788 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P52790 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name HXK3_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2772 bp
ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTAAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGACGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGGGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA
Enzyme 6 GenBank Gene ID U51333 Link Image
Enzyme 6 GeneCard ID HK3 Link Image
Enzyme 6 GenAtlas ID HK3 Link Image
Enzyme 6 HGNC ID HGNC:4925 Link Image
Enzyme 6 Chromosome Location 5
Enzyme 6 Locus 5q35.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [PubMed Link Image]
  2. Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5445
Enzyme 7 Name Hexokinase-2
Enzyme 7 Synonyms
  1. Hexokinase type II
  2. HK II
  3. Muscle form hexokinase
Enzyme 7 Gene Name HK2
Enzyme 7 Protein Sequence >Hexokinase-2
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR
Enzyme 7 Number of Residues 917
Enzyme 7 Molecular Weight 102381
Enzyme 7 Theoretical pI 5.93
Enzyme 7 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 587202 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P52789 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name HXK2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2754 bp
ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCCTTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTACTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCACCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG
Enzyme 7 GenBank Gene ID Z46376 Link Image
Enzyme 7 GeneCard ID HK2 Link Image
Enzyme 7 GenAtlas ID HK2 Link Image
Enzyme 7 HGNC ID HGNC:4923 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 2p13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [PubMed Link Image]
  2. Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed Link Image]
  3. Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed Link Image]
  4. Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed Link Image]
  5. Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed Link Image]
  6. Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6041
Enzyme 8 Name Pyruvate kinase isozymes R/L
Enzyme 8 Synonyms
  1. R-type/L-type pyruvate kinase
  2. Red cell/liver pyruvate kinase
  3. Pyruvate kinase 1
Enzyme 8 Gene Name PKLR
Enzyme 8 Protein Sequence >Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Enzyme 8 Number of Residues 574
Enzyme 8 Molecular Weight 61831
Enzyme 8 Theoretical pI 7.83
Enzyme 8 GO Classification
Function
  • catalytic activity
  • kinase activity
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 3327365 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P30613 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name KPYR_HUMAN Link Image
Enzyme 8 PDB ID 1LIU Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1725 bp
ATGTCGATCCAGGAGAACATATCATCCCTGCAGCTTCGGTCATGGGTCTCTAAGTCCCAA
AGAGACTTAGCAAAGTCCATCCTGATTGGGGCTCCAGGAGGGCCAGCGGGGTATCTGCGG
CGGGCCAGTGTGGCCCAACTGACCCAGGAGCTGGGCACTGCCTTCTTCCAGCAGCAGCAG
CTGCCAGCTGCTATGGCAGACACCTTCCTGGAACACCTCTGCCTACTGGACATTGACTCC
GAGCCCGTGGCTGCTCGCAGTACCAGCATCATTGCCACCATCGGGCCAGCATCTCGCTCC
GTGGAGCGCCTCAAGGAGATGATCAAGGCCGGGATGAACATTGCGCGACTCAACTTCTCC
CACGGCTCCCACGAGTACCATGCTGAGTCCATCGCCAACGTCCGGGAGGCGGTGGAGAGC
TTTGCAGGTTCCCCACTCAGCTACCGGCCCGTGGCCATCGCCCTGGACACCAAGGGACCG
GAGATCCGCACTGGGATCCTGCAGGGGGGTCCAGAGTCGGAAGTGGAGCTGGTGAAGGGC
TCCCAGGTGCTGGTGACTGTGGACCCCGCGTTCCGGACGCGGGGGAACGCGAACACCGTG
TGGGTGGACTACCCCAATATTGTCCGGGTCGTGCCGGTGGGGGGCCGCATCTACATTGAC
GACGGGCTCATCTCCCTAGTGGTCCAGAAAATCGGCCCAGAGGGACTGGTGACCCAAGTG
GAGAACGGCGGCGTCCTGGGCAGCCGGAAGGGCGTGAACTTGCCAGGGGCCCAGGTGGAC
TTGCCCGGGCTGTCCGAGCAGGACGTCCGAGACCTGCGCTTCGGGGTGGAGCATGGGGTG
GACATCGTCTTTGCCTCCTTTGTGCGGAAAGCCAGCGACGTGGCTGCCGTCAGGGCTGCT
CTGGGTCCGGAAGGACACGGCATCAAGATCATCAGCAAAATTGAGAACCACGAAGGCGTG
AAGAGGTTTGATGAAATCCTGGAGGTGAGCGACGGCATCATGGTGGCACGGGGGGACCTA
GGCATCGAGATCCCAGCAGAGAAGGTTTTCCTGGCTCAGAAGATGATGATTGGGCGCTGC
AACTTGGCGGGCAAGCCTGTTGTCTGTGCCACACAGATGCTGGAGAGCATGATTACCAAG
CCCCGGCCAACGAGGGCAGAGACAAGCGATGTCGCCAATGCTGTGCTGGATGGGGCTGAC
TGCATCATGCTGTCAGGGGAGACTGCCAAGGGCAACTTCCCTGTGGAAGCGGTGAAGATG
CAGCATGCGATTGCCCGGGAGGCAGAGGCCGCAGTGTACCACCGGCAGCTGTTTGAGGAG
CTACGTCGGGCAGCGCCACTAAGCCGTGATCCCACTGAGGTCACCGCCATTGGTGCTGTG
GAGGCTGCCTTCAAGTGCTGTGCTGCTGCCATCATTGTGCTGACCACAACTGGCCGCTCA
GCCCAGCTTCTGTCTCGGTACCGACCTCGGGCAGCAGTCATTGCTGTCACCCGCTCTGCC
CAGGCTGCCCGCCAGGTCCACTTATGCCGAGGAGTCTTCCCCTTGCTTTACCGTGAACCT
CCAGAAGCCATCTGGGCAGATGATGTAGATCGCCGGGTGCAATTTGGCATTGAAAGTGGA
AAGCTCCGTGGCTTCCTCCGTGTTGGAGACCTGGTGATTGTGGTGACAGGCTGGCGACCT
GGCTCCGGCTACACCAACATCATGAGGGTGCTAAGCATATCCTGA
Enzyme 8 GenBank Gene ID AB015983 Link Image
Enzyme 8 GeneCard ID PKLR Link Image
Enzyme 8 GenAtlas ID PKLR Link Image
Enzyme 8 HGNC ID HGNC:9020 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1q21
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Kanno H, Fujii H, Hirono A, Miwa S: cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8218-21. [PubMed Link Image]
  2. Tani K, Fujii H, Nagata S, Miwa S: Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1792-5. [PubMed Link Image]
  3. Tani K, Fujii H, Tsutsumi H, Sukegawa J, Toyoshima K, Yoshida MC, Noguchi T, Tanaka T, Miwa S: Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment. Biochem Biophys Res Commun. 1987 Mar 13;143(2):431-8. [PubMed Link Image]
  4. Kanno H, Fujii H, Tsujino G, Miwa S: Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. Biochem Biophys Res Commun. 1993 Apr 15;192(1):46-52. [PubMed Link Image]
  5. Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed Link Image]
  6. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase. Blood Cells Mol Dis. 1996;22(1):85-9. [PubMed Link Image]
  7. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (1st update). Blood Cells Mol Dis. 1996;22(3):259-64. [PubMed Link Image]
  8. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (2nd update). Blood Cells Mol Dis. 1998 Sep;24(3):273-9. [PubMed Link Image]
  9. Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (Third update). Blood Cells Mol Dis. 2000 Feb;26(1):47-53. [PubMed Link Image]
  10. Neubauer B, Lakomek M, Winkler H, Parke M, Hofferbert S, Schroter W: Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. Blood. 1991 May 1;77(9):1871-5. [PubMed Link Image]
  11. Kanno H, Fujii H, Hirono A, Omine M, Miwa S: Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. Blood. 1992 Mar 1;79(5):1347-50. [PubMed Link Image]
  12. Kanno H, Fujii H, Miwa S: Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. Blood. 1993 May 1;81(9):2439-41. [PubMed Link Image]
  13. Baronciani L, Beutler E: Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1993 May 1;90(9):4324-7. [PubMed Link Image]
  14. Kanno H, Ballas SK, Miwa S, Fujii H, Bowman HS: Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. Blood. 1994 Apr 15;83(8):2311-6. [PubMed Link Image]
  15. Lenzner C, Nurnberg P, Thiele BJ, Reis A, Brabec V, Sakalova A, Jacobasch G: Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. Blood. 1994 May 15;83(10):2817-22. [PubMed Link Image]
  16. Baronciani L, Beutler E: Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. J Clin Invest. 1995 Apr;95(4):1702-9. [PubMed Link Image]
  17. Beutler E, Westwood B, van Zwieten R, Roos D: G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. [PubMed Link Image]
  18. Zarza R, Alvarez R, Pujades A, Nomdedeu B, Carrera A, Estella J, Remacha A, Sanchez JM, Morey M, Cortes T, Perez Lungmus G, Bureo E, Vives Corrons JL: Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients. Red Cell Pathology Group of the Spanish Society of Haematology (AEHH). Br J Haematol. 1998 Nov;103(2):377-82. [PubMed Link Image]
  19. Cohen-Solal M, Prehu C, Wajcman H, Poyart C, Bardakdjian-Michau J, Kister J, Prome D, Valentin C, Bachir D, Galacteros F: A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha2 globin gene variant (Hb Conakry). Br J Haematol. 1998 Dec;103(4):950-6. [PubMed Link Image]
  20. Pastore L, Della Morte R, Frisso G, Alfinito F, Vitale D, Calise RM, Ferraro F, Zagari A, Rotoli B, Salvatore F: Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy. Hum Mutat. 1998;11(2):127-34. [PubMed Link Image]
  21. Zanella A, Bianchi P, Fermo E, Iurlo A, Zappa M, Vercellati C, Boschetti C, Baronciani L, Cotton F: Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients. Br J Haematol. 2001 Apr;113(1):43-8. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6238
Enzyme 9 Name DNA polymerase beta
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name POLB
Enzyme 9 Protein Sequence >DNA polymerase beta
MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAK
KLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIK
TLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGS
FRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQ
LPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRP
LGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
Enzyme 9 Number of Residues 335
Enzyme 9 Molecular Weight 38178
Enzyme 9 Theoretical pI 9.41
Enzyme 9 GO Classification
Function
  • DNA binding
  • DNA-directed DNA polymerase activity
  • beta DNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • DNA metabolism
  • DNA repair
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • cell
  • intracellular
Enzyme 9 General Function Replication, recombination and repair
Enzyme 9 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 9 Pathways
Enzyme 9 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 9 Pfam Domain Function Not Available
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 292397 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P06746 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name DPOLB_HUMAN Link Image
Enzyme 9 PDB ID 8ICK Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1008 bp
ATGAGCAAACGGAAGGCGCCGCAGGAGACTCTCAACGGGGGAATCACCGACATGCTCACA
GAACTCGCAAACTTTGAGAAGAACGTGAGCCAAGCTATCCACAAGTACAATGCTTACAGA
AAAGCAGCATCTGTTATAGCAAAATACCCACACAAAATAAAGAGTGGAGCTGAAGCTAAG
AAATTGCCTGGAGTAGGAACAAAAATTGCTGAAAAGATTGATGAGTTTTTAGCAACTGGA
AAATTACGTAAACTGGAAAAGATTCGGCAGGATGATACGAGTTCATCCATCAATTTCCTG
ACTCGAGTTAGTGGCATTGGTCCATCTGCTGCAAGGAAGTTTGTAGATGAAGGAATTAAA
ACACTAGAAGATCTCAGAAAAAATGAAGATAAATTGAACCATCATCAGCGAATTGGGCTG
AAATATTTTGGGGACTTTGAAAAAAGAATTCCTCGTGAAGAGATGTTACAAATGCAAGAT
ATTGTACTAAATGAAGTTAAAAAAGTGGATTCTGAATACATTGCTACAGTCTGTGGCAGT
TTCAGAAGAGGTGCAGAGTCCAGTGGTGACATGGATGTTCTCCTGACCCATCCCAGCTTC
ACTTCAGAATCAACCAAACAGCCAAAACTGTTACATCAGGTTGTGGAGCAGTTACAAAAG
GTTCATTTTATCACAGATACCCTGTCAAAGGGTGAGACAAAGTTCATGGGTGTTTGCCAG
CTTCCCAGTAAAAATGATGAAAAAGAATATCCACACAGAAGAATTGATATCAGGTTGATA
CCCAAAGATCAGTATTACTGTGGTGTTCTCTATTTCACTGGGAGTGATATTTTCAATAAG
AATATGAGGGCTCATGCCCTAGAAAAGGGTTTCACAATCAATGAGTACACCATCCGTCCC
TTGGGAGTCACTGGAGTTGCAGGAGAACCCCTGCCAGTGGATAGTGAAAAAGACATCTTT
GATTACATCCAGTGGAAATACCGGGAACCCAAGGACCGGAGCGAATGA
Enzyme 9 GenBank Gene ID L11607 Link Image
Enzyme 9 GeneCard ID POLB Link Image
Enzyme 9 GenAtlas ID POLB Link Image
Enzyme 9 HGNC ID HGNC:9174 Link Image
Enzyme 9 Chromosome Location 8
Enzyme 9 Locus 8p11.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6239
Enzyme 10 Name DNA polymerase alpha catalytic subunit
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name POLA1
Enzyme 10 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 10 Number of Residues 1462
Enzyme 10 Molecular Weight 165914
Enzyme 10 Theoretical pI 5.59
Enzyme 10 GO Classification
Function
  • 3'-5' exonuclease activity
  • DNA binding
  • DNA-directed DNA polymerase activity
  • binding
  • catalytic activity
  • exonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
  • nucleotide binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • DNA metabolism
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 10 General Function Replication, recombination and repair
Enzyme 10 Specific Function Polymerase alpha in a complex with DNA primase is a replicative polymerase
Enzyme 10 Pathways
Enzyme 10 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 35568 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P09884 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name DPOLA_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 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 10 GenBank Gene ID X06745 Link Image
Enzyme 10 GeneCard ID POLA1 Link Image
Enzyme 10 GenAtlas ID POLA1 Link Image
Enzyme 10 HGNC ID HGNC:9173 Link Image
Enzyme 10 Chromosome Location X
Enzyme 10 Locus Xp22.1-p21.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6240
Enzyme 11 Name DNA polymerase subunit delta 3
Enzyme 11 Synonyms
  1. DNA polymerase subunit delta p66
Enzyme 11 Gene Name POLD3
Enzyme 11 Protein Sequence >DNA polymerase subunit delta 3
MADQLYLENIDEFVTDQNKIVTYKWLSYTLGVHVNQAKQMLYDYVERKRKENSGAQLHVT
YLVSGSLIQNGHSCHKVAVVREDKLEAVKSKLAVTASIHVYSIQKAMLKDSGPLFNTDYD
ILKSNLQNCSKFSAIQCAAAVPRAPAESSSSSKKFEQSHLHMSSETQANNELTTNGHGPP
ASKQVSQQPKGIMGMFASKAAAKTQETNKETKTEAKEVTNASAAGNKAPGKGNMMSNFFG
KAAMNKFKVNLDSEQAVKEEKIVEQPTVSVTEPKLATPAGLKKSSKKAEPVKVLQKEKKR
GKRVALSDDETKETENMRKKRRRIKLPESDSSEDEVFPDSPGAYEAESPSPPPPPSPPLE
PVPKTEPEPPSVKSSSGENKRKRKRVLKSKTYLDGEGCIVTEKVYESESCTDSEEELNMK
TSSVHRPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK
Enzyme 11 Number of Residues 466
Enzyme 11 Molecular Weight 51401
Enzyme 11 Theoretical pI 9.96
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function The function of subunit 3 is not clear
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function Not Available
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 436222 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q15054 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name DPOD3_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1476 bp
AGACGTTTCCCGCCGGCGGGAGCTGTGGCTGTGATTGAGAGAGGGGTTAGAGGCGGGTCC
CAGCGCTGCCGCACCATGGCGGACCAGCTTTATCTGGAAAATATAGACGAGTTCGTCACG
GACCAAAACAAGATCGTGACATACAAATGGCTGAGCTATACACTAGGGGTTCATGTTAAC
CAGGCCAAACAGATGCTGTATGATTATGTTGAAAGGAAACGAAAAGAAAATTCAGGAGCC
CAACTGCATGTTACCTACTTGGTGTCTGGCAGTCTCATTCAGAATGGACATTCCTGCCAC
AAGGTTGCAGTAGTGAGAGAAGATAAATTGGAAGCAGTGAAGTCCAAGCTAGCTGTGACT
GCCAGCATCCATGTGTACAGCATCCAGAAAGCCATGCTAAAGGACAGTGGGCCTCTGTTC
AATACTGACTATGACATCCTTAAAAGCAACTTGCAGAACTGCAGCAAATTTAGTGCTATA
CAATGTGCAGCTGCCGTCCCTAGAGCTCCTGCTGAATCCTCTTCGTCTTCCAAAAAGTTT
GAGCAGTCACATCTTCACATGTCAAGTGAGACACAAGCCAACAATGAGCTGACCACCAAT
GGTCATGGCCCACCTGCATCCAAGCAGGTTTCCCAGCAGCCCAAAGGAATTATGGGAATG
TTTGCCTCCAAAGCTGCTGCTAAAACCCAAGAAACCAACAAGGAAACGAAAACAGAGGCT
AAAGAAGTAACAAATGCATCTGCAGCAGGCAACAAGGCACCAGGGAAAGGGAATATGATG
AGCAACTTTTTTGGAAAAGCTGCTATGAATAAATTTAAAGTCAATTTGGACTCAGAACAA
GCAGTGAAAGAAGAAAAAATAGTGGAGCAGCCTACAGTGTCTGTCACGGAACCAAAGCTG
GCAACTCCTGCAGGCCTGAAAAAATCCAGCAAAAAAGCAGAGCCTGTTAAGGTGCTGCAG
AAGGAAAAAAAAAGGGGGAAGCGAGTAGCATTATCTGATGATGAGACAAAGGAAACTGAA
AACATGAGGAAAAAGAGGAGAAGAATCAAACTTCCTGAATCTGATAGCAGTGAAGATGAA
GTCTTTCCAGACTCTCCTGGGGCTTATGAAGCTGAGTCACCATCCCCACCTCCTCCTCCG
TCTCCACCTCTTGAACCAGTGCCAAAGACTGAGCCTGAACCTCCTTCTGTCAAGAGCTCA
AGTGGAGAAAACAAAAGAAAACGAAAACGCGTACTAAAATCTAAAACTTACCTGGATGGG
GAAGGCTGCATAGTGACTGAAAAAGTCTACGAGAGTGAATCCTGCACAGATAGTGAAGAG
GAGCTTAACATGAAGACATCCTCAGTACACAGACCCCCTGCCATGACTGTGAAAAAAGAA
CCCAGAGAGGAACGAAAGGGCCCCAAGAAAGGGACTGCTGCTCTGGGCAAAGCCAACAGA
CAGGTGTCCATTACTGGCTTCTTCCAGAGGAAATAA
Enzyme 11 GenBank Gene ID D26018 Link Image
Enzyme 11 GeneCard ID POLD3 Link Image
Enzyme 11 GenAtlas ID POLD3 Link Image
Enzyme 11 HGNC ID HGNC:20932 Link Image
Enzyme 11 Chromosome Location 11
Enzyme 11 Locus 11q14
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6243
Enzyme 12 Name DNA polymerase lambda
Enzyme 12 Synonyms
  1. Pol Lambda
  2. DNA polymerase kappa
  3. DNA polymerase beta-2
  4. Pol beta2
Enzyme 12 Gene Name POLL
Enzyme 12 Protein Sequence >DNA polymerase lambda
MDPRGILKAFPKRQKIHADASSKVLAKIPRREEGEEAEEWLSSLRAHVVRTGIGRARAEL
FEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYERALRLLRLPQLPPGAQLVKSAWLSLCLQ
ERRLVDVAGFSIFIPSRYLDHPQPSKAEQDASIPPGTHEALLQTALSPPPPPTRPVSPPQ
KAKEAPNTQAQPISDDEASDGEETQVSAADLEALISGHYPTSLEGDCEPSPAPAVLDKWV
CAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEAC
SIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSL
EDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRR
GKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLP
GPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNT
HGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
Enzyme 12 Number of Residues 575
Enzyme 12 Molecular Weight 63483
Enzyme 12 Theoretical pI 7.94
Enzyme 12 GO Classification
Function
  • DNA binding
  • DNA-directed DNA polymerase activity
  • beta DNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • DNA metabolism
  • DNA repair
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • cell
  • intracellular
Enzyme 12 General Function Replication, recombination and repair
Enzyme 12 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 12 Pathways
Enzyme 12 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 12 Pfam Domain Function Not Available
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 6687796 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9UGP5 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name DPOLL_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 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 12 GenBank Gene ID AJ131890 Link Image
Enzyme 12 GeneCard ID POLL Link Image
Enzyme 12 GenAtlas ID POLL Link Image
Enzyme 12 HGNC ID HGNC:9184 Link Image
Enzyme 12 Chromosome Location 10
Enzyme 12 Locus 10q23
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6244
Enzyme 13 Name DNA polymerase epsilon subunit 4
Enzyme 13 Synonyms
  1. DNA polymerase II subunit 4
  2. DNA polymerase epsilon subunit p12
Enzyme 13 Gene Name POLE4
Enzyme 13 Protein Sequence >DNA polymerase epsilon subunit 4
MAAAAAAGSGTPREEEGPAGEAAASQPQAPTSVPGARLSRLPLARVKALVKADPDVTLAG
QEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD
Enzyme 13 Number of Residues 117
Enzyme 13 Molecular Weight 12209
Enzyme 13 Theoretical pI 4.55
Enzyme 13 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function May play a role in allowing polymerase epsilon to carry out its replication and/or repair function
Enzyme 13 Pathways
Enzyme 13 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 9623361 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9NR33 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name DPOE4_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >354 bp
ATGGCGGCGGCGGCGGCGGCAGGAAGCGGGACGCCCCGAGAGGAGGAGGTACCTGCTGGG
GAGGCAGCGGCCTCGCAGCCCCAGGCCCCAACGAGTGTGCCTGGGGCTCGTCTCTCGAGG
TTGCCTCTGGCGCGAGTGAAGGCCTTGGTGAAGGCAGATCCCGACGTGACGCTAGCGGGA
CAGGAAGCCATCTTCATTCTGGCACGAGCCGCGGAACTGTTTGTGGAGACCATTGCAAAA
GATGCCTACTGTTGCGCTCAGCAGGGAAAAAGGAAAACCCTTCAGAGGAGAGACTTGGAT
AATGCAATAGAAGCTGTGGATGAATTTGCTTTTCTGGAAGGTACTTTAGATTGA
Enzyme 13 GenBank Gene ID AF261688 Link Image
Enzyme 13 GeneCard ID POLE4 Link Image
Enzyme 13 GenAtlas ID POLE4 Link Image
Enzyme 13 HGNC ID HGNC:18755 Link Image
Enzyme 13 Chromosome Location 2
Enzyme 13 Locus 2p12
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. 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 Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6245
Enzyme 14 Name DNA polymerase eta
Enzyme 14 Synonyms
  1. RAD30 homolog A
  2. Xeroderma pigmentosum variant type protein
Enzyme 14 Gene Name POLH
Enzyme 14 Protein Sequence >DNA polymerase eta
MATGQDRVVALVDMDCFFVQVEQRQNPHLRNKPCAVVQYKSWKGGGIIAVSYEARAFGVT
RSMWADDAKKLCPDLLLAQVRESRGKANLTKYREASVEVMEIMSRFAVIERASIDEAYVD
LTSAVQERLQKLQGQPISADLLPSTYIEGLPQGPTTAEETVQKEGMRKQGLFQWLDSLQI
DNLTSPDLQLTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSH
GSVPQLFSQMPIRKIRSLGGKLGASVIEILGIEYMGELTQFTESQLQSHFGEKNGSWLYA
MCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATREQVQWWLLQLAQELEERLTKDRNDND
RVATQLVVSIRVQGDKRLSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLT
MLFLCATKFSASAPSSSTDITSFLSSDPSSLPKVPVTSSEAKTQGSGPAVTATKKATTSL
ESFFQKAAERQKVKEASLSSLTAPTQAPMSNSPSKPSLPFQTSQSTGTEPFFKQKSLLLK
QKQLNNSSVSSPQQNPWSNCKALPNSLPTEYPGCVPVCEGVSKLEESSKATPAEMDLAHN
SQSMHASSASKSVLEVTQKATPNPSLLAAEDQVPCEKCGSLVPVWDMPEHMDYHFALELQ
KSFLQPHSSNPQVVSAVSHQGKRNPKSPLACTNKRPRPEGMQTLESFFKPLTH
Enzyme 14 Number of Residues 713
Enzyme 14 Molecular Weight 78414
Enzyme 14 Theoretical pI 8.56
Enzyme 14 GO Classification
Function
Process
  • DNA metabolism
  • DNA repair
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 14 General Function Replication, recombination and repair
Enzyme 14 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 14 Pathways
Enzyme 14 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 5138988 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9Y253 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name POLH_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID AB024313 Link Image
Enzyme 14 GeneCard ID POLH Link Image
Enzyme 14 GenAtlas ID POLH Link Image
Enzyme 14 HGNC ID HGNC:9181 Link Image
Enzyme 14 Chromosome Location 6
Enzyme 14 Locus 6p21.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6246
Enzyme 15 Name DNA polymerase delta catalytic subunit
Enzyme 15 Synonyms
  1. DNA polymerase subunit delta p125
Enzyme 15 Gene Name POLD1
Enzyme 15 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 15 Number of Residues 1107
Enzyme 15 Molecular Weight 123633
Enzyme 15 Theoretical pI 7.03
Enzyme 15 GO Classification
Function
  • 3'-5' exonuclease activity
  • DNA binding
  • DNA-directed DNA polymerase activity
  • binding
  • catalytic activity
  • exonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
  • nucleotide binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • DNA metabolism
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 15 General Function Replication, recombination and repair
Enzyme 15 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 15 Pathways
Enzyme 15 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 181620 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P28340 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name DPOD1_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >3324 bp
ATGGATGGCAAGCGGCGGCCAGGCCCAGGGCCCGGGGTGCCCCCAAAGCGGGCCCGTGGG
GGCCTCTGGGATGATGATGATGCACCTTGGCCATCCCAATTCGAGGAGGACCTGGCACTG
ATGGAGGAGATGGAGGCAGAACACAGGCTGCAGGAGCAGGAGGAGGAGGAGCTGCAGTCA
GTCCTGGAGGGGGTTGCAGACGGGCAGGTCCCACCATCAGCCATAGATCCTCGCTGGCTT
CGGCCCACACCACCAGCGCTGGACCCCCAGACAGAGCCCCTCATCTTCCAACAGTTGGAG
ATTGACCATTATGTGGGCCCAGCGCAGCCTGTGCCTGGGGGGCCCCCACCATCCCGCGGC
TCCGTGCCTGTGCTCCGCGCCTTCGGGGTCACCGATGAGGGGTTCTCTGTCTGCTGCCAC
ATCCACGGCTTCGCTCCCTACTTCTACACCCCAGCGCCCCCTGGTTTCGGGCCCGAGCAC
ATGGGTGACCTGCAACGGGAGCTGAACTTGGCCATCAGCCGGGACAGTCGCGGGGGGAGG
GAGCTGACTGGGCCGGCCGTGCTGGCTGTGGAACTGTGCTCCCGAGAGAGCATGTTTGGG
TACCACGGGCACGGCCCCTCCCCGTTCCTGCGCATCACCGTGGCGCTGCCGCGCCTCGTG
GCCCCGGCCCGCCGTCTCCTGGAACAGGGCATCCGTGTGGCAGGCCTGGGCACGCCCAGC
TTCGCGCCCTACGAGGCCAACGTCGACTTTGAGATCCGGTTCATGGTGGACACGGACATC
GTCGGCTGCAACTGGCTGGAGCTCCCAGCTGGGAAATACGCCCTGAGGCTGAAGGAGAAG
GCTACGCAGTGCCAGCTGGAGGCGGACGTGCTGTGGTCTGACGTGGTCAGTCACCCACCG
GAAGGGCCATGGCAGCGCATTGCGCCCTTGCGCGTGCTCAGCTTCGATATCGAGTGCGCC
GGCCGCAAAGGCATCTTCCCTGAGCCTGAGCGGGACCCTGTCATCCAGATCTGCTCGCTG
GGCCTGCGCTGGGGGGAGCCGGAGCCCTTCCTACGCCTGGCGCTCACCCTGCGGCCCTGT
GCCCCCATCCTGGGTGCCAAGGTGCAGAGCTACGAGAAGGAGGAGGACCTGCTGCAGGCC
TGGTCCACCTTCATCCGTATCATGGACCCCGACGTGATCACCGGTTACAACATCCAGAAC
TTCGACCTTCCGTACCTCATCTCTCGGGCCCAGACCCTCAAGGTACAAACATTCCCTTTC
CTGGGCCGTGTGGCCGGCCTTTGCTCCAACATCCGGGACTCTTCATTCCAGTCCAAGCAG
ACGGGCCGGCGGGACACCAAGGTTGTCAGCATGGTGGGCCGCGTGCAGATGGACATGCTG
CAGGTGCTGCTGCGGGAGTACAAGCTCCGCTCCCACACGCTCAATGCCGTGAGCTTCCAC
TTCCTGGGCGAGCAGAAGGAGGACGTGCAGCACAGCATCATCACCGACCTGCAGAATGGG
AACGACCAGACCCGCCGCCGCCTGGCTGTGTACTGCCTGAAGGATGCCTACCTGCCACTG
CGGCTGCTGGAGCGGCTCATGGTGCTGGTGAACGCCGTGGAGATGGCGAGGGTCACTGGC
GTGCCCCTCAGCTACCTGCTCAGTCGTGGCCAGCAGGTCAAAGTCGTATCCCAGCTGTTG
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 15 GenBank Gene ID M80397 Link Image
Enzyme 15 GeneCard ID POLD1 Link Image
Enzyme 15 GenAtlas ID POLD1 Link Image
Enzyme 15 HGNC ID HGNC:9175 Link Image
Enzyme 15 Chromosome Location 19
Enzyme 15 Locus 19q13.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6247
Enzyme 16 Name DNA polymerase zeta catalytic subunit
Enzyme 16 Synonyms
  1. hREV3
Enzyme 16 Gene Name REV3L
Enzyme 16 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 16 Number of Residues 3130
Enzyme 16 Molecular Weight 352779
Enzyme 16 Theoretical pI 8.61
Enzyme 16 GO Classification Not Available
Enzyme 16 General Function Replication, recombination and repair
Enzyme 16 Specific Function Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 16 Pathways
Enzyme 16 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 16 Pfam Domain Function Not Available
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 3063675 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O60673 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name DPOLZ_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 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
GATGGGACGTTAGAAACTGAGCAGTCCTTTGGACTATATGGAAATAAATACACACTTAGA
GCCAAACGCAAGGTAAATTATGAGACTGAAGACAGTGAGTCAAGTTTTGTAACTCACAAC
TCAAAAATTAGTCTACCTCATCCCATGGAAATTGGTGAAAGTTTAGATGGAACTCTCAAA
TCCCGAAAACGAAGAAAAATGTCTAAAAAGCTGCCCCCTGTCATCATAAAGTATATTATT
ATTAATAGATTTAGAGGGAGAAAAAATATGCTTGTGAAGCTAGGAAAAATAGACTCTAAA
GAAAAACAAGTAATATTAACAGAAGAAAAAATGGAACTATATAAAAAGCTTGCACCTTTG
AAGGACTTTTGGCCAAAAGTTCCCGACTCCCCTGCAACCAAATATCCCATTTATCCACTA
ACACCAAAGAAAAGTCACAGAAGAAAGTCAAAACATAAATCTGCTAAGAAAAAAACTGGT
AAACAACAAAGGACAAATAATGAAAATATTAAAAGAACTTTGTCTTTCAGGAAAAAACGG
TCACATGCTATTCTTTCTCCTCCCTCACCATCTTACAATGCTGAAACCGAAGATTGTGAC
TTGAATTATAGTGATGTTATGTCTAAACTAGGTTTTCTTTCTGAGAGAAGCACAAGTCCC
ATAAATTCTTCTCCACCTCGCTGCTGGTCTCCCACAGATCCAAGAGCTGAAGAAATCATG
GCTGCTGCAGAAAAAGAGGCAATGCTTTTTAAGGGTCCTAATGTATATAAGAAGACTGTT
AATTCTCGTATAGGAAAAACTAGTCGCGCAAGAGCACAGATTAAGAAATCAAAAGCAAAG
CTTGCTAATCCCTCTATAGTTACTAAGAAAAGGAACAAACGAAATCAGACAAATAAACTA
GTAGATGATGGAAAAAAGAAACCAAGAGCAAAACAAAAAACAAATGAGAAAGGTACATCG
AGAAAGCATATAACACTTAAGGATGAAAAAATAAAATCTCAGTCTGGTGCTGAGGTTAAG
TTTGTACTGAAACACCAGAATGTGTCTGAATTTGCAAGTAGTTCTGGAGGCTCTCAACTA
CTTTTTAAACAGAAAGATATGCCACTAATGGGCTCTGCTGTAGATCATCCCCTTTCTGCT
TCCCTACCCACTGGAATTAATGCACAACAGAAGTTATCTGGCTGCTTTTCTTCTTTCTTA
GAAAGCAAGAAGTCTGTAGATTTGCAGACATTCCCCAGTTCACGAGATGATTTGCATCCA
TCAGTTGTTTGTAATTCTATAGGACCTGGAGTCTCAAAAATTAATGTTCAAAGGCCTCAT
AATCAAAGTGCTATGTTTACTCTAAAGGAATCAACGTTAATTCAAAAAAATATATTTGAC
CTTTCCAATCATTTATCTCAGGTAGCACAGAATACACAGATATCTTCTGGTATGTCCTCA
AAGATAGAAGATAATGCAAATAATATACAAAGAAACTATTTGTCATCAATCGGAAAGTTA
AGTGAATATCGCAATTCCCTAGAATCAAAGCTGGACCAAGCATATACCCCTAATTTTTTG
CATTGCAAAGACAGTCAGCAGCAGATTGTATGCATAGCGGAACAGTCAAAGCACAGTGAA
ACTTGTTCTCCGGGAAATACAGCTTCAGAGGAAAGCCAAATGCCTAATAATTGCTTTGTA
ACTTCCTTGAGAAGTCCAATCAAACAAATAGCATGGGAGCAAAAGCAAAGGGGCTTTATT
TTAGATATGTCAAATTTTAAACCTGAAAGAGTAAAACCGAGGTCATTATCAGAAGCAATT
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 16 GenBank Gene ID AF058701 Link Image
Enzyme 16 GeneCard ID REV3L Link Image
Enzyme 16 GenAtlas ID REV3L Link Image
Enzyme 16 HGNC ID HGNC:9968 Link Image
Enzyme 16 Chromosome Location 6
Enzyme 16 Locus 6q21
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6249
Enzyme 17 Name DNA polymerase epsilon, catalytic subunit A
Enzyme 17 Synonyms
  1. DNA polymerase II subunit A
Enzyme 17 Gene Name POLE
Enzyme 17 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 17 Number of Residues 2286
Enzyme 17 Molecular Weight 261521
Enzyme 17 Theoretical pI 6.35
Enzyme 17 GO Classification
Function
  • 3'-5' exonuclease activity
  • DNA binding
  • DNA-directed DNA polymerase activity
  • binding
  • catalytic activity
  • exonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
  • nucleotide binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • DNA metabolism
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 17 General Function Replication, recombination and repair
Enzyme 17 Specific Function Participates in DNA repair and in chromosomal DNA replication
Enzyme 17 Pathways
Enzyme 17 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 303157 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q07864 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name DPOE1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >6774 bp
ATGTCTCTGAGGAGCGGCGGGCGGCGGCGCGCGGACCCAGGCGCGGATGGCGAGGCCAGC
AGGGATGATGGCGCCACTTCCTCAGTTTCGGCACTCAAGCGCCTGGAACGGAGTCAGTGG
ACGGATAAGATGGATTTGCGGTTTGGTTTTGAGCGGCTGAAGGAGCCTGGTGAGAAGACA
GGCTGGCTCATTAACATGCATCCTGTGGCTTTGCCCTATAAACCGTATTTCTACATTGCG
ACCAGAAAGGGTTGTGAGCGAGAAGTTTCATCTTTTCTCTCCAAGAAGTTTCAGGGCAAA
ATTGCAAAAGTGGAGACTGTCCCCAAAGAGGATCTGGACTTGCCAAATCACTTGGTGGGT
TTGAAGCGAAATTACATCAGGCTGTCCTTCCACACTGTGGAGGATCTTGTCAAAGTGAGG
AAGGAGATCTCCCCTGCCGTGAAGAAGAACAGGGAGCAGGATCACGCCAGCGACGCGTAC
ACAGCTCTGCTTTCCAGTGTTCTGCAGAGGGGCGGTGTCATTACTGATGAAGAGGAAACC
TCTAAGAAGATAGCTGACCAGTTGGACAACATTGTGGACATGCGCGAGTACGATGTTCCC
TACCACATCCGCCTCTCCATTGACCTGAAGATCCACGTGGCTCATTGGTACAATGTCAGA
TACCGAGGAAATGCTTTTCCGGTAGAAATCACCCGCCGAGATGACCTTGTTGAACGACCT
GACCCTGTGGTTTTGGCATTTGACATTGAGACGACCAAACTGCCCCTCAAGTTTCCTGAT
GCTGAGACAGACCAGATTATGATGATTTCCTACATGATCGATGGCCAGGGCTACCTCATC
ACCAACAGGGAGATTGTTTCAGAAGATATTGAAGATTTTGAGTTCACCCCCAAGCCAGAA
TATGAAGGCCCCTTTTGTGTCTTCAATGAACCCGATGAGGCTCATCTGATCCAAAGGTGG
TTTGAACACGTCCAGGAGACCAAACCCACCATCATGGTCACCTACAACGGGGACTTTTTT
GACTGGCCATTTGTGGAGGCCCGGGCAGCAGTCCACGGTCTGAGCATGCAGCAGGAGATA
GGCTTCCAGAAGGACAGCCAGGGGGAGTACAAGGCGCCCCAGTGCATCCACATGGACTGC
CTCAGGTGGGTGAAGAGGGACAGTTACCTTCCTGTGGGCAGTCATAATCTCAAGGCGGCC
GCAAGCAAGCTAGGCTATGATCCCGTGGAGCTAGACCCGGAGACATGTGCCGGATCGACG
GAGCAGCCCCAGACTCTGGCCACGTATTCTGTGTCAGATGCTGTCGCCACTTACTACCTG
TACATGAAGTACGTCCACCCATTCATCTTTGCTCTGTGCACCATTATTCCCATGGAGCCC
GACGAGGTGCTGCGGAAGGGCTCTGGCACTCTGTGTGAGGCCTTGCTGATGGTGCAGGCC
TTCCACGCCAACATCATCTTCCCCAACAAGCAAGAGCAGGAGTTCAATAAGCTGACGGAC
GACGGACACGTGCTGGACTCTGAGACCTACGTCGGGGGCCACGTGGAGGCCCTCGAGTCT
GGGGTTTTCCGCAGCGATATCCCTTGCCGGTTTAGGATGAATCCTGCCGCCTTTGACTTC
CTGCTGCAGCGGGTTGAGAAGACCTTGCGCCACGCCCTTGAGGAAGAGGAGAAAGTGCCT
GTGGAGCAAGTCACCAACTTTGAAGAGGTGTGTGATGAGATTAAGAGCAAGCTTGCCTCC
CTGAAGGACGTTCCCAGCCGCATCGAGTGTCCACTCATCTACCACCTGGACGTGGGGGCC
ATGTACCCCAACATCATCCTGACCAACCGCCTGCAGCCCTCTGCCATGGTGGACGAAGCC
ACCTGTGCTGCCTGTGACTTCAATAAGCCTGGAGCAAACTGCCAGCGGAAGATGGCCTGG
CAGTGGAGGGGCGAGTTCATGCCAGCCAGTCGCAGCGAATACCATCGGATCCAGCACCAG
CTGGAGTCAGAGAAGTTCCCCCCCTTGTTCCCAGAGGGGCCAGCTCGGGCCTTTCATGAA
CTGTCCCGCGAGGAACAGGCGAAATACGAGAAGAGAAGGCTGGCGGATTACTGCCGGAAA
GCCTACAAGAAGATCCACATCACCAAGGTGGAAGAGCGTCTCACCACCATCTGCCAGCGG
GAAAACTCCTTCTACGTGGACACCGTGCGTGCCTTCCGGGACAGGCGTTACGAGTTCAAA
GGGCTCCACAAGGTGTGGAAAAAGAAGCTCTCGGCGGCCGTGGAGGTGGGCGACGCGGCT
GAGGTGAAGCGCTGCAAGAACATGGAGGTGCTGTATGACTCGCTGCAGCTGGCCCACAAG
TGCATCCTGAACTCCTTCTATGGCTATGTCATGCGCAAGGGGGCTCGCTGGTACTCCATG
GAGATGGCTGGCATCGTCTGCTTCACAGGGGCCAACATCATCACCCAGGCACGGGAGCTG
ATCGAGCAGATTGGGAGGCCCTTAGAGCTGGACACAGATGGTATATGGTGCGTCCTGCCC
AACAGCTTCCCAGAAAATTTTGTCTTCAAGACGACCAATGTGAAGAAGCCCAAAGTGACC
ATCTCCTACCCAGGCGCCATGTTGAACATCATGGTCAAGGAAGGCTTCACCAATGACCAG
TACCAGGAGCTGGCTGAGCCGTCCTCACTCACCTACGTCACCCGCTCAGAGAACAGCATC
TTTTTTGAGGTTGATGGGCCCTACCTTGCCATGATTCTTCCAGCCTCCAAGGAAGAAGGC
AAGAAATTGAAGAAGAGGTATGCTGTGTTCAATGAAGACGGTTCTCTGGCTGAGCTCAAG
GGCTTTGAGGTCAAACGCCGCGGGGAACTGCAGCTGATTAAGATCTTCCAATCCTCGGTG
TTTGAGGCCTTCCTCAAGGGCAGCACGCTGGAAGAGGTGTATGGCTCTGTAGCCAAGGTG
GCTGACTACTGGCTGGACGTGCTGTACAGCAAGGCAGCCAACATGCCTGACTCTGAGCTA
TTCGAGCTCATCTCTGAGAACCGTTCCATGTCTCGGAAGCTGGAAGATTACGGGGAGCAG
AAGTCTACGTCCATCAGCACAGCAAAGCGCCTGGCCGAGTTCCTGGGAGACCAGATGGTC
AAGGATGCAGGGCTGAGTTGCCGCTACATCATCTCCCGCAACGCCGAGGGCTCCCCTGTC
ACGGAGAGGGCCATCCCACTTGCCATTTTCCAAGCAGAGCCCACGGTGAGGAAGCACTTT
CTCCGGAAATGGCTCAAGAGCTCTTCCCTTCAAGACTTTGATATTCGAGCAATTCTGGAT
TGGGACTACTACATTGAGCGGCTGGGAAGCGCCATCCAGAAGATCATCACCATCCCTGCG
GCCCTGCAGCAGGTAAAGAACCCAGTGCCACGTGTCAAACACCCCGACTGGCTGCACAAA
AAACTGCTGGAGAAGAATGATGTCTACAAGCAGAAGAAGATCAGTGAGCTCTTCACCCTG
GAGGGCAGGAGACAGGTCACGATGGCCGAGGCCTCAGAAGACAGTCCGAGGCCAAGTGCT
CCTGACATGGAGGACTTCGGCCTCGTAAAGCTGCCTCACCCAGCAGCCCCTGTCACTGTG
AAGAGGAAGCGAGTTCTTTGGGAGAGCCAGGAGGAGTCCCAGGACCTCACGCCGACTGTG
CCCTGGCAGGAAATCTTGGGGCAGCCTCCCGCCCTGGGAACCAGCCAGGAGGAATGGCTT
GTCTGGCTCCGGTTCCACAAGAAGAAGTGGCAGCTGCAGGCCCGGCAGCGCCTCGCCCGC
AGGAAGAGGCAGCGTCTGGAGTCGGCAGAGGGTGTGCTCAGGCCCGGGGCCATCCGGGAT
GGTCCTGCCACGGGGCTGGGGAGCTTCTTGCGAAGAACTGCCCGCAGCATCCTGGACCTT
CCGTGGCAGATTGTGCAGATCAGCGAGACCAGCCAGGCCGGCCTGTTCAGGCTGTGGGCG
CTCGTTGGCAGTGACTTGCACTGCATCAGGCTGAGCATCCCCCGTGTGTTCTACGTGAAC
CAGCGAGTGCCTAAAGCGGAGGAGGGTGCTTCGTATCGCAAGGTAAATCGGGTCCTTCCT
CGCTCCAACATGGTCTACAATCTCTATGAGTATTCAGTGCCAGAGGACATGTACCAGGAA
CACATCAACGAGATCAACGCTGAGCTGTCAGCGCCAGACATCGAGGGCGTATATGAGACT
CAGGTTCCGTTACTGTTCCGGGCCCTGGTGCACCTGGGCTGTGTGTGTGTGGTCAATAAA
CAGCTGGTGAGGCACCTTTCAGGCTGGGAAGCAGAGACCTTTGCTCTTGAGCACCTGGAG
ATGCGCTCTCTGGCCCAGTTCAGCTACCTGGAACCAGGGAGTATCCGCCATATCTACCTG
TACCACCACGCACAGGCCCACAAAGCGCTCTTCGGGATCTTCATCCCCTCACAGCGCAGG
GCATCCGTCTTTGTGCTGGACACTGTGCGCACAGACCAGATGCCCAGCCTTGGCGCCCTG
TACTCAGCAGAGCACGGCCTCCTCCTGGAGAAGGTGGGCCCTGAGCTCCTGCCACCCCCC
AAACACACCTTCGAAGTTCGGGCAGAAACTGACCTGAAGACCATCTGCAGAGCCATCCAG
CGATTCCTGCTCGCCTACAAGGAGGAGCGCCGGGGGCCCACACTCATCGCTGTTCAGTCC
AGCTGGGAGCTGAAGAGGCTGGCCAGTGAAATTCCTGTCTTGGAGGAATTCCCACTGGTG
CCTATCTGTGTGGCTGACAAGATCAACTATGGGGTCCTGGACTGGCAGCGCCATGGAGCC
CGGCGCATGATCCGTCACTACCTCAACCTGGACACCTGCCTGTCGCAGGCCTTCGAGATG
AGCAGGTACTTTCACATTCCCATTGGGAACCTACCAGAGGACATCTCCACATTCGGCTCC
GACCTCTTCTTTGCCCGCCACCTCCAGCGCCACAACCACCTGCTCTGGCTGTCCCCTACA
GCCCGCCCTGACCTGGGTGGAAAGGAGGCTGATGACAACTGTCTTGTCATGGAGTTCGAT
GACCAAGCCACTGTTGAGATCAACAGTTCAGGCTGTTACTCCACAGTGTGTGTGGAGCTG
GACCTTCAGAACCTGGCCGTCAACACCATTCTCCAGTCTCACCATGTCAACGACATGGAG
GGGGCCGACAGCATGGGGATCAGCTTCGACGTGATCCAGCAGGCCTCCCTGGAGGACATG
ATCACGGGTGGTCAGGCTGCCAGTGCCCCGGCCAGCTACGATGAGACAGCCCTGTGCTCT
AACACCTTCAGGATCCTGAAGAGCATGGTCGTGGGCTGGGTGAAGGAGATCACCCAGTAC
CACAACATCTATGCAGACAACCAGGTGATGCACTTCTACCGCTGGCTTCGGTCGCCATCC
TCTCTGCTTCATGACCCTGCCCTGCACCGCACACTCCACAACATGATGAAGAAGCTCTTC
CTGCAGCTCATCGCTGAGTTCAAGCGCCTGGGGTCATCAGTCATCTACGCCAACTTCAAC
CGCATCATCCTCTGTACAAAGAAGCGCCGTGTGGAAGATGCCATCGCTTACGTGGAGTAC
ATCACCAGCAGCATCCATTCAAAGGAGACCTTCCATTCTCTGACAATTTCTTTCTCTCGA
TGCTGGGAATTTCTTCTCTGGATGGATCCATCTAACTATGGCGGAATCAAAGGAAAAGTT
TCATCTCGTATTCACTGTGGACTGCAAGACTCCCAGAAAGCAGGGGGAGCAGAGGATGAG
CAGGAAAATGAGGACGATGAGGAGGAAAGAGATGGGGAGGAGGAGGAAGAGGCGGAGGAA
TCCAACGTGGAGGATTTACTGGAAAACAACTGGAACATTTTGCAGTTTTTGCCACAGGCA
GCCTCCTGCCAGAACTACTTCCTCATGATTGTTTCAGCGTACATCGTGGCCGTGTACCAC
TGCATGAAGGACGGGCTGAGGCGCAGTGCTCCAGGGAGCACCCCCGTGAGGAGGAGGGGG
GCCAGCCAGCTCTCCCAGGAGGCCGAGGGGGCGGTCGGAGCCCTTCCCGGAATGATCACC
TTCTCTCAGGATTATGTCGCAAATGAGCTCACTCAGAGCTTCTTCACCATCACTCAGAAG
ATTCAGAAGAAAGTCACAGGCTCTCGGAACTCCACTGAGCTCTCAGAGATGTTTCCTGTC
CTCCCCGGTTCCCACTTGCTGCTCAATAACCCTGCCCTGGAGTTCATCAAATACGTGTGC
AAGGTGCTGTCCCTGGACACCAACATCACAAACCAGGTGAATAAGCTGAACCGAGACCTG
CTTCGCCTGGTGGATGTCGGCGAGTTCTCCGAGGAGGCCCAGTTCCGAGACCCCTGCCGC
TCCTACGTGCTTCCTGAGGTCATCTGCCGCAGCTGTAACTTCTGCCGCGACCTGGACCTG
TGTAAAGACTCTTCCTTCTCAGAGGATGGGGCGGTCCTGCCTCAGTGGCTCTGCTCCAAC
TGTCAGGCGCCCTACGACTCCTCTGCCATCGAGATGACGCTGGTGGAAGTTCTACAGAAG
AAGCTGATGGCCTTCACCCTGCAGGACCTGGTCTGCCTGAAGTGCCGCGGGGTGAAGGAG
ACCAGCATGCCTGTGTACTGCACGTGCGCGGGAGACTTCGCCCTCACCATCCACACCCAG
GTCTTCATGGAACAGATCGGAATATTCCGGAACATTGCCCAGCACTACGGCATGTCGTAC
CTCCTGGAGACCCTGGAGTGGCTGCTGCAGAAGAACCCACAGCTGGGCCATTAG
Enzyme 17 GenBank Gene ID S60080 Link Image
Enzyme 17 GeneCard ID POLE Link Image
Enzyme 17 GenAtlas ID POLE Link Image
Enzyme 17 HGNC ID HGNC:9177 Link Image
Enzyme 17 Chromosome Location 12
Enzyme 17 Locus 12q24.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6252
Enzyme 18 Name DNA polymerase mu
Enzyme 18 Synonyms
  1. Pol Mu
Enzyme 18 Gene Name POLM
Enzyme 18 Protein Sequence >DNA polymerase mu
MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLD
ACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECR
HRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFC
RAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKLF
TQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQKAGLQHHQDLSTPVLRSDVDALQQ
VVEEAVGQALPGATVTLTGGFRRGKLQGHDVDFLITHPKEGQEAGLLPRVMCRLQDQGLI
LYHQHQHSCCESPTRLAQQSHMDAFERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLV
VAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFDPEQKTFFQAASEEDIFR
HLGLEYLPPEQRNA
Enzyme 18 Number of Residues 494
Enzyme 18 Molecular Weight 54816
Enzyme 18 Theoretical pI 8.50
Enzyme 18 GO Classification
Function
  • DNA binding
  • DNA nucleotidylexotransferase activity
  • DNA-directed DNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • DNA metabolism
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • cell
  • intracellular
Enzyme 18 General Function Replication, recombination and repair
Enzyme 18 Specific Function Seems to act as an Ig mutase which is responsible for immunoglobulin (Ig) gene hypermutation
Enzyme 18 Pathways
Enzyme 18 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 18 Pfam Domain Function Not Available
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 6822168 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9NP87 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name DPOLM_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 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 18 GenBank Gene ID AJ131891 Link Image
Enzyme 18 GeneCard ID POLM Link Image
Enzyme 18 GenAtlas ID POLM Link Image
Enzyme 18 HGNC ID HGNC:9185 Link Image
Enzyme 18 Chromosome Location 7
Enzyme 18 Locus 7p13
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6254
Enzyme 19 Name DNA polymerase epsilon subunit 3
Enzyme 19 Synonyms
  1. DNA polymerase II subunit 3
  2. DNA polymerase epsilon subunit p17
  3. Chromatin accessibility complex 17
  4. HuCHRAC17
  5. CHRAC-17
  6. Arsenic- transactivated protein
  7. AsTP
Enzyme 19 Gene Name POLE3
Enzyme 19 Protein Sequence >DNA polymerase epsilon subunit 3
MAERPEDLNLPNAVITRIIKEALPDGVNISKEARSAISRAASVFVLYATSCANNFAMKGK
RKTLNASDVLSAMEEMEFQRFVTPLKEALEAYRREQKGKKEASEQKKKDKDKKTDSEEQD
KSRDEDNDEDEERLEEEEQNEEEEVDN
Enzyme 19 Number of Residues 147
Enzyme 19 Molecular Weight 16860
Enzyme 19 Theoretical pI 4.38
Enzyme 19 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
Enzyme 19 General Function Chromatin structure and dynamics
Enzyme 19 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 remodelling activity of ISWI/SNF2H and ACF1
Enzyme 19 Pathways
Enzyme 19 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 8100806 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9NRF9 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name DPOE3_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >444 bp
ATGGCGGAGAGGCCCGAGGACCTAAACCTGCCCAATGCCGTGATCACCAGGATCATCAAG
GAGGCGCTCCCGGACGGTGTCAACATCTCCAAGGAGGCCCGGAGCGCCATCTCCCGCGCC
GCCAGCGTCTTCGTGCTGTACGCCACATCCTGTGCTAACAACTTTGCAATGAAAGGAAAG
CGGAAGACGCTGAATGCCAGTGATGTGCTCTCAGCCATGGAAGAGATGGAGTTCCAGCGG
TTCGTTACCCCATTGAAAGAAGCTCTGGAAGCATATAGGCGGGAGCAGAAAGGCAAGAAG
GAGGCCTCAGAGCAAAAGAAGAAGGACAAAGACAAAAAAACAGACTCGGAAGAGCAAGAC
AAGAGCAGGGATGAGGACAATGATGAAGACGAAGAAAGGCTGGAAGAAGAAGAACAGAAT
GAAGAGGAAGAAGTAGACAACTGA
Enzyme 19 GenBank Gene ID AF226077 Link Image
Enzyme 19 GeneCard ID POLE3 Link Image
Enzyme 19 GenAtlas ID POLE3 Link Image
Enzyme 19 HGNC ID HGNC:13546 Link Image
Enzyme 19 Chromosome Location 9
Enzyme 19 Locus 9q33
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6256
Enzyme 20 Name DNA polymerase subunit gamma 1
Enzyme 20 Synonyms
  1. Mitochondrial DNA polymerase catalytic subunit
  2. PolG-alpha
Enzyme 20 Gene Name POLG
Enzyme 20 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 20 Number of Residues 1239
Enzyme 20 Molecular Weight 139564
Enzyme 20 Theoretical pI 6.89
Enzyme 20 GO Classification
Function
  • DNA binding
  • DNA-directed DNA polymerase activity
  • binding
  • catalytic activity
  • gamma DNA-directed DNA polymerase activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • DNA metabolism
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • gamma DNA polymerase complex
  • protein complex
Enzyme 20 General Function Replication, recombination and repair
Enzyme 20 Specific Function Involved in the replication of mitochondrial DNA
Enzyme 20 Pathways
Enzyme 20 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 1399956 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P54098 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name DPOG1_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 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 20 GenBank Gene ID U60325 Link Image
Enzyme 20 GeneCard ID POLG Link Image
Enzyme 20 GenAtlas ID POLG Link Image
Enzyme 20 HGNC ID HGNC:9179 Link Image
Enzyme 20 Chromosome Location 15
Enzyme 20 Locus 15q25
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6257
Enzyme 21 Name DNA polymerase iota
Enzyme 21 Synonyms
  1. RAD30 homolog B
  2. Eta2
Enzyme 21 Gene Name POLI
Enzyme 21 Protein Sequence >DNA polymerase iota
MELADVGAAASSQGVHDQVLPTPNASSRVIVHVDLDCFYAQVEMISNPELKDKPLGVQQK
YLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTRYREMSYKVTELLEEFSPVV
ERLGFDENFVDLTEMVEKRLQQLQSDELSAVTVSGHVYNNQSINLLDVLHIRLLVGSQIA
AEMREAMYNQLGLTGCAGVASNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNHIKEIP
GIGYKTAKCLEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQ
SFSEEDSFKKCSSEVEAKNKIEELLASLLNRVCQDGRKPHTVRLIIRRYSSEKHYGRESR
QCPIPSHVIQKLGTGNYDVMTPMVDILMKLFRNMVNVKMPFHLTLLSVCFCNLKALNTAK
KGLIDYYLMPSLSTTSRSGKHSFKMKDTHMEDFPKDKETNRDFLPSGRIESTRTRESPLD
TTNFSKEKDINEFPLCSLPEGVDQEVFKQLPVDIQEEILSGKSREKFQGKGSVSCPLHAS
RGVLSFFSKKQMQDIPINPRDHLSSSKQVSSVSPCEPGTSGFNSSSSSYMSSQKDYSYYL
DNRLKDERISQGPKEPQGFHFTNSNPAVSAFHSFPNLQSEQLFSRNHTTDSHKQTVATDS
HEGLTENREPDSVDEKITFPSDIDPQVFYELPEAVQKELLAEWKRTGSDFHIGHK
Enzyme 21 Number of Residues 715
Enzyme 21 Molecular Weight 80347
Enzyme 21 Theoretical pI 6.82
Enzyme 21 GO Classification
Function
  • DNA binding
  • DNA-directed DNA polymerase activity
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • DNA metabolism
  • DNA repair
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 21 General Function Replication, recombination and repair
Enzyme 21 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 21 Pathways
Enzyme 21 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 5739208 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9UNA4 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name POLI_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 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 21 GenBank Gene ID AF140501 Link Image
Enzyme 21 GeneCard ID POLI Link Image
Enzyme 21 GenAtlas ID POLI Link Image
Enzyme 21 HGNC ID HGNC:9182 Link Image
Enzyme 21 Chromosome Location 18
Enzyme 21 Locus 18q21.1
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6258
Enzyme 22 Name DNA polymerase epsilon subunit 2
Enzyme 22 Synonyms
  1. DNA polymerase II subunit 2
  2. DNA polymerase epsilon subunit B
Enzyme 22 Gene Name POLE2
Enzyme 22 Protein Sequence >DNA polymerase epsilon subunit 2
MAPERLRSRALSAFKLRGLLLRGEAIKYLTEALQSISELELEDKLEKIINAVEKQPLSSN
MIERSVVEAAVQECSQSVDETIEHVFNIIGAFDIPRFVYNSERKKFLPLLMTNHPAPNLF
GTPRDKAEMFRERYTILHQRTHRHELFTPPVIGSHPDESGSKFQLKTIETLLGSTTKIGD
AIVLGMITQLKEGKFFLEDPTGTVQLDLSKAQFHSGLYTEACFVLAEGWFEDQVFHVNAF
GFPPTEPSSTTRAYYGNINFFGGPSNTSVKTSAKLKQLEEENKDAMFVFLSDVWLDQVEV
LEKLRIMFAGYSPAPPTCFILCGNFSSAPYGKNQVQALKDSLKTLADIICEYPDIHQSSR
FVFVPGPEDPGFGSILPRPPLAESITNEFRQRVPFSVFTTNPCRIQYCTQEITVFREDLV
NKMCRNCVRFPSSNLAIPNHFVKTILSQGHLTPLPLYVCPVYWAYDYALRVYPVPDLLVI
ADKYDPFTTTNTECLCINPGSFPRSGFSFKVFYPSNKTVEDSKLQGF
Enzyme 22 Number of Residues 527
Enzyme 22 Molecular Weight 59538
Enzyme 22 Theoretical pI 6.30
Enzyme 22 GO Classification
Function
  • DNA binding
  • DNA-directed DNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • DNA metabolism
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function Participates in DNA repair and in chromosomal DNA replication
Enzyme 22 Pathways
Enzyme 22 Reactions
  • deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • 1-25
Enzyme 22 Transmembrane Regions Not Available
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 2697123 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P56282 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name DPOE2_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1581 bp
ATGGCGCCGGAGCGGCTGCGGAGCCGGGCGCCCTCCGCCTTCAAGTTGCGGGGCTTGCTG
CTCCGTGGTGAAGCTATTAAGTACCTCACAGAAGCTCTTCAGTCTATCAGTGAATTAGAG
CTTGAAGATAAACTGGAAAAGATAATTAATGCAGTTGAGAAGCAACCCTTGTCATCAAAC
ATGATTGAACGATCTGTGGTGGAAGCAGCAGTCCAGGAATGCAGTCAGTCTGTTGATGAA
ACTATAGAGCACGTTTTCAATATCATAGGAGCATTTGATATTCCACGCTTTGTGTACAAT
TCAGAAAGAAAAAAATTTCTTCCTCTGTTAATGACCAACCACCCTGCACCAAATTTATTT
GGAACACCAAGAGATAAAGCAGAGATGTTTCGTGAGCGATATACCATTTTGCACCAGAGG
ACCCACAGGCATGAATTATTTACTCCTCCGGTGATAGGTTCTCACCCTGATGAAAGCGGA
AGCAAATTCCAGCTTAAAACAATAGAAACCTTATTGGGTAGTACAACCAAAATCGGAGAT
GCGATTGTTCTTGGAATGATAACGCAGTTAAAAGAGGGAAAATTTTTTCTGGAAGATCCT
ACTGGAACAGTCCAACTAGACCTTAGTAAAGCTCAGTTCCATAGTGGTTTATACACAGAG
GCATGCTTTGTCTTAGCAGAAGGTTGGTTTGAAGATCAAGTGTTTCATGTCAATGCCTTT
GGATTTCCACCCACTGAGCCCTCTAGTACTACTAGGGCATACTATGGAAATATTAATTTT
TTTGGAGGTCCTTCTAATACATCTGTGAAGACTTCTGCAAAACTAAAACAGCTAGAAGAG
GAGAATAAAGATGCTATGTTTGTGTTTTTATCTGATGTTTGGTTGGACCAGGTGGAAGTA
TTGGAAAAACTTCGCATAATGTTTGCTGGTTATTCACCAGCACCTCCAACCTGCTTTATT
CTGTGTGGTAATTTTTCATCTGCACCATATGGAAAAAATCAAGTTCAAGCTTTGAAAGAT
TCCCTAAAAACTTTGGCAGATATAATATGTGAATACCCAGATATTCACCAAAGTCGTTTT
GTGTTTGTACCTGGTCCAGAGGATCCTGGATTTGGTTCCATCTTACCAAGGCCACCACTT
GCTGAAAGCATCACTAATGAATTCAGACAAAGGGTACCATTTTCAGTTTTTACTACTAAT
CCTTGCAGAATTCAGTACTGTACACAGGAAATTACTGTCTTCCGTGAAGACTTAGTAAAT
AAAATGTGCAGAAACTGCGTCCGTTTTCCTAGCAGCAATTTGGCTATTCCTAATCACTTT
GTAAAGACTATCTTATCCCAAGGACATCTGACTCCCCTACCTCTTTATGTCTGCCCAGTG
TATTGGGCATATGACTATGCTTTGAGAGTGTATCCTGTGCCCGATCTACTTGTCATTGCA
GACAAATATGATCCTTTCACTACGACAAATACCGAATGCCTCTGCATAAACCCTGGCTCT
TTTCCAAGAAGTGGATTTTCATTCAAAGTTTTTTATCCTTCTAATAAGACAGTAGAAGAT
AGCAAACTTCAAGGCTTTTGA
Enzyme 22 GenBank Gene ID AF025840 Link Image
Enzyme 22 GeneCard ID POLE2 Link Image
Enzyme 22 GenAtlas ID POLE2 Link Image
Enzyme 22 HGNC ID HGNC:9178 Link Image
Enzyme 22 Chromosome Location 14
Enzyme 22 Locus 14q21-q22
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 7769
Enzyme 23 Name Apoptotic protease-activating factor 1
Enzyme 23 Synonyms
  1. Apaf-1
Enzyme 23 Gene Name APAF1
Enzyme 23 Protein Sequence >Apoptotic protease-activating factor 1
MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMI
LKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGITSYVRTVLCEGGVP
QRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPG
GVHWVSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRILMLRKHPRSLL
ILDDVWDSWVLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVN
MKKADLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIRKSSSYD
YEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVN
KSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQFQRYHQPHTLSPDQEDC
MYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAV
SENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINK
KNITNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEV
LCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFTNSSHHLLLATGS
SDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKS
INVKQFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHH
STIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTS
SDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTGQIDYLT
EAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLIS
SSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKVWNIITGNKEKD
FVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDST
LLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIK
WWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE
Enzyme 23 Number of Residues 1248
Enzyme 23 Molecular Weight 141841
Enzyme 23 Theoretical pI 6.37
Enzyme 23 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
  • apoptosis
  • cell death
  • death
  • physiological process
  • programmed cell death
  • regulation of apoptosis
  • regulation of biological process
  • regulation of cellular physiological process
  • regulation of physiological process
  • regulation of programmed cell death
Component
  • cell
  • intracellular
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 2330015 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID O14727 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name APAF_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >3585 bp
ATGGATGCAAAAGCTCGAAATTGTTTGCTTCAACATAGAGAAGCTCTGGAAAAGGACATC
AAGACATCCTACATCATGGATCACATGATTAGTGATGGATTTTTAACAATATCAGAAGAG
GAAAAAGTAAGAAATGAGCCCACTCAACAGCAAAGAGCAGCTATGCTGATTAAAATGATA
CTTAAAAAAGATAATGATTCCTACGTATCATTCTACAATGCTCTACTACATGAAGGATAT
AAAGATCTTGCTGCCCTTCTCCATGATGGCATTCCTGTTGTCTCTTCTTCCAGTGTAAGG
ACAGTCCTGTGTGAAGGTGGAGTACCACAGAGGCCAGTTGTTTTTGTCACAAGGAAGAAG
CTGGTGAATGCAATTCAGCAGAAGCTCTCCAAATTGAAAGGTGAACCAGGATGGGTCACC
ATACATGGAATGGCAGGCTGTGGGAAGTCTGTATTAGCTGCAGAAGCTGTTAGAGATCAT
TCCCTTTTAGAAGGTTGTTTCCCAGGGGGAGTGCATTGGGTTTCAGTTGGGAAACAAGAC
AAATCTGGGCTTCTGATGAAACTGCAGAATCTTTGCACACGGTTGGATCAGGATGAGAGT
TTTTCCCAGAGGCTTCCACTTAATATTGAAGAGGCTAAAGACCGTCTCCGCATTCTGATG
CTTCGCAAACACCCAAGGTCTCTCTTGATCTTGGATGATGTTTGGGACTCTTGGGTGTTG
AAAGCTTTTGACAGTCAGTGTCAGATTCTTCTTACAACCAGAGACAAGAGTGTTACAGAT
TCAGTAATGGGTCCTAAATATGTAGTCCCTGTGGAGAGTTCCTTAGGAAAGGAAAAAGGA
CTTGAAATTTTATCCCTTTTTGTTAATATGAAGAAGGCAGATTTGCCAGAACAAGCTCAT
AGTATTATAAAAGAATGTAAAGGCTCTCCCCTTGTAGTATCTTTAATTGGTGCACTTTTA
CGTGATTTTCCCAATCGCTGGGAGTACTACCTCAAACAGCTTCAGAATAAGCAGTTTAAG
AGAATAAGGAAATCTTCGTCTTATGATTATGAGGCTCTAGATGAAGCCATGTCTATAAGT
GTTGAAATGCTCAGAGAAGACATCAAAGATTATTACACAGATCTTTCCATCCTTCAGAAG
GACGTTAAGGTGCCTACAAAGGTGTTATGTATTCTCTGGGACATGGAAACTGAAGAAGTT
GAAGACATACTGCAGGAGTTTGTAAATAAGTCTCTTTTATTCTGTGATCGGAATGGAAAG
TCGTTTCGTTATTATTTACATGATCTTCAAGTAGATTTTCTTACAGAGAAGAATTGCAGC
CAGCTTCAGGATCTACATAAGAAGATAATCACTCAGTTTCAGAGATATCACCAGCCGCAT
ACTCTTTCACCAGATCAGGAAGACTGTATGTATTGGTACAACTTTCTGGCCTATCACATG
GCCAGTGCCAAGATGCACAAGGAACTTTGTGCTTTAATGTTTTCCCTGGATTGGATTAAA
GCAAAAACAGAACTTGTAGGCCCTGCTCATCTGATTCATGAATTTGTGGAATACAGACAT
ATACTAGATGAAAAGGATTGTGCAGTCAGTGAGAATTTTCAGGAGTTTTTATCTTTAAAT
GGACACCTTCTTGGACGACAGCCATTTCCTAATATTGTACAACTGGGTCTCTGTGAGCCG
GAAACTTCAGAAGTTTATCAGCAAGCTAAGCTGCAGGCCAAGCAGGAGGTCGATAATGGA
ATGCTTTACCTGGAATGGATAAACAAAAAAAACATCACGAATCTTTCCCGCTTAGTTGTC
CGCCCCCACACAGATGCTGTTTACCATGCCTGCTTTTCTGAGGATGGTCAGAGAATAGCT
TCTTGTGGAGCTGATAAAACCTTACAGGTGTTCAAAGCTGAAACAGGAGAGAAACTTCTA
GAAATCAAGGCTCATGAGGATGAAGTGCTTTGTTGTGCATTCTCTACAGATGACAGATTT
ATAGCAACCTGCTCAGTGGATAAAAAAGTGAAGATTTGGAATTCTATGACTGGGGAACTA
GTACACACCTATGATGAGCACTCAGAGCAAGTCAATTGCTGCCATTTCACCAACAGTAGT
CATCATCTTCTCTTAGCCACTGGGTCAAGTGACTGCTTCCTCAAACTTTGGGATTTGAAT
CAAAAAGAATGTCGAAATACCATGTTTGGTCATACAAATTCAGTCAATCACTGCAGATTT
TCACCAGATGATAAGCTTTTGGCTAGTTGTTCAGCTGATGGAACCTTAAAGCTTTGGGAT
GCGACATCAGCAAATGAGAGGAAAAGCATTAATGTGAAACAGTTCTTCCTAAATTTGGAG
GACCCTCAAGAGGATATGGAAGTGATAGTGAAGTGTTGTTCGTGGTCTGCTGATGGTGCA
AGGATAATGGTGGCAGCAAAAAATAAAATCTTTTTGTGGAATACAGACTCACGTTCAAAG
GTGGCTGATTGCAGAGGACATTTAAGTTGGGTTCATGGTGTGATGTTTTCTCCTGATGGA
TCATCATTTTTGACATCTTCTGATGACCAGACAATCAGGCTCTGGGAGACAAAGAAAGTA
TGTAAGAACTCTGCTGTAATGTTAAAGCAAGAAGTAGATGTTGTGTTTCAAGAAAATGAA
GTGATGGTCCTTGCAGTTGACCATATAAGACGTCTGCAACTCATTAATGGAAGAACAGGT
CAGATTGATTATCTGACTGAAGCTCAAGTTAGCTGCTGTTGCTTAAGTCCACATCTTCAG
TACATTGCATTTGGAGATGAAAATGGAGCCATTGAGATTTTAGAACTTGTAAACAATAGA
ATCTTCCAGTCCAGGTTTCAGCACAAGAAAACTGTATGGCACATCCAGTTCACAGCCGAT
GAGAAGACTCTTATTTCAAGTTCTGATGATGCTGAAATTCAGGTATGGAATTGGCAATTG
GACAAATGTATCTTTCTACGAGGCCATCAGGAAACAGTGAAAGACTTTAGACTCTTGAAA
AATTCAAGACTGCTTTCTTGGTCATTTGATGGAACAGTGAAGGTATGGAATATTATTACT
GGAAATAAAGAAAAAGACTTTGTCTGTCACCAGGGTACAGTACTTTCTTGTGACATTTCT
CACGATGCTACCAAGTTTTCATCTACCTCTGCTGACAAGACTGCAAAGATCTGGAGTTTT
GATCTCCTTTTGCCACTTCATGAATTGAGGGGCCACAACGGCTGTGTGCGCTGCTCTGCC
TTCTCTGTGGACAGTACCCTGCTGGCAACGGGAGATGACAATGGAGAAATCAGGATATGG
AATGTCTCAAACGGTGAGCTTCTTCATTTGTGTGCTCCGCTTTCAGAAGAAGGAGCTGCT
ACCCATGGAGGCTGGGTGACTGACCTTTGCTTTTCTCCAGATGGCAAAATGCTTATCTCT
GCTGGAGGATATATTAAGTGGTGGAACGTTGTCACTGGGGAATCCTCACAGACCTTCTAC
ACAAATGGAACCAATCTTAAGAAAATACACGTGTCCCCTGACTTCAAAACATATGTGACT
GTGGATAATCTTGGTATTTTATATATTTTACAGACTTTAGAATAA
Enzyme 23 GenBank Gene ID AF013263 Link Image
Enzyme 23 GeneCard ID APAF1 Link Image
Enzyme 23 GenAtlas ID APAF1 Link Image
Enzyme 23 HGNC ID HGNC:576 Link Image
Enzyme 23 Chromosome Location 12
Enzyme 23 Locus 12q23
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Zou H, Henzel WJ, Liu X, Lutschg A, Wang X: Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell. 1997 Aug 8;90(3):405-13. [PubMed Link Image]
  2. Hahn C, Hirsch B, Jahnke D, Durkop H, Stein H: Three new types of Apaf-1 in mammalian cells. Biochem Biophys Res Commun. 1999 Aug 11;261(3):746-9. [PubMed Link Image]
  3. Saleh A, Srinivasula SM, Acharya S, Fishel R, Alnemri ES: Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. J Biol Chem. 1999 Jun 18;274(25):17941-5. [PubMed Link Image]
  4. Hu Y, Benedict MA, Ding L, Nunez G: Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis. EMBO J. 1999 Jul 1;18(13):3586-95. [PubMed Link Image]
  5. Ogawa T, Shiga K, Hashimoto S, Kobayashi T, Horii A, Furukawa T: APAF-1-ALT, a novel alternative splicing form of APAF-1, potentially causes impeded ability of undergoing DNA damage-induced apoptosis in the LNCaP human prostate cancer cell line. Biochem Biophys Res Commun. 2003 Jun 27;306(2):537-43. [PubMed Link Image]
  6. Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed Link Image]
  7. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  8. Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES: Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol Cell. 1998 Jun;1(7):949-57. [PubMed Link Image]
  9. Moroni MC, Hickman ES, Lazzerini Denchi E, Caprara G, Colli E, Cecconi F, Muller H, Helin K: Apaf-1 is a transcriptional target for E2F and p53. Nat Cell Biol. 2001 Jun;3(6):552-8. [PubMed Link Image]
  10. Vaughn DE, Rodriguez J, Lazebnik Y, Joshua-Tor L: Crystal structure of Apaf-1 caspase recruitment domain: an alpha-helical Greek key fold for apoptotic signaling. J Mol Biol. 1999 Oct 29;293(3):439-47. [PubMed Link Image]
  11. Day CL, Dupont C, Lackmann M, Vaux DL, Hinds MG: Solution structure and mutagenesis of the caspase recruitment domain (CARD) from Apaf-1. Cell Death Differ. 1999 Nov;6(11):1125-32. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 8075
Enzyme 24 Name Uridine-cytidine kinase 2
Enzyme 24 Synonyms
  1. UCK 2
  2. Uridine monophosphokinase 2
  3. Cytidine monophosphokinase 2
Enzyme 24 Gene Name UCK2
Enzyme 24 Protein Sequence >Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
Enzyme 24 Number of Residues 261
Enzyme 24 Molecular Weight 29299
Enzyme 24 Theoretical pI 6.68
Enzyme 24 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 24 General Function Nucleotide transport and metabolism
Enzyme 24 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, 4-N-acetylcytidine, 4-N- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and 4-N-anisoylcytidine
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP + uridine = ADP + UMP
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 1655420 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q9BZX2 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name UCK2_HUMAN Link Image
Enzyme 24 PDB ID 1XRJ Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >336 bp
ATGAAGCTTTTTGTGGATACAGATGCGGACACCCGGCTCTCACGCAGAGTATTAAGGGAC
ATCAGCGAGAGAGGCAGGGATCTTGAGCAGATTTTATCTCAGTACATTACGTTCGTCAAG
CCTGCCTTTGAGGAATTCTGCTTGCCAACAAAGCAGTATGCTGATGTGATCATCCCTAGA
GGTGCAGATAATCTGGTGGCCATCAACCTCATCGAGCAGCACATCCAGGACATCCTGAAT
GGAGGGCCCTCCAAACGGCAGACCAATGGCTGTCTCAACGGCTACACCCCTTCACGCAAG
AGGCAGGCATCGGAGTCCAGCAGCAGGCCGCATTGA
Enzyme 24 GenBank Gene ID D78335 Link Image
Enzyme 24 GeneCard ID UCK2 Link Image
Enzyme 24 GenAtlas ID UCK2 Link Image
Enzyme 24 HGNC ID HGNC:12562 Link Image
Enzyme 24 Chromosome Location 1
Enzyme 24 Locus 1q23
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 13098
Enzyme 25 Name Uridine/cytidine kinase-like 1
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name UCKL1
Enzyme 25 Protein Sequence >Uridine/cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
Enzyme 25 Number of Residues 548
Enzyme 25 Molecular Weight 61142
Enzyme 25 Theoretical pI 7.40
Enzyme 25 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 25 General Function Nucleotide transport and metabolism
Enzyme 25 Specific Function May contribute to UTP accumulation needed for blast transformation and proliferation
Enzyme 25 Pathways
Enzyme 25 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964] ALL_REAC R00964
  • (other) R00513 R00516 R00517 R00962 R00967 R00968 R00970 R01548 R01549 R01880 R02091 R02096 R02097 R02327 R02332 R02371 R02372
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 38228699 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q9NWZ5 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name UCKL1_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence Not Available
Enzyme 25 GenBank Gene ID AJ605558 Link Image
Enzyme 25 GeneCard ID Q9NWZ5 Link Image
Enzyme 25 GenAtlas ID UCKL1 Link Image
Enzyme 25 HGNC ID HGNC:15938 Link Image
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 15191
Enzyme 26 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 26 Synonyms Not Available
Enzyme 26 Gene Name NME7
Enzyme 26 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 26 Number of Residues 376
Enzyme 26 Molecular Weight 42492
Enzyme 26 Theoretical pI 6.44
Enzyme 26 GO Classification Not Available
Enzyme 26 General Function Nucleotide transport and metabolism
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
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 158254838 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID A8K3T6 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name A8K3T6_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 26 GenBank Gene ID AK290701 Link Image
Enzyme 26 GeneCard ID A8K3T6 Link Image
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 Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 15200
Enzyme 27 Name Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name UCK1
Enzyme 27 Protein Sequence >Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
Enzyme 27 Number of Residues 201
Enzyme 27 Molecular Weight 22761
Enzyme 27 Theoretical pI 6.23
Enzyme 27 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 27 General Function Nucleotide transport and metabolism
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 57162360 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q5JT13 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name Q5JT13_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >807 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGTCGACCGTGTGTGAGAAGATCATGGAGTTGCTGGGACAG
AACGAGGTGGAACAGCGGCAGCGGAAGGTGGTCATCCTGAGCCAGGACAGGTTCTACAAG
GTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTGAAAGGACAGTACAATTTTGACCATCCA
GATGCCTTTGATAATGATTTGATGCACAGGACTCTGAAGAACATCGTGGAGGGCAAAACG
GTGGAGGTGCCGACCTATGATTTTGTGACACACTCAAGGTTACCAGAGACCACGGTGGTC
TACCCTGCGGACGTGGTTCTGTTTGAGGGCATCTTGGTGTTCTACAGCCAGGAGATCCGG
GACATGTTCCACCTGCGCCTCTTCGTGGACACCGACTCCGACGTCAGGCTGTCTCGAAGA
GTTCTCCGGGACGTGCGCCGAGGGAGGGACCTGGAGCAGATTCTGACGCAGTACACCACC
TTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTGCCGACAAAGAAGTATGCCGATGTGATC
ATCCCGCGAGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGAC
ATTCTGAATGGTGACATCTGCAAATGGCACCGAGGAGGGTCCAATGGGCGGAGCTACAAG
CGGACCTTTTCTGAGCCAGGGGACCACCCTGGGATGCTGACCTCTGGCAAACGGTCACAT
TTGGAGTCCAGCAGCAGACCCCACTGA
Enzyme 27 GenBank Gene ID AL358781 Link Image
Enzyme 27 GeneCard ID Q5JT13 Link Image
Enzyme 27 GenAtlas ID UCK1 Link Image
Enzyme 27 HGNC ID HGNC:14859 Link Image
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 15209
Enzyme 28 Name cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name Not Available
Enzyme 28 Protein Sequence >cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQGYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
Enzyme 28 Number of Residues 917
Enzyme 28 Molecular Weight 102388
Enzyme 28 Theoretical pI 6.70
Enzyme 28 GO Classification Not Available
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function Not Available
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 158257456 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID A8K7J7 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name A8K7J7_HUMAN Link Image
Enzyme 28 PDB ID 1HKB Link Image
Enzyme 28 PDB File Show
Enzyme 28 3D Structure
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >2754 bp
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGGACGAATATTCCCTAAATGCTGGGAAACAAGGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGCTGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
Enzyme 28 GenBank Gene ID AK292012 Link Image
Enzyme 28 GeneCard ID A8K7J7 Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs Not Available
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 15252
Enzyme 29 Name Myb-binding protein 1A
Enzyme 29 Synonyms Not Available
Enzyme 29 Gene Name MYBBP1A
Enzyme 29 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 29 Number of Residues 1328
Enzyme 29 Molecular Weight 148856
Enzyme 29 Theoretical pI 9.87
Enzyme 29 GO Classification
Function
  • DNA binding
  • DNA-directed DNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • transcription
Component
Enzyme 29 General Function Not Available
Enzyme 29 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 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 6959304 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q9BQG0 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name MBB1A_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 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 29 GenBank Gene ID AF147709 Link Image
Enzyme 29 GeneCard ID Q9BQG0 Link Image
Enzyme 29 GenAtlas ID MYBBP1A Link Image
Enzyme 29 HGNC ID HGNC:7546 Link Image
Enzyme 29 Chromosome Location 17
Enzyme 29 Locus 17p13.3
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 15253
Enzyme 30 Name DNA polymerase theta
Enzyme 30 Synonyms Not Available
Enzyme 30 Gene Name POLQ
Enzyme 30 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 30 Number of Residues 2590
Enzyme 30 Molecular Weight 289663
Enzyme 30 Theoretical pI 7.42
Enzyme 30 GO Classification
Function
  • ATP binding
  • DNA binding
  • DNA-directed DNA polymerase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • helicase activity
  • nucleic acid binding
  • nucleotide binding
  • nucleotidyltransferase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • DNA metabolism
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Not Available
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 76364226 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q6VMB5 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name Q6VMB5_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 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 30 GenBank Gene ID AY338826 Link Image
Enzyme 30 GeneCard ID Q6VMB5 Link Image
Enzyme 30 GenAtlas ID POLQ Link Image
Enzyme 30 HGNC ID HGNC:9186 Link Image
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. 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 Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 15254
Enzyme 31 Name cDNA FLJ76751, highly similar to Homo sapiens polymerase (DNA directed) sigma (POLS), mRNA (Polymerase (DNA directed) sigma)
Enzyme 31 Synonyms Not Available
Enzyme 31 Gene Name POLS
Enzyme 31 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 31 Number of Residues 542
Enzyme 31 Molecular Weight 59874
Enzyme 31 Theoretical pI 9.81
Enzyme 31 GO Classification Not Available
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function Not Available
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function Not Available
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 158260737 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID A8K1E2 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name A8K1E2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 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 31 GenBank Gene ID AK289857 Link Image
Enzyme 31 GeneCard ID A8K1E2 Link Image
Enzyme 31 GenAtlas ID Not Available
Enzyme 31 HGNC ID Not Available
Enzyme 31 Chromosome Location Not Available
Enzyme 31 Locus Not Available
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References Not Available
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 16476
Enzyme 32 Name cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
Enzyme 32 Synonyms Not Available
Enzyme 32 Gene Name PKM2
Enzyme 32 Protein Sequence >cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
Enzyme 32 Number of Residues 531
Enzyme 32 Molecular Weight 57938
Enzyme 32 Theoretical pI 7.94
Enzyme 32 GO Classification
Function
  • catalytic activity
  • kinase activity
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 32 General Function Carbohydrate transport and metabolism
Enzyme 32 Specific Function Not Available
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein Not Available
Enzyme 32 UniProtKB/Swiss-Prot ID B2R5N8 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name B2R5N8_HUMAN Link Image
Enzyme 32 PDB ID 1F3X Link Image
Enzyme 32 PDB File Show
Enzyme 32 3D Structure
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence Not Available
Enzyme 32 GenBank Gene ID AK312253 Link Image
Enzyme 32 GeneCard ID B2R5N8 Link Image
Enzyme 32 GenAtlas ID Not Available
Enzyme 32 HGNC ID Not Available
Enzyme 32 Chromosome Location 15
Enzyme 32 Locus 15q22
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References Not Available
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 16536
Enzyme 33 Name Polymerase (DNA directed) kappa, isoform CRA_b
Enzyme 33 Synonyms
  1. SubName: cDNA, FLJ95449, Homo sapiens polymerase (DNA directed) kappa (POLK), mRNA
Enzyme 33 Gene Name POLK
Enzyme 33 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 33 Number of Residues 870
Enzyme 33 Molecular Weight 98810
Enzyme 33 Theoretical pI 8.22
Enzyme 33 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 33 General Function Replication, recombination and repair
Enzyme 33 Specific Function Not Available
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein Not Available
Enzyme 33 UniProtKB/Swiss-Prot ID B2RBD2 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name B2RBD2_HUMAN Link Image
Enzyme 33 PDB ID 1T94 Link Image
Enzyme 33 PDB File Show
Enzyme 33 3D Structure
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence Not Available
Enzyme 33 GenBank Gene ID AK314610 Link Image
Enzyme 33 GeneCard ID B2RBD2 Link Image
Enzyme 33 GenAtlas ID Not Available
Enzyme 33 HGNC ID Not Available
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References Not Available
Enzyme 33 Metabolite References Not Available