We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for Uridine triphosphate (HMDB00285)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-11-24 22:49:17
Accession Number HMDB00285
Secondary Accession Numbers Not Available
Common Name Uridine triphosphate
Description Uridine 5'-(tetrahydrogen triphosphate). A uracil nucleotide containing three phosphate groups esterified to the sugar moiety. Uridine triphosphate has the role of a source of energy or an activator of substrates in metabolic reactions, like that of adenosine triphosphate, but more specific. When Uridine triphosphate activates a substrate, UDP-substrate is usually formed and inorganic phosphate is released. (Wikipedia)
Synonyms
  1. 5'-UTP
  2. UTP
  3. Uridine 5'-triphosphate
  4. Uridine mono(tetrahydrogen triphosphate)
  5. Uridine triphosphate
  6. Uridine triphosphic acid
  7. Uteplex
Chemical IUPAC Name [[[5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxyphosphonic acid
Chemical Formula C9H15N2O15P3
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
  • 1,2-diol
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Aminosugars metabolism
  • Component of Galactose metabolism
  • Component of Nucleotide sugars metabolism
  • Component of Pyrimidine metabolism
  • Component of Starch and sucrose metabolism
Application
Source
  • Endogenous
Average Molecular Weight 484.141
Monoisotopic Molecular Weight 483.968536
Isomeric SMILES O[C@@H]1[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O[C@H]([C@@H]1O)N1C=CC(=O)NC1=O
Canonical SMILES OC1C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)OC(C1O)N1C=CC(=O)NC1=O
KEGG Compound ID C00075 Link Image
BioCyc ID UTP Link Image
BiGG ID 33760 Link Image
Wikipedia Link Uridine triphosphate Link Image
NuGOwiki Link HMDB00285 Link Image
Metagene Link HMDB00285 Link Image
METLIN ID 5277 Link Image
PubChem Compound 6133 Link Image
PubChem Substance 11367153 Link Image
ChEBI ID 15713 Link Image
CAS Registry Number 63-39-8
InChI Identifier InChI=1/C9H15N2O15P3/c12-5-1-2-11(9(15)10-5)8-7(14)6(13)4(24-8)3-23-28(19,20)26-29(21,22)25-27(16,17)18/h1-2,4,6-8,13-14H,3H2,(H,19,20)(H,21,22)(H,10,12,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1
Synthesis Reference Kenner, G. W.; Todd, A. R.; Webb, R. F.; Weymouth, F. J. Nucleotides. XXVIII. Synthesis of uridine 5'-triphosphate. Journal of the Chemical Society (1954), 46-52 2288-93.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 138.0 mg/mL [MEYLAN,WM et al. (1996)]; 8.37 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.07 [Predicted by ALOGPS]; -6.2 [Predicted by PubChem via XLOGP]; -4.09 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1GX6 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
  • nucleus
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
DNA Replication Fork SMP00477 Link Image
Lactose Synthesis SMP00444 Link Image
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
Transcription/Translation SMP00019 Link Image
General References
  1. Kunzelmann K, Mall M: Pharmacotherapy of the ion transport defect in cystic fibrosis: role of purinergic receptor agonists and other potential therapeutics. Am J Respir Med. 2003;2(4):299-309. [PubMed Link Image]
  2. Erlinge D, Harnek J, van Heusden C, Olivecrona G, Jern S, Lazarowski E: Uridine triphosphate (UTP) is released during cardiac ischemia. Int J Cardiol. 2005 Apr 28;100(3):427-33. [PubMed Link Image]
  3. Oosterhuis GJ, Mulder AB, Kalsbeek-Batenburg E, Lambalk CB, Schoemaker J, Vermes I: Measuring apoptosis in human spermatozoa: a biological assay for semen quality? Fertil Steril. 2000 Aug;74(2):245-50. [PubMed Link Image]
  4. Holstege A, Manglitz D, Gerok W: Depletion of blood plasma cytidine due to increased hepatocellular salvage in D-galactosamine-treated rats. Eur J Biochem. 1984 Jun 1;141(2):339-44. [PubMed Link Image]
  5. Wikipedia Link Image
Metabolic Enzymes
  1. Ectonucleoside triphosphate diphosphohydrolase 1
  2. Soluble calcium-activated nucleotidase 1
  3. Nucleoside diphosphate kinase, mitochondrial precursor
  4. Nucleoside diphosphate kinase A
  5. Nucleoside diphosphate kinase B
  6. Nucleoside diphosphate kinase 6
  7. Inosine triphosphate pyrophosphatase
  8. GTP:AMP phosphotransferase mitochondrial
  9. Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
  10. CTP synthase 1
  11. 6-phosphofructokinase type C
  12. DNA-directed RNA polymerase III subunit D
  13. DNA-directed RNA polymerase II largest subunit
  14. DNA-directed RNA polymerase, mitochondrial precursor
  15. DNA-directed RNA polymerase I 135 kDa polypeptide
  16. DNA-directed RNA polymerase I-associated factor 53 kDa subunit
  17. 6-phosphofructokinase, liver type
  18. DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide
  19. DNA-directed RNA polymerases III 12.5 kDa polypeptide
  20. 6-phosphofructokinase, muscle type
  21. Pyruvate kinase isozymes R/L
  22. UTP--glucose-1-phosphate uridylyltransferase 2
  23. Uridine-cytidine kinase 2
  24. CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase
  25. Uncharacterized protein POLR3G
  26. Uridine/cytidine kinase-like 1
  27. Ectonucleoside triphosphate diphosphohydrolase 8
  28. 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)
  29. DNA-directed RNA polymerase III subunit RPC1
  30. DNA-directed RNA polymerase I subunit RPA1
  31. DNA-directed RNA polymerase subunit
  32. DNA-directed RNA polymerases I and III subunit RPAC2
  33. cDNA FLJ75210, highly similar to H.sapiens RNA polymerase II 140 kDa subunit (Polymerase (RNA) II (DNA directed) polypeptide B, 140kDa)
  34. DNA-directed RNA polymerase (EC 2.7.7.6)
  35. DNA-directed RNA polymerase III subunit RPC7-like
  36. POLR1C protein (Fragment)
  37. Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
  38. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  39. cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
  40. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
  41. cDNA, FLJ93080, highly similar to Homo sapiens UDP-N-acteylglucosamine pyrophosphorylase 1 (UAP1), mRNA (UDP-N-acteylglucosamine pyrophosphorylase 1, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5313
Enzyme 1 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 1 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. CD39 antigen
Enzyme 1 Gene Name ENTPD1
Enzyme 1 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 1 Number of Residues 510
Enzyme 1 Molecular Weight 57965
Enzyme 1 Theoretical pI 6.29
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 17-37 479-499
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 765256 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1533 bp
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
Enzyme 1 GenBank Gene ID S73813 Link Image
Enzyme 1 GeneCard ID ENTPD1 Link Image
Enzyme 1 GenAtlas ID ENTPD1 Link Image
Enzyme 1 HGNC ID HGNC:3363 Link Image
Enzyme 1 Chromosome Location 10
Enzyme 1 Locus 10q24
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed Link Image]
  2. Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed Link Image]
  3. Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed Link Image]
  4. Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed Link Image]
  5. Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed Link Image]
  6. Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed Link Image]
  7. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  8. Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5314
Enzyme 2 Name Soluble calcium-activated nucleotidase 1
Enzyme 2 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
Enzyme 2 Gene Name CANT1
Enzyme 2 Protein Sequence >Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 2 Number of Residues 401
Enzyme 2 Molecular Weight 44840
Enzyme 2 Theoretical pI 5.98
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 45-62
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 22218108 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 2 PDB ID 1S1D Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1116 bp
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 2 GenBank Gene ID AF328554 Link Image
Enzyme 2 GeneCard ID CANT1 Link Image
Enzyme 2 GenAtlas ID CANT1 Link Image
Enzyme 2 HGNC ID HGNC:19721 Link Image
Enzyme 2 Chromosome Location 17
Enzyme 2 Locus 17q25.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed Link Image]
  2. Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed Link Image]
  3. Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5338
Enzyme 3 Name Nucleoside diphosphate kinase, mitochondrial precursor
Enzyme 3 Synonyms
  1. NDP kinase, mitochondrial
  2. NDK
  3. nm23-H4
  4. Nucleoside diphosphate kinase D
  5. NDPKD
Enzyme 3 Gene Name NME4
Enzyme 3 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial precursor
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 3 Number of Residues 187
Enzyme 3 Molecular Weight 20659
Enzyme 3 Theoretical pI 10.75
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 Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-15
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1945762 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 3 PDB ID 1EHW Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 3 GenBank Gene ID Y07604 Link Image
Enzyme 3 GeneCard ID NME4 Link Image
Enzyme 3 GenAtlas ID NME4 Link Image
Enzyme 3 HGNC ID HGNC:7852 Link Image
Enzyme 3 Chromosome Location 16
Enzyme 3 Locus 16p13.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5341
Enzyme 4 Name Nucleoside diphosphate kinase A
Enzyme 4 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 4 Gene Name NME1
Enzyme 4 Protein Sequence >Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 4 Number of Residues 152
Enzyme 4 Molecular Weight 17149
Enzyme 4 Theoretical pI 6.11
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
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 35068 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 4 PDB ID 1JXV Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >543 bp
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
Enzyme 4 GenBank Gene ID X17620 Link Image
Enzyme 4 GeneCard ID NME1 Link Image
Enzyme 4 GenAtlas ID NME1 Link Image
Enzyme 4 HGNC ID HGNC:7849 Link Image
Enzyme 4 Chromosome Location 17
Enzyme 4 Locus 17q21.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5344
Enzyme 5 Name Nucleoside diphosphate kinase B
Enzyme 5 Synonyms
  1. NDK B
  2. NDP kinase B
  3. nm23-H2
  4. C-myc purine-binding transcription factor PUF
Enzyme 5 Gene Name NME2
Enzyme 5 Protein Sequence >Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 5 Number of Residues 152
Enzyme 5 Molecular Weight 17298
Enzyme 5 Theoretical pI 8.69
Enzyme 5 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 5 General Function Nucleotide transport and metabolism
Enzyme 5 Specific Function Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3)
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 4467843 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 5 PDB ID 1NSK Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 5 GenBank Gene ID X58965 Link Image
Enzyme 5 GeneCard ID NME2 Link Image
Enzyme 5 GenAtlas ID NME2 Link Image
Enzyme 5 HGNC ID HGNC:7850 Link Image
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17q21.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5346
Enzyme 6 Name Nucleoside diphosphate kinase 6
Enzyme 6 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. nm23-H6
  4. Inhibitor of p53-induced apoptosis-alpha
  5. IPIA-alpha
Enzyme 6 Gene Name NME6
Enzyme 6 Protein Sequence >Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 6 Number of Residues 186
Enzyme 6 Molecular Weight 21142
Enzyme 6 Theoretical pI 8.49
Enzyme 6 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 6 General Function Nucleotide transport and metabolism
Enzyme 6 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 6 Pathways
Enzyme 6 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-24
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 3228530 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 6 GenBank Gene ID AF051941 Link Image
Enzyme 6 GeneCard ID NME6 Link Image
Enzyme 6 GenAtlas ID NME6 Link Image
Enzyme 6 HGNC ID HGNC:20567 Link Image
Enzyme 6 Chromosome Location 3
Enzyme 6 Locus 3p21
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5668
Enzyme 7 Name Inosine triphosphate pyrophosphatase
Enzyme 7 Synonyms
  1. ITPase
  2. Inosine triphosphatase
  3. Putative oncogene protein hlc14-06-p
Enzyme 7 Gene Name ITPA
Enzyme 7 Protein Sequence >Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
Enzyme 7 Number of Residues 194
Enzyme 7 Molecular Weight 21446
Enzyme 7 Theoretical pI 5.34
Enzyme 7 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 7 General Function Nucleotide transport and metabolism
Enzyme 7 Specific Function Hydrolyzes ITP and dITP to their respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) is also a potential substrate. May be the major enzyme responsible for regulating ITP concentration in cells
Enzyme 7 Pathways
Enzyme 7 Reactions
  • A nucleoside triphosphate + H2O = a nucleotide + diphosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 13398328 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9BY32 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ITPA_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCACGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAGGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAGTACTTTGGCAGTTTGGCAGCTTGA
Enzyme 7 GenBank Gene ID AF219116 Link Image
Enzyme 7 GeneCard ID ITPA Link Image
Enzyme 7 GenAtlas ID ITPA Link Image
Enzyme 7 HGNC ID HGNC:6176 Link Image
Enzyme 7 Chromosome Location 20
Enzyme 7 Locus 20p
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Lin S, McLennan AG, Ying K, Wang Z, Gu S, Jin H, Wu C, Liu W, Yuan Y, Tang R, Xie Y, Mao Y: Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. J Biol Chem. 2001 Jun 1;276(22):18695-701. Epub 2001 Mar 13. [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]
  3. Sumi S, Marinaki AM, Arenas M, Fairbanks L, Shobowale-Bakre M, Rees DC, Thein SL, Ansari A, Sanderson J, De Abreu RA, Simmonds HA, Duley JA: Genetic basis of inosine triphosphate pyrophosphohydrolase deficiency. Hum Genet. 2002 Oct;111(4-5):360-7. Epub 2002 Aug 15. [PubMed Link Image]
  4. Cao H, Hegele RA: DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency. J Hum Genet. 2002;47(11):620-2. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5845
Enzyme 8 Name GTP:AMP phosphotransferase mitochondrial
Enzyme 8 Synonyms
  1. Adenylate kinase 3
  2. AK3
  3. Adenylate kinase 3 alpha-like 1
Enzyme 8 Gene Name AK3
Enzyme 8 Protein Sequence >GTP:AMP phosphotransferase mitochondrial
MGASARLLRAVIMGAPGSGKGTVSSRITTHFELKHLSSGDLLRDNMLRGTEIGVLAKAFI
DQGKLIPDDVMTRLALHELKNLTQYSWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEV
IKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEDQT
KPVLEYYQKKGVLETFSGTETNKIWPYVYAFLQTKVPQRSQKASVTP
Enzyme 8 Number of Residues 227
Enzyme 8 Molecular Weight 25566
Enzyme 8 Theoretical pI 9.64
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleotide binding
  • nucleotide kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 8 General Function Nucleotide transport and metabolism
Enzyme 8 Specific Function NTP + AMP = NDP + ADP
Enzyme 8 Pathways
Enzyme 8 Reactions
  • nucleoside triphosphate + AMP = nucleoside diphosphate + ADP
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 6518533 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9UIJ7 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name KAD3_HUMAN Link Image
Enzyme 8 PDB ID 2AK3 Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >684 bp
ATGGGGGCGTCGGGGCGGCTGCTGCGAGCGGTGATCATGGGGGCCCCGGGCTCGGGCAAG
GGCACCGTGTCGTCCCGCATCACTACACACTTCGAGCTGAAGCACCTCTCCCGCGGGGAC
CTGCTCCGGGACAACATGCTGCGGGGCACAGAAATTGGCGTGTTAGCCCAGGCTTTCATT
GACCAAGGGAAACTCATCCCAGATTATGTCACGACTCGGCTGGCCCTTCATGAGCTGAAA
AACCTCACCCAGTATAGCTGGCTGTTGGATGGTTTTCCAAGGACACTTCCACAGGCAGAA
GCCCTAGATAGAGCTTATCAGATCGACACAGTGATTAACCTGAATGTGCCCTTTGAGGTC
ATTAAACAACGCCTTACTGCTCGCTGGATTCATCCCGCCAGTGGCCGAGTCTATAACATT
GAATTCAACCCTCCCAAAACTGTGGGCATTGATGACCTGACTGGGGAGCCTCTCATTCAG
CGTGAGGATGATAAACCAGAGACGGTTATCAAGAGACTAAAGGCTTATGAAGACCAAACA
AAGCCAGTCCTGGAATATTACCAGAAAAAAGGGGTGTTGGAAACATTCTCCGGAACAGAA
ACCAACAAGATTTGGCCCTATGTATATGCTTTCCTACAAACTAAAGTTCCACAAAGAAGC
CAGAAAGCTTCAGTTACTCCATGA
Enzyme 8 GenBank Gene ID AB021870 Link Image
Enzyme 8 GeneCard ID AK3 Link Image
Enzyme 8 GenAtlas ID AK3 Link Image
Enzyme 8 HGNC ID HGNC:17376 Link Image
Enzyme 8 Chromosome Location 9
Enzyme 8 Locus 9p24.1-p24.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5893
Enzyme 9 Name Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
Enzyme 9 Synonyms
  1. Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
  2. Diadenosine tetraphosphatase
  3. Ap4A hydrolase
  4. Ap4Aase
  5. Nucleoside diphosphate-linked moiety X motif 2
  6. Nudix motif 2
Enzyme 9 Gene Name NUDT2
Enzyme 9 Protein Sequence >Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
MALRACGLIIFRRCLIPKVDNNAIEFLLLQASDGIHHWTPPKGHVEPGEDDLETALRETQ
EEAGIEAGQLTIIEGFKRELNYVARNKPKTVIYWLAEVKDYDVEIRLSHEHQAYRWLGLE
EACQLAQFKEMKAALQEGHQFLCSIEA
Enzyme 9 Number of Residues 147
Enzyme 9 Molecular Weight 16829
Enzyme 9 Theoretical pI 5.06
Enzyme 9 GO Classification
Function
  • bis(5'-nucleosyl)-tetraphosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleotide diphosphatase activity
  • pyrophosphatase activity
Process
Component
Enzyme 9 General Function Replication, recombination and repair
Enzyme 9 Specific Function Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis
Enzyme 9 Pathways
Enzyme 9 Reactions
  • P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 1050960 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P50583 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name AP4A_HUMAN Link Image
Enzyme 9 PDB ID 1XSC Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >60 bp
ATGCCAGCCCTGTTTTACAGGGAGCCCTGGAGGAGTTGGGATAGAGGCCACATTGACTGA
Enzyme 9 GenBank Gene ID U30313 Link Image
Enzyme 9 GeneCard ID NUDT2 Link Image
Enzyme 9 GenAtlas ID NUDT2 Link Image
Enzyme 9 HGNC ID HGNC:8049 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Thorne NM, Hankin S, Wilkinson MC, Nunez C, Barraclough R, McLennan AG: Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases. Biochem J. 1995 Nov 1;311 ( Pt 3):717-21. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5949
Enzyme 10 Name CTP synthase 1
Enzyme 10 Synonyms
  1. UTP--ammonia ligase 1
  2. CTP synthetase 1
Enzyme 10 Gene Name CTPS
Enzyme 10 Protein Sequence >CTP synthase 1
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
Enzyme 10 Number of Residues 591
Enzyme 10 Molecular Weight 66691
Enzyme 10 Theoretical pI 6.42
Enzyme 10 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
Component
Enzyme 10 General Function Nucleotide transport and metabolism
Enzyme 10 Specific Function Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 30293 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P17812 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PYRG1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1776 bp
ATGAAGTACATTCTGGTTACTGGTGGTGTTATATCAGGAATTGGAAAAGGAATCATTGCC
AGCAGTGTGGGCACAATACTCAAGTCATGTGGTTTACATGTAACTTCAATCAAAATTGAC
CCCTACATTAACATTGATGCAGGAACATTCTCTCCTTATGAGCATGGTGAGGTTTTTGTG
CTGGATGATGGTGGGGAAGTAGACCTTGACCTGGGTAACTATGAGCGGTTCCTTGACATC
CGCCTCACCAAGGACAATAATCTGACCACTGGAAAGATATACCAGTATGTCATTAACAAG
GAACGGAAAGGAGATTACTTGGGGAAAACTGTCCAAGTTGTCCCTCATATCACAGATGCA
ATCCAGGAGTGGGTGATGAGACAGGCGTTAATACCTGTAGATGAAGATGGCCTGGAACCT
CAAGTGTGTGTTATTGAGCTTGGTGGAACCGTGGGGGACATAGAAAGCATGCCCTTTATT
GAGGCCTTCCGTCAGTTCCAATTCAAGGTCAAAAGAGAGAACTTTTGTAACATCCACGTC
AGTCTAGTTCCCCAGCCAAGTTCAACAGGGGAACAGAAGACTAAACCTACCCAGAATAGT
GTTCGGGAACTTAGAGGACTTGGGCTTTCCCCAGATCTGGTTGTATGCAGGTGCTCAAAT
CCACTTGACACATCAGTGAAGGAGAAAATATCAATGTTCTGCCATGTTGAGCCTGAACAA
GTGATCTGTGTCCACGATGTCTCATCCATCTACCGAGTCCCCTTGTTGTTAGAGGAGCAA
GGGGTTGTAGATTATTTTCTTCGAAGACTTGACCTTCCTATTGAGAGGCAGCCAAGAAAA
ATGCTGATGAAATGGAAAGAGATGGCTGACAGATATGATCGCTTGCTGGAGACCTGCTCT
ATTGCCCTTGTGGCGAAATACACCGAGTTCTCAGACTCCTATGCCTCTGTCATTAAGGCT
CTGGAGCATTCTGCACTGGCCATCAACCACAAATTGGAAATCAAGTACATAGATTCTGCG
GACTTGGAGCCCATCACCTCGCAAGAAGAGCCCGTGCGCTACCACGAAGCTTGGCAGAAG
CTCTGTAGTGCTCATGGAGTGCTGGTTCCAGGAGGATTTGGTGTTCGAGGAACAGAAGGA
AAAATCCAAGCAATTGCCTGGGCTCGGAATCAGAAAAAGCCTTTTTTGGGCGTGTGCTTA
GGGATGCAGTTGGCAGTGGTTGAATTCTCAAGAAACGTGCTGGGATGGCAAGATGCCAAT
TCTACAGAGTTTGACCCTACGACCAGTCATCCCGTGGTCGTAGACATGCCAGAACACAAC
CCAGGGCAGATGGGCGGAACCATGAGGCTGGGCAAGAGGAGAACCCTGTTCCAGACCAAG
AACTCAGTCATGAGGAAACTCTATGGAGACGCAGACTACTTGGAAGAGAGGCACCGCCAC
CGATTTGAGGTGAATCCAGTCTGGAAAAAGTGTTTGGAAGAACAAGGCTTGAAGTTTGTT
GGCCAAGATGTTGAAGGAGAGAGAATGGAAATTGTGGAGTTAGAAGATCATCCCTTTTTT
GTTGGGGTTCAGTACCACCCTGAGTTCCTGTCCAGGCCTATCAAGCCCTCCCCACCATAC
TTTGGCCTCCTCCTGGCCTCTGTGGGGCGGCTCTCACATTACCTCCAGAAAGGCTGCAGG
CTCTCACCCAGGGACACCTATAGTGACAGGAGTGGAAGCAGCTCCCCTGACTCTGAAATC
ACCGAACTGAAGTTTCCATCAATAAATCATGACTGA
Enzyme 10 GenBank Gene ID X52142 Link Image
Enzyme 10 GeneCard ID CTPS Link Image
Enzyme 10 GenAtlas ID CTPS Link Image
Enzyme 10 HGNC ID HGNC:2519 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p34.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Yamauchi M, Yamauchi N, Meuth M: Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes. EMBO J. 1990 Jul;9(7):2095-9. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6009
Enzyme 11 Name 6-phosphofructokinase type C
Enzyme 11 Synonyms
  1. Phosphofructokinase 1
  2. Phosphohexokinase
  3. Phosphofructo-1-kinase isozyme C
  4. PFK-C
  5. 6- phosphofructokinase, platelet type
Enzyme 11 Gene Name PFKP
Enzyme 11 Protein Sequence >6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
Enzyme 11 Number of Residues 784
Enzyme 11 Molecular Weight 85597
Enzyme 11 Theoretical pI 7.60
Enzyme 11 GO Classification
Function
  • 6-phosphofructokinase activity
  • catalytic activity
  • phosphofructokinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • 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
  • 6-phosphofructokinase complex
  • cell
  • cytoplasm
  • intracellular
  • protein complex
Enzyme 11 General Function Carbohydrate transport and metabolism
Enzyme 11 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 11 Pathways
Enzyme 11 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 560105 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q01813 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name K6PP_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2355 bp
ATGGACGCGGACGACTCCCGGGCCCCCAAGGGCTCCTTGCGGAAGTTCCTGGAGCACCTC
TCCGGGGCCGGCAAGGCCATCGGCGTGCTGACCAGCGGCGGGGATGCTCAAGGTATGAAC
GCTGCCGTCCGTGCCGTGGTGCGCATGGGTATCTACGTGGGGGCCAAGGTGTACTTCATC
TACGAGGGCTACCAGGGCATGGTGGACGGAGGCTCAAACATCGCAGAGGCCGACTGGGAG
AGTGTCTCCAGCATCCTGCAAGTGGGCGGGACGATCATTGGCAGTGCGCGGTGCCAGGCC
TTCCGCACGCGGGAAGGCCGCCTGAAGGCTGCTTGCAACCTGCTGCAGCGCGGCATCACC
AACCTGTGTGTGATCGGCGGGGACGGGAGCCTCACCGGGGCCAACCTCTTCCGGAAGGAG
TGGAGTGGGCTGCTGGAGGAGCTGGCCAGGAACGGCCAGATCGATAAGGAGGCCGTGCAG
AAGTACGCCTACCTCAACGTGGTGGGCATGGTGGGCTCCATCGACAATGATTTCTGCGGC
ACCGACATGACCATCGGCACGGACTCCGCCCTGCACAGGATCATCGAGGTCGTCGACGCC
ATCATGACCACGGCCCAGAGCCACCAGAGGACCTTCGTTCTGGAGGTGATGGGACGACAC
TGTGGGTACCTGGCCCTGGTGAGTGCCTTGGCCTGCGGTGCGGACTGGGTGTTCCTTCCA
GAATCTCCACCAGAGGAAGGCTGGGAGGAGCAGATGTGTGTCAAACTCTCGGAGAACCGT
GCCCGGAAAAAAAGGCTGAATATTATTATTGTGGCTGAAGGAGCAATTGATACCCAAAAT
AAACCCATCACCTCTGAGAAAATCAAAGAGCTTGTCGTCACGCAGCTGGGCTATGACACA
CGTGTGACCATCCTCGGGCACGTGCAGAGAGGAGGGACCCCTTCGGCATTCGACAGGATC
TTGGCCAGCCGCATGGGAGTGGAGGCAGTCATCGCCTTGCTAGAGGCCACCCCGGACACC
CCAGCTTGCGTCGTGTCACTGAACGGGAACCACGCCGTGCGCCTGCCGCTGATGGAGTGC
GTGCAGATGACTCAGGATGTGCAGAAGGCGATGGACGAGAGGAGATTTCAAGATGCGGTT
CGACTCCGAGGGAGGAGCTTTGCGGGCAACCTGAACACCTACAAGCGACTTGCCATCAAG
CTGCCGGATGATCAGATCCCAAAGACCAATTGCAACGTAGCTGTCATCAACGTGGGGGCA
CCCGCGGCTGGGATGAACGCGGCCGTACGCTCAGCTGTGCGCGTGGGCATTGCCGACGGC
CACAGGATGCTCGCCATCTATGATGGCTTTGACGGCTTCGCCAAGGGCCAGATCAAAGAA
ATCGGCTGGACAGATGTCGGGGGCTGGACCGGCCAAGGAGGCTCCATTCTTGGGACAAAA
CGCGTTCTCCCGGGGAAGTACTTGGAAGAGATCGCCACACAGATGCGCACGCACAGCATC
AACGCGCTGCTGATCATCGGTGGATTCGAGGCCTACCTGGGACTCCTGGAGCTGTCAGCC
GCCCGGGAGAAGCACGAGGAGTTCTGTGTCCCCATGGTCATGGTTCCCGCTACTGTGTCC
AACAATGTGCCGGGTTCCGATTTCAGCATCGGGGCAGACACCGCCCTGAACACTATCACC
GACACCTGCGACCGCATCAAGCAGTCCGCCAGCGGAACCAAGCGGCGCGTGTTCATCATC
GAGACCATGGGCGGCTACTGTGGCTACCTGGCCAACATGGGGGGGCTCGCGGCCGGAGCT
GATGCCGCATACATTTTCGAAGAGCCCTTCGACATCAGGGATCTGCAGTCCAACGTGGAG
CACCTGACGGAGAAAATGAAGACCACCATCCAGAGAGGCCTTGTGCTCAGAAATGAGAGC
TGCAGTGAAAACTACACCACCGACTTCATTTACCAGCTGTATTCAGAAGAGGGCAAAGGC
GTGTTTGACTGCAGGAAGAACGTGCTGGGTCACATGCAGCAGGGTGGGGCACCCTCTCCA
TTTGATAGAAACTTTGGAACCAAAATCTCTGCCAGAGCTATGGAGTGGATCACTGCAAAA
CTCAAGGAGGCCCGGGGCAGAGGAAAAAAATTTACCACCGATGATTCCATTTGTGTGCTG
GGAATAAGCAAAAGAAACGTTATTTTTCAACCTGTGGCAGAGCTGAAGAAGCAAACGGAT
TTTGAGCACAGGATTCCCAAAGAACAGTGGTGGCTCAAGCTACGGCCCCTCATGAAAATC
CTGGCCAAGTACAAGGCCAGCTATGACGTGTCGGACTCAGGCCAGCTGGAACATGTGCAG
CCCTGGAGTGTCTGA
Enzyme 11 GenBank Gene ID D25328 Link Image
Enzyme 11 GeneCard ID PFKP Link Image
Enzyme 11 GenAtlas ID PFKP Link Image
Enzyme 11 HGNC ID HGNC:8878 Link Image
Enzyme 11 Chromosome Location 10
Enzyme 11 Locus 10p15.3-p15.2
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Eto K, Sakura H, Yasuda K, Hayakawa T, Kawasaki E, Moriuchi R, Nagataki S, Yazaki Y, Kadowaki T: Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet. Biochem Biophys Res Commun. 1994 Feb 15;198(3):990-8. [PubMed Link Image]
  2. Simpson CJ, Fothergill-Gilmore LA: Isolation and sequence of a cDNA encoding human platelet phosphofructokinase. Biochem Biophys Res Commun. 1991 Oct 15;180(1):197-203. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6011
Enzyme 12 Name DNA-directed RNA polymerase III subunit D
Enzyme 12 Synonyms
  1. DNA-directed RNA polymerase III 47 kDa polypeptide
  2. RNA polymerase C subunit 4
  3. RPC4
  4. RPC53
  5. Protein BN51
Enzyme 12 Gene Name POLR3D
Enzyme 12 Protein Sequence >DNA-directed RNA polymerase III subunit D
MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTP
NIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKK
GNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQL
PLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAAR
KTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVL
IKQEKDREAKLAENACTLADLTEGQVGKLLIRKSGRVQLLLGKVTLDVTMGTACSFLQEL
VSVGLGDSRTGEMTVLGHVKHKLVCSPDFESLLDHKHR
Enzyme 12 Number of Residues 398
Enzyme 12 Molecular Weight 44396
Enzyme 12 Theoretical pI 6.97
Enzyme 12 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • RNA metabolism
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA metabolism
  • transcription
Component
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 12 Pathways
Enzyme 12 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 179513 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P05423 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name RPO3D_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1188 bp
ATGTCGGAAGGAAACGCCGCCGGACGCCCAGCACGGCAGGGCCCGGACCTTCTCCTGACT
GGGGCCCGGGGGTCATCGGGCGGCGGCGGCCTCCCCTCACCCCCGGCCGTTCCCTCCATC
CGTTCCAGGGACCTAACCCTCGGGGGAGTCAAGAAGAAAACCTTCACCCCAAATATCATC
AGTCGGAAGATCAAGGAAGAGCCCAAGGAAGAAGTAACTGTCAAGAAGGAGAAGCGTGAA
AGGGACAGAGACCGACAACGAGAGGGGCATGGACGAGGGCGACGCCGTCCAGAAGTGATC
CAGTCTCACTCCATCTTTGAGCAGGGCCCAGCTGAAATGATGAAGAAAAAAGGGAACTGG
GATAAGACAGTGGATGTGTCAGACATGGGACCTTCTCATATCATCAACATCAAAAAAGAG
AAGAGAGAGACAGACGAAGAAACTAAACAGATCTTGCGTATGCTGGAGAAGGACGATTTC
CTCGATGACCCCGGCCTGAGGAACGACACTCGAAATATGCCTGTGCAGCTGCCGCTGGCT
CACTCAGGATGGCTTTTTAAGGAAGAAAATGACGAACCAGATGTTAAACCTTGGCTGGCT
GGCCCCAAGGAAGAGGACATGGAGGTGGACATACCTGCTGTGAAAGTGAAAGAGGAGCCA
CGAGATGAGGAGGAAGAGGCCAAGATGAAGGCTCCTCCCAAAGCAGCCAGGAAGACTCCA
GGCCTCCCGAAGGATGTATCTGTGGCAGAGCTGCTGAGGGAGCTGAGCCTCACCAAGGAA
GAGGAACTGCTGTTTCTGCAGCTGCCAGACACCCTCCCTGGCCAGCCACCCACCCAGGAC
ATCAAGCCTATCAAGACAGAGGTGCAGGGCGAGGACGGACAGGTGGTGCTCATCAAGCAG
GAGAAAGACCGAGAAGCCAAATTGGCAGAGAATGCTTGTACCCTGGCTGACCTGACAGAG
GGTCAGGTTGGCAAGCTACTCATCCGCAAGTCTGGAAGGGTGCAACTCCTCTTGGGCAAG
GTGACTCTGGACGTGACCATGGGAACTGCCTGCTCCTTCCTGCAGGAGCTGGTGTCCGTG
GGCCTTGGAGACAGTAGGACAGGGGAGATGACAGTCCTGGGACACGTGAAGCACAAACTT
GTATGTTCCCCTGATTTTGAATCCCTCTTGGATCACAAACACCGGTAA
Enzyme 12 GenBank Gene ID M17754 Link Image
Enzyme 12 GeneCard ID POLR3D Link Image
Enzyme 12 GenAtlas ID POLR3D Link Image
Enzyme 12 HGNC ID HGNC:1080 Link Image
Enzyme 12 Chromosome Location 8
Enzyme 12 Locus 8q21
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Ittmann M, Greco A, Basilico C: Isolation of the human gene that complements a temperature-sensitive cell cycle mutation in BHK cells. Mol Cell Biol. 1987 Oct;7(10):3386-93. [PubMed Link Image]
  2. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
  3. Chong SS, Hu P, Hernandez N: Reconstitution of transcription from the human U6 small nuclear RNA promoter with eight recombinant polypeptides and a partially purified RNA polymerase III complex. J Biol Chem. 2001 Jun 8;276(23):20727-34. Epub 2001 Feb 27. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6014
Enzyme 13 Name DNA-directed RNA polymerase II largest subunit
Enzyme 13 Synonyms
  1. RPB1
Enzyme 13 Gene Name POLR2A
Enzyme 13 Protein Sequence >DNA-directed RNA polymerase II largest subunit
MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDP
RQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVD
SNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKG
HGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEP
RYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAA
HVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVD
FSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYII
RDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWS
TFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQD
TLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHI
NCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEM
GHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKA
HNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKIN
ISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHA
MGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGES
VEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMR
EDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKL
VIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAI
AHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLT
VFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMP
DFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIR
IMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKI
IITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALER
ELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLM
EAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTG
MFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPG
YSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSP
SYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSP
TSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPS
YSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPT
SPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPTSPKY
SPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTS
PKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN
Enzyme 13 Number of Residues 1970
Enzyme 13 Molecular Weight 217208
Enzyme 13 Theoretical pI 7.38
Enzyme 13 GO Classification
Function
  • DNA binding
  • DNA-directed RNA 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
  • transcription from RNA polymerase II promoter
  • transcription, DNA-dependent
Component
  • DNA-directed RNA polymerase II, core complex
  • RNA polymerase complex
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
  • protein complex
Enzyme 13 General Function Transcription
Enzyme 13 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 13 Pathways
Enzyme 13 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(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 36124 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P24928 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name RPB1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >5913 bp
ATGCACGGGGGTGGCCCCCCCTCGGGGGACAGCGCATGCCCGCTGCGCACCATCAAGAGA
GTCCAGTTCGGAGTCCTGAGTCCGGATGAACTGAAGCGAATGTCTGTGACGGAGGGTGGC
ATCAAATACCCAGAGACGACTGAGGGAGGCCGCCCCAAGCTTGGGGGGCTGATGGACCCG
AGGCAGGGGGTGATTGAGCGGACTGGCCGCTGCCAAACATGTGCAGGAAACATGACAGAG
TGTCCTGGCCACTTTGGCCACATTGAACTGGCCAAGCCTGTGTTTCACGTGGGCTTCCTG
GTGAAGACAATGAAAGTTTTGCGCTGTGTCTGCTTCTTCTGCTCCAAACTGCTTGTGGAC
TCTAACAACCCAAAGATCAAGGATATCCTGGCTAAGTCCAAGGGACAGCCCAAGAAGCGG
CTCACACATGTCTACGACCTTTGCAAGGGCAAAAACATATGCGAGGGTGGGGAGGAGATG
GACAACAAGTTCGGTGTGGAACAACCTGAGGGTGACGAGGATCTGACCAAAGAAAAGGGC
CATGGTGGCTGTGGGCGGTACCAGCCCAGGATCCGGCGTTCTGGCCTAGAGCTGTATGCG
GAATGGAAGCACGTTAATGAGGACTCTCAGGAGAAGAAGATCCTGCTGAGTCCAGAGCGA
GTGCATGAGATCTTCAAACGCATCTCAGATGAGGAGTGTTTTGTGCTGGGCATGGAGCCC
CGCTATGCACGGCCAGAGTGGATGATTGTCACAGTGCTGCCTGTGCCCCCGCTCTCCGTG
CGGCCTGCTGTTGTGATGCAGGGCTCTGCCCGTAACCAGGATGACCTGACTCACAAACTG
GCTGACATCGTGAAGATCAACAATCAGCTGCGGCGCAATGAGCAGAACGGCGCAGCGGCC
CATGTCATTGCAGAGGATGTGAAGCTCCTCCAGTTCCATGTGGCCACCATGGTGGACAAT
GAGCTGCCTGGCTTGCCCCGTGCCATGCAGAAGTCTGGGCGTCCCCTCAAGTCCCTGAAG
CAGCGGTTGAAGGGCAAGGAAGGCCGGGTGCGAGGGAACCTGATGGGCAAAAGAGTGGAC
TTCTCGGCCCGTACTGTCATCACCCCCGACCCCAACCTCTCCATTGACCAGGTTGGCGTG
CCCCGCTCCATTGCTGCCAACATGACCTTTGCGGAGATTGTCACCCCCTTCAACATTGAC
AGACTTCAAGAACTAGTGCGCAGGGGGAACAGTCAGTACCCAGGCGCCAAGTACATCATC
CGAGACAATGGTGATCGCATTGACTTGCGTTTCCACCCCAAGCCCAGTGACCTTCACCTG
CAGACCGGCTATAAGGTGGAACGGCACATGTGTGATGGGGACATTGTTATCTTCAACCGG
CAGCCAACTCTGCACAAAATGTCCATGATGGGGCATCGGGTCCGCATTCTCCCATGGTCT
ACCTTTCGCTTGAATCTTAGCGTGACAACTCCGTACAATGCAGACTTTGACGGGGATGAG
ATGAACTTGCACCTGCCACAGTCTCTGGAGACGCGAGCAGAGATCCAGGAGCTGGCCATG
GTTCCTCGCATGATTGTCACCCCCCAGAGCAATCGGCCTGTCATGGGTATTGTGCAGGAC
ACACTCACAGCAGTGCGCAAATTCACCAAGAGAGACGTCTTCCTGGAGCGGGGTGAAGTG
ATGAACCTCCTGATGTTCCTGTCGACGTGGGATGGGAAGGTCCCACAGCCGGCCATCCTA
AAGCCCCGGCCCCTGTGGACAGGCAAGCAAATCTTCTCCCTCATCATACCTGGTCACATC
AATTGTATCCGTACCCACAGCACCCATCCCGATGATGAAGACAGTGGCCCTTACAAGCAC
ATCTCTCCTGGGGACACCAAGGTGGTGGTGGAGAATGGGGAGCTGATCATGGGCATCCTG
TGTAAGAAGTCTCTGGGCACGTCAGCTGGCTCCCTGGTCCACATCTCCTACCTAGAGATG
GGTCATGACATCACTCGCCTCTTCTACTCCAACATTCAGACTGTCATTAACAACTGGCTC
CTCATCGAGGGTCATACTATTGGCATTGGGGACTCCATTGCTGATTCTAAGACTTACCAG
GACATTCAGAACACTATTAAGAAGGCCAAGCAGGACGTAATAGAGGTCATCGAGAAGGCA
CACAACAATGAGCTGGAGCCCACCCCAGGGAACACTCTGCGGCAGACGTTTGAGAATCAG
GTGAACCGCATTCTTAACGATGCCCGAGACAAGACTGGCTCCTCTGCTCAGAAATCCCTG
TCTGAATACAACAACTTCAAGTCTATGGTCGTGTCCGGAGCTAAAGGTTCCAAGATTAAC
ATCTCCCAGGTCATTGCTGTCGTTGGACAGCAGAACGTCGAGGGCAAGCGGATTCCATTT
GGCTTCAAGCACCGGACTCTGCCTCACTTCATCAAGGATGACTACGGGCCTGAGAGCCGT
GGCTTTGTGGAGAACTCCTACCTAGCCGGCCTCACACCCACTGAGTTCTTTTTCCACGCC
ATGGGGGGTCGTGAGGGGCTCATTGACACGGCTGTCAAGACTGCTGAGACTGGATACATC
CAGCGGCGGCTGATCAAGTCCATGGAGTCAGTGATGGTGAAGTACGACGCGACTGTGCGG
AACTCCATCAACCAGGTGGTGCAGCTGCGCTACGGCGAAGACGGCCTGGCAGGCGAGAGC
GTTGAGTTCCAGAACCTGGCTACGCTTAAGCCTTCCAACAAGGCTTTTGAGAAGAAGTTC
CGCTTTGATTATACCAATGAGAGGGCCCTGCGGCGCACTCTGCAGGAGGACCTGGTGAAG
GACGTGCTGAGCAACGCACACATCCAGAACGAGTTGGAGCGGGAATTTGAGCGGATGCGG
GAGGATCGGGAGGTGCTCAGGGTCATCTTCCCAACTGGAGACAGCAAGGTCGTCCTCCCC
TGTAACCTGCTGCGGATGATCTGGAATGCTCAGAAAATCTTCCACATCAACCCACGCCTT
CCCTCCGACCTGCACCCCATCAAAGTGGTGGAGGGAGTCAAGGAATTGAGCAAGAAGCTG
GTGATTGTGAATGGGGATGACCCACTAAGTCGACAGGCCCAGGAAAATGCCACGCTGCTC
TTCAACATCCACCTGCGGTCCACGTTGTGTTCCCGCCGCATGGCAGAGGAGTTTCGGCTC
AGTGGGGAGGCCTTCGACTGGCTGCTTGGGGAGATTGAGTCCAAGTTCAACCAAGCCATT
GCGCATCCCGGGGAAATGGTGGGGGCTCTGGCTGCGCAGTCCCTTGGAGAACCTGCCACC
CAGATGACCTTGAATACCTTCCACTATGCTGGTGTGTCTGCCAAGAATGTGACGCTGGGT
GTGCCCCGACTTAAGGAGCTCATCAACATTTCCAAGAAGCCAAAGACTCCTTCGCTTACT
GTCTTCCTGTTGGGCCAGTCCGCTCGAGATGCTGAGAGAGCCAAGGATATTCTGTGCCGT
CTGGAGCATACAACGTTGAGGAAGGTGACTGCCAACACAGCCATCTACTATGACCCCAAC
CCCCAGAGCACGGTGGTGGCAGAGGATCAGGAATGGGTGAATGTCTACTATGAAATGCCT
GACTTTGATGTGGCCCGAATCTCCCCCTGGCTGTTGCGGGTGGAGCTGGATCGGAAGCAC
ATGACTGACCGGAAGCTCACCATGGAGCAGATTGCTGAAAAGATCAATGCTGGTTTTGGT
GACGACTTGAACTGCATCTTTAATGATGACAATGCAGAGAAGCTGGTGCTCCGTATTCGC
ATCATGAACAGCGATGAGAACAAGATGCAAGAGGAGGAAGAGGTGGTGGACAAGATGGAT
GATGATGTCTTCCTGCGCTGCATCGAGTCCAACATGCTGACAGATATGACCCTGCAGGGC
ATCGAGCAGATCAGCAAGGTGTACATGCACTTGCCACAGACAGACAACAAGAAGAAGATC
ATCATCACGGAGGATGGGGAATTCAAGGCCCTGCAGGAGTGGATCCTGGAGACGGACGGC
GTGAGCTTGATGCGGGTGCTGAGTGAGAAGGACGTGGACCCCGTACGCACCACGTCCAAT
GACATTGTGGAGATCTTCACGGTGCTGGGCATTGAAGCCGTGCGGAAGGCCCTGGAGCGG
GAGCTGTACCACGTCATCTCCTTTGATGGCTCCTATGTCAATTACCGACACTTGGCTCTC
TTGTGTGATACCATGACCTGTCGTGGCCACTTGATGGCCATCACCCGACACGGAGTCAAC
CGCCAGGACACAGGACCACTCATGAAGTGTTCCTTTGAGGAAACGGTGGACGTGCTTATG
GAAGCAGCCGCACACGGTGAGAGTGACCCCATGAAGGGGGTCTCTGAGAATATCATGCTG
GGCCAGCTGGCTCCGGCCGGCACTGGCTGCTTTGACCTCCTGCTTGATGCAGAGAAGTGC
AAGTATGGCATGGAGATCCCCACCAATATCCCCGGCCTGGGGGCTGCTGGACCCACCGGC
ATGTTCTTTGGTTCAGCACCCAGTCCCATGGGTGGAATCTCTCCTGCCATGACACCTTGG
AACCAGGGTGCAACCCCTGCCTATGGCGCCTGGTCCCCCAGTGTTGGGAGTGGAATGACC
CCAGGGGCAGCCGGTTTCTCTCCCAGTGCTGCGTCAGATGCCAGCGGCTTCAGCCCAGGT
TACTCCCCTGCCTGGTCTCCCACACCGGGCTCCCCGGGGTCCCCAGGTCCCTCAAGCCCC
TACATCCCTTCACCAGGTGGCGCCATGTCTCCCAGCTACTCGCCAACGTCACCTGCCTAC
GAGCCCCGCTCTCCTGGGGGCTACACACCCCAGAGTCCCTCTTATTCCCCCACTTCACCC
TCCTACTCCCCTACCTCTCCATCCTATTCTCCAACCAGTCCCAACTATAGTCCCACATCA
CCCAGCTATTCGCCAACGTCACCCAGCTACTCACCGACCTCTCCCAGCTACTCACCCACC
TCTCCCAGCTACTCGCCCACCTCTCCCAGCTATTCGCCCACCTCTCCCAGCTACTCACCC
ACTTCCCCTAGCTATTCGCCCACTTCCCCTAGCTACTCGCCAACGTCTCCCAGCTACTCG
CCGACATCTCCCAGCTACTCGCCAACTTCACCCAGCTATTCTCCCACTTCTCCCAGCTAC
TCACCTACCTCTCCAAGCTATTCACCCACCTCCCCCAGCTACTCACCCACTTCCCCAAGT
TACTCACCCACCAGCCCGAACTATTCTCCAACCAGTCCCAATTACACCCCAACATCACCC
AGCTACAGCCCGACATCACCCAGCTATTCCCCTACTAGTCCCAACTACACACCTACCAGC
CCTAACTACAGCCCAACCTCTCCAAGCTACTCTCCAACATCACCCAGCTATTCCCCGACC
TCACCAAGTTACTCCCCTTCCAGCCCACGATACACACCACAGTCTCCAACCTATACCCCA
AGCTCACCCAGCTACAGCCCCAGTTCGCCCAGCTACAGCCCAACCTCACCCAAGTACACC
CCAACCAGTCCTTCTTATAGTCCCAGCTCCCCAGAGTATACCCCAACCTCTCCCAAGTAC
TCACCTACCAGTCCCAAATATTCACCCACCTCTCCCAAGTACTCGCCTACCAGTCCCACC
TATTCACCCACCACCCCAAAATACTCCCCAACATCTCCTACTTATTCCCCAACCTCTCCA
GTCTACACCCCAACCTCTCCCAAGTACTCACCTACTAGCCCCACTTACTCGCCCACTTCC
CCCAAGTACTCGCCCACCAGCCCCACCTACTCGCCCACCTCCCCCAAAGGCTCAACCTAC
TCTCCCACTTCCCCTGGTTACTCGCCCACCAGCCCCACCTACAGTCTCACAAGCCCGGCT
ATCAGCCCGGATGACAGTGACGAGGAGAACTGA
Enzyme 13 GenBank Gene ID X63564 Link Image
Enzyme 13 GeneCard ID POLR2A Link Image
Enzyme 13 GenAtlas ID POLR2A Link Image
Enzyme 13 HGNC ID HGNC:9187 Link Image
Enzyme 13 Chromosome Location 17
Enzyme 13 Locus 17p13.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Wintzerith M, Acker J, Vicaire S, Vigneron M, Kedinger C: Complete sequence of the human RNA polymerase II largest subunit. Nucleic Acids Res. 1992 Feb 25;20(4):910. [PubMed Link Image]
  2. Mita K, Tsuji H, Morimyo M, Takahashi E, Nenoi M, Ichimura S, Yamauchi M, Hongo E, Hayashi A: The human gene encoding the largest subunit of RNA polymerase II. Gene. 1995 Jul 4;159(2):285-6. [PubMed Link Image]
  3. Nayler O, Stratling W, Bourquin JP, Stagljar I, Lindemann L, Jasper H, Hartmann AM, Fackelmayer FO, Ullrich A, Stamm S: SAF-B protein couples transcription and pre-mRNA splicing to SAR/MAR elements. Nucleic Acids Res. 1998 Aug 1;26(15):3542-9. [PubMed Link Image]
  4. Allen M, Friedler A, Schon O, Bycroft M: The structure of an FF domain from human HYPA/FBP11. J Mol Biol. 2002 Oct 25;323(3):411-6. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6017
Enzyme 14 Name DNA-directed RNA polymerase, mitochondrial precursor
Enzyme 14 Synonyms
  1. MtRPOL
Enzyme 14 Gene Name POLRMT
Enzyme 14 Protein Sequence >DNA-directed RNA polymerase, mitochondrial precursor
MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHV
ELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCG
RWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTR
QAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLP
LAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYA
AALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSL
PPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKP
TLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVV
RMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASD
AEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSS
RLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHS
GAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQL
FQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEAL
YRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDW
LKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCME
VANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVA
AQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDF
PQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQ
PYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCY
RKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILE
ASQLKETLQAVPKPGAFDLEQVKRSTYFFS
Enzyme 14 Number of Residues 1230
Enzyme 14 Molecular Weight 138622
Enzyme 14 Theoretical pI 9.25
Enzyme 14 GO Classification
Function
  • DNA binding
  • DNA-directed RNA 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 14 General Function Not Available
Enzyme 14 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 14 Pathways
Enzyme 14 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(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 2114396 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O00411 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name RPOM_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >3693 bp
ATGTCGGCACTTTGCTGGGGCCGCGGAGCGGCGGGGCTCAAACGAGCCCTACGGCCTTGC
GGCCGCCCGGGACTCCCCGGCAAAGAAGGGACCGCCGGTGGCGTCTGCGGCCCCAGGAGG
AGCTCGTCCGCCAGCCCCCAGGAGCAAGACCAAGACCGCAGGAAGGACTGGGGCCACGTG
GAGCTGCTGGAGGTGCTCCAGGCGCGGGTGCGGCAGCTGCAGGCTGAGAGCGTGTCGGAG
GTGGTGGTGAACAGGGTGGATGTGGCGCGGCTCCCAGAATGTGGCAGTGGAGATGGTAGC
CTCCAGCCACCCAGGAAGGTCCAGATGGGGGCCAAGGATGCCACCCCGGTGCCCTGTGGC
CGCTGGGCAAAGATACTGGAGAAGGATAAGCGGACCCAGCAGATGCGTATGCAGCGGTTG
AAGGCGAAGCTGCAGATGCCATTCCAGAGCGGGGAGTTCAAGGCGCTGACCAGGCGCCTG
CAGGTGGAGCCCCGGCTCCTGAGCAAGCAGATGGCCGGGTGCCTGGAGGACTGCACGCGC
CAGGCCCCCGAGAGCCCCTGGGAGGAGCAGCTGGCCCGGCTGCTGCAGGAGGCCCCTGGG
AAGCTGAGCCTCGATGTGGAGCAGGCCCCGTCGGGGCAGCACTCGCAGGCCCAGCTCTCA
GGTCAGCAGCAGAGGCTCCTGGCCTTCTTCAAGTGCTGCCTGCTCACTGACCAGCTGCCC
CTCGCCCACCACCTGCTGGTCGTCCACCACGGCCAGCGGCAGAAGCGGAAGCTGCTCACG
CTGGACATGTACAACGCCGTGATGCTTGGCTGGGCGCGGCAGGGTGCTTTCAAGGAGCTG
GTATATGTGTTATTCATGGTGAAGGATGCCGGCTTGACCCCGGACCTGCTGTCCTATGCG
GCTGCCCTCCAGTGCATGGGGAGGCAGGACCAGGACGCCGGGACCATCGAAAGGTGTCTG
GAACAGATGAGCCAGGAGGGGCTGAAGCTGCAGGCACTCTTCACCGCCGTTCTGCTGTCT
GAGGAGGATCGGGCCACTGTTCTGAAGGCCGTGCACAAGGTGAAGCCCACCTTCAGCCTC
CCGCCGCAGCTGCCGCCCCCGGTCAACACCTCCAAGCTGCTCAGGGACGTGTATGCCAAG
GATGGGCGTGTGTCCTACCCGAAGCTGCACCTGCCCTTGAAGACCCTGCAGTGCTTCTTT
GAGAAGCAGCTCCACATGGAGCTGGCCAGCAGGGTGTGCGTGGTGTCCGTGGAGAAGCCC
ACGTTGCCAAGCAAGGAGGTCAAGCACGCGCGGAAGACCCTGAAGACCCTGCGGGACCAA
TGGGAGAAAGCACTGTGCCGGGCGCTGCGGGAGACCAAGAACCGCCTAGAGCGCGAGGTG
TACGAGGGCCGGTTCTCACTTTACCCCTTCCTGTGCCTGCTGGACGAGCGCGAGGTGGTG
CGGATGCTCCTGCAGGTCCTGCAGGCGCTGCCCGCCCAAGGTGAGTCCTTCACCACCCTG
GCCCGGGAGCTGAGTGCGCGCACTTTCAGCCGGCACGTGGTGCAGAGGCAGCGGGTCAGT
GGCCAGGTGCAGGCGCTGCAGAACCACTACAGGAAGTACCTCTGCTTGCTGGCCTCCGAC
GCCGAGGTGCCCGAGCCCTGCCTGCCGCGGCAGTACTGGGAGGAGCTGGGGGCGCCCGAG
GCCCTGCGGGAGCAGCCCTGGCCCCTGCCAGTGCAGATGGAGCTGGGCAAGCTGCTGGCG
GAGATGCTGGTGCAGGCTACGCAGATGCCATGCAGCCTGGACAAGCCGCATCGTTCCTCT
CGGCTTGTCCCCGTGCTCTACCACGTGTATTCCTTCCGCAACGTCCAGCAAATCGGCATC
CTGAAGCCGCACCCGGCCTACGTGCAGCTGCTGGAGAAGGCCGCGGAACCCACGCTGACC
TTCGAGGCGGTGGATGTACCCATGCTTTGCCCCCCGCTGCCCTGGACATCGCCGCACTCT
GGTGCTTTCCTGCTCAGCCCCACCAAGCTGATGCGCACGGTGGAAGGCGCCACGCAACAC
CAGGAGCTGCTGGAAACCTGCCCACCCACCGCGCTGCATGGCGCACTGGACGCCCTCACC
CAACTGGGCAACTGCGCCTGGCGCGTCAACGGGCGCGTGCTGGACCTGGTGCTGCAGCTC
TTCCAGGCCAAGGGCTGCCCCCAGCTAGGCGTGCCGGCCCCGCCCTCCGAGGCGCCCCAG
CCGCCCGAGGCCCACCTGCCGCACAGCGCCGCGCCCGCCCGCAAGGCCGAGCTGCGCCGT
GAGCTGGCGCACTGCCAGAAGGTGGCCCGGGAGATGCACAGCCTGCGGGCGGAGGCGCTG
TACCGCCTCTCGCTGGCGCAGCACCTGCGGGACCGCGTCTTCTGGCTGCCGCACAACATG
GACTTCCGCGGCCGCACCTACCCCTGCCCGCCGCACTTCAACCACCTGGGCAGCGACGTG
GCGCGGGCCCTGCTGGAGTTCGCCCAGGGCCGCCCGCTCGGCCCGCACGGCCTGGATTGG
CTCAAGATCCACCTGGTCAATCTCACGGGGTTGAAGAAGCGGGAGCCGCTGCGGAAGCGC
CTGGCCTTTGCGGAGGAGGTGATGGATGACATCCTGGACTCCGCGGACCAACCCTTGACG
GGCCGAAAGTGGTGGATGGGCGCGGAGGAACCCTGGCAGACGCTGGCCTGCTGTATGGAG
GTGGCGAACGCTGTGCGCGCCTCCGACCCTGCCGCCTATGTCTCCCACCTCCCCGTCCAT
CAGGACGGCTCTTGCAACGGCCTGCAGCATTATGCTGCTCTGGGCCGCGACAGCGTGGGC
GCCGCCTCCGTCAACCTGGAGCCCTCGGATGTGCCGCAGGACGTGTACAGCGGCGTGGCC
GCGCAGGTGGAGGTGTTCCGTAGGCAGGACGCCCAGCGGGGCATGCGGGTGGCACAGGTG
CTGGAAAGTTTCATCACCCGCAAGGTGGTGAAGCAGACGGTGATGACGGTGGTGTACGGG
GTCACGCGCTATGGCGGGCGCCTGCAGATTGAGAAGCGCCTCCGGGAGCTGAGCGACTTT
CCCCAGGAGTTCGTGTGGGAGGCCTCTCACTATCTCGTACGCCAGGTCTTCAAGAGTCTA
CAGGAGATGTTCTCGGGGACCCGGGCCATCCAGCACTGGCTGACCGAGAGTGCCCGCCTC
ATCTCCCACATGGGCTCTGTGGTGGAGTGGGTCACACCCCTGGGCGTCCCCGTCATCCAG
CCGTATCGCCTGGACTCCAAGGTCAAGCAAATAGGAGGTGGAATTCAGAGCATCACCTAC
ACCCACAACGGAGACATCAGCCGAAAGCCCAACACACGTAAGCAGAAGAACGGCTTCCCG
CCCAACTTCATCCACTCGCTGGACTCCTCCCACATGATGCTCACCGCCCTGCACTGCTAC
AGGAAGGGCCTGACCTTCGTCTCTGTGCACGACTGTTACTGGACTCACGCAGCTGATGTC
TCCGTCATGAACCAGGTGTGCCGGGAGCAGTTTGTCCGCTTGCACAGCGAGCCCATCCTG
CAGGACCTGTCCAGATTCCTGGTCAAGCGGTTCTGCTCTGAGCCCCAGAAGATCTTGGAG
GCCAGCCAGCTGAAGGAGACACTGCAGGCGGTGCCCAAGCCAGGGGCCTTCGACCTGGAG
CAGGTGAAGCGTTCCACCTACTTCTTCAGCTGA
Enzyme 14 GenBank Gene ID U75370 Link Image
Enzyme 14 GeneCard ID POLRMT Link Image
Enzyme 14 GenAtlas ID POLRMT Link Image
Enzyme 14 HGNC ID HGNC:9200 Link Image
Enzyme 14 Chromosome Location 19
Enzyme 14 Locus 19p13.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Tiranti V, Savoia A, Forti F, D'Apolito MF, Centra M, Rocchi M, Zeviani M: Identification of the gene encoding the human mitochondrial RNA polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database. Hum Mol Genet. 1997 Apr;6(4):615-25. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6018
Enzyme 15 Name DNA-directed RNA polymerase I 135 kDa polypeptide
Enzyme 15 Synonyms
  1. RNA polymerase I subunit 2
  2. RPA135
Enzyme 15 Gene Name POLR1B
Enzyme 15 Protein Sequence >DNA-directed RNA polymerase I 135 kDa polypeptide
MDPGSRWRNLPSGPSLKHLTDPSYGIPREQQKAALQELTRAHVESFNYAVHEGLGLAVQA
IPPFEFAFKDERISFTILDAVISPPTVPKGTICKEANVYPAECRGRRSTYRGKLTADINW
AVNGISKGIIKQFLGYVPIMVKSKLCNLRNLPPQALIEHHEEAEEMGGYFIINGIEKVIR
MLIMPRRNFPIAMIRPKWKTRGPGYTQYGVSMHCVREEHSAVNMNLHYLENGTVMLNFIY
RKELFFLPLGFALKALVSFSDYQIFQELIKGKEDDSFLRNSVSQMLRIVMEEGCSTQKQV
LNYLGECFRVKLNVPDWYPNEQAAEFLFNQCICIHLKSNTEKFYMLCLMTRKLFALAKGE
CMEDNPDSLVNQEVLTPGQLFLMFLKEKLEGWLVSIKIAFDKKAQKTSVSMNTDNLMRIF
TMGIDLTKPFEYLFATGNLRSKTGLGLLQDSGLCVVADKLNFIRYLSHFRCVHRGADFAK
MRTTTVRRLLPESWGFLCPVHTPDGEPCGLMNHLTAVCEVVTQFVYTASIPALLCNLGVT
PIDGAPHRSYSECYPVLLDGVMVGWVDKDLAPGIADSLRHFKVLREKRIPPWMEVVLIPM
TGKPSLYPGLFLFTTPCRLVRPVQNLALGKEELIGTMEQIFMNVAIFEDEVFAGVTTHQE
LFPHSLLSVIANFIPFSDHNQSPRNMYQCQMGKQTMGFPLLTYQDRSDNKLYRLQTPQSP
LVRPSMYDYYDMDNYPIGTNAIVAVISYTGYDMEDAMIVNKASWERGFAHGSVYKSEFID
LSEKIKQGDSSLVFGIKPGDPRVLQKLDDDGLPFIGAKLQYGDPYYSYLNLNTGESFVMY
YKSKENCVVDNIKVCSNDTGSGKFKCVCITMRVPRNPTIGDKFASRHGQKGILSRLWPAE
DMPFTESGMVPDILFNPHGFPSRMTIGMLIESMAGKSAALHGLCHDATPFIFSEENSALE
YFGEMLKAAGYNFYGTERLYSGISGLELEADIFIGVVYYQRLRHMVSDKFQVRTTGARDR
VTNQPIGGRNVQGGIRFGEMERDALLAHGTSFLLHDRLFNCSDRSVAHVCVKCGSLLSPL
LEKPPPSWSAMRNRKYNCTLCSRSDTIDTVSVPYVFRYFVAELAAMNIKVKLDVV
Enzyme 15 Number of Residues 1135
Enzyme 15 Molecular Weight 128231
Enzyme 15 Theoretical pI 7.88
Enzyme 15 GO Classification
Function
  • DNA binding
  • DNA-directed RNA 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
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 15 General Function Transcription
Enzyme 15 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. RNA polymerase I is essentially used to transcribe ribosomal DNA units
Enzyme 15 Pathways
Enzyme 15 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(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 10433976 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9H9Y6 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name RPA2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >3240 bp
ATGGATCCTGGCAGCCGGTGGCGGAACCTGCCCAGCGGGCCTAGCCTAAAGCACTTGACT
GACCCCTCTTATGGAATCCCGCGGGAACAGCAAAAGGCAGCGTTGCAGGAGCTGACGCGG
GCGCACGTGGAGTCCTTCAACTACGCTGTGCACGAGGGTCTCGGCCTCGCGGTGCAGGCT
GATATCAACTGGGCAGTGAATGGAATCTCAAAAGGAATCATTAAGCAGTTTCTTGGCTAC
GTTCCCATCATGGTGAAATCCAAGCTTTGCAACTTACGTAACCTTCCCCCACAAGCCCTC
ATTGAGCACCATGAGGAGGCAGAGGAAATGGGGGGCTATTTTATAATCAATGGCATTGAA
AAAGTCATCCGAATGTTGATTATGCCTCGGAGAAATTTTCCCATTGCAATGATAAGACCA
AAATGGAAAACCAGAGGGCCTGGTTATACTCAGTATGGAGTTTCAATGCACTGTGTGAGG
GAAGAACATTCCGCTGTCAATATGAACCTCCACTACTTGGAAAATGGCACAGTTATGTTG
AACTTTATTTACCGAAAAGAACTGTTCTTTCGTCCTTTGGGATTTGCACTTAAGGCACTT
GTCAGCTTTTCTGATTATCAGATCTTTCAGGAGCTCATCAAAGGAAAAGAGGATGATTCT
TTCCTTAGGAACTCTGTTTCTCAGATGTTAAGGATTGTAATGGAAGAGGGTTGTTTGACA
CAAAAACAGGTCCTTAACTACCTAGGTGAATGCTTCAGAGTAAAACTCAATGTTCCTGAC
TGGTACCCAAATGAGCAAGCTGCGGAGTTCCTGTTTAACCAGTGCATCTGTATCCACTTG
AAATCCAATACTGAAAAGTTTTATATGCTTTGTCTCATGACGCGAAAGCTCTTTGCTTTA
GCCAAAGGAGAGTGCATGGAGGACAATCCTGATAGTTTGGTGAACCAGGAAGTCCTCACA
CCGGGTCAGCTCTTCCTTATGTTCCTGAAGGAAAAACTGGAAGGTTGGTTAGTGTCTATT
AAAATAGCTTTTGATAAGAAGGCTCAGAAGACCAGTGTTTCCATGAACACTGACAATTTG
ATGAGGATTTTTACAATGGGCATAGACCTTACAAAACCATTTGAATACCTTTTTGCTACT
GGGAATCTGCGTTCTAAAACAGGTCTTGGCCTCCTACAAGATTCTGGACTTTGTGTTGTG
GCTGACAAGCTGAACTTCATACGCTACCTCTCCCATTTCCGCTGCGTGCACAGAGGGGCT
GATTTTGCCAAGATGAGGACCACCACAGTACGCAGGCTGCTGCCAGAGTCCTGGGGCTTC
CTTTGTCCCGTGCATACCCCAGACGGGGAGCCCTGTGGCCTGATGAACCACCTAACTGCC
GTATGTGAGGTTGTCACACAGTTTGTGTATACGGCATCTATTCCAGCTTTACTGTGCAAC
TTGGGGGTCACTCCCATTGATGGAGCTCCCCACCGATCATACAGTGAGTGCTACCCTGTC
CTGCTGGACGGTGTCATGGTTGGCTGGGTGGATAAGGATCTTGCTCCAGGCATCGCAGAT
TCTCTTCGTCATTTTAAGGTGTTGAGAGAGAAAAGAATTCCTCCCTGGATGGAAGTGGTC
CTTATACCCATGACAGGAAAACCAAGTCTGTACCCAGGATTGTTCCTTTTTACCACTCCT
TGTAGACTGGTACGGCCTGTGCAGAACTTAGCATTGGGCAAAGAAGAGCTAATTGGAACT
ATGGAACAGATCTTCATGAATGTCGCTATCTTTGAGGATGAAGTTTTTGCTGGAGTTACC
ACACACCAGGAACTCTTTCCACACAGCCTGCTGAGTGTGATTGCCAACTTCATCCCTTTC
TCTGATCACAACCAGAGTCCACGGAACATGTACCAATGCCAGATGGGTAAGCAAACTATG
GGCTTTCCACTTCTCACTTATCAAGACCGATCGGATAACAAACTGTATCGTCTTCAGACT
CCTCAGAGTCCCTTGGTGAGACCCTCCATGTATGATTATTATGACATGGATAACTATCCA
ATTGGGACCAATGCCATCGTTGCTGTGATTTCTTACACTGGCTATGATATGGAAGATGCC
ATGATTGTGAATAAGGCCTCTTGGGAACGAGGCTTTGCCCATGGAAGTGTCTACAAGTCT
GAGTTCATAGACCTCTCTGAAAAAATTAAACAAGGAGATAGTAGCCTGGTGTTTGGCATC
AAACCTGGTGACCCACGCGTTCTGCAGAAGTTAGATGACGATGGATTGCCGTTTATAGGA
GCAAAACTGCAGTACGGAGATCCGTATTACAGCTACCTCAACCTCAACACCGGGGAAAGT
TTTGTGATGTACTATAAGAGTAAAGAAAATTGTGTTGTGGATAACATCAAAGTGTGCAGT
AATGACACTGGGAGTGGAAAATTCAAGTGTGTTCGCATCACTATGAGAGTGCCTCGGAAC
CCAACTATCGGAGATAAATTTGCCAGTCGCCATGGGCGGAAGGGCATTTTAAGCAGATTG
TGGCCGGCTGAGGACATGCCTTTTACTGAGAGTGGGATGGTCCCAGACATTCTGTTCAAT
CCCCATGGTTTTCCATCCCGCATGACCATTGGGATGTTAATTGAGAGTATGGCCGGGAAG
TCTGCAGCTTTGCATGGTCTCTGCCATGATGCTACACCCTTCATCTTCTCAGAGGAGAAC
TCGGCCTTAGAATACTTTGGTGAGATGTTAAAGGCTGCTGGCTACAATTTCTATGGCACC
GAGAGGTTATATAGTGGCATCAGTGGGCTAGAACTGGAAGCAGACATCTTCATAGGAGTG
GTTTATTATCAGCGCTTACGCCATATGGTCTCAGACAAATTTCAAGTAAGGACAACTGGA
GCCCGAGACAGAGTCACCAACCAGCCTATTGGGGGAAGAAATGTCCAGGGTGGAATCCGT
TTTGGGGAGATGGAACGGGATGCGCTTTTAGCTCATGGTACATCTTTTCTCCTTCATGAC
CGCCTCTTCAACTGCTCAGATCGGTCGGTAGCCCATGTGTGTGTGAAGTGTGGCAGTTTA
CTCTCTCCACTGTTGGAGAAGCCACCCCCTTCTTGGTCTGCCATGCGCAACAGAAAATAC
AACTGTACTCTGTGTAGTCGCAGTGACACTATCGATACTGTTTCTGTGCCTTATGTTTTT
CGGTATTTTGTAGCTGAACTGGCAGCTATGAACATCAAAGTGAAACTGGATGTTGTTTAA
Enzyme 15 GenBank Gene ID AK022533 Link Image
Enzyme 15 GeneCard ID POLR1B Link Image
Enzyme 15 GenAtlas ID POLR1B Link Image
Enzyme 15 HGNC ID HGNC:20454 Link Image
Enzyme 15 Chromosome Location 2
Enzyme 15 Locus 2q13
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6031
Enzyme 16 Name DNA-directed RNA polymerase I-associated factor 53 kDa subunit
Enzyme 16 Synonyms
  1. RNA polymerase I polypeptide E
  2. RNA polymerase I- associated factor 1
Enzyme 16 Gene Name POLR1E
Enzyme 16 Protein Sequence >DNA-directed RNA polymerase I-associated factor 53 kDa subunit
MYQASAVSLLPRDIPSCHSPSPGFSHLPTSSSQLAPDLLQFPLGQDPSFLAIPILTLPPS
DSLVPPYIVWYIVWPSALISFLGCTLTVQFSNGKLQSPGNMRFTLYENKDSTNPRKRNQR
ILAAETDRLSYVGNNFGTGALKCNTLCRHFVGILNKTSGQMEVYDAELFNMQPLFSDVSV
ESELALESQTKTYREKMDSCIEAFGTTKQKRALNTRRMNRVGNESLNRAVAKAAETIIDT
KGVTALVSDAIHNDLQDDSLYLPPCYDDAAKPEDVYKFEDLLSPAEYEALQSPSEAFRNV
TSEEILKMIEENSHCTFVIEALKSLPSDVESRDRQARCIWFLDTLIKFRAHRVVKRKSAL
GPGVPHIINTKLLKHFTCLTYNNGRLRNLISDSMKAKITAYVIILALHIHDFQIDLTVLQ
RDLKLSEKRMMEIAKAMRLKISKRRVSVAAGSEEDHKLGTLSLPLPPAQTSDRLAKRRKI
T
Enzyme 16 Number of Residues 481
Enzyme 16 Molecular Weight 53963
Enzyme 16 Theoretical pI 8.74
Enzyme 16 GO Classification
Function
  • DNA binding
  • DNA-directed RNA 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
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Required for the initiation of transcription by the DNA- dependent RNA polymerase I holoenzyme. This complex catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 16 Pathways
Enzyme 16 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 10435392 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9GZS1 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name RPF53_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1260 bp
ATGGCGGCGGAGGTGTTGCCGAGTGCGAGGTGGCAGTATTGTGGGGCGCCCGACGGGAGC
CAGAGAGCTGTACTGGTCCAGTTCTCCAACGGGAAGCTACAGAGTCCAGGCAACATGCGC
TTTACCTTGTATGAGAACAAAGATTCCACCAACCCCAGGAAGAGGAATCAACGGATCCTG
GCAGCTGAAACAGATAGGCTCTCCTATGTGGGAAACAATTTTGGGACTGGAGCCCTCAAA
TGCAACACTTTGTGCAGGCACTTTGTGGGAATTTTGAACAAGACCTCTGGCCAAATGGAA
GTATATGATGCTGAATTGTTCAACATGCAGCCACTATTTTCAGATGTATCAGTTGAGAGT
GAACTGGCGCTAGAGAGTCAGACCAAAACTTACAGAGAAAAGATGGATTCTTGTATTGAA
GCCTTTGGTACCACCAAACAGAAGCGAGCTCTGAACACCAGGAGAATGAACAGAGTTGGC
AATGAATCTTTGAATCGTGCAGTGGCTAAAGCTGCAGAGACTATCATTGATACGAAGGGT
GTGACTGCTCTGGTCAGCGATGCTATCCACAATGACTTGCAAGATGACTCCCTCTACCTT
CCTCCCTGCTATGATGATGCAGCCAAGCCTGAAGACGTGTATAAATTTGAAGATCTTCTT
TCCCCTGCGGAGTATGAAGCTCTTCAGAGCCCATCTGAAGCTTTCAGGAACGTCACGTCA
GAAGAAATACTGAAGATGATTGAGGAGAACAGCCATTGCACCTTTGTCATAGAAGCGTTG
AAGTCTTTGCCATCAGATGTGGAGAGCCGAGACCGCCAGGCCCGATGCATATGGTTTCTG
GATACCCTCATCAAATTTCGAGCTCATAGGGTAGTTAAGCGGAAAAGTGCTCTGGGACCT
GGAGTTCCCCACATCATCAACACCAAACTGCTGAAGCACTTTACTTGCTTGACCTACAAC
AATGGCAGATTACGGAACTTAATTTCGGATTCTATGAAGGCGAAGATTACTGCATATGTG
ATCATACTTGCCTTGCACATACATGACTTCCAAATTGACCTGACAGTGTTACAGAGGGAC
TTGAAGCTCAGTGAGAAAAGGATGATGGAGATAGCCAAAGCCATGAGGCTGAAGATCTCC
AAAAGAAGGGTGTCTGTGGCCGCCGGCAGTGAAGAAGATCACAAACTGGGCACCCTGTCC
CTCCCGCTGCCTCCAGCCCAGACCTCAGACCGCCTGGCAAAGCGGAGGAAGATTACCTAG
Enzyme 16 GenBank Gene ID AK023452 Link Image
Enzyme 16 GeneCard ID POLR1E Link Image
Enzyme 16 GenAtlas ID POLR1E Link Image
Enzyme 16 HGNC ID HGNC:17631 Link Image
Enzyme 16 Chromosome Location 9
Enzyme 16 Locus 9p13.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6033
Enzyme 17 Name 6-phosphofructokinase, liver type
Enzyme 17 Synonyms
  1. Phosphofructokinase 1
  2. Phosphohexokinase
  3. Phosphofructo-1-kinase isozyme B
  4. PFK-B
Enzyme 17 Gene Name PFKL
Enzyme 17 Protein Sequence >6-phosphofructokinase, liver type
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVE
GGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDG
SLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDS
ALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWE
NFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQ
RGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQK
AMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRS
AVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESI
VENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLG
SDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFN
IHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGH
LQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFS
PVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
Enzyme 17 Number of Residues 780
Enzyme 17 Molecular Weight 85020
Enzyme 17 Theoretical pI 7.54
Enzyme 17 GO Classification
Function
  • 6-phosphofructokinase activity
  • catalytic activity
  • phosphofructokinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • 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
  • 6-phosphofructokinase complex
  • cell
  • cytoplasm
  • intracellular
  • protein complex
Enzyme 17 General Function Carbohydrate transport and metabolism
Enzyme 17 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 17 Pathways
Enzyme 17 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 35431 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P17858 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name K6PL_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >2343 bp
ATGGCCGCGGTGGACCTGGAGAAGCTGCGGGCGTCGGGCGCGGGCAAGGCCATCGGCGTC
CTGACCAGCGGCGGCGACCGGCAAGGCATGAACGCTGCTGTCCGGGCTGTGACGCGCATG
GGCATTTATGTGGGTGCCAAAGTCTTCCTCATCTACGAGGGCTATGAGGGCCTCGTGGAG
GGAGGTGAGAACATCAAGCAGGCCAACTGGCTGAGCGTCTCCAACATCATCCAGCTGGGC
GGCACTATCATTGGCAGCGCTCGCTCGAAGGCCTTTACCACCAGGGAGGGGCGCCGGGCA
GCGGCCTACAACCTGGTCCAGCACGGCATCACCAACCTGTGCGTCATCGGCGGGGATGGC
AGCCTCACAGGTGCCAACATCTTCCGCAGCGAGTGGGGCAGCCTGCTGGAGGAGCTGGTG
GCGGAAGGTAAGATCTCAGAGACTACAGCCTGGACCTACTCGCACCTGAACATCGCGGGC
CTAGTGGGCTCCATCGATAACGACTTCTGCGGCACCGACATGACCATCGGCACGGACTCG
GCCCTCCACCGCATCATGGAGGTCATCGATGCCATCACCACCACTGCCCAGAGCCACCAG
AGGACCTTCGTGCTGGAAGTGATGGGCCGGCACTGCGGGTACCTGGCGCTGGTATCTGCA
CTGGCCTCAGGGGCCGACTGGCTGTTCATCCCCGAGGCTCCACCCGAGGACGGCTGGGAG
AACTTCATGTGTGAGAGGCTGGGTGAGACTCGGAGCCGTGGGTCCCGACTGAACATCATC
ATCATCGCTGAGGGTGCCATTGACCGCAACGGGAAGCCCATCTCGTCCAGCTACGTGAAG
GACCTGGTGGTTCAGAGGCTGGGCTTCGACACCCGTGTAACTGTGCTGGGCCACGTGCAG
CGGGGAGGGACGCCCTCTGCCTTCGACCGGATCCTGAGCAGCAAGATGGGCATGGAGGCG
GTGATGGCGCTGCTGGAAGCCACGCCTGACACGCCGGCCTGCGTGGTCACCCTCTCGGGG
AACCAGTCAGTGCGGCTGCCCCTCATGGAGTGCGTGCAGATGACCAAGGAAGTGCAGAAA
GCCATGGATGACAAGAGGTTTGACGAGGCCACCCAGCTCCGTGGTGGGAGCTTCGAGAAC
AACTGGAACATTTACAAGCTCCTCACCCACCAGAAGCCCCCCAAGGAGAAGTCTAACTTC
TCCCTGGCCATCCTGAATGTGGGGGCCCCGGCGGCTGGCATGAATGCGGCCGTGCGCTCG
GCGGTGCGGACCGGCATCTCCCATGGACACACAGTATACGTGGTGCACGATGGCTTCGAA
GGCCTAGCCAAGGGTCAGGTGCAAGAAGTAGGCTGGCACGACGTGGCCGGCTGGTTGGGG
CGTGGTGGCTCCATGCTGGGGACCAAGAGGACCCTGCCCAAGGGCCAGCTGGAGTCCATT
GTGGAGAACATCCGCATCTATGGTATTCACGCCCTGCTGGTGGTCGGTGGGTTTGAGGCC
TATGAAGGGGTGCTGCAGCTGGTGGAGGCTCGCGGGCGCTACGAGGAGCTCTGCATCGTC
ATGTGTGTCATCCCAGCCACCATCAGCAACAACGTCCCTGGCACCGACTTCAGCCTGGGC
TCCGACACTGCTGTAAATGCCGCCATGGAGAGCTGTGACCGCATCAAACAGTCTGCCTCG
GGGACCAAGCGCCGTGTGTTCATCGTGGAGACCATGGGGGGTTACTGTGGCTACCTGGCC
ACCGTGACTGGCATTGCTGTGGGGGCCGACGCCGCCTACGTCTTCGAGGACCCTTTCAAC
ATCCACGACTTAAAGGTCAACGTGGAGCACATGACGGAGAAGATGAAGACAGACATTCAG
AGGGGCCTGGTGCTGCGGAACGAGAAGTGCCATGACTACTACACCACGGAGTTCCTGTAC
AACCTGTACTCATCAGAGGGCAAGGGCGTCTTCGACTGCAGGACCAATGTCCTGGGCCAC
CTGCAGCAGGGTGGCGCTCCAACCCCCTTTGACCGGAACTATGGGACCAAGCTGGGGGTG
AAGGCCATGCTGTGGTTGTCGGAGAAGCTGCGCGAGGTTTACCGCAAGGGACGGGTGTTC
GCCAATGCCCCAGACTCGGCCTGCGTGATCGGCCTGAAGAAGAAGGCGGTGGCCTTCAGC
CCCGTCACTGAGCTCAAGAAAGACACTGATTTCGAGCACCGCATGCCACGGGAGCAGTGG
TGGCTGAGCCTGCGGCTCATGCTGAAGATGCTGGCACAATACCGCATCAGTATGGCCGCC
TACGTGTCAGGGGAGCTGGAGCACGTGACCCGCCGCACCCTGAGCATGGACAAGGGCTTC
TGA
Enzyme 17 GenBank Gene ID X15573 Link Image
Enzyme 17 GeneCard ID PFKL Link Image
Enzyme 17 GenAtlas ID PFKL Link Image
Enzyme 17 HGNC ID HGNC:8876 Link Image
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Levanon D, Danciger E, Dafni N, Bernstein Y, Elson A, Moens W, Brandeis M, Groner Y: The primary structure of human liver type phosphofructokinase and its comparison with other types of PFK. DNA. 1989 Dec;8(10):733-43. [PubMed Link Image]
  2. Elson A, Levanon D, Brandeis M, Dafni N, Bernstein Y, Danciger E, Groner Y: The structure of the human liver-type phosphofructokinase gene. Genomics. 1990 May;7(1):47-56. [PubMed Link Image]
  3. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6035
Enzyme 18 Name DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide
Enzyme 18 Synonyms
  1. RPC8
Enzyme 18 Gene Name POLR3H
Enzyme 18 Protein Sequence >DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide
MFVLVEMVDTVRIPPWQFERKLNDSIAEELNKKLANKVVYNVGLCICLFDITKLEDAYVF
PGDGASHTKVHFRCVVFHPFLDEILIGKIKGCSPEGVHVSLGFFDDILIPPESLQQPAKF
DEAEQVWVWEYETEEGAHDLYMDTGEEIRFRVVDESFVDTSPTGPSSADATTSSEELPKK
EAPYTLVGSISEPGLGLLSWWTSN
Enzyme 18 Number of Residues 204
Enzyme 18 Molecular Weight 22918
Enzyme 18 Theoretical pI 4.21
Enzyme 18 GO Classification
Function
  • DNA-directed RNA polymerase activity
  • catalytic activity
  • 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 18 General Function Transcription
Enzyme 18 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 18 Pathways
Enzyme 18 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 24429623 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9Y535 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name RPC8_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >615 bp
ATGTTCGTCCTGGTGGAAATGGTGGACACCGTCCGGATCCCCCCTTGGCAGTTTGAGAGG
AAGCTCAACGACTCCATTGCCGAGGAGCTGAACAAGAAGTTGGCCAACAAGGTCGTGTAC
AACGTGGGACTCTGCATTTGTCTGTTTGATATCACCAAACTGGAGGATGCCTATGTATTC
CCTGGGGATGGCGCATCACACACCAAAGTCCATTTTCGCTGCGTGGTGTTTCATCCATTC
CTAGATGAGATTCTCATTGGGAAGATCAAAGGCTGCAGCCCAGAAGGAGTGCACGTCTCT
CTAGGCTTCTTCGATGACATTCTCATCCCCCCAGAGTCACTGCAGCAGCCAGCCAAGTTC
GACGAAGCGGAGCAGGTGTGGGTGTGGGAGTACGAGACGGAGGAAGGAGCACACGACCTC
TACATGGACACCGGCGAGGAGATCCGCTTCCGGGTGGTGGACGAGAGCTTTGTTGACACG
TCCCCCACAGGGCCCAGCTCAGCAGATGCCACCACTTCCAGTGAGGAGCTGCCAAAGAAG
GAGGCTCCGTACACGCTTGTGGGATCCATCAGTGAGCCAGGCCTGGGCCTTCTCTCCTGG
TGGACCAGCAACTAG
Enzyme 18 GenBank Gene ID AY092087 Link Image
Enzyme 18 GeneCard ID POLR3H Link Image
Enzyme 18 GenAtlas ID POLR3H Link Image
Enzyme 18 HGNC ID HGNC:30349 Link Image
Enzyme 18 Chromosome Location 22
Enzyme 18 Locus 22q13.2
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
  2. Hirosawa M, Nagase T, Murahashi Y, Kikuno R, Ohara O: Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping. DNA Res. 2001 Feb 28;8(1):1-9. [PubMed Link Image]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6036
Enzyme 19 Name DNA-directed RNA polymerases III 12.5 kDa polypeptide
Enzyme 19 Synonyms
  1. RNA polymerase III subunit K
  2. RNA polymerase III C11 subunit
  3. HsC11p
  4. hRPC11
Enzyme 19 Gene Name POLR3K
Enzyme 19 Protein Sequence >DNA-directed RNA polymerases III 12.5 kDa polypeptide
MLLFCPGCGNGLIVEEGQRCHRFSCNTCPYVHNITRKVTNRKYPKLKEVDDVLGGAAAWE
NVDSTAESCPKCEHPRAYFMQLQTRSADEPMTTFYKCCNAQCGHRWRD
Enzyme 19 Number of Residues 108
Enzyme 19 Molecular Weight 12336
Enzyme 19 Theoretical pI 7.89
Enzyme 19 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transcription factor activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • RNA elongation
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • transcription
  • transcription, DNA-dependent
Component
Enzyme 19 General Function Transcription
Enzyme 19 Specific Function Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 19 Pathways
Enzyme 19 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(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 4877775 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9Y2Y1 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name RPC11_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >327 bp
ATGCTGCTGTTCTGCCCCGGCTGCGGGAACGGGCTGATCGTGGAGGAGGGACAACGCTGC
CACCGCTTCGCCTGCAACACGTGCCCCTACGTGCACAACATCACCCGCAAGGTAACAAAT
CGGAAGTACCCAAAACTGAAAGAAGTGGATGATGTGCTTGGTGGAGCAGCTGCCTGGGAG
AATGTTGACTCTACTGCAGAGTCGTGTCCCAAATGCGAACATCCTCGTGCTTACTTCATG
CAGCTTCAGACCCGCTCTGCAGATGAGCCGATGACCACCTTCTACAAGTGCTGCAATGCT
CAGTGTGGACACCGCTGGAGGGATTAG
Enzyme 19 GenBank Gene ID AF126531 Link Image
Enzyme 19 GeneCard ID POLR3K Link Image
Enzyme 19 GenAtlas ID POLR3K Link Image
Enzyme 19 HGNC ID HGNC:14121 Link Image
Enzyme 19 Chromosome Location 16
Enzyme 19 Locus 16p13.3
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Chedin S, Riva M, Schultz P, Sentenac A, Carles C: The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination. Genes Dev. 1998 Dec 15;12(24):3857-71. [PubMed Link Image]
  2. Spakovskii GV, Lebedenko EN: [Molecular identification and characteristics of hRPC11, the smallest specific subunit of human RNA polymerase III] Bioorg Khim. 1998 Nov;24(11):877-80. [PubMed Link Image]
  3. 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]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6037
Enzyme 20 Name 6-phosphofructokinase, muscle type
Enzyme 20 Synonyms
  1. Phosphofructokinase 1
  2. Phosphohexokinase
  3. Phosphofructo-1-kinase isozyme A
  4. PFK-A
  5. Phosphofructokinase-M
Enzyme 20 Gene Name PFKM
Enzyme 20 Protein Sequence >6-phosphofructokinase, muscle type
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVD
GGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDG
SLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDS
ALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWE
EHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQ
RGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTK
AMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVR
STVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQ
ISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSV
GADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPF
TIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLG
HMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVF
QPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
Enzyme 20 Number of Residues 780
Enzyme 20 Molecular Weight 85184
Enzyme 20 Theoretical pI 8.07
Enzyme 20 GO Classification
Function
  • 6-phosphofructokinase activity
  • catalytic activity
  • phosphofructokinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • 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
  • 6-phosphofructokinase complex
  • cell
  • cytoplasm
  • intracellular
  • protein complex
Enzyme 20 General Function Carbohydrate transport and metabolism
Enzyme 20 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 20 Pathways
Enzyme 20 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 1101758 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P08237 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name K6PF_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >2343 bp
ATGACCCATGAAGAGCACCATGCAGCCAAAACCCTGGGGATTGGCAAAGCCATTGCTGTC
TTAACCTCTGGTGGAGATGCCCAAGGTATGAATGCTGCTGTCAGGGCTGTGGTTCGAGTT
GGTATCTTCACCGGTGCCCGTGTCTTCTTTGTCCATGAGGGTTATCAAGGCCTGGTGGAT
GGTGGAGATCACATCAAGGAAGCCACCTGGGAGAGCGTTTCGATGATGCTTCAGCTGGGA
GGCACGGTGATTGGAAGTGCCCGGTGCAAGGACTTTCGGGAACGAGAAGGACGACTCCGA
GCTGCCTACAACCTGGTGAAGCGTGGGATCACCAATCTCTGTGTCATTGGGGGTGATGGC
AGCCTCACTGGGGCTGACACCTTCCGTTCTGAGTGGAGTGACTTGTTGAGTGACCTCCAG
AAAGCAGGTAAGATCACAGATGAGGAGGCTACGAAGTCCAGCTACCTGAACATTGTGGGC
CTGGTTGGGTCAATTGACAATGACTTCTGTGGCACTGATATGACCATTGGCACTGACTCT
GCCCTGCATCGGATCATGGAAATTGTAGATGCCATCACTACCACTGCCCAGAGCCACCAG
AGGACATTTGTGTTAGAAGTAATGGGCCGCCACTGTGGATACCTGGCCCTTGTCACCTCT
CTGTCCTGTGGGGCCGACTGGGTTTTTATTCCTGAATGTCCACCAGATGACGACTGGGAG
GAACACCTTTGTCGCCGACTCAGCGAGACAAGGACCCGTGGTTCTCGTCTCAACATCATC
ATTGTGGCTGAGGGTGCAATTGACAAGAATGGAAAACCAATCACCTCAGAAGACATCAAG
AATCTGGTGGTTAAGCGTCTGGGATATGACACCCGGGTTACTGTCTTGGGGCATGTGCAG
AGGGGTGGGACGCCATCAGCCTTTGACAGAATTCTGGGCAGCAGGATGGGTGTGGAAGCA
GTGATGGCACTTTTGGAGGGGACCCCAGATACCCCAGCCTGTGTAGTGAGCCTCTCTGGT
AACCAGGCTGTGCGCCTGCCCCTCATGGAATGTGTCCAGGTGACCAAAGATGTGACCAAG
GCCATGGATGAGAAGAAATTTGACGAAGCCCTGAAGCTGAGAGGCCGGAGCTTCATGAAC
AACTGGGAGGTGTACAAGCTTCTAGCTCATGTCAGACCCCCGGTATCTAAGAGTGGTTCG
CACACAGTGGCTGTGATGAACGTGGGGGCTCCGGCTGCAGGCATGAATGCTGCTGTTCGC
TCCACTGTGAGGATTGGCCTTATCCAGGGCAACCGAGTGCTCGTTGTCCATGATGGTTTC
GAGGGCCTGGCCAAGGGGCAGATAGAGGAAGCTGGCTGGAGCTATGTTGGGGGCTGGACT
GGCCAAGGTGGCTCTAAACTTGGGACTAAAAGGACTCTACCCAAGAAGAGCTTTGAACAG
ATCAGTGCCAATATAACTAAGTTTAACATTCAGGGCCTTGTCATCATTGGGGGCTTTGAG
GCTTACACAGGGGGCCTGGAACTGATGGAGGGCAGGAAGCAGTTTGATGAGCTCTGCATC
CCATTTGTGGTCATTCCTGCTACAGTCTCCAACAATGTCCCTGGCTCAGACTTCAGCGTT
GGGGCTGACACAGCACTCAATACTATCTGCACAACCTGTGACCGCATCAAGCAGTCAGCA
GCTGGCACCAAGCGTCGGGTGTTTATCATTGAGACTATGGGTGGCTACTGTGGCTACCTG
GCTACCATGGCTGGACTGGCAGCTGGGGCCGATGCTGCCTACATTTTTGAGGAGCCCTTC
ACCATTCGAGACCTGCAGGCAAATGTTGAACATCTGGTGCAAAAGATGAAAACAACTGTG
AAAAGGGGCTTGGTGTTAAGGAATGAAAAGTGCAATGAGAACTATACCACTGACTTCATT
TTCAACCTGTACTCTGAGGAGGGGAAGGGCATCTTCGACAGCAGGAAGAATGTGCTTGGT
CACATGCAGCAGGGTGGGAGCCCAACCCCATTTGATAGGAATTTTGCCACTAAGATGGGC
GCCAAGGCTATGAACTGGATGTCTGGGAAAATCAAAGAGAGTTACCGTAATGGGCGGATC
TTTGCCAATACTCCAGATTCGGGCTGTGTTCTGGGGATGCGTAAGAGGGCTCTGGTCTTC
CAACCAGTGGCTGAGCTGAAGGACCAGACAGATTTTGAGCATCGAATCCCCAAGGAACAG
TGGTGGCTGAAACTGAGGCCCATCCTCAAAATCCTAGCCAAGTACGAGATTGACTTGGAC
ACTTCAGACCATGCCCACCTGGAGCACATCACCCGGAAGCGGTCCGGGGAAGCTGCCGTC
TAA
Enzyme 20 GenBank Gene ID M59741 Link Image
Enzyme 20 GeneCard ID PFKM Link Image
Enzyme 20 GenAtlas ID PFKM Link Image
Enzyme 20 HGNC ID HGNC:8877 Link Image
Enzyme 20 Chromosome Location 12
Enzyme 20 Locus 12q13.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Yamasaki T, Nakajima H, Kono N, Hotta K, Yamada K, Imai E, Kuwajima M, Noguchi T, Tanaka T, Tarui S: Structure of the entire human muscle phosphofructokinase-encoding gene: a two-promoter system. Gene. 1991 Aug 15;104(2):277-82. [PubMed Link Image]
  2. Sharma PM, Reddy GR, Vora S, Babior BM, McLachlan A: Cloning and expression of a human muscle phosphofructokinase cDNA. Gene. 1989 Apr 15;77(1):177-83. [PubMed Link Image]
  3. Nakajima H, Noguchi T, Yamasaki T, Kono N, Tanaka T, Tarui S: Cloning of human muscle phosphofructokinase cDNA. FEBS Lett. 1987 Oct 19;223(1):113-6. [PubMed Link Image]
  4. Sharma PM, Reddy GR, Babior BM, McLachlan A: Alternative splicing of the transcript encoding the human muscle isoenzyme of phosphofructokinase. J Biol Chem. 1990 Jun 5;265(16):9006-10. [PubMed Link Image]
  5. Valdez BC, Chen Z, Sosa MG, Younathan ES, Chang SH: Human 6-phosphofructo-1-kinase gene has an additional intron upstream of start codon. Gene. 1989 Mar 15;76(1):167-9. [PubMed Link Image]
  6. Raben N, Sherman JB: Mutations in muscle phosphofructokinase gene. Hum Mutat. 1995;6(1):1-6. [PubMed Link Image]
  7. Tsujino S, Servidei S, Tonin P, Shanske S, Azan G, DiMauro S: Identification of three novel mutations in non-Ashkenazi Italian patients with muscle phosphofructokinase deficiency. Am J Hum Genet. 1994 May;54(5):812-9. [PubMed Link Image]
  8. Raben N, Exelbert R, Spiegel R, Sherman JB, Nakajima H, Plotz P, Heinisch J: Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency. Am J Hum Genet. 1995 Jan;56(1):131-41. [PubMed Link Image]
  9. Hamaguchi T, Nakajima H, Noguchi T, Nakagawa C, Kuwajima M, Kono N, Tarui S, Matsuzawa Y: Novel missense mutation (W686C) of the phosphofructokinase-M gene in a Japanese patient with a mild form of glycogenosis VII. Hum Mutat. 1996;8(3):273-5. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6041
Enzyme 21 Name Pyruvate kinase isozymes R/L
Enzyme 21 Synonyms
  1. R-type/L-type pyruvate kinase
  2. Red cell/liver pyruvate kinase
  3. Pyruvate kinase 1
Enzyme 21 Gene Name PKLR
Enzyme 21 Protein Sequence >Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Enzyme 21 Number of Residues 574
Enzyme 21 Molecular Weight 61831
Enzyme 21 Theoretical pI 7.83
Enzyme 21 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 21 General Function Carbohydrate transport and metabolism
Enzyme 21 Specific Function ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 21 Pathways
Enzyme 21 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 3327365 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P30613 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name KPYR_HUMAN Link Image
Enzyme 21 PDB ID 1LIU Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 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 21 GenBank Gene ID AB015983 Link Image
Enzyme 21 GeneCard ID PKLR Link Image
Enzyme 21 GenAtlas ID PKLR Link Image
Enzyme 21 HGNC ID HGNC:9020 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 1q21
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6363
Enzyme 22 Name UTP--glucose-1-phosphate uridylyltransferase 2
Enzyme 22 Synonyms
  1. UDP- glucose pyrophosphorylase 2
  2. UDPGP 2
  3. UGPase 2
Enzyme 22 Gene Name UGP2
Enzyme 22 Protein Sequence >UTP--glucose-1-phosphate uridylyltransferase 2
MSRFVQDLSKAMSQDGASQFQEVIRQELELSVKKELEKILTTASSHEFEHTKKDLDGFRK
LFHRFLQEKGPSVDWGKIQRPPEDSIQPYEKIKARGLPDNISSVLNKLVVVKLNGGLGTS
MGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNH
CRVKIYTFNQSRYPRINKESLLPVAKDVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFI
GEGKEYIFVSNIDNLGATVDLYILNHLMNPPNGKRCEFVMEVTNKTRADVKGGTLTQYEG
KLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLD
GGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSE
KREFPTVPLVKLGSSFTKVQDYLRRFESIPDMLELDHLTVSGDVTFGKNVSLKGTVIIIA
NHGDRIDIPPGAVLENKIVSGNLRILDH
Enzyme 22 Number of Residues 508
Enzyme 22 Molecular Weight 56941
Enzyme 22 Theoretical pI 8.40
Enzyme 22 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolism
  • physiological process
Component
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function Plays a central role as a glucosyl donor in cellular metabolic pathways
Enzyme 22 Pathways
Enzyme 22 Reactions
  • UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 881394 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q16851 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name UGPA2_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1494 bp
ATGTCTCAAGATGGTGCTTCTCAGTTCCAAGAAGTCATTCGGCAAGAGCTAGAATTATCT
GTGAAGAAGGAACTAGAAAAAATACTCACCACAGCATCATCACATGAATTTGAGCACACC
AAAAAAGACCTGGATGGATTTCGGAAGCTATTTCATAGATTTTTGCAAGAAAAGGGGCCT
TCTGTGGATTGGGGAAAAATCCAGAGACCCCCTGAAGATTCGATTCAACCCTATGAAAAG
ATAAAGGCCAGGGGCCTGCCTGATAATATATCTTCCGTGTTGAACAAACTAGTGGTGGTG
AAACTCAATGGTGGTTTGGGAACCAGCATGGGCTGCAAAGGCCCTAAAAGTCTGATTGGT
GTGAGGAATGAGAATACCTTTCTGGATCTGACTGTTCAGCAAATTGAACATTTGAACAAA
ACCTACAATACAGATGTCCCTCTTGTTTTAATGAACTCTTTTAACACGGATGAAGATACC
AAAAAAATACTACAGAAGTACAATCATTGTCGTGTGAAAATCTACACTTTCAATCAAAGC
AGGTACCCGAGGATTAATAAAGAATCTTTACGGCCTGTAGCAAAGGACGTGTCTTACTCA
GGGGAAAATACAGAAGCTTGGTACCCTCCAGGTCATGGTGATATTTACGCCAGTTTCTAC
AACTCTGGATTGCTTGATACCTTTATAGGAGAAGGCAAAGAGTATATTTTTGTGTCTAAC
ATAGATAATCTGGGTGCCACAGTGGATCTGTATATTCTTAATCATCTAATCAACCCACCC
AATGGAAAACGCTGTGAATTTGTCATGGAAGTCACAAATAAAACACGTGCAGATGTAAAG
GGCGGGACACTCACTCAATATGAAGGCAAACTGAGACTGGTGGAAATTGCTCAAGTGCCA
AAAGCACATGTTGACGAGTTCAAGTCTGTATCAAAGTTCAAAATATTTAATACAAACAAC
CTATGGATTTCTCTTGCAGCAGTTAAAAGACTGCAGGAGCAAAATGCCATTGACATGGAA
ATCATTGTGAATGCAAAGACTTTGGATGGAGGCCTGAATGTCATTCAATTAGAAACTGCA
GTAGGGGCTGCCATCAAAAGCTTTGAGAATTCTCTAGGTATTAATGTGCCAAGGAGCCGT
TTTCTGCCTGTCAAAACCACATCAGATCTCTTGCTGGTGATGTCAAACCTCTATAGTCTT
AATGCAGGATCTCTGACAATGAGTGAAAAGCGGGAATTTCCTACAGTGCCCTTGGTTAAA
TTAGGCAGTTCTTTTACGAAGGTTCAAGATTATCTAAGAAGATTTGAAAGTATACCAGAT
ATGCTTGAATTGGATCACCTCACAGTTTCAGGAGATGTGACATTTGGAAAAAATGTTTCA
TTAAAGGGAACGGTTATCATCATTGCAAATCATGGTGACAGAATTGATATCCCACCTGGA
GCAGTATTAGAGAACAAGATAGTGTCTGGAAACCTTCGCATCTTGGACCACTGA
Enzyme 22 GenBank Gene ID U27460 Link Image
Enzyme 22 GeneCard ID UGP2 Link Image
Enzyme 22 GenAtlas ID UGP2 Link Image
Enzyme 22 HGNC ID HGNC:12527 Link Image
Enzyme 22 Chromosome Location 2
Enzyme 22 Locus 2p14-p13
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Duggleby RG, Chao YC, Huang JG, Peng HL, Chang HY: Sequence differences between human muscle and liver cDNAs for UDPglucose pyrophosphorylase and kinetic properties of the recombinant enzymes expressed in Escherichia coli. Eur J Biochem. 1996 Jan 15;235(1-2):173-9. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 8075
Enzyme 23 Name Uridine-cytidine kinase 2
Enzyme 23 Synonyms
  1. UCK 2
  2. Uridine monophosphokinase 2
  3. Cytidine monophosphokinase 2
Enzyme 23 Gene Name UCK2
Enzyme 23 Protein Sequence >Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
Enzyme 23 Number of Residues 261
Enzyme 23 Molecular Weight 29299
Enzyme 23 Theoretical pI 6.68
Enzyme 23 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 23 General Function Nucleotide transport and metabolism
Enzyme 23 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 23 Pathways
Enzyme 23 Reactions
  • ATP + uridine = ADP + UMP
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 1655420 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q9BZX2 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name UCK2_HUMAN Link Image
Enzyme 23 PDB ID 1XRJ Link Image
Enzyme 23 PDB File Show
Enzyme 23 3D Structure
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >336 bp
ATGAAGCTTTTTGTGGATACAGATGCGGACACCCGGCTCTCACGCAGAGTATTAAGGGAC
ATCAGCGAGAGAGGCAGGGATCTTGAGCAGATTTTATCTCAGTACATTACGTTCGTCAAG
CCTGCCTTTGAGGAATTCTGCTTGCCAACAAAGCAGTATGCTGATGTGATCATCCCTAGA
GGTGCAGATAATCTGGTGGCCATCAACCTCATCGAGCAGCACATCCAGGACATCCTGAAT
GGAGGGCCCTCCAAACGGCAGACCAATGGCTGTCTCAACGGCTACACCCCTTCACGCAAG
AGGCAGGCATCGGAGTCCAGCAGCAGGCCGCATTGA
Enzyme 23 GenBank Gene ID D78335 Link Image
Enzyme 23 GeneCard ID UCK2 Link Image
Enzyme 23 GenAtlas ID UCK2 Link Image
Enzyme 23 HGNC ID HGNC:12562 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 1q23
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 8876
Enzyme 24 Name CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name CAD
Enzyme 24 Protein Sequence >CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase
MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNY
GIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVD
TRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILA
LDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVL
SEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVE
TDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEA
TAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAI
KALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQT
ALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQ
AQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEI
EYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLG
IVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRN
SVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKAL
RMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRM
KRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAV
KQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQ
QLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLP
NNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQT
VGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAV
ASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFN
LQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVG
VKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIG
SYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSI
LEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL
GQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMV
CAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLN
ETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEE
ILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVI
DCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIF
HLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVL
VPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASD
PGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHS
LVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSF
AAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRR
PVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVS
LRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEA
CFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLAT
VLGRF
Enzyme 24 Number of Residues 2225
Enzyme 24 Molecular Weight 242987
Enzyme 24 Theoretical pI 6.42
Enzyme 24 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • amine binding
  • amino acid binding
  • aspartate carbamoyltransferase activity
  • binding
  • carbamoyl-phosphate synthase activity
  • carboxyl- and carbamoyltransferase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • 'de novo' pyrimidine base biosynthesis
  • amino acid and derivative metabolism
  • amino acid metabolism
  • arginine biosynthesis
  • arginine metabolism
  • biosynthesis
  • cellular metabolism
  • glutamine family amino acid metabolism
  • glutamine metabolism
  • metabolism
  • nitrogen compound metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • pyrimidine base biosynthesis
  • pyrimidine base metabolism
  • urea cycle intermediate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 24 General Function Amino acid transport and metabolism
Enzyme 24 Specific Function This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase)
Enzyme 24 Pathways
Enzyme 24 Reactions
  • 2 ATP + L-glutamine + CO2 + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals Not Available
Enzyme 24 Transmembrane Regions Not Available
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 1228049 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P27708 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PYR1_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >6678 bp
ATGGCGGCCCTAGTGTTGGAGGACGGGTCGGTCCTGCGGGGCCAGCCCTTTGGGGCCGCC
GTGTCGACTGCCGGGGAAGTGGTGTTTCAAACCGGCATGGTCGGCTACCCCGAGGCCCTC
ACTGATCCCTCCTACAAGGCACAGATCTTAGTGCTCACCTATCCTCTGATCGGCAACTAT
GGCATCCCCCCAGATGAAATGGATGAGTTCGGTCTCTGCAAGTGGTTTGAATCCTCGGGC
ATCCACGTAGCAGCACTGGTAGTGGGAGAGTGCTGTCCTACTCCCAGCCACTGGAGTGCC
ACCCGCACCCTGCATGAGTGGCTGCAGCAGCATGGCATCCCTGGCTTGCAAGGAGTAGAC
ACTCGGGAGCTGACCAAGAAGTTGCGGGAACAGGGGTCTCTGCTGGGGAAGCTGGTCCAG
AATGGAACAGAACCTTCATCCCTGCCATTCTTGGACCCCAATGCCCGCCCCCTGGTACCA
GAGGTCTCCATTAAGACTCCACGGGTATTCAATACAGGGGGTGCCCCTCGGATCCTTGCT
TTGGACTGTGGCCTCAAGTATAATCAGATCCGATGCCTCTGCCAGCGTGGGGCTGAGGTC
ACTGTGGTACCCTGGGACCATGCACTAGACAGCCAAGAGTATGAGGGTCTCTTCTTAAGT
AATGGGCCTGGTGACCCTGCCTCCTATCCCAGTGTCGTATCCACACTGAGCCGTGTTTTA
TCTGAGCCTAATCCCCGACCTGTCTTTGGGATCTGCCTGGGACACCAGCTATTGGCCTTA
GCCATTGGGGCCAAGACTTACAAGATGAGATATGGGAACCGAGGCCATAACCAGCCCTGC
TTGTTGGTGGGCTCTGGGCGCTGCTTTCTGACATCCCAGAACCATGGGTTTGCTGTGGAG
ACAGACTCACTGCCAGCAGACTGGGCTCCTCTCTTCACCAACGCCAATGATGGTTCCAAT
GAAGGCATTGTGCACAACAGCTTGCCTTTCTTCAGTGTCCAGTTTCACCCAGAGCACCAA
GCTGGCCCTTCAGATATGGAACTGCTTTTCGATATCTTTCTGGAAACTGTGAAAGAGGCC
ACAGCTGGGAACCCTGGGGGCCAGACAGTTAGAGAGCGGCTGACTGAGCGCCTCTGTCCC
CCTGGGATTCCCACTCCCGGCTCTGGACTTCCACCACCACGAAAGGTTCTGATCCTGGGC
TCAGGGGGCCTCTCCATTGGCCAAGCTGGAGAATTTGACTACTCGGGCTCTCAGGCAATT
AAGGCCCTGAAGGAGGAAAACATCCAGACGTTGCTGATCAACCCCAATATTGCCACAGTG
CAGACCTCCCAGGGGCTGGCCGACAAGGTCTATTTTCTTCCCATAACACCTCATTATGTA
ACCCAGGTGATACGTAATGAACGCCCCGATGGTGTGTTACTGACTTTTGGGGGCCAGACT
GCTCTGAACTGTGGTGTGGAGCTGACCAAGGCCGGGGTGCTGGCTCGGTATGGGGTCCGG
GTCCTGGGCACAACAGTGGAGACCATTGAGCTGACCGAGGATCGACGGGCCTTTGCTGCC
AGAATGGCAGAGATCGGAGAGCATGTGGCCCCGAGCGAGGCAGGAAATTCTCTTGAACAG
GCCCAGGCAGCCGCTGAACGGCTGGGGTACCCTGTGCTAGTGCGTGCAGCCTTTGCCGTG
GGTGGCCTGGGCTCTGGCTTTGCCTCTAACAGGGAGGAGCTCTCTGCTCTCGTGGCCCCA
GCTTTTGCCCATACCAGCCAAGTGCTAGTAGACAAGTCTCTGAAGGGATGGAAGGAGATT
GAGTACGAGGTGGTGAGAGACGCCTATGGCAACTGTGTCACGGTGTGTAACATGGAGAAC
TTGGACCCACTGGGCATCCACACTGGTGAGTCCATAGTGGTGGCCCCTAGCCAGACACTG
AATGACAGGGAGTATCAGCTCCTGAGGCAGACAGCTATCAAGGTGACCCAGCACCTGGGA
ATTGTTGGGGAGTGCAATGTGCAGTATGCCTTGAACCCTGAGTCTGAGCAGTATTACATC
ATTGAAGTGAATGCCAGGCTCTCTCGCAGCTCTGCCCTGGCCAGTAAGGCCACAGGTTAT
CCACTGGCTTATGTGGCAGCCAAGCTAGCATTGGGCATCCCTTTGCCTGAGCTCAGGAAC
TCTGTGACAGGGGGTACAGCAGCCTTTGAACCCAGCGTGGATTATTGTGTGGTGAAGATT
CCTCGATGGGACCTTAGCAAGTTCCTGCGAGTCAGCACAAAGATTGGGAGCTGCATGAAG
AGCGTTGGTGAAGTCATGGGCATTGGGCGTTCATTTGAGGAGGCCTTCCAGAAGGCCCTG
CGCATGGTGGATGAGAACTGTGTGGGCTTTGATCACACAGTGAAACCAGTCAGCGATATG
GAGTTGGAGACTCCAACAGATAAGCGGATTTTTGTGGTGGCAGCTGCTTTGTGGGCTGGT
TATTCAGTGGACCGCCTGTATGAGCTCACACGCATCGACCGCTGGTTCCTGCACCGAATG
AAGCGTATCATCGCACATGCCCAGCTGCTAGAACAACACCGTGGACAGCCTTTGCCGCCA
GACCTGCTGCAACAGGCCAAGTGTCTTGGCTTCTCAGACAAACAGATTGCCCTTGCAGTT
CTGAGCACAGAGCTGGCTGTTCGCAAGCTGCGTCAGGAACTGGGGATCTGTCCAGCAGTG
AAACAGATTGACACAGTTGCAGCTGAGTGGCCAGCCCAGACAAATTACCTATACCTAACG
TATTGGGGCACCACCCATGACCTCACCTTTCGAACACCTCATGTCCTAGTCCTTGGCTCT
GGCGTCTACCGTATTGGCTCCAGTGTTGAGTTTGACTGGTGTGCTGTAGGCTGCATCCAG
CAGCTCCGAAAGATGGGATATAAGACCATCATGGTGAACTATAACCCAGAGACAGTCAGC
ACCGACTATGACATGTGTGATCGACTCTACTTTGATGAGATCTCTTTTGAGGTGGTGATG
GACATCTATGAGCTCGAGAACCCTGAAGGTGTGATCCTATCCATGGGTGGACAGCTGCCC
AACAACATGGCCATGGCGTTGCATCGGCAGCAGTGCCGGGTGCTGGGCACCTCCCCTGAA
GCCATTGACTCGGCTGAGAACCGTTTCAAGTTTTCCCGGCTCCTTGACACCATTGGTATC
AGCCAGCCTCAGTGGAGGGAGCTCAGTGACCTCGAGTCTGCTCGCCAATTCTGCCAGACC
GTGGGGTACCCCTGTGTGGTGCGCCCCTCCTATGTGCTGAGCGGTGCTGCTATGAATGTG
GCCTACGCGGATGGAGACCTGGAGCGCTTCCTGAGCAGCGCAGCAGCCGTCTCCAAAGAG
CATCCCGTGGTCATCTCCAAGTTCATCCAGGAGGCTAAGGAGATTGACGTGGATGCCGTG
GCCTCTGATGGTGTGGTGGCAGCCATCGCCATCTCTGAGCATGTGGAGAATGCAGGTGTG
CATTCAGGTGATGCGACGCTGGTGACCCCCCCACAAGATATCACTGCCAAAACCCTGGAG
CGGATCAAAGCCATTGTGCATGCTGTGGGCCAGGAGCTACAGGTCACAGGACCCTTCAAT
CTGCAGCTCATTGCCAAGGATGACCAGCTGAAAGTTATTGAATGCAACGTACGTGTCTCT
CGCTCCTTCCCCTTCGTTTCCAAGACACTGGGTGTGGACCTAGTAGCCTTGGCCACGCGG
GTCATCATGGGGGAAGAAGTGGAACCTGTGGGGCTAATGACTGGTTCTGGAGTCGTGGGA
GTAAAGGTGCCTCAGTTCTCCTTCTCCCGCTTGGCGGGTGCTGACGTGGTGTTGGGTGTG
GAAATGACCAGTACTGGGGAGGTGGCCGGCTTTGGGGAGAGCCGCTGTGAGGCATACCTC
AAGGCCATGCTAAGCACTGGCTTTAAGATCCCCAAGAAGAATATCCTGCTGACCATTGGC
AGCTATAAGAACAAAAGCGAGCTGCTCCCAACTGTGCGGCTACTGGAGAGCCTGGGCTAC
AGCCTCTATGCCAGTCTCGGCACAGCTGACTTCTACACTGAGCATGGCGTCAAGGTAACA
GCTGTGGACTGGCACTTTGAGGAGGCTGTGGATGGTGAGTGCCCACCACAGCGGAGCATC
CTGGAGCAGCTAGCTGAGAAAAACTTTGAGCTGGTGATTAACCTGTCAATGCGTGGAGCT
GGGGGCCGGCGTCTCTCCTCCTTTGTCACCAAGGGCTACCGCACCCGACGCTTGGCCGCT
GACTTCTCCGTGCCCCTAATCATCGATATCAAGTGCACCAAACTCTTTGTGGAGGCCCTA
GGCCAGATCGGGCCAGCCCCTCCTTTGAAGGTGCATGTTGACTGTATGACCTCCCAAAAG
CTTGTGCGACTGCCGGGATTGATTGATGTCCATGTGCACCTGCGGGAACCAGGTGGGACA
CATAAGGAGGACTTTGCTTCAGGCACAGCCGCTGCCCTGGCTGGGGGTATCACCATGGTG
TGTGCCATGCCTAATACCCGGCCCCCCATCATTGACGGCCCTGCTCTGGCCCTGGCCCAG
AAGCTGGCAGAGGCTGGCGCCCGGTGCGACTTTGCGCTATTCCTTGGGGCCTCGTCTGAA
AATGCAGGAACCTTGGGCACCGTGGCCGGGTCTGCAGCCGGGCTGAAGCTTTACCTCAAT
GAGACCTTCTCTGAGCTGCGGCTGGACAGCGTGGTCCAGTGGATGGAGCATTTCGAGACA
TGGCCCTCCCACCTCCCCATTGTGGCTCACGCAGAGCAGCAAACCGTGGCTGCTGTCCTC
ATGGTGGCTCAGCTCACTCAGCGCTCAGTGCACATATGTCACGTGGCACGGAAGGAGGAG
ATCCTGCTAATTAAAGCTGCAAAGGCACGGGGCTTGCCAGTGACCTGCGAGGTGGCTCCC
CACCACCTGTTCCTAAGCCATGATGACCTGGAGCGCCTGGGGCCTGGGAAGGGGGAGGTC
CGGCCTGAGCTTGGCTCCCGCCAGGATGTGGAAGCCCTGTGGGAGGACATGGCTGTCATC
GACTGCTTTGCCTCAGACCATGCTCCCCATACCTTGGAGGAGAAGTGTGGGTCCAGGCCC
CCACCTGGGTTCCCAGGGTTAGAGACCATGCTGCCACTACTCCTGACGGCTGTAAGCGAG
GGCCGGCTCAGCCTGGACGACCTGCTGCAGCGATTGCACCACAATCCTCGGCGCATCTTT
CACCTGCCCCCGCAGGAGGACACCTATGTGGAGGTGGATCTGGAGCATGAGTGGACAATT
CCCAGCCACATGCCCTTCTCCAAGGCCCACTGGACACCTTTTGAAGGGCAGAAAGTGAAG
GGCACCGTCCGCCGTGTGGTCCTGCGAGGGGAGGTTGCCTATATCGATGGGCAGGTTCTG
GTACCCCCGGGCTATGGACAGGATGTACGGAAGTGGCCACAGGGGGCTGTTCCTCAGCTC
CCACCCTCAGCCCCTGCCACTAGTGAGATGACCACGACACCTGAAAGACCCCGCCGTGGC
ATCCCAGGGCTTCCTGATGGCCGCTTCCATCTGCCGCCCCGAATCCATCGAGCCTCCGAC
CCAGGTTTGCCAGCTGAGGAGCCAAAGGAGAAGTCCTCTCGGAAGGTAGCCGAGCCAGAG
CTGATGGGAACCCCTGATGGCACCTGCTACCCTCCACCACCAGTACCGAGACAGGCATCT
CCCCAGAACCTGGGGACCCCTGGCTTGCTGCACCCCCAGACCTCACCCCTGCTGCACTCA
TTAGTGGGCCAACATATCCTGTCCGTCCAGCAGTTCACCAAGGATCAGATGTCTCACCTG
TTCAATGTGGCACACACACTGCGTATGATGGTGCAGAAGGAGCGGAGCCTCGACATCCTG
AAGGGGAAGGTCATGGCCTCCATGTTCTATGAAGTGAGCACACGGACCAGCAGCTCCTTT
GCAGCAGCCATGGCCCGGCTGGGAGGTGCTGTGCTCAGCTTCTCGGAAGCCACATCGTCC
GTCCAGAAGGGCGAATCCCTGGCTGACTCCGTGCAGACCATGAGCTGCTATGCCGACGTC
GTCGTGCTCCGGCACCCCCAGCCTGGAGCAGTGGAGCTGGCCGCCAAGCACTGCCGGAGG
CCAGTGATCAATGCTGGGGATGGGGTCGGAGAGCACCCCACCCAGGCCCTGCTGGACATC
TTCACCATCCGTGAGGAGCTGGGAACTGTCAATGGCATGACGATCACGATGGTGGGTGAC
CTGAAGCACGGACGCACAGTACATTCCCTGGCCTGCCTGCTCACCCAGTATCGTGTCAGC
CTGCGCTACGTGGCACCTCCCAGCCTGCGCATGCCACCCACTGTGCGGGCCTTCGTGGCC
TCCCGCGGCACCAAGCAGGAGGAATTCGAGAGCATTGAGGAGGCGCTGCCTGACACTGAT
GTGCTCTACATGACTCGAATCCAGAAGGAACGATTTGGCTCTACCCAGGAGTACGAAGCT
TGCTTTGGTCAGTTCATCCTCACTCCCCACATCATGACCCGGGCCAAGAAGAAGATGGTG
GTGATGCACCCGATGCCCCGTGTCAACGAGATAAGCGTGGAAGTGGACTCGGATCCCCGC
GCAGCCTACTTCCGCCAGGCTGAGAACGGCATGTACATCCGCATGGCTCTGTTAGCCACC
GTGCTGGGCCGTTTCTAG
Enzyme 24 GenBank Gene ID D78586 Link Image
Enzyme 24 GeneCard ID CAD Link Image
Enzyme 24 GenAtlas ID CAD Link Image
Enzyme 24 HGNC ID HGNC:1424 Link Image
Enzyme 24 Chromosome Location 2
Enzyme 24 Locus 2p22-p21
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Iwahana H, Fujimura M, Ii S, Kondo M, Moritani M, Takahashi Y, Yamaoka T, Yoshimoto K, Itakura M: Molecular cloning of a human cDNA encoding a trifunctional enzyme of carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase in de Novo pyrimidine synthesis. Biochem Biophys Res Commun. 1996 Feb 6;219(1):249-55. [PubMed Link Image]
  2. Davidson JN, Rao GN, Niswander L, Andreano C, Tamer C, Chen KC: Organization and nucleotide sequence of the 3' end of the human CAD gene. DNA Cell Biol. 1990 Nov;9(9):667-76. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 13093
Enzyme 25 Name Uncharacterized protein POLR3G
Enzyme 25 Synonyms
  1. Polymerase
  2. RNAIII
  3. DNA directedpolypeptide G
  4. 32kD, isoform CRA_a
Enzyme 25 Gene Name POLR3G
Enzyme 25 Protein Sequence >Uncharacterized protein POLR3G
MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLAL
KQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAG
PKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDD
DAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDEATY
Enzyme 25 Number of Residues 223
Enzyme 25 Molecular Weight 25915
Enzyme 25 Theoretical pI 4.26
Enzyme 25 GO Classification Not Available
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Not Available
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function Not Available
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein Not Available
Enzyme 25 UniProtKB/Swiss-Prot ID A8MTH0 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name A8MTH0_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 AC027323 Link Image
Enzyme 25 GeneCard ID A8MTH0 Link Image
Enzyme 25 GenAtlas ID POLR3G Link Image
Enzyme 25 HGNC ID HGNC:30075 Link Image
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References Not Available
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 13098
Enzyme 26 Name Uridine/cytidine kinase-like 1
Enzyme 26 Synonyms Not Available
Enzyme 26 Gene Name UCKL1
Enzyme 26 Protein Sequence >Uridine/cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
Enzyme 26 Number of Residues 548
Enzyme 26 Molecular Weight 61142
Enzyme 26 Theoretical pI 7.40
Enzyme 26 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 26 General Function Nucleotide transport and metabolism
Enzyme 26 Specific Function May contribute to UTP accumulation needed for blast transformation and proliferation
Enzyme 26 Pathways
Enzyme 26 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 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 38228699 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q9NWZ5 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name UCKL1_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence Not Available
Enzyme 26 GenBank Gene ID AJ605558 Link Image
Enzyme 26 GeneCard ID Q9NWZ5 Link Image
Enzyme 26 GenAtlas ID UCKL1 Link Image
Enzyme 26 HGNC ID HGNC:15938 Link Image
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 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 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 13379
Enzyme 27 Name Ectonucleoside triphosphate diphosphohydrolase 8
Enzyme 27 Synonyms
  1. NTPDase 8
  2. NTPDase8
  3. E-NTPDase 8
Enzyme 27 Gene Name ENTPD8
Enzyme 27 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
Enzyme 27 Number of Residues 495
Enzyme 27 Molecular Weight 53904
Enzyme 27 Theoretical pI 4.96
Enzyme 27 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolyzis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP
Enzyme 27 Pathways
Enzyme 27 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085] ALL_REAC R00085
  • (other) R00086 R00122 R00155 R00159 R00328 R00335 R00514 R00569 R00719 R00961 R02092 R02095
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • 9-29 472-492
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 59003409 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q5MY95 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name ENTP8_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1488 bp
ATGGGGCTGTCCCGGAAGGAGCAGGTCTTCTTGGCCCTGCTGGGGGCCTCGGGGGTCTCA
GGCCTCACGGCACTCATTCTCCTCCTGGTGGAGGCCACCAGCGTGCTCCTGCCCACAGAC
ATCAAGTTTGGGATCGTGTTTGATGCGGGCTCCTCCCACACGTCCCTCTTCCTGTATCAG
TGGCCGGCGAACAAGGAGAATGGCACGGGTGTGGTCAGCCAGGCCCTGGCCTGCCAGGTG
GAAGGGCCTGGAATCTCCTCCTACACTTCTAATGCTGCACAGGCTGGTGAGAGCCTGCAG
GGCTGCTTGGAGGAGGCGCTGGTGCTGATCCCAGAGGCCCAGCATCGGAAAACACCCACG
TTCCTGGGGGCCACGGCTGGCATGAGGTTGCTCAGCCGGAAGAACAGCTCTCAGGCCAGG
GACATCTTTGCAGCAGTCACCCAGGTCCTGGGCCGGTCTCCCGTGGACTTTTGGGGTGCC
GAGCTCCTGGCCGGGCAGGCCGAAGGTGCCTTTGGTTGGATCACTGTCAACTACGGCTTG
GGGACGCTGGTCAAGTACTCCTTCACTGGAGAATGGATCCAGCCTCCGGAGGAGATGCTG
GTGGGTGCCCTGGACATGGGAGGGGCCTCCACCCAGATCACGTTCGTGCCTGGGGGCCCC
ATCTTGGACAAGAGCACCCAGGCCGATTTTCGCCTCTACGGCTCCGACTACAGCGTCTAC
ACTCACAGCTACCTGTGCTTTGGACGGGACCAGATGCTGAGCAGGCTCCTCGTGGGGCTG
GTGCAGAGCCGCCCGGCTGCCCTGCTCCGTCACCCGTGCTACCTCAGCGGCTACCAGACC
ACACTGGCCCTGGGCCCGCTGTATGAGTCACCCTGTGTCCACGCCACGCCCCCGCTGAGC
CTCCCCCAGAACCTCACAGTTGAAGGGACAGGCAACCCTGGAGCCTGCGTCTCAGCCATC
CGGGAACTTTTCAACTTCTCCAGCTGCCAGGGCCAGGAGGACTGCGCCTTTGACGGGGTC
TACCAGCCCCCGCTGCGGGGCCAGTTCTATGCCTTCTCCAACTTCTACTACACCTTCCAC
TTCCTGAACCTCACCTCCAGGCAGCCCCTGAGCACGGTCAACGCCACCATCTGGGAGTTT
TGCCAGAGGCCCTGGAAACTGGTGGAGGCCAGCTACCCTGGGCAGGACCGCTGGCTGCGG
GACTACTGTGCCTCAGGCCTGTACATCCTCACCCTCCTGCACGAGGGCTACGGGTTCAGC
GAGGAGACCTGGCCCAGCCTCGAGTTCCGAAAGCAGGCGGGCGGTGTGGACATTGGCTGG
ACACTGGGCTACATGCTGAACCTGACCGGGATGATCCCGGCCGATGCGCCGGCTCAGTGG
CGGGCAGAGAGCTACGGCGTCTGGGTGGCCAAAGTGGTGTTCATGGTGCTGGCCCTGGTG
GCGGTGGTGGGGGCTGCCTTGGTCCAGCTCTTCTGGTTGCAGGACTAG
Enzyme 27 GenBank Gene ID AY903953 Link Image
Enzyme 27 GeneCard ID Q5MY95 Link Image
Enzyme 27 GenAtlas ID ENTPD8 Link Image
Enzyme 27 HGNC ID HGNC:24860 Link Image
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 15191
Enzyme 28 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 28 Synonyms Not Available
Enzyme 28 Gene Name NME7
Enzyme 28 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 28 Number of Residues 376
Enzyme 28 Molecular Weight 42492
Enzyme 28 Theoretical pI 6.44
Enzyme 28 GO Classification Not Available
Enzyme 28 General Function Nucleotide transport and metabolism
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 158254838 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID A8K3T6 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name A8K3T6_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 28 GenBank Gene ID AK290701 Link Image
Enzyme 28 GeneCard ID A8K3T6 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 SNPJam Report Link Image
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 15192
Enzyme 29 Name DNA-directed RNA polymerase III subunit RPC1
Enzyme 29 Synonyms
  1. RNA polymerase III subunit C1
  2. DNA-directed RNA polymerase III subunit A
  3. DNA-directed RNA polymerase III largest subunit
  4. RPC155
  5. C160
Enzyme 29 Gene Name POLR3A
Enzyme 29 Protein Sequence >DNA-directed RNA polymerase III subunit RPC1
MVKEQFRETDVAKKISHICFGMKSPEEMRQQAHIQVVSKNLYSQDNQHAPLLYGVLDHRM
GTSEKDRPCETCGKNLADCLGHYGYIDLELPCFHVGYFRAVIGILQMICKTCCHIMLSQE
EKKQFLDYLKRPGLTYLQKRGLKKKISDKCRKKNICHHCGAFNGTVKKCGLLKIIHEKYK
TNKKVVDPIVSNFLQSFETAIEHNKEVEPLLGRAQENLNPLVVLNLFKRIPAEDVPLLLM
NPEAGKPSDLILTRLLVPPLCIRPSVVSDLKSGTNEDDLTMKLTEIIFLNDVIKKHRISG
AKTQMIMEDWDFLQLQCALYINSELSGIPLNMAPKKWTRGFVQRLKGKQGRFRGNLSGKR
VDFSGRTVISPDPNLRIDEVAVPVHVAKILTFPEKVNKANINFLRKLVQNGPEVHPGANF
IQQRHTQMKRFLKYGNREKMAQELKYGDIVERHLIDGDVVLFNRQPSLHKLSIMAHLARV
KPHRTFRFNECVCTPYNADFDGDEMNLHLPQTEEAKAEALVLMGTKANLVTPRNGEPLIA
AIQDFLTGAYLLTLKDTFFDRAKACQIIASILVGKDEKIKVRLPPPTILKPVTLWTGKQI
FSVILRPSDDNPVRANLRTKGKQYCGKGEDLCANDSYVTIQNSELMSGSMDKGTLGSGSK
NNIFYILLRDWGQNEAADAMSRLARLAPVYLSNRGFSIGIGDVTPGQGLLKAKYELLNAG
YKKCDEYIEALNTGKLQQQPGCTAEETLEALILKELSVIRDHAGSACLRELDKSNSPLTM
ALCGSKGSFINISQMIACVGQQAISGSRVPDGFENRSLPHFEKHSKLPAAKGFVANSFYS
GLTPTEFFFHTMAGREGLVDTAVKTAETGYMQRRLVKSLEDLCSQYDLTVRSSTGDIIQF
IYGGDGLDPAAMEGKDEPLEFKRVLDNIKAVFPCPSEPALSKNELILTTESIMKKSEFLC
CQDSFLQEIKKFIKGVSEKIKKTRDKYGINDNGTTEPRVLYQLDRITPTQVEKFLETCRD
KYMRAQMEPGSAVGALCAQSIGEPGTQMTLKTFHFAGVASMNITLGVPRIKEIINASKAI
STPIITAQLDKDDDADYARLVKGRIEKTLLGEISEYIEEVFLPDDCFILVKLSLERIRLL
RLEVNAETVRYSICTSKLRVKPGDVAVHGEAVVCVTPRENSKSSMYYVLQFLKEDLPKVV
VQGIPEVSRAVIHIDEQSGKEKYKLLVEGDNLRAVMATHGVKGTRTTSNNTYEVEKTLGI
EAARTTIINEIQYTMVNHGMSIDRRHVMLLSDLMTYKGEVLGITRFGLAKMKESVLMLAS
FEKTADHLFDAAYFGQKDSVCGVSECIIMGIPMNIGTGLFKLLHKADRDPNPPKRPLIFD
TNEFHIPLVT
Enzyme 29 Number of Residues 1390
Enzyme 29 Molecular Weight 155644
Enzyme 29 Theoretical pI 8.62
Enzyme 29 GO Classification
Function
  • DNA binding
  • DNA-directed RNA 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
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 29 General Function Transcription
Enzyme 29 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition
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 2460208 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID O14802 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name RPC1_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >4176 bp
ATGGTGAAGGAGCAGTTCCGGGAGACGGATGTGGCCAAGAAAACAAGCCACATCTGTTTT
GGAATGAAGTCACCTGAGGAGATGCGCCAGCAGGCGCACATCCAAGTTGTGAGTAAGAAC
CTGTACAGCCAGGACAACCAACATGCCCCCTTGCTATATGGGGTGCTCGACCATAGGATG
GGTACGAGTGAGAAGGATCGTCCATGTGAAACCTGTGGGAAAAACTTGGCTGACTGTCTA
GGCCACTATGGGTATATCGACCTGGAGTTGCCGTGTTTTCATGTAGGGTACTTCAGAGCA
GTCATAGGCATCTTACAGATGATCTGCAAAACCTGCTGCCACATCATGCTGTCCCAAGAG
GAGAAGAAGCAGTTTCTGGACTATCTAAAGAGGCCCGGCCTGACCTACCTTCAGAAGCGA
GGACTGAAAAAGAAAATCTCTGACAAGTGCCGGAAGAAAAACATCTGCCATCACTGTGGC
GCTTTTAATGGTACCGTAAAGAAGTGTGGACTGCTGAAAATAATTCATGAGAAATACAAG
ACCAACAAAAAAGTGGTGGATCCCATTGTATCAAATTTCCTTCAGTCTTTTGAAACAGCC
ATTGAACATAATAAAGAAGTGGAGCCTCTGCTGGGAAGGGCACAGGAAAACTTGAATCCC
TTAGTAGTTCTGAATTTATTTAAACGAATCCCAGCTGAAGATGTTCCTCTACTTCTGATG
AACCCAGAAGCCGGAAAGCCGTCTGATTTGATTCTCACACGACTTTTGGTGCCTCCTTTG
TGTTTCAGACCCTCCGTTGTGAGTGATTTGAAGTCTGGCACCAATGAAGATGATCTGACA
ATGAAACTGACAGAAATCATTTTCCTAAACGATGTTATTAAAAAGCATCGGATCTCAGGA
GCCAAGACCCAGATGATCATGGAGGACTGGGATTTCCTGCAGCTGCAGTGTGCCCTCTAC
ATTAACAGTGAGCTCTCGGGCATTCCCCTCAACATGGCACCCAAGAAGTGGACCAGAGGC
TTCGTCCAACGCCTGAAGGGAAAACAGGGTCGATTTAGAGGAAATCTCTCAGGAAAGAGA
GTGGATTTTTCTGGCAGAACAGTCATCTCGCCCGACCCCAACCTCCGGATTGATGAGGTA
GCTGTGCCAGTTCATGTGGCCAAAATTCTAACTTTTCCTGAGAAGGTAAACAAAGCAAAC
ATCAATTTCTTGAGGAAACTGGTTCAAAACGGCCCTGAGGTTCACCCAGGAGCAAACTTC
ATTCAGCAGAGACATACGCAGATGAAAAGGTTTTTGAAATACGGAAATCGAGAAAAGATG
GCTCAAGAGCTCAAGTATGGTGACATCGTAGAGAGACACCTCATCGATGGAGATGTGGTG
CTGTTCAATCGGCAGCCCTCGCTGCACAAATTGAGCATTATGGCTCATCTGGCCAGGGTC
AAGCCCCACCGGACCTTCAGATTTAATGAGTGTGTCTGTACACCCTATAATGCTGACTTT
GATGGTGATGAAATGAACCTTCATCTTCCTCAAACAGAAGAAGCTAAAGCAGAGGCCCTT
GTTCTGATGGGGACTAAAGCAAATCTTGTAACCCCGAGGAATGGGGAACCGCTGATTGCT
GCTATTCAGGATTTTCTAACAGGTGCCTATCTCCTCACTCTCAAGGACACTTTCTTTGAT
CGAGCCAAGGCTTGCCAAATCATTGCTTCAATACTGGTTGGCAAGGATGAGAAAATTAAA
GTTCGCCTCCCACCGCCTACAATCCTAAAGCCTGTCACCCTGTGGACGGGAAAGCAGATC
TTCAGTGTCATCCTCAGGCCTAGCGATGACAATCCAGTGAGGGCCAACCTGCGAACCAAG
GGCAAGCAGTACTGTGGCAAAGGGGAAGATCTCTGTGCCAATGATTCCTATGTTACAATC
CAGAACAGTGAGTTGATGAGTGGCAGCATGGACAAAGGAACCCTAGGGTCAGGATCCAAG
AACAATATTTTTTACATTTTGCTGCGAGACTGGGGACAGAATGAAGCTGCAGATGCCATG
TCACGGCTCGCCAGGCTGGCTCCTGTCTACCTGTCTAACCGTGGTTTCTCAATTGGGATC
GGTGATGTCACACCTGGCCAAGGACTGCTGAAGGCCAAGTATGAGTTGCTGAATGCCGGC
TACAAGAAATGTGATGAGTACATCGAAGCCCTGAACACGGGCAAGCTGCAGCAGCAGCCT
GGCTGCACTGCTGAGGAGACCCTGGAGGCACTGATCCTGAAGGAGCTGTCTGTGATCCGT
GACCACGCTGGCAGTGCCTGCCTCCGGGAGCTGGACAAGAGCAACAGCCCCCTCACCATG
GCTCTGTGCGGCTCCAAAGGTTCCTTCATTAACATATCACAGATGATTGCCTGTGTGGGA
CAGCAGGCCATCAGTGGCTCTCGAGTGCCAGACGGCTTTGAAAACAGGTCCTTGCCTCAT
TTTGAAAAACACTCAAAGCTCCCAGCTGCCAAAGGCTTTGTGGCTAATAGCTTTTATTCC
GGTTTGACACCAACTGAGTTTTTCTTCCACACAATGGCCGGCCGGGAAGGTCTAGTCGAC
ACGGCTGTAAAGACAGCTGAAACGGGATACATGCAGCGAAGGCTTGTCAAATCTCTTGAA
GATCTTTGCTCCCAGTATGATCTGACAGTCCGAAGCTCTACTGGCGATATTATCCAGTTC
ATTTATGGAGGAGATGGCTTAGATCCTGCAGCTATGGAGGGAAAAGATGAACCTTTGGAG
TTTAAAAGGGTTCTGGACAACATCAAAGCAGTCTTCCCGTGTCCCAGTGAGCCTGCTCTC
AGCAAAAACGAGCTGATCCTGACCACAGAGTCCATCATGAAGAAGAGTGAGTTCCTCTGC
TGCCAGGACAGCTTCCTGCAGGAAATAAAAAAATTCATTAAGGGGGTCTCTGAGAAGATC
AAGAAAACCAGAGATAAATATGGCATCAATGATAACGGCACAACAGAGCCCCGTGTGCTG
TACCAGCTGGACCGCATCACCCCCACCCAAGTAGAAAAGTTTCTGGAGACCTGTAGGGAC
AAGTACATGAGGGCACAGATGGAGCCAGGTTCTGCAGTGGGTGCTCTGTGTGCCCAGAGC
ATTGGTGAGCCAGGCACCCAGATGACCCTGAAGACTTTCCACTTTGGAGGTGTGGCCTCC
ATGAACATCACCCTGGGCGTGCCCCGGATTAAAGAGATCATCAACGCTTCCAAGGCCATC
AGCACTCCAATTATCACAGCACAGCTAGACAAGGATGACGACGCGGATTATGCTCGCCTC
GTGAAAGGGAGAATTGAGAAAACCCTCTTGGGAGAGATTTCCGAGTATATTGAAGAAGTG
TTTCTTCCTGATGACTGCTTTATTCTCGTCAAGCTCTCCCTGGAACGGATTAGGCTTCTG
AGACTGGAAGTGAACGCTGAGACAGTGAGATATTCCATCTGCACATCCAAGCTCCGTGTG
AAGCCCGGTGATGTGGCTGTTCATGGTGAGGCTGTGGTGTGTGTCACCCCCAGAGAGAAC
AGCAAGAGCTCCATGTACTACGTGCTGCAGTTCCTGAAAGAGGATCTCCCCAAGGTGGTG
GTGCAGGGCATTCCAGAGGTGTCCAGAGCTGTCATCCACATTGACGAGCAGAGTGGAAAG
GAGAAGTACAAGCTTCTGGTGGAAGGTGATAACCTGCGGGCAGTCATGGCCACACACGGT
GTGAAGGGCACCCGAACCACCTCCAATAACACCTATGAGGTGGAGAAAACTCTGGGCATC
GAGGCCGCCCGGACAACGATCATCAATGAAATCCAGTACACCATGGTGGTGAACCACGGC
ATGAGCATCGACAGGAGGCACGTGATGCTGCTCTCCGACCTCATGACCTACAAGGGTGAA
GTCCTGGGCATCACTAGGTTTGGCCTGGCCAAGATGAAGGAGAGTGTGCTGATGCTGGCC
TCCTTTGAGAAGACGGCTGACCATCTCTTTGACGCTGCCTACTTCGGGCAGAAGGACTCT
GTGTGTGGGGTGTCTGAGTGCATCATCATGGGAATCCCAATGAACATTGGAACCGGGCTC
TTCAAGCTGCTTCACAAGGCTGACAGGGACCCGAACCCTCCCAAGAGGCCCCTGATCTTC
GACACAAATGAATTCCACATCCCCCTTGTCACATAG
Enzyme 29 GenBank Gene ID AF021351 Link Image
Enzyme 29 GeneCard ID O14802 Link Image
Enzyme 29 GenAtlas ID POLR3A Link Image
Enzyme 29 HGNC ID HGNC:30074 Link Image
Enzyme 29 Chromosome Location 10
Enzyme 29 Locus 10q22-q23
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Sepehri S, Hernandez N: The largest subunit of human RNA polymerase III is closely related to the largest subunit of yeast and trypanosome RNA polymerase III. Genome Res. 1997 Oct;7(10):1006-19. [PubMed Link Image]
  2. Kuwana M, Kimura K, Kawakami Y: Identification of an immunodominant epitope on RNA polymerase III recognized by systemic sclerosis sera: application to enzyme-linked immunosorbent assay. Arthritis Rheum. 2002 Oct;46(10):2742-7. [PubMed Link Image]
  3. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 15193
Enzyme 30 Name DNA-directed RNA polymerase I subunit RPA1
Enzyme 30 Synonyms
  1. RNA polymerase I subunit A1
  2. DNA-directed RNA polymerase I subunit A
  3. DNA-directed RNA polymerase I largest subunit
  4. RNA polymerase I 194 kDa subunit
  5. RPA194
  6. A190
Enzyme 30 Gene Name POLR1A
Enzyme 30 Protein Sequence >DNA-directed RNA polymerase I subunit RPA1
MLISKNMPWRRLQGISFGMYSAEELKKLSVKSITNPRYLDSLGNPSANGLYDLALGPADS
KEVCSTCVQDFSNCSGHLGHIELPLTVYNPLLFDKLYLLLRGSCLNCHMLTCPRAVIHLL
LCQLRVLEVGALQAVYELERILNRFLEENPDPSASEIREELEQYTTEIVQNNLLGSQGAH
VKNVCESKSKLIALFWKAHMNAKRCPHCKTGRSVVRKEHNSKLTITFPAMVHRTAGQKDS
EPLGIEEAQIGKRGYLTPTSAREHLSALWKNEGFFLNYLFSGMDDDGMESRFNPSVFFLD
FLVVPPSRYRPVSRLGDQMFTNGQTVNLQAVMKDVVLIRKLLALMAQEQKLPEEVATPTT
DEEKDSLIAIDRSFLSTLPGQSLIDKLYNIWIRLQSHVNIVFDSEMDKLMMDKYPGIRQI
LEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQEL
RQAVINGPNVHPGASMVINEDGSRTALSAVDMTQREAVAKQLLTPATGAPKPQGTKIVCR
HVKNGDILLLNRQPTLHRPSIQAHRARILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQ
SELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGASMTTRGCFFTREHYMELVYRG
LTDKVGRVKLLSPSILKPFPLWTGKQVVSTLLINIIPEDHIPLNLSGKAKITGKAWVKET
PRSVPGFNPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGKVLTC
LARLFTAYLQLYRGFTLGVEDILVKPKADVKRQRIIEESTHCGPQAVRAALNLPEAASYD
EVRGKWQDAHLGKDQRDFNMIDLKFKEEVNHYSNEINKACMPFGLHRQFPENSLQMMVQS
GAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIK
PPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVVQYDLTVRDSDGSVVQFLYG
EDGLDIPKTQFLQPKQFPFLASNYEVIMKSQHLHEVLSRADPKKALHHFRAIKKWQSKHP
NTLLRRGAFLSYSQKIQEAVKALKLESENRNGRSPGTQEMLRMWYELDEESRRKYQKKAA
ACPDPSLSVWRPDIYFASVSETFETKVDDYSQEWAAQTEKSYEKSELSLDRLRTLLQLKW
QRSLCEPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIK
TPMMSVPVLNTKKALKRVKSLKKQLTRVCLGEVLQKIDVQESFCMEEKQNKFQVYQLRFQ
FLPHAYYQQEKCLRPEDILRFMETRFFKLLMESIKKKNNKASAFRNVNTRRATQRDLDNA
GELGRSRGEQEGDEEEEGHIVDAEAEEGDADASDAKRKEKQEEEVDYESEEEEEREGEEN
DDEDMQEERNPHREGARKTQEQDEEVGLGTEEDPSLPALLTQPRKPTHSQEPQGPEAMER
RVQAVREIHPFIDDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHGAVIYATKGIT
RCLLNETTNNKNEKELVLNTEGINLPELFKYAEVLDLRRLYSNDIHAIANTYGIEAALRV
IEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIRSNSSPLQQMTFETSFQF
LKQATMLGSHDELRSPSACLVVGKVVRGGTGLFELKQPLR
Enzyme 30 Number of Residues 1720
Enzyme 30 Molecular Weight 194814
Enzyme 30 Theoretical pI 7.03
Enzyme 30 GO Classification
Function
  • DNA binding
  • DNA-directed RNA 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
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 30 General Function Transcription
Enzyme 30 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition
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 4096591 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID O95602 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name RPA1_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >5154 bp
ATGTTGATCTCCAAGAACATGCCCTGGCGGCGGCTGCAGGGCATTTCCTTCGGGATGTAT
TCGGCTGAAGAGCTCAAGAAATTAAGTGTTAAATCCATTACGAACCCTCGATACCTGGAC
AGCCTGGGGAACCCATCGGCAAACGGCCTGTACGATTTAGCTTTGGGCCCTGCAGATTCC
AAAGAGGTGTGCTCCACCTGCGTGCAGGACTTCAGCAACTGTTCTGGGCACCTGGGCCAC
ATTGAGCTCCCACTCACAGTGTATAACCCTCTCCTCTTCGATAAGCTGTACCTGCTGCTT
CGGGGCTCTTGTTTAAACTGCCACATGCTGACTTGTCCCCGGGCCGTGATTCACCTCTTA
CTCTGCCAGCTGAGGGTTCTGGAAGTCGGGGCCCTACAAGCAGTCTACGAGCTTGAGAGA
ATTCTGAGCAGGTTTCTGGAAGAAAATGCCGATCCCTCTGCCTCTGAAATTCGGGAGGAA
TTAGAACAATACACAACTGAAATTGTGCAGAACAACCTCCTGGGGTCCCAGGGCGCACAT
GTAAAGAACGTGTGTGAGAGCAAGAGCAAGCTCATTGCTCTCTTCTGGAAGGCACATATG
AATGCTAAGCGCTGTCCCCACTGCAAGACCGGGCGATCCGTTGTCCGAAAGGAACACAAC
AGCAAGTTGACTATCACATTTCCAGCCATGGTGCACAGGACAGCTGGCCAGAAGGACTCT
GAGCCCCTGGGAATTGAGGAAGCTCAGATAGGAAAACGAGGATACTTAACACCCACCAGT
GCCCGCGAACACCTTTCTGCCCTGTGGAAGAATGAAGGATTCTTTCTGAACTACCTTTTT
TCGGGAATGGATGATGATGGTATGGAATCCAGATTCAATCCCAGTGTGTTCTTTCTAGAT
TTCTTGGTGGTGCCGCCCTCAAGGTCTCGCCCAGTCAGTCGCCTAGGAGACCAGATGTTT
ACTAATGGCCAGACGGTGAACTTGCAGGCTGTCATGAAGGATGTAGTTCTGATTCGAAAA
CTTCTGGCATTGATGGCCCAAGAACAGAAGTTGCCAGAGGAAGTGGCCACACCCACTACA
GATGAGGAAAAAGACTCTTTGATTGCTATTGACCGATCCTTTTTGAGTACACTTCCAGGC
CAGTCCCTCATAGACAAACTTTACAACATTTGGATTCGCCTTCAGAGCCACGTCAATATT
GTGTTTGATAGCGAGATGGACAAACTAATGAGGGACAAGTACCCAGGCATTAGGCAGATC
CTGGAGAAGAAAGAAGGCCTGTTCCGAAAACACATGATGGGAAAGCGAGTGGACTCGACT
GCGCGCTCAGTCATCTGCCCAGACATGTACATCAACACCAACGAAATTGGAATTCCCATG
GTGTTTGCCACAAAACTGACCTACCCACAGCCAGTTACCCCATGGAATGTTCAGGAACTT
AGGCAAGCGGTCATCAACGGCCCTAATGTGCACCCAGGAGCCTCCATGGTCATCAATGAG
GACGGCAGCCGCACAGCCCTGAGCGCTGTGGACATGACCCAGCGAGAGGCCGTGGCCAAG
CAGCTTCTGACCCCAGCCACGGGGGCACCTAAGCCCCAGGGGACAAAAATTGTGTGCCGG
CATGTGAAGAATGGGGACATTCTGCTACTGAACCGACAGCCCACACTGCACAGACCCTCC
ATCCAGGCCCACCGTGCCCGCATCCTGCCTGAAGAGAAAGTGCTGCGGCTCCACTATGCC
AACTGCAAGGCCTATAATGCCGACTTTGATGGAGACGAGATGAATGCCCATTTCCCCCAG
AGTGAGCTGGGCCGGGCCGAGGCCTACGTCCTGGCCTGCACTGATCAGCAGTACCTTGTT
CCCAAGGATGGCCAACCATTGGCGGGACTGATCCAGGATCACATGGTTTCAGGGGCAAGC
ATGACTACTCGGGGTTGCTTTTTCACCCGGGAGCACTATATGGAGCTGGTGTACCGAGGA
CTCACGGACAAAGTGGGGCGCGTGAAGCTCCTTTCTCCTTCCATCCTGAAGCCCTTTCCG
CTGTGGACAGGAAAACAGGTTGTGTCAACGCTGCTCATAAATATAATCCCAGAGGACCAC
ATCCCACTGAACTTATCTGGAAAGGCGAAAATCACTGGGAAAGCCTGGGTGAAGGAAACT
CCTCGATCCGTTCCTGGCTTTAACCCTGACTCGATGTGCGAGTCCCAGGTGATCATCAGG
GAAGGGGAGCTGCTCTGCGGAGTGCTGGACAAGGCGCACTATGGGAGCTCCGCCTACGGC
CTGGTCCACTGCTGCTATGAGATCTATGGAGGCGAGACCAGCGGCAAGGTTCTAACCTGC
CTGGCCCGCCTCTTCACCGCCTACCTGCAGCTCTACAGAGGCTTCACCTTGGGCGTGGAA
GACATTTTGGTGAAGCCAAAGCGAGATGTCAAGAGGCAACGTATCATTGAAGAATCCACC
CACTGCGGGCCCCAGGCTGTCAGGGCTGCATTAAACCTGCCAGAAGCCGCATCATATGAT
GAGGTCCGAGGAAAATGGCAGGATGCCCATCTGGGCAAGGACCAGAGGGATTTTAACATG
ATTGATCTGAAGTTCAAGGAGGAAGTGAACCATTACAGCAATGAGATTAACAAGGCATGC
ATGCCTTTTGGCCTACACAGACAGTTCCCAGAGAACACGCTGCAGCTGATGGTGCAGTCG
GGAGCCAAAGGTTCAACTGTGAACACGATGCAGATCTCGTGCCTGCTGGGCCAGATTGAA
CTGGAAGGTCGGAGCACCCCGCTGATGGCGTCTGGCAAGTCACTGCCCTGCTTTGAGCCT
TATGAGTTCACCCCCAGGGCTGGTGGCTTTGTCACTGGCAGGTTCCTCACCGGCATCAAA
CCTCCTGAGTTCTTCTTCCACTGCATGGCAGGACGAGAGGGCCTGGTGGACACTGCTGTG
AAAACCAGCCGCTCAGGCTATCTCCAAAGGTGCATCATCAAGCACCTAGAGGGGCTGGTC
GTGCAGTATGATCTCACGGTCCGTGACAGTGACGGCAGTGTGGTGCAGTTCCTGTATGGG
GAGGATGGCCTGGACATCCCCAAGACACAGTTCCTGCAGCCCAAGCAGTTCCCCTTCCTG
GCCAGCAACTACGAGGTGATAATGAAATCACAGCATCTCCATGAAGTTTTATCCAGAGCA
GATCCCAAAAAAGCTCTCCACCACTTCAGAGCTATCAAAAAATGGCAAAGCAAGCACCCC
AACACCCTGCTGAGAAGAGGCGCCTTCTTGAGTTATTCCCAGAAAATTCAGGAAGCTGTG
AAAGCCCTGAAACTTGAGAGTGAAAACCGCAATGGCCGCAGACCCTGGGACTCAGGGAGG
ATGCTGAGGATGTGGTATGAGTTGGATGAGGAAAGCCGAAGGAAATACCAGAAGAAGGCG
GCCGCTTGTCCTGACCCCAGTCTGTCTGTCTGGCGTCCTGACATCTACTTTGCATCAGTG
TCAGAAACATTTGAAACAAAGGTTGATGACTACAGTCAAGAGTGGGCAGCTCAAACAGAG
AAGAGTTATGAGAAATCAGAGCTTTCTCTCGACAGGTTGAGGACCTTGCTGCAGCTGAAG
TGGCAGCGCTCACTGTGTGAGCCGGGCGAGGCTGTGGGCCTGCTGGCTGCCCAGAGCATC
GGAGAGCCCTCCACCCAGATGACCCTCAACACCTTCCACTTTGCAGGCAGAGGCGAGATG
AACGTCACCCTGGGCATTCCAAGGTTGCGGGAGATTCTCATGGTGGCCAGCGCCAACATC
AAGACACCCATGATGAGCGTGCCCGTGCTCAACACCAAGAAAGCCCTGAAGAGAGTGAAA
AGCCTGAAGAAGCAACTCACCAGGGTGTGCTTGGGGGAGGTGTTGCAGAAAATTGACGTC
CAGGAGTCCTTCTGTATGGAAGAAAAACAGAACAAATTCCAGGTGTACCAGCTGCGGTTT
CAGTTCCTGCCACATGCATATTACCAGCAGGAGAAGTGCCTGAGACCCGAGGACATCCTG
CGCTTCATGGAAACAAGATTCTTTAAACTTCTGATGGAATCCATCAAAAAGAAGAATAAT
AAAGCATCAGCTTTCAGGAACGTAAACACTCGAAGAGCTACACAGCGGGATCTGGACAAC
GCTGGGGAGTTGGGGAGGAGTCGGGGAGAGCAGGAGGGTGATGAGGAAGAGGAGGGGCAC
ATTGTGGATGCTGAAGCTGAGGAGGGAGACGCCGATGCCTCTGATGCCAAACGCAAGGAG
AAGCAGGAGGAGGAGGTTGATTATGAGAGTGAGGAAGAGGAGGAGAGGGAGGGCGAGGAG
AACGACGATGAAGACATGCAGGAGGAACGAAATCCCCACAGGGAAGGTGCTCGAAAGACC
CAAGAGCAAGATGAAGAGGTGGGCTTAGGAGGACCCGTCCCTTCCCACCCTCCTGACGCA
GCCCCGGAAACCCACCCACAGCCAGGAGCCCCAGGGGCCGAGGCCATGGAGCGCCGGGTC
CAGGCTGTGCGTGAGATCCACCCGTTCATAGATGACTACCAGTACGACACCGAGGAGAGC
CTGTGGTGCCAGGTGACAGTGAAGCTCCCTCTGATGAAGATCAACTTTGACATGAGCTCC
CTGGTAGTATCTTTGGCCCATGGTGCCGTCATCTATGCGACCAAGGGCATCACTCGGTGC
CTCCTGAATGAAACAACCAACAATAAGAACGAGAAGGAGCTTGTGCTAAACACAGAAGGA
ATCAACCTCCCAGAGCTATTCAAGTATGCAGAGGTCCTGGATCTGCGCCGCCTCTACTCC
AACGACATCCACGCCATAGCCAACACGTATGGCATTGAGGCGCTGCGGGTGATCGAGAAG
GAGATCAAGGATGTGTTTGCCGTGTATGGCATCGCGGTCGACCCTCGCCATCTCTCCCTG
GTTGCTGATTATATGTGCTTCGAGGGTGTTTACAAGCCACTGAATCGCTTTGGGATCCGG
TCAAACTCTTCCCCGCTACAGCAGATGACATTTGAAACCAGCTTCCAGTTTCTGAAGCAA
GCCACCATGCTGGGATCCCACGATGAGCTGAGGTCTCCTTCTGCCTGCCTTGTGGTCGGG
AAAGTCGTCAGGGGCGGGACAGGCCTGTTCGAGCTCAAGCAGCCTCTGAGATAG
Enzyme 30 GenBank Gene ID U33460 Link Image
Enzyme 30 GeneCard ID O95602 Link Image
Enzyme 30 GenAtlas ID POLR1A Link Image
Enzyme 30 HGNC ID HGNC:17264 Link Image
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References Not Available
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 15194
Enzyme 31 Name DNA-directed RNA polymerase subunit
Enzyme 31 Synonyms Not Available
Enzyme 31 Gene Name ZNRD1
Enzyme 31 Protein Sequence >DNA-directed RNA polymerase subunit
MSVMDLANTCSSFQSDLDFCSDCGSVLPLPGAQDTVTCIRCGFNINVRDFEGKVVKTSVV
FHQLGTAMPMSVEEGPECQGPVVDRRCPRCGHEGMAYHTRQMRSADEGQTVFYTCTNCKF
QEKEDS
Enzyme 31 Number of Residues 126
Enzyme 31 Molecular Weight 13904
Enzyme 31 Theoretical pI 4.68
Enzyme 31 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transcription factor activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • RNA elongation
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • transcription
  • transcription, DNA-dependent
Component
Enzyme 31 General Function Transcription
Enzyme 31 Specific Function Not Available
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 86197925 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q2L6J2 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name Q2L6J2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >381 bp
ATGTCTGTCATGGACCTCGCCAATACTTGCTCCAGCTTTCAGTCGGACCTGGATTTCTGT
TCAGATTGCGGCTCGGTCCTGCCTCTGCCCGGGGCTCAGGATACGGTCACCTGTATTCGC
TGTGGCTTCAACATCAACGTTCGGGACTTTGAGGGGAAGGTTGTGAAGACTTCGGTTGTG
TTCCACCAACTGGGGACAGCCATGCCTATGTCGGTGGAGGAAGGGCCTGAGTGCCAGGGA
CCTGTGGTTGACAGGCGCTGCCCTCGATGTGGTCATGAAGGAATGGCATACCACACCAGA
CAGATGCGTTCAGCCGATGAAGGGCAAACTGTCTTCTACACCTGTACCAACTGCAAGTTC
CAGGAGAAGGAAGACTCTTGA
Enzyme 31 GenBank Gene ID AB202082 Link Image
Enzyme 31 GeneCard ID Q2L6J2 Link Image
Enzyme 31 GenAtlas ID ZNRD1 Link Image
Enzyme 31 HGNC ID HGNC:13182 Link Image
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 15195
Enzyme 32 Name DNA-directed RNA polymerases I and III subunit RPAC2
Enzyme 32 Synonyms
  1. RNA polymerases I and III subunit AC2
  2. DNA-directed RNA polymerase I subunit D
  3. DNA-directed RNA polymerase I 16 kDa polypeptide
  4. RPA16
  5. RPC16
  6. hRPA19
  7. AC19
Enzyme 32 Gene Name POLR1D
Enzyme 32 Protein Sequence >DNA-directed RNA polymerases I and III subunit RPAC2
MEEDQELERKISGLKTSMAEGERKTALEMVQAAGTDRHCVTFVLHEEDHTLGNSLRYMIM
KNPEVEFCGYTTTHPSESKINLRIQTRGTLPAVEPFQRGLNELMNVCQHVLDKFEASIKD
YKDQKASRNESTF
Enzyme 32 Number of Residues 133
Enzyme 32 Molecular Weight 15237
Enzyme 32 Theoretical pI 5.62
Enzyme 32 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • protein binding
  • protein dimerization 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 32 General Function Transcription
Enzyme 32 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively
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 4689136 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q9Y2S0 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name RPAC2_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >402 bp
ATGGAAGAGGATCAGGAGCTGGAGAGAAAAATATCTGGATTGAAGACCTCAATGGCTGAA
GGCGAGAGGAAGACAGCCCTGGAAATGGTCCAGGCAGCTGGAACAGATAGACACTGTGTG
ACATTTGTATTGCACGAGGAAGACCATACCCTAGGAAATTCTCTACGTTACATGATCATG
AAGAACCCGGAAGTGGAATTTTGTGGTTACACTACGACCCATCCTTCAGAGAGCAAAATT
AATTTACGCATTCAGACTCGAGGTACCCTTCCAGCTGTTGAGCCATTTCAGAGAGGCCTG
AATGAGCTCATGAATGTCTGCCAACATGTGCTTGACAAGTTTGAGGCCAGCATAAAGGAC
TATAAGGATCAAAAAGCAAGCAGAAATGAATCCACATTCTAG
Enzyme 32 GenBank Gene ID AF077044 Link Image
Enzyme 32 GeneCard ID Q9Y2S0 Link Image
Enzyme 32 GenAtlas ID POLR1D Link Image
Enzyme 32 HGNC ID HGNC:20422 Link Image
Enzyme 32 Chromosome Location 13
Enzyme 32 Locus 13q12.2
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 15196
Enzyme 33 Name cDNA FLJ75210, highly similar to H.sapiens RNA polymerase II 140 kDa subunit (Polymerase (RNA) II (DNA directed) polypeptide B, 140kDa)
Enzyme 33 Synonyms Not Available
Enzyme 33 Gene Name POLR2B
Enzyme 33 Protein Sequence >cDNA FLJ75210, highly similar to H.sapiens RNA polymerase II 140 kDa subunit (Polymerase (RNA) II (DNA directed) polypeptide B, 140kDa)
MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVE
DAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTY
SAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLD
PGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSML
ARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEM
VKPSLDEAFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEMLPHVGVSDFCETK
KAYFLGYMVHRLLLAALGRRELDDRDHYGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQ
KFIDRGKDFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLS
HLRRLNSPIGRDGKLAKPRQLHNTLWGMVCPAETPEGHAVGLVKNLALMAYISVGSQPSP
ILEFLEEWSMENLEEISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQMDIIVSE
VSMIRDIREREIRIYTDAGRICRPLLIVEKQKLLLKKRHIDQLKEREYNNYSWQDLVASG
VVEYIDTLEEETVMLAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFPDHNQSP
RNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPQKPLVTTRSMEYLRFRELPAGINSIV
AIASYTGYNQEDSVIMNRSAVDRGFFRSVFYRSYKEQESKKGFDQEEVFEKPTRETCQGM
RHAIYDKLDDDGLIAPGVRVSGDDVIIGKTVTLPENEDELESTNRRYTKRDCSTFLRTSE
TGIVDQVMVTLNQEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMPFTCEG
ITPDIIINPHAIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQKISNLLSDYGY
HLRGNEVLYNGFTGRKITSQIFIGPTYYQRLKHMVDDKIHSRARGPIQILNRQPMEGRSR
DGGLRFGEMERDCQIAHGAAQFLRERLFEASDPYQVHVCNLCGIMAIANTRTHTYECRGC
RNKTQISLVRMPYACKLLFQELMSMSIAPRMMSV
Enzyme 33 Number of Residues 1174
Enzyme 33 Molecular Weight 133898
Enzyme 33 Theoretical pI 6.87
Enzyme 33 GO Classification Not Available
Enzyme 33 General Function Transcription
Enzyme 33 Specific Function Not Available
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function Not Available
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 158260669 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID A8K1A8 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name A8K1A8_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >3525 bp
ATGTACGACGCGGATGAGGATATGCAATATGATGAGGATGATGATGAAATCACCCCGGAT
TTGTGGCAAGAAGCATGCTGGATTGTAATCAGTTCCTATTTTGACGAGAAAGGCTTGGTT
AGACAACAGCTGGATTCTTTTGATGAGTTTATTCAGATGTCTGTTCAAAGAATTGTGGAA
GACGCTCCTCCTATAGACCTACAGGCTGAAGCTCAGCATGCTAGTGGAGAAGTTGAAGAA
CCGCCACGATATTTGCTGAAGTTTGAACAAATTTATCTTTCCAAGCCTACCCATTGGGAA
AGAGATGGTGCTCCTTCACCAATGATGCCCAATGAAGCTAGATTAAGGAATCTCACGTAT
TCTGCTCCGCTTTATGTTGATATAACAAAAACAGTCATTAAAGAAGGTGAAGAACAACTT
CAGACTCAGCATCAGAAAACTTTTATAGGAAAAATTCCAATTATGTTGCGGTCAACTTAC
TGCCTTTTGAATGGCTTGACAGATCGTGATCTTTGTGAGTTAAATGAATGCCCTTTGGAT
CCTGGTGGCTATTTCATTATTAATGGATCAGAAAAGGTTCTGATTGCCCAAGAGAAAATG
GCAACAAACACAGTTTATGTGTTTGCCAAAAAGGATTCTAAATATGCCTACACAGGAGAG
TGTAGATCATGTCTTGAGAATTCTTCCCGACCCACCAGTACTATATGGGTTAGCATGCTG
GCAAGAGGAGGACAGGGTGCCAAGAAGAGTGCTATTGGTCAGCGCATTGTGGCAACTCTA
CCATATATCAAGCAAGAAGTTCCCATCATTATTGTGTTCAGAGCATTAGGTTTTGTGTCC
GACAGAGATATTTTAGAACATATTATTTATGATTTTGAAGATCCAGAGATGATGGAAATG
GTTAAACCTTCTCTCGATGAAGCTTTTGTCATCCAAGAACAGAATGTTGCACTAAATTTC
ATTGGTTCAAGAGGAGCAAAGCCTGGTGTTACTAAAGAGAAAAGAATTAAATATGCAAAG
GAAGTTTTACAAAAAGAAATGCTCCCTCATGTTGGTGTCAGTGATTTTTGTGAGACCAAA
AAAGCCTATTTCTTGGGATACATGGTTCATAGGTTACTTCTGGCAGCTTTGGGTAGAAGA
GAACTAGATGACAGAGATCACTATGGAAACAAGAGATTGGATCTTGCTGGGCCGCTGCTT
GCATTCTTATTTAGAGGTATGTTTAAGAATTTGCTTAAAGAAGTGCGGATCTATGCACAG
AAATTTATTGATCGAGGAAAGGATTTTAACTTGGAGTTGGCAATTAAAACACGGATCATA
TCTGATGGCCTAAAATACTCTTTAGCTACTGGAAACTGGGGTGATCAAAAGAAAGCTCAT
CAAGCCAGAGCTGGAGTATCTCAGGTGTTAAACCGCCTGACTTTTGCGTCTACTCTTTCT
CACCTGCGTCGTTTAAATTCTCCTATTGGTAGAGACGGCAAGCTAGCAAAACCAAGACAG
TTGCATAATACGTTGTGGGGAATGGTGTGTCCTGCCGAGACCCCAGAGGGCCATGCTGTA
GGACTTGTGAAGAATTTAGCCTTGATGGCGTATATTTCAGTTGGATCTCAACCATCTCCA
ATTCTGGAATTTTTAGAAGAATGGAGTATGGAAAATTTAGAAGAAATTTCTCCTGCAGCT
ATTGCTGATGCAACCAAGATTTTTGTTAATGGCTGCTGGGTTGGAATACATAAAGATCCC
GAACAACTTATGAACACCCTAAGGAAATTGAGACGTCAGATGGACATCATTGTGTCTGAA
GTTTCTATGATCAGAGATATTCGAGAGAGGGAGATTCGGATCTATACGGATGCAGGCCGT
ATTTGTAGACCACTTCTGATTGTGGAAAAACAAAAGCTACTTTTGAAGAAGAGGCATATT
GACCAATTGAAAGAGAGAGAATATAACAACTATAGTTGGCAGGATCTTGTGGCCAGTGGG
GTAGTGGAGTATATTGATACCCTGGAAGAAGAAACAGTGATGCTTGCAATGACTCCAGAT
GATTTACAGGAGAAAGAAGTAGCTTATTGTTCCACATATACACACTGTGAGATTCATCCC
TCAATGATCCTTGGTGTCTGTGCATCTATTATTCCCTTTCCTGATCATAACCAGTCCCCT
AGAAACACATACCAGTCTGCTATGGGTAAGCAGGCTATGGGAGTTTACATCACCAACTTC
CATGTTCGCATGGACACATTGGCCCATGTTCTCTATTATCCTCAAAAGCCACTTGTGACT
ACACGGTCTATGGAATATCTACGATTTAGAGAGCTGCCAGCAGGCATCAACTCAATTGTG
GCCATTGCATCATACACTGGATATAATCAGGAAGACTCTGTTATCATGAATCGTTCAGCT
GTAGACCGCGGCTTCTTCAGGTCTGTTTTCTATCGCTCATACAAAGAACAGGAGTCTAAA
AAAGGATTTGATCAAGAAGAAGTTTTTGAGAAGCCTACACGTGAAACATGCCAGGGCATG
AGGCATGCCATTTACGACAAGCTGGATGATGATGGTTTGATAGCTCCAGGGGTTCGTGTA
TCAGGAGATGATGTTATTATAGGCAAAACAGTCACCTTGCCTGAAAATGAAGATGAATTG
GAGAGCACCAATAGACGCTATACCAAGAGAGACTGTAGCACTTTTCTCAGAACTAGTGAG
ACGGGCATTGTGGATCAGGTTATGGTAACTCTCAATCAGGAAGGATATAAATTTTGTAAA
ATAAGGGTACGCTCTGTTAGGATTCCACAGATTGGAGACAAATTTGCTAGTCGACATGGT
CAAAAGGGTACTTGTGGTATTCAGTATAGACAAGAGGATATGCCTTTCACCTGTGAAGGT
ATCACCCCTGATATCATCATCAATCCCCATGCCATCCCCTCTCGTATGACTATTGGTCAC
TTAATTGAATGCCTTCAAGGGAAGGTATCGGCTAACAAGGGTGAAATTGGTGATGCCACT
CCATTTAATGATGCTGTTAACGTGCAGAAGATTTCTAATCTTTTATCTGATTATGGCTAT
CATCTCAGAGGAAATGAGGTCCTGTACAATGGGTTCACTGGTCGAAAAATCACATCACAA
ATATTTATTGGCCCCACTTATTACCAGCGTTTGAAGCATATGGTGGATGATAAGATTCAC
TCTCGTGCTAGGGGACCTATTCAGATCCTCAATAGACAGCCCATGGAGGGTAGATCTCGT
GATGGTGGCCTGCGTTTTGGAGAAATGGAACGAGATTGTCAGATTGCCCATGGAGCAGCC
CAGTTTTTAAGGGAAAGATTGTTTGAGGCATCAGATCCATATCAGGTTCATGTTTGCAAT
CTTTGTGGAATAATGGCGATTGCCAACACCAGGACCCATACATATGAATGCAGGGGCTGC
CGCAATAAAACCCAGATTTCTTTGGTGCGAATGCCTTACGCATGCAAACTATTGTTTCAG
GAACTTATGTCTATGAGTATTGCACCGCGAATGATGAGTGTTTAG
Enzyme 33 GenBank Gene ID AK289823 Link Image
Enzyme 33 GeneCard ID A8K1A8 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
Enzyme 34 [top]
Enzyme 34 ID 15197
Enzyme 34 Name DNA-directed RNA polymerase (EC 2.7.7.6)
Enzyme 34 Synonyms Not Available
Enzyme 34 Gene Name DKFZp686D10173
Enzyme 34 Protein Sequence >DNA-directed RNA polymerase (EC 2.7.7.6)
MDVLAEEFGNLTPEQLAAPIPTVEEKWRLLPAFLKVKGLVKQHIDSFNYFINVEIKKIMK
ANEKVTSDADPMWYLKYLNIYVGLPDVEESFNVTRPVSPHECRLRDMTYSAPITVDIEYT
RGSQRIIRNALPIGRMPIMLRSSNCVLTGKTPAEFAKLNECPLDPGGYFIVKGVEKVILI
QEQLSKNRIIVEADRKGAVGASVTSSTHEKKSRTNMAVKQGRFYLRHNTLSEDIPIVIIF
KAMGVESDQEIVQMIGTEEHVMAAFGPSLEECQKAQIFTQMQALKYIGNKVRRQRMWGGG
PKKTKIEEARELLASTILTHVPVKEFNFRAKCIYTAVMVRRVILAQGDNKVDDRDYYGNK
RLELAGQLLSLLFEDLFKKFNSEMKKIADQVIPKQRAAQFDVVKHMRQDQITNGMVNAIS
TGNWSLKRFKMDRQGVTQVLSRLSYISALGMMTRISSQFEKTRKVSGPRSLQPSQWGMLC
PSDTPEGEACGLVKNLALMTHITTDMEDGPIVKLASNLGVEDVNLLCGEELSYPNVFLVF
LNGNILGVIRDHKKLVNTFRLMRRAGYINEFVSISTNLTDRCVYISSDGGRLCRPYIIVK
KQKPAVTNKHMEELAQGYRNFEDFLHESLVEYLDVNEENDCNIALYEHTINKDTTHLEIE
PFTLLGVCAGLIPYPHHNQSPRNTYQCAMGKQAMGTIGYNQRNRIDTLMYLLAYPQKPMV
KTKTIELIEFEKLPAGQNATVAVMSYSGYDIEDALVLNKASLDRGFGRCLVYKNAKCTLK
RYTNQTFDKVMGPMLDAATRKPIWRHEILDADGICSPGEKVENKQVLVNKSMPTVTQIPL
EGSNVPQQPQYKDVPITYKGATDSYIEKVMISSNAEDAFLIKMLLRQTRRPEIGDKFSSR
HGQKGVCGLIVPQEDMPFCDSGICPDIIMNPHGFPSRMTVGKLIELLAGKAGVLDGRFHY
GTAFGGSKVKDVCEDLVRHGYNYLGKDYVTSGITGEPFEAYIYFGPVYYQKLKHMVLDKM
HARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCLIGYGASMLLLERLMISSDAFEVDVC
GQCGLLGYSGWCHYCKSSCHVSSLRIPYACKLLFQELQSMNIIPRLKLSKYNE
Enzyme 34 Number of Residues 1133
Enzyme 34 Molecular Weight 127821
Enzyme 34 Theoretical pI 8.64
Enzyme 34 GO Classification
Function
  • DNA binding
  • DNA-directed RNA 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 34 General Function Transcription
Enzyme 34 Specific Function Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444] ALL_REAC R00444 > R00435 R00441 R00442 R00443
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 31873396 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q7Z3R8 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name Q7Z3R8_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >3402 bp
ATGGACGTGCTAGCGGAGGAGTTTGGGAACCTGACTCCGGAGCAGCTGGCGGCGCCGATC
CCGACTGTAGAGGAAAAATGGAGGCTGCTTCCAGCATTTTTAAAGGTGAAAGGCCTTGTG
AAACAGCATATAGATTCATTTAACTATTTCATTAATGTAGAGATAAAGAAGATAATGAAA
GCCAATGAAAAGGTTACAAGTGACGCTGACCCTATGTGGTACTTAAAATATCTTAATATC
TATGTTGGGCTTCCTGATGTTGAAGAAAGCTTCAATGTAACTAGACCAGTGTCCCCTCAT
GAGTGCCGTTTGAGAGACATGACATACTCTGCCCCTATTACAGTGGATATTGAATATACC
CGAGGCAGCCAGAGGATCATCCGCAATGCCTTACCTATCGGCAGAATGCCCATAATGCTA
CGTAGTTCAAACTGTGTTCTTACAGGAAAAACGCCAGCAGAATTTGCCAAACTGAACGAA
TGTCCCTTAGATCCAGGTGGCTACTTCATTGTTAAAGGAGTAGAAAAAGTTATTCTTATC
CAAGAGCAGCTGTCTAAGAACAGGATCATCGTGGAGGCTGATAGAAAAGGGGCTGTTGGA
GCTTCAGTTACCAGCTCTACCCATGAGAAAAAAAGCAGAACCAATATGGCTGTGAAACAA
GGACGATTTTATTTGAGGCATAATACTTTGTCAGAAGATATACCCATTGTCATCATATTT
AAGGCCATGGGTGTTGAGAGTGACCAGGAAATTGTGCAGATGATTGGAACAGAGGAGCAC
GTGATGGCTGCATTTGGGCCCAGTCTGGAAGAGTGCCAGAAAGCTCAGATTTTCACACAG
ATGCAGGCATTAAAATATATAGGGAACAAAGTAAGAAGGCAAAGGATGTGGGGAGGTGGA
CCAAAGAAAACCAAAATAGAAGAAGCAAGAGAGCTCCTGGCTTCCACCATTCTGACCCAT
GTCCCAGTTAAGGAATTCAATTTCCGAGCCAAATGTATCTATACTGCAGTGATGGTGCGA
AGAGTTATTCTGGCCCAAGGAGATAATAAAGTTGACGACAGAGATTATTATGGTAACAAG
CGACTGGAATTGGCAGGACAGCTTTTATCTCTTCTTTTTGAAGACTTGTTCAAAAAATTT
AATTCTGAAATGAAAAAGATTGCCGACCAGGTGATTCCTAAGCAAAGAGCAGCCCAGTTT
GATGTTGTCAAACACATGCGCCAAGACCAGATCACCAATGGCATGGTGAATGCTATTTCT
ACCGGAAATTGGTCTTTAAAGAGATTTAAAATGGACCGCCAGGGTGTAACCCAAGTGCTG
TCTCGCTTGTCATATATATCCGCACTGGGCATGATGACAAGAATCTCTTCCCAGTTTGAA
AAAACGAGAAAAGTGAGTGGTCCTCGCTCCCTCCAGCCATCTCAGTGGGGAATGCTGTGT
CCTTCGGACACTCCTGAAGGAGAGGCATGTGGTTTGGTTAAAAACTTGGCCCTTATGACA
CACATCACAACTGATATGGAAGATGGACCCATTGTTAAATTAGCCAGTAACTTGGGAGTA
GAAGATGTGAATTTATTATGTGGGGAAGAGCTCTCTTACCCAAATGTGTTTCTTGTCTTT
CTTAATGGTAACATCTTAGGTGTCATTCGAGACCACAAAAAGCTAGTGAATACATTTCGA
CTCATGAGAAGAGCAGGATATATCAATGAATTTGTTTCCATCTCAACAAATCTTACAGAT
CGATGTGTCTATATTTCTTCTGATGGGGGAAGGCTATGCAGACCCTACATAATTGTCAAG
AAACAGAAGCCAGCAGTCACAAATAAACATATGGAAGAGCTGGCCCAAGGGTACAGGAAT
TTTGAAGATTTCTTACATGAGAGTCTGGTTGAATATTTAGATGTGAATGAAGAAAATGAT
TGTAACATTGCACTGTACGAACACACAATTAATAAAGACACCACCCACTTGGAGATTGAA
CCCTTCACTCTTCTCGGCGTGTGTGCTGGACTTATCCCATACCCTCACCATAACCAGTCA
CCGAGAAACACTTATCAGTGTGCCATGGGGAAACAAGCCATGGGTACTATAGGATACAAC
CAGCGAAACAGAATTGATACTCTCATGTATCTACTAGCATATCCACAAAAACCCATGGTT
AAGACAAAAACCATTGAATTGATAGAATTTGAGAAACTGCCAGCTGGACAGAATGCAACA
GTTGCTGTGATGAGCTATAGTGGCTATGATATTGAAGATGCTCTTGTTTTAAACAAGGCC
TCTTTAGACAGAGGCTTTGGGCGTTGCCTTGTATATAAAAATGCTAAATGTACGTTGAAA
CGATACACCAATCAGACTTTTGATAAAGTGATGGGGCCCATGTTGGATGCTGCTACAAGG
AAACCTATCTGGCGACATGAAATCTTAGATGCAGATGGTATTTGTTCTCCAGGTGAGAAA
GTAGAAAACAAACAAGTGCTTGTAAATAAGTCCATGCCCACAGTGACTCAGATTCCTTTG
GAAGGAAGTAATGTACCACAGCAACCACAGTACAAAGATGTACCCATAACCTACAAAGGA
GCAACAGACTCATATATTGAAAAAGTGATGATATCTTCAAATGCTGAAGATGCTTTTCTG
ATCAAAATGCTGCTGAGACAGACAAGGCGTCCAGAAATTGGAGACAAATTCAGCAGTCGT
CATGGGCAAAAAGGTGTTTGTGGCTTGATCGTCCCCCAGGAAGACATGCCATTTTGTGAT
TCTGGCATCTGTCCGGACATCATCATGAACCCACACGGCTTCCCATCACGAATGACGGTG
GGGAAGCTCATTGAGCTGCTGGCTGGCAAGGCCGGTGTGCTGGACGGCAGATTCCACTAC
GGCACTGCGTTTGGAGGCAGTAAAGTGAAGGATGTGTGTGAGGACCTCGTTCGCCATGGT
TATAACTACTTGGGGAAAGACTATGTTACATCCGGCATCACAGGTGAGCCCTTCGAAGCA
TACATCTATTTTGGCCCCGTGTACTATCAGAAGCTGAAACACATGGTGCTAGATAAAATG
CATGCCCGGGCCCGGGGCCCACGAGCCGTCCTTACCAGGCAACCCACTGAAGGACGGTCT
CGTGATGGTGGCTTGCGTCTCGGGGAAATGGAACGTGACTGTTTAATCGGTTATGGAGCC
AGTATGCTTTTGCTAGAGAGACTAATGATTTCAAGTGATGCCTTTGAGGTTGATGTCTGT
GGGCAGTGTGGACTTCTGGGGTATTCTGGCTGGTGCCATTACTGCAAGTCATCCTGCCAC
GTGTCTTCCCTCCGTATTCCGTATGCCTGCAAGCTGCTCTTCCAGGAACTACAGTCTATG
AACATCATCCCCAGGTTAAAACTGTCCAAGTACAATGAATGA
Enzyme 34 GenBank Gene ID BX537447 Link Image
Enzyme 34 GeneCard ID Q7Z3R8 Link Image
Enzyme 34 GenAtlas ID DKFZp686D10173 Link Image
Enzyme 34 HGNC ID HGNC:30348 Link Image
Enzyme 34 Chromosome Location Not Available
Enzyme 34 Locus Not Available
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References Not Available
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 15198
Enzyme 35 Name DNA-directed RNA polymerase III subunit RPC7-like
Enzyme 35 Synonyms
  1. RNA polymerase III subunit C7-like
  2. DNA-directed RNA polymerase III subunit G-like
Enzyme 35 Gene Name POLR3GL
Enzyme 35 Protein Sequence >DNA-directed RNA polymerase III subunit RPC7-like
MASRGGGRGRGRGQLTFNVEAVGIGKGDALPPPTLQPSPLFPPLEFRPVPLPSGEEGEYV
LALKQELRGAMRQLPYFIRPAVPKRDVERYSDKYQMSGPIDNAIDWNPDWRRLPRELKIR
VRKLQKERITILLPKRPPKTTEDKEETIQKLETLEKKEEEVTSEEDEEKEEEEEKEEEEE
EEYDEEEHEEETDYIMSYFDNGEDFGGDSDDNMDEAIY
Enzyme 35 Number of Residues 218
Enzyme 35 Molecular Weight 25334
Enzyme 35 Theoretical pI 4.19
Enzyme 35 GO Classification Not Available
Enzyme 35 General Function Transcription
Enzyme 35 Specific Function Not Available
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function Not Available
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 16552536 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q9BT43 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name RPC7L_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >657 bp
ATGGCCAGCCGGGGTGGGGGCCGGGGTCGTGGCCGGGGCCAGTTGACCTTCAACGTGGAG
GCCGTGGGCATTGGGAAAGGGGATGCTTTGCCCCCACCCACCCTGCAGCCTTCTCCACTC
TTCCCTCCCTTGGAGTTCCGCCCAGTACCTTTGCCCTCAGGCGAGGAAGGGGAATATGTC
CTGGCACTGAAGCAAGAGCTACGAGGAGCCATGAGGCAGCTCCCCTACTTCATCCGGCCA
GCTGTCCCCAAGAGAGATGTGGAGCGTTATTCAGACAAATATCAGATGTCAGGTCCGATT
GACAATGCCATCGATTGGAACCCTGATTGGCGGCGTCTACCCCGGGAGCTAAAGATCCGA
GTGCGGAAGCTACAGAAGGAACGGATTACAATTCTGCTCCCCAAGAGGCCCCCTAAGACC
ACAGAAGATAAGGAGGAAACAATACAGAAACTAGAGACCCTGGAGAAGAAGGAAGAAGAA
GTAACTTCAGAGGAGGATGAGGAGAAAGAAGAAGAAGAAGAGAAGGAAGAGGAGGAAGAA
GAAGAGTATGATGAAGAAGAACATGAAGAGGAAACTGATTACATCATGTCATATTTTGAC
AATGGAGAGGACTTTGGTGGTGACAGTGATGACAATATGGACGAGGCTATATACTGA
Enzyme 35 GenBank Gene ID AK056984 Link Image
Enzyme 35 GeneCard ID Q9BT43 Link Image
Enzyme 35 GenAtlas ID POLR3GL Link Image
Enzyme 35 HGNC ID HGNC:28466 Link Image
Enzyme 35 Chromosome Location Not Available
Enzyme 35 Locus Not Available
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References Not Available
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 15199
Enzyme 36 Name POLR1C protein (Fragment)
Enzyme 36 Synonyms Not Available
Enzyme 36 Gene Name POLR1C
Enzyme 36 Protein Sequence >POLR1C protein (Fragment)
EMRSRVVLGEFGVRNVHTTDFPGNYSGYDDAWDQDRFEKNFRVDVVHMDENSLEFDMVGI
DAAIANAFRRILLAEVPTMAVEKVLVYNNTSIVQDEILAHRLGLIPIHADPRLFEYRNQG
DEEGTEIDTLQFRLQVRCTRNPHAAKDSSDPNELYVNHKVYTRHMTWIPLGNQADLFPEG
TIRPVHDDILIAQLRPGQEIDLLMHCVKGIGKDHAKFSPVATASYRLLPDITLLEPVEGE
AAEELSRCFSPGVIEVQEVQGKKVARVANPRLDTFSREIFRNEKLKKVVRLARVRDHYIF
SVESTGVLPPDVLVSEAIKVLMGKCRRFLDELDAVQMD
Enzyme 36 Number of Residues 338
Enzyme 36 Molecular Weight 38462
Enzyme 36 Theoretical pI 5.30
Enzyme 36 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • protein binding
  • protein dimerization activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • transcription
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 36 General Function Transcription
Enzyme 36 Specific Function Not Available
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 14198113 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q96HT3 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name Q96HT3_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1018 bp
GGAAATGCGGAGCCGCGTGGTTCTGGGGGAGTTTGGGGTTCGCAATGTCCATACTACTGA
CTTTCCCGGTAACTATTCCGGTTATGATGATGCCTGGGACCAGGACCGCTTCGAGAAGAA
TTTCCGTGTGGATGTAGTACACATGGATGAAAACTCACTGGAGTTTGACATGGTGGGAAT
TGACGCAGCCATTGCCAATGCTTTTCGACGAATTCTGCTAGCTGAGGTGCCAACTATGGC
TGTGGAGAAGGTCCTGGTGTACAATAATACATCCATTGTTCAGGATGAGATTCTTGCTCA
CCGTCTGGGGCTCATTCCCATTCATGCTGATCCCCGTCTTTTTGAGTATCGGAACCAAGG
AGATGAAGAAGGCACAGAGATAGATACTCTACAGTTTCGTCTCCAGGTCAGATGCACTCG
GAACCCCCATGCTGCTAAAGATTCCTCTGACCCCAACGAACTGTACGTGAACCACAAAGT
GTATACCAGGCATATGACATGGATCCCCCTGGGGAACCAGGCTGATCTCTTTCCAGAGGG
CACTATCCGACCAGTGCATGATGATATCCTCATCGCTCAGCTGCGGCCTGGCCAAGAAAT
TGACCTGCTCATGCACTGTGTCAAGGGCATTGGCAAAGATCATGCCAAGTTTTCACCAGT
GGCAACAGCCAGTTACAGGCTCCTGCCAGACATCACCCTGCTTGAGCCCGTGGAAGGGGA
GGCAGCTGAGGAGTTGAGCAGGTGCTTCTCACCTGGTGTTATTGAGGTGCAGGAAGTCCA
AGGTAAAAAGGTGGCCAGAGTTGCCAACCCCCGGCTGGATACCTTCAGCAGAGAAATCTT
CCGGAATGAGAAGCTAAAGAAGGTTGTGAGGCTTGCCCGGGTTCGAGATCATTATATCTT
CTCTGTTGAGTCAACGGGGGTGTTGCCACCAGATGTGCTGGTGAGTGAAGCCATCAAAGT
ACTGATGGGGAAGTGCCGGCGCTTCTTGGATGAACTAGATGCGGTTCAGATGGACTGA
Enzyme 36 GenBank Gene ID BC008118 Link Image
Enzyme 36 GeneCard ID Q96HT3 Link Image
Enzyme 36 GenAtlas ID POLR1C Link Image
Enzyme 36 HGNC ID HGNC:20194 Link Image
Enzyme 36 Chromosome Location Not Available
Enzyme 36 Locus Not Available
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 15200
Enzyme 37 Name Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
Enzyme 37 Synonyms Not Available
Enzyme 37 Gene Name UCK1
Enzyme 37 Protein Sequence >Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
Enzyme 37 Number of Residues 201
Enzyme 37 Molecular Weight 22761
Enzyme 37 Theoretical pI 6.23
Enzyme 37 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 37 General Function Nucleotide transport and metabolism
Enzyme 37 Specific Function Not Available
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 57162360 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q5JT13 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name Q5JT13_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >807 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGTCGACCGTGTGTGAGAAGATCATGGAGTTGCTGGGACAG
AACGAGGTGGAACAGCGGCAGCGGAAGGTGGTCATCCTGAGCCAGGACAGGTTCTACAAG
GTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTGAAAGGACAGTACAATTTTGACCATCCA
GATGCCTTTGATAATGATTTGATGCACAGGACTCTGAAGAACATCGTGGAGGGCAAAACG
GTGGAGGTGCCGACCTATGATTTTGTGACACACTCAAGGTTACCAGAGACCACGGTGGTC
TACCCTGCGGACGTGGTTCTGTTTGAGGGCATCTTGGTGTTCTACAGCCAGGAGATCCGG
GACATGTTCCACCTGCGCCTCTTCGTGGACACCGACTCCGACGTCAGGCTGTCTCGAAGA
GTTCTCCGGGACGTGCGCCGAGGGAGGGACCTGGAGCAGATTCTGACGCAGTACACCACC
TTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTGCCGACAAAGAAGTATGCCGATGTGATC
ATCCCGCGAGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGAC
ATTCTGAATGGTGACATCTGCAAATGGCACCGAGGAGGGTCCAATGGGCGGAGCTACAAG
CGGACCTTTTCTGAGCCAGGGGACCACCCTGGGATGCTGACCTCTGGCAAACGGTCACAT
TTGGAGTCCAGCAGCAGACCCCACTGA
Enzyme 37 GenBank Gene ID AL358781 Link Image
Enzyme 37 GeneCard ID Q5JT13 Link Image
Enzyme 37 GenAtlas ID UCK1 Link Image
Enzyme 37 HGNC ID HGNC:14859 Link Image
Enzyme 37 Chromosome Location Not Available
Enzyme 37 Locus Not Available
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References Not Available
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 16437
Enzyme 38 Name cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
Enzyme 38 Synonyms Not Available
Enzyme 38 Gene Name ENTPD3
Enzyme 38 Protein Sequence >cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 38 Number of Residues 529
Enzyme 38 Molecular Weight 59106
Enzyme 38 Theoretical pI 6.40
Enzyme 38 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 38 General Function Not Available
Enzyme 38 Specific Function Not Available
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein Not Available
Enzyme 38 UniProtKB/Swiss-Prot ID B2R8D0 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name B2R8D0_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence Not Available
Enzyme 38 GenBank Gene ID AK313322 Link Image
Enzyme 38 GeneCard ID B2R8D0 Link Image
Enzyme 38 GenAtlas ID Not Available
Enzyme 38 HGNC ID Not Available
Enzyme 38 Chromosome Location Not Available
Enzyme 38 Locus Not Available
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References Not Available
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 16463
Enzyme 39 Name cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
Enzyme 39 Synonyms
  1. SubName: cDNA FLJ43358 fis, clone NT2RP7014005, highly similar to CTP synthase 2 (EC 6.3.4.2)
  2. SubName: CTP synthase II, isoform CRA_a
Enzyme 39 Gene Name CTPS2
Enzyme 39 Protein Sequence >cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFV
LNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDA
VQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFVEAFRQFQFKAKRENFCNIHV
SLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ
VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLFKWRNMADRYERLQKICS
IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQK
LCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDAD
STEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH
RFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPY
LGLLLAATGNLNAYLQQGCKLSSSDRYSDASDDSFSEPRIAELEIS
Enzyme 39 Number of Residues 586
Enzyme 39 Molecular Weight 65678
Enzyme 39 Theoretical pI 6.91
Enzyme 39 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
Component
Enzyme 39 General Function Nucleotide transport and metabolism
Enzyme 39 Specific Function Not Available
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571] ALL_REAC R00571
  • (other) R00573
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein Not Available
Enzyme 39 UniProtKB/Swiss-Prot ID B3KWM2 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name B3KWM2_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence Not Available
Enzyme 39 GenBank Gene ID AK125332 Link Image
Enzyme 39 GeneCard ID B3KWM2 Link Image
Enzyme 39 GenAtlas ID Not Available
Enzyme 39 HGNC ID Not Available
Enzyme 39 Chromosome Location Not Available
Enzyme 39 Locus Not Available
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References Not Available
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 16476
Enzyme 40 Name cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name PKM2
Enzyme 40 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 40 Number of Residues 531
Enzyme 40 Molecular Weight 57938
Enzyme 40 Theoretical pI 7.94
Enzyme 40 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 40 General Function Carbohydrate transport and metabolism
Enzyme 40 Specific Function Not Available
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein Not Available
Enzyme 40 UniProtKB/Swiss-Prot ID B2R5N8 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name B2R5N8_HUMAN Link Image
Enzyme 40 PDB ID 1F3X Link Image
Enzyme 40 PDB File Show
Enzyme 40 3D Structure
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence Not Available
Enzyme 40 GenBank Gene ID AK312253 Link Image
Enzyme 40 GeneCard ID B2R5N8 Link Image
Enzyme 40 GenAtlas ID Not Available
Enzyme 40 HGNC ID Not Available
Enzyme 40 Chromosome Location 15
Enzyme 40 Locus 15q22
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References Not Available
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 16538
Enzyme 41 Name cDNA, FLJ93080, highly similar to Homo sapiens UDP-N-acteylglucosamine pyrophosphorylase 1 (UAP1), mRNA (UDP-N-acteylglucosamine pyrophosphorylase 1, isoform CRA_a)
Enzyme 41 Synonyms Not Available
Enzyme 41 Gene Name UAP1
Enzyme 41 Protein Sequence >cDNA, FLJ93080, highly similar to Homo sapiens UDP-N-acteylglucosamine pyrophosphorylase 1 (UAP1), mRNA (UDP-N-acteylglucosamine pyrophosphorylase 1, isoform CRA_a)
MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSS
HQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAY
PKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTK
HKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDME
QRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQ
VVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPY
VDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTT
ARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRLKDANDVPIQCEISPLISYAGEGLESY
VADKEFHAPLIIDENGVHELVKNGI
Enzyme 41 Number of Residues 505
Enzyme 41 Molecular Weight 57029
Enzyme 41 Theoretical pI 6.33
Enzyme 41 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolism
  • physiological process
Component
Enzyme 41 General Function Not Available
Enzyme 41 Specific Function Not Available
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein Not Available
Enzyme 41 UniProtKB/Swiss-Prot ID B2R6R8 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name B2R6R8_HUMAN Link Image
Enzyme 41 PDB ID 1JV3 Link Image
Enzyme 41 PDB File Show
Enzyme 41 3D Structure
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence Not Available
Enzyme 41 GenBank Gene ID AK312685 Link Image
Enzyme 41 GeneCard ID B2R6R8 Link Image
Enzyme 41 GenAtlas ID Not Available
Enzyme 41 HGNC ID Not Available
Enzyme 41 Chromosome Location Not Available
Enzyme 41 Locus Not Available
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References Not Available
Enzyme 41 Metabolite References Not Available