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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 Link Image
SDF File Show Link Image
PDB File Show Link Image
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. Ectonucleoside triphosphate diphosphohydrolase 3
  4. Nucleoside diphosphate kinase, mitochondrial
  5. Nucleoside diphosphate kinase A
  6. Nucleoside diphosphate kinase B
  7. Nucleoside diphosphate kinase 6
  8. Inosine triphosphate pyrophosphatase
  9. GTP:AMP phosphotransferase, mitochondrial
  10. Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
  11. CTP synthase 1
  12. 6-phosphofructokinase type C
  13. DNA-directed RNA polymerase III subunit RPC4
  14. DNA-directed RNA polymerase II subunit RPB1
  15. DNA-directed RNA polymerase, mitochondrial
  16. DNA-directed RNA polymerase I subunit RPA2
  17. DNA-directed RNA polymerase III subunit RPC7
  18. DNA-directed RNA polymerase I subunit RPA49
  19. 6-phosphofructokinase, liver type
  20. DNA-directed RNA polymerase III subunit RPC8
  21. DNA-directed RNA polymerase III subunit RPC10
  22. 6-phosphofructokinase, muscle type
  23. Pyruvate kinase isozymes M1/M2
  24. Pyruvate kinase isozymes R/L
  25. UTP--glucose-1-phosphate uridylyltransferase
  26. UDP-N-acetylhexosamine pyrophosphorylase
  27. Uridine-cytidine kinase 2
  28. CAD protein
  29. CTP synthase 2
  30. Uncharacterized protein POLR3G
  31. Uridine-cytidine kinase-like 1
  32. Ectonucleoside triphosphate diphosphohydrolase 8
  33. 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)
  34. DNA-directed RNA polymerase III subunit RPC1
  35. DNA-directed RNA polymerase I subunit RPA1
  36. Zinc ribbon domain containing 1
  37. DNA-directed RNA polymerases I and III subunit RPAC2
  38. cDNA FLJ75210, highly similar to H.sapiens RNA polymerase II 140 kDa subunit (Polymerase (RNA) II (DNA directed) polypeptide B, 140kDa)
  39. DNA-directed RNA polymerase
  40. DNA-directed RNA polymerase III subunit RPC7-like
  41. POLR1C protein
  42. Uridine kinase
  43. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  44. cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
  45. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
  46. 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 1
  3. Ecto-ATPDase 1
  4. Ecto-ATPase 1
  5. Ecto-apyrase
  6. Lymphoid cell activation antigen
  7. 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 57964.1
Enzyme 1 Theoretical pI 6.29
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 1 General Function Involved in hydrolase activity
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 [RN:R00085]
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 45580700 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 NM_001776.5 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 1
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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  6. 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]
  7. 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]
  8. 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]
  9. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  10. 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]
  11. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  12. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed 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 MAPK-activating protein PM09
  4. Putative NF-kappa-B-activating protein 107
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 44839.2
Enzyme 2 Theoretical pI 5.98
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion binding
  • metal ion binding
  • pyrophosphatase activity
Process
Component
Enzyme 2 General Function Involved in calcium ion binding
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 [RN:R00329]
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 229577440 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 >1206 bp
ATGCCCGTGCAGCTGTCTGAGCACCCGGAATGGAATGAGTCTATGCACTCCCTCCGGATC
AGTGTGGGGGGCCTTCCTGTGCTGGCGTCCATGACCAAGGCCGCGGACCCCCGCTTCCGC
CCCCGCTGGAAGGTGATCCTGACGTTCTTTGTGGGTGCTGCCATCCTCTGGCTGCTCTGC
TCCCACCGCCCGGCCCCCGGCAGGCCCCCCACCCACAATGCACACAACTGGAGGCTCGGC
CAGGCGCCCGCCAACTGGTACAATGACACCTACCCCCTGTCTCCCCCACAAAGGACACCG
GCTGGGATTCGGTATCGAATCGCAGTTATCGCAGACCTGGACACAGAGTCAAGGGCCCAA
GAGGAAAACACCTGGTTCAGTTACCTGAAAAAGGGCTACCTGACCCTGTCAGACAGTGGG
GACAAGGTGGCCGTGGAATGGGACAAAGACCATGGGGTCCTGGAGTCCCACCTGGCGGAG
AAGGGGAGAGGCATGGAGCTATCCGACCTGATTGTTTTCAATGGGAAACTCTACTCCGTG
GATGACCGGACGGGGGTCGTCTACCAGATCGAAGGCAGCAAAGCCGTGCCCTGGGTGATT
CTGTCCGACGGCGACGGCACCGTGGAGAAAGGCTTCAAGGCCGAATGGCTGGCAGTGAAG
GACGAGCGTCTGTACGTGGGCGGCCTGGGCAAGGAGTGGACGACCACTACGGGTGATGTG
GTGAACGAGAACCCGGAGTGGGTGAAGGTGGTGGGCTACAAGGGCAGCGTGGACCACGAG
AACTGGGTGTCCAACTACAACGCCCTGCGGGCTGCTGCCGGCATCCAGCCGCCAGGCTAC
CTCATCCATGAGTCTGCCTGCTGGAGTGACACGCTGCAGCGCTGGTTCTTCCTGCCGCGC
CGCGCCAGCCAGGAGCGCTACAGCGAGAAGGACGACGAGCGCAAGGGCGCCAACCTGCTG
CTGAGCGCCTCCCCTGACTTCGGCGACATCGCTGTGAGCCACGTCGGGGCGGTGGTCCCC
ACTCACGGCTTCTCGTCCTTCAAGTTCATCCCCAACACCGACGACCAGATCATTGTGGCC
CTCAAATCCGAGGAGGACAGCGGCAGAGTCGCCTCCTACATCATGGCCTTCACGCTGGAC
GGGCGCTTCCTGTTGCCGGAGACCAAGATCGGAAGCGTGAAATACGAAGGCATCGAGTTC
ATTTAA
Enzyme 2 GenBank Gene ID NM_001159772.1 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 1
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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Yang M, Kirley TL: Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change. Biochemistry. 2004 Jul 20;43(28):9185-94. [PubMed Link Image]
  7. Dai J, Liu J, Deng Y, Smith TM, Lu M: Structure and protein design of a human platelet function inhibitor. Cell. 2004 Mar 5;116(5):649-59. [PubMed Link Image]
  8. Huber C, Oules B, Bertoli M, Chami M, Fradin M, Alanay Y, Al-Gazali LI, Ausems MG, Bitoun P, Cavalcanti DP, Krebs A, Le Merrer M, Mortier G, Shafeghati Y, Superti-Furga A, Robertson SP, Le Goff C, Muda AO, Paterlini-Brechot P, Munnich A, Cormier-Daire V: Identification of CANT1 mutations in Desbuquois dysplasia. Am J Hum Genet. 2009 Nov;85(5):706-10. Epub 2009 Oct 22. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5318
Enzyme 3 Name Ectonucleoside triphosphate diphosphohydrolase 3
Enzyme 3 Synonyms
  1. NTPDase 3
  2. CD39 antigen-like 3
  3. Ecto-ATP diphosphohydrolase 3
  4. Ecto-ATPDase 3
  5. Ecto-ATPase 3
  6. Ecto-apyrase 3
  7. HB6
Enzyme 3 Gene Name ENTPD3
Enzyme 3 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 3
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 3 Number of Residues 529
Enzyme 3 Molecular Weight 59104.8
Enzyme 3 Theoretical pI 6.40
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 3 General Function Involved in hydrolase activity
Enzyme 3 Specific Function Has a threefold preference for the hydrolysis of ATP over ADP
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 23-43 486-506
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 13817037 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O75355 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ENTP3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1590 bp
ATGTTCACTGTGCTGACCCGCCAACCATGTGAGCAAGCAGGCCTCAAGGCCCTCTACCGA
ACTCCAACCATCATTGCCTTGGTGGTCTTGCTTGTGAGTATTGTGGTACTTGTGAGTATC
ACTGTCATCCAGATCCACAAGCAAGAGGTCCTCCCTCCAGGACTGAAGTATGGTATTGTG
CTGGATGCCGGGTCTTCAAGAACCACAGTCTACGTGTATCAATGGCCAGCAGAAAAAGAG
AATAATACCGGAGTGGTCAGTCAAACCTTCAAATGTAGTGTGAAAGGCTCTGGAATCTCC
AGCTATGGAAATAACCCCCAAGATGTCCCCAGAGCCTTTGAGGAGTGTATGCAAAAAGTC
AAGGGGCAGGTTCCATCCCACCTCCACGGATCCACCCCCATTCACCTGGGAGCCACGGCT
GGGATGCGCTTGCTGAGGTTGCAAAATGAAACAGCAGCTAATGAAGTCCTTGAAAGCATC
CAAAGCTACTTCAAGTCCCAGCCCTTTGACTTTAGGGGTGCTCAAATCATTTCTGGGCAA
GAAGAAGGGGTATATGGATGGATTACAGCCAACTATTTAATGGGAAATTTCCTGGAGAAG
AACCTGTGGCACATGTGGGTGCACCCGCATGGAGTGGAAACCACGGGTGCCCTGGACTTA
GGTGGTGCCTCCACCCAAATATCCTTCGTGGCAGGAGAGAAGATGGATCTGAACACCAGC
GACATCATGCAGGTGTCCCTGTATGGCTACGTATACACGCTCTACACACACAGCTTCCAG
TGCTATGGCCGGAATGAGGCTGAGAAGAAGTTTCTGGCAATGCTCCTGCAGAATTCTCCT
ACCAAAAACCATCTCACCAATCCCTGTTACCCTCGGGATTATAGCATCAGCTTCACCATG
GGCCATGTATTTGATAGCCTGTGCACTGTGGACCAGAGGCCAGAAAGTTATAACCCCAAT
GATGTCATCACTTTTGAAGGAACTGGGGACCCATCTCTGTGTAAGGAGAAGGTGGCTTCC
ATATTTGACTTCAAAGCTTGCCATGATCAAGAAACCTGTTCTTTTGATGGGGTTTATCAG
CCAAAGATTAAAGGGCCATTTGTGGCTTTTGCAGGATTCTACTACACAGCCAGTGCTTTA
AATCTTTCAGGTAGCTTTTCCCTGGACACCTTCAACTCCAGCACCTGGAATTTCTGCTCA
CAGAATTGGAGTCAGCTCCCACTGCTGCTCCCCAAATTTGATGAGGTATATGCCCGCTCT
TACTGCTTCTCAGCCAACTACATCTACCACTTGTTTGTGAACGGTTACAAATTCACAGAG
GAGACTTGGCCCCAAATACACTTTGAAAAAGAAGTGGGGAATAGCAGCATAGCCTGGTCT
CTTGGCTACATGCTCAGCCTGACCAACCAGATCCCAGCTGAAAGCCCTCTGATCCGTCTG
CCCATAGAACCACCTGTCTTTGTGGGCACCCTCGCTTTCTTCACAGCGGCAGCCTTGCTG
TGTCTGGCATTTCTTGCATACCTGTGTTCAGCAACCAGAAGAAAGAGGCACTCCGAGCAT
GCCTTTGACCATGCAGTGGATTCTGACTGA
Enzyme 3 GenBank Gene ID AF034840 Link Image
Enzyme 3 GeneCard ID ENTPD3 Link Image
Enzyme 3 GenAtlas ID ENTPD3 Link Image
Enzyme 3 HGNC ID HGNC:3365 Link Image
Enzyme 3 Chromosome Location 3
Enzyme 3 Locus 3p21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed Link Image]
  2. Smith TM, Kirley TL: Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1. Biochim Biophys Acta. 1998 Jul 28;1386(1):65-78. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Smith TM, Lewis Carl SA, Kirley TL: Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase. Biochemistry. 1999 May 4;38(18):5849-57. [PubMed Link Image]
  5. Yang F, Hicks-Berger CA, Smith TM, Kirley TL: Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry. 2001 Apr 3;40(13):3943-50. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5338
Enzyme 4 Name Nucleoside diphosphate kinase, mitochondrial
Enzyme 4 Synonyms
  1. NDK
  2. NDP kinase, mitochondrial
  3. Nucleoside diphosphate kinase D
  4. NDPKD
  5. nm23-H4
Enzyme 4 Gene Name NME4
Enzyme 4 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 4 Number of Residues 187
Enzyme 4 Molecular Weight 20658.5
Enzyme 4 Theoretical pI 10.75
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 4 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 4 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 14336697 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 4 PDB ID 1EHW Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCG
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 4 GenBank Gene ID AE006463 Link Image
Enzyme 4 GeneCard ID NME4 Link Image
Enzyme 4 GenAtlas ID NME4 Link Image
Enzyme 4 HGNC ID HGNC:7852 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 16p13.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5341
Enzyme 5 Name Nucleoside diphosphate kinase A
Enzyme 5 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Granzyme A-activated DNase
  4. GAAD
  5. Metastasis inhibition factor nm23
  6. Tumor metastatic process-associated protein
  7. nm23-H1
Enzyme 5 Gene Name NME1
Enzyme 5 Protein Sequence >Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 5 Number of Residues 152
Enzyme 5 Molecular Weight 17148.6
Enzyme 5 Theoretical pI 6.11
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 5 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 5 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 4557797 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 5 PDB ID 1JXV Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >459 bp
ATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAACCAGATGGGGTCCAGCGGGGTCTT
GTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGATTCCGCCTTGTTGGTCTGAAATTC
ATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTACGTTGACCTGAAGGACCGTCCATTC
TTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCGGTAGTTGCCATGGTCTGGGAGGGG
CTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGGGAGACCAACCCTGCAGACTCCAAG
CCTGGGACCATCCGTGGAGACTTCTGCATACAAGTTGGCAGGAACATTATACATGGCAGT
GATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTGTGGTTTCACCCTGAGGAACTGGTA
GATTACACGAGCTGTGCTCAGAACTGGATCTATGAATGA
Enzyme 5 GenBank Gene ID NM_000269.2 Link Image
Enzyme 5 GeneCard ID NME1 Link Image
Enzyme 5 GenAtlas ID NME1 Link Image
Enzyme 5 HGNC ID HGNC:7849 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 17q21.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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. 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]
  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. 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]
  5. Ni X, Gu S, Dai J, Cheng H, Guo L, Li L, Ji C, Xie Y, Ying K, Mao Y: Isolation and characterization of a novel human NM23-H1B gene, a different transcript of NM23-H1. J Hum Genet. 2003;48(2):96-100. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. 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]
  10. MacDonald NJ, Freije JM, Stracke ML, Manrow RE, Steeg PS: Site-directed mutagenesis of nm23-H1. Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells. J Biol Chem. 1996 Oct 11;271(41):25107-16. [PubMed Link Image]
  11. 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]
  12. 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]
  13. Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed Link Image]
  14. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed Link Image]
  15. Garzia L, D'Angelo A, Amoresano A, Knauer SK, Cirulli C, Campanella C, Stauber RH, Steegborn C, Iolascon A, Zollo M: Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility. Oncogene. 2008 Mar 20;27(13):1853-64. Epub 2007 Oct 1. [PubMed Link Image]
  16. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  17. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  19. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  20. 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]
  21. 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]
  22. 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5344
Enzyme 6 Name Nucleoside diphosphate kinase B
Enzyme 6 Synonyms
  1. NDK B
  2. NDP kinase B
  3. C-myc purine-binding transcription factor PUF
  4. nm23-H2
Enzyme 6 Gene Name NME2
Enzyme 6 Protein Sequence >Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 6 Number of Residues 152
Enzyme 6 Molecular Weight 17297.9
Enzyme 6 Theoretical pI 8.69
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 6 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 6 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752)
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 4467843 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 6 PDB ID 1NSK Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 6 GenBank Gene ID X58965 Link Image
Enzyme 6 GeneCard ID NME2 Link Image
Enzyme 6 GenAtlas ID NME2 Link Image
Enzyme 6 HGNC ID HGNC:7850 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 17q21.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. 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]
  2. 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]
  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. Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed Link Image]
  5. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Seifert M, Seib T, Engel M, Dooley S, Welter C: Characterization of the human nm23-H2 promoter region and localization of the microsatellite D17S396. Biochem Biophys Res Commun. 1995 Oct 24;215(3):910-4. [PubMed Link Image]
  8. Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M: Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. 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]
  13. 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5346
Enzyme 7 Name Nucleoside diphosphate kinase 6
Enzyme 7 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. Inhibitor of p53-induced apoptosis-alpha
  4. IPIA-alpha
  5. nm23-H6
Enzyme 7 Gene Name NME6
Enzyme 7 Protein Sequence >Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 7 Number of Residues 186
Enzyme 7 Molecular Weight 21142.0
Enzyme 7 Theoretical pI 8.49
Enzyme 7 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 7 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 7 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 7 Pathways
Enzyme 7 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 3228530 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 7 GenBank Gene ID AF051941 Link Image
Enzyme 7 GeneCard ID NME6 Link Image
Enzyme 7 GenAtlas ID NME6 Link Image
Enzyme 7 HGNC ID HGNC:20567 Link Image
Enzyme 7 Chromosome Location 3
Enzyme 7 Locus 3p21
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5668
Enzyme 8 Name Inosine triphosphate pyrophosphatase
Enzyme 8 Synonyms
  1. ITPase
  2. Inosine triphosphatase
  3. Putative oncogene protein hlc14-06-p
Enzyme 8 Gene Name ITPA
Enzyme 8 Protein Sequence >Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
Enzyme 8 Number of Residues 194
Enzyme 8 Molecular Weight 21445.5
Enzyme 8 Theoretical pI 5.34
Enzyme 8 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 8 General Function Involved in hydrolase activity
Enzyme 8 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 8 Pathways
Enzyme 8 Reactions
  • a nucleoside triphosphate + H2O = a nucleotide + diphosphate [RN:R01532]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 21104378 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9BY32 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name ITPA_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCATGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAAGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAATACTTTGGCAGTTTGGCAGCTTGA
Enzyme 8 GenBank Gene ID AB062127 Link Image
Enzyme 8 GeneCard ID ITPA Link Image
Enzyme 8 GenAtlas ID ITPA Link Image
Enzyme 8 HGNC ID HGNC:6176 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 20p
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Stenmark P, Kursula P, Flodin S, Graslund S, Landry R, Nordlund P, Schuler H: Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T. J Biol Chem. 2007 Feb 2;282(5):3182-7. Epub 2006 Nov 29. [PubMed Link Image]
  5. 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]
  6. 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5845
Enzyme 9 Name GTP:AMP phosphotransferase, mitochondrial
Enzyme 9 Synonyms
  1. Adenylate kinase 3
  2. AK 3
  3. Adenylate kinase 3 alpha-like 1
Enzyme 9 Gene Name AK3
Enzyme 9 Protein Sequence >GTP:AMP phosphotransferase, mitochondrial
MGASARLLRAVIMGAPGSGKGTVSSRITTHFELKHLSSGDLLRDNMLRGTEIGVLAKAFI
DQGKLIPDDVMTRLALHELKNLTQYSWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEV
IKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEDQT
KPVLEYYQKKGVLETFSGTETNKIWPYVYAFLQTKVPQRSQKASVTP
Enzyme 9 Number of Residues 227
Enzyme 9 Molecular Weight 25565.2
Enzyme 9 Theoretical pI 9.64
Enzyme 9 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside binding
  • nucleotide kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
Component
Enzyme 9 General Function Involved in ATP binding
Enzyme 9 Specific Function NTP + AMP = NDP + ADP
Enzyme 9 Pathways
Enzyme 9 Reactions
  • nucleoside triphosphate + AMP = nucleoside diphosphate + ADP [RN:R00333]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 6518533 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9UIJ7 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name KAD3_HUMAN Link Image
Enzyme 9 PDB ID 2AK3 Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >684 bp
ATGGGGGCGTCGGGGCGGCTGCTGCGAGCGGTGATCATGGGGGCCCCGGGCTCGGGCAAG
GGCACCGTGTCGTCCCGCATCACTACACACTTCGAGCTGAAGCACCTCTCCCGCGGGGAC
CTGCTCCGGGACAACATGCTGCGGGGCACAGAAATTGGCGTGTTAGCCCAGGCTTTCATT
GACCAAGGGAAACTCATCCCAGATTATGTCACGACTCGGCTGGCCCTTCATGAGCTGAAA
AACCTCACCCAGTATAGCTGGCTGTTGGATGGTTTTCCAAGGACACTTCCACAGGCAGAA
GCCCTAGATAGAGCTTATCAGATCGACACAGTGATTAACCTGAATGTGCCCTTTGAGGTC
ATTAAACAACGCCTTACTGCTCGCTGGATTCATCCCGCCAGTGGCCGAGTCTATAACATT
GAATTCAACCCTCCCAAAACTGTGGGCATTGATGACCTGACTGGGGAGCCTCTCATTCAG
CGTGAGGATGATAAACCAGAGACGGTTATCAAGAGACTAAAGGCTTATGAAGACCAAACA
AAGCCAGTCCTGGAATATTACCAGAAAAAAGGGGTGTTGGAAACATTCTCCGGAACAGAA
ACCAACAAGATTTGGCCCTATGTATATGCTTTCCTACAAACTAAAGTTCCACAAAGAAGC
CAGAAAGCTTCAGTTACTCCATGA
Enzyme 9 GenBank Gene ID AB021870 Link Image
Enzyme 9 GeneCard ID AK3 Link Image
Enzyme 9 GenAtlas ID AK3 Link Image
Enzyme 9 HGNC ID HGNC:17376 Link Image
Enzyme 9 Chromosome Location 9
Enzyme 9 Locus 9p24.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5893
Enzyme 10 Name Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
Enzyme 10 Synonyms
  1. Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
  2. Ap4A hydrolase
  3. Ap4Aase
  4. Diadenosine tetraphosphatase
  5. Nucleoside diphosphate-linked moiety X motif 2
  6. Nudix motif 2
Enzyme 10 Gene Name NUDT2
Enzyme 10 Protein Sequence >Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
MALRACGLIIFRRCLIPKVDNNAIEFLLLQASDGIHHWTPPKGHVEPGEDDLETALRETQ
EEAGIEAGQLTIIEGFKRELNYVARNKPKTVIYWLAEVKDYDVEIRLSHEHQAYRWLGLE
EACQLAQFKEMKAALQEGHQFLCSIEA
Enzyme 10 Number of Residues 147
Enzyme 10 Molecular Weight 16829.1
Enzyme 10 Theoretical pI 5.06
Enzyme 10 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 10 General Function Involved in hydrolase activity
Enzyme 10 Specific Function Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis
Enzyme 10 Pathways
Enzyme 10 Reactions
  • P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP [RN:R01232]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 55958893 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P50583 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name AP4A_HUMAN Link Image
Enzyme 10 PDB ID 1XSC Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >444 bp
ATGGCCTTGAGAGCATGTGGCTTGATCATCTTCCGAAGATGCCTCATTCCCAAAGTGGAC
AACAATGCAATTGAGTTTTTACTGCTGCAGGCATCAGATGGCATTCATCACTGGACTCCT
CCCAAAGGCCATGTGGAACCAGGAGAGGATGACTTGGAAACAGCCCTGAGGGAGACCCAA
GAGGAAGCAGGCATAGAAGCAGGCCAGCTGACCATTATTGAGGGGTTCAAAAGGGAACTC
AATTATGTGGCCAGGAACAAGCCTAAAACAGTCATTTACTGGCTGGCGGAGGTGAAGGAC
TATGACGTGGAGATCCGCCTCTCCCATGAGCACCAAGCCTACCGCTGGCTGGGGCTGGAG
GAGGCCTGCCAGTTGGCTCAGTTCAAGGAGATGAAGGCAGCGCTCCAAGAAGGACACCAG
TTTCTTTGCTCCATAGAGGCCTGA
Enzyme 10 GenBank Gene ID AL356494 Link Image
Enzyme 10 GeneCard ID NUDT2 Link Image
Enzyme 10 GenAtlas ID NUDT2 Link Image
Enzyme 10 HGNC ID HGNC:8049 Link Image
Enzyme 10 Chromosome Location 9
Enzyme 10 Locus 9p13
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Swarbrick JD, Buyya S, Gunawardana D, Gayler KR, McLennan AG, Gooley PR: Structure and substrate-binding mechanism of human Ap4A hydrolase. J Biol Chem. 2005 Mar 4;280(9):8471-81. Epub 2004 Dec 13. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5949
Enzyme 11 Name CTP synthase 1
Enzyme 11 Synonyms
  1. CTP synthetase 1
  2. UTP--ammonia ligase 1
Enzyme 11 Gene Name CTPS
Enzyme 11 Protein Sequence >CTP synthase 1
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
Enzyme 11 Number of Residues 591
Enzyme 11 Molecular Weight 66689.9
Enzyme 11 Theoretical pI 6.42
Enzyme 11 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
Component
Enzyme 11 General Function Involved in CTP synthase activity
Enzyme 11 Specific Function Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen
Enzyme 11 Pathways
Enzyme 11 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 30293 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P17812 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PYRG1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 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 11 GenBank Gene ID X52142 Link Image
Enzyme 11 GeneCard ID CTPS Link Image
Enzyme 11 GenAtlas ID CTPS Link Image
Enzyme 11 HGNC ID HGNC:2519 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 1p34.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  5. Han GS, Sreenivas A, Choi MG, Chang YF, Martin SS, Baldwin EP, Carman GM: Expression of Human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A. J Biol Chem. 2005 Nov 18;280(46):38328-36. Epub 2005 Sep 22. [PubMed Link Image]
  6. Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed Link Image]
  7. Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  10. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  11. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  12. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  13. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  14. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  15. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  16. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6009
Enzyme 12 Name 6-phosphofructokinase type C
Enzyme 12 Synonyms
  1. 6-phosphofructokinase, platelet type
  2. Phosphofructo-1-kinase isozyme C
  3. PFK-C
  4. Phosphofructokinase 1
  5. Phosphohexokinase
Enzyme 12 Gene Name PFKP
Enzyme 12 Protein Sequence >6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
Enzyme 12 Number of Residues 784
Enzyme 12 Molecular Weight 85595.4
Enzyme 12 Theoretical pI 7.60
Enzyme 12 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 metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • 6-phosphofructokinase complex
  • cell part
  • cytoplasm
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 12 General Function Involved in 6-phosphofructokinase activity
Enzyme 12 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 12 Pathways
Enzyme 12 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID Q01813 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name K6PP_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 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 12 GenBank Gene ID D25328 Link Image
Enzyme 12 GeneCard ID PFKP Link Image
Enzyme 12 GenAtlas ID PFKP Link Image
Enzyme 12 HGNC ID HGNC:8878 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 10p15.3-p15.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  9. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  13. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6011
Enzyme 13 Name DNA-directed RNA polymerase III subunit RPC4
Enzyme 13 Synonyms
  1. RNA polymerase III subunit C4
  2. DNA-directed RNA polymerase III subunit D
  3. Protein BN51
  4. RNA polymerase III 47 kDa subunit
  5. RPC53 homolog
Enzyme 13 Gene Name POLR3D
Enzyme 13 Protein Sequence >DNA-directed RNA polymerase III subunit RPC4
MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTP
NIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKK
GNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQL
PLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAAR
KTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVL
IKQEKDREAKLAENACTLADLTEGQVGKLLIRKSGRVQLLLGKVTLDVTMGTACSFLQEL
VSVGLGDSRTGEMTVLGHVKHKLVCSPDFESLLDHKHR
Enzyme 13 Number of Residues 398
Enzyme 13 Molecular Weight 44395.5
Enzyme 13 Theoretical pI 6.97
Enzyme 13 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
  • transcription from RNA polymerase III promoter
  • transcription, DNA-dependent
Component
  • DNA-directed RNA polymerase III complex
  • intracellular organelle part
  • nuclear part
  • nucleoplasm part
  • organelle part
Enzyme 13 General Function Involved in DNA binding
Enzyme 13 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway
Enzyme 13 Pathways
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 55769552 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P05423 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name RPC4_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1197 bp
ATGTCGGAAGGAAACGCCGCCGGCGAGCCCAGCACGCCGGGAGGGCCCCGACCTCTCCTG
ACTGGGGCCCGGGGGCTCATCGGGCGGCGGCCGGCGCCTCCCCTCACCCCCGGCCGCCTT
CCCTCCATCCGTTCCAGGGACCTCACCCTCGGGGGAGTCAAGAAGAAAACCTTCACCCCA
AATATCATCAGTCGGAAGATCAAGGAAGAGCCCAAGGAAGAAGTAACTGTCAAGAAGGAG
AAGCGTGAAAGGGACAGAGACCGACAACGAGAGGGGCATGGACGAGGGCGAGGCCGTCCA
GAAGTGATCCAGTCTCACTCCATCTTTGAGCAGGGCCCAGCTGAAATGATGAAGAAAAAA
GGGAACTGGGATAAGACAGTGGATGTGTCAGACATGGGACCTTCTCATATCATCAACATC
AAAAAAGAGAAGAGAGAGACAGACGAAGAAACTAAACAGATCTTGCGTATGCTGGAGAAG
GACGATTTCCTCGATGACCCCGGCCTGAGGAACGACACTCGAAATATGCCTGTGCAGCTG
CCGCTGGCTCACTCAGGATGGCTTTTTAAGGAAGAAAATGACGAACCAGATGTTAAACCT
TGGCTGGCTGGCCCCAAGGAAGAGGACATGGAGGTGGACATACCTGCTGTGAAAGTGAAA
GAGGAGCCACGAGATGAGGAGGAAGAGGCCAAGATGAAGGCTCCTCCCAAAGCAGCCAGG
AAGACTCCAGGCCTCCCGAAGGATGTATCTGTGGCAGAGCTGCTGAGGGAGCTGAGCCTC
ACCAAGGAAGAGGAACTGCTGTTTCTGCAGCTGCCAGACACCCTCCCTGGCCAGCCACCC
ACCCAGGACATCAAGCCTATCAAGACAGAGGTGCAGGGCGAGGACGGACAGGTGGTGCTC
ATCAAGCAGGAGAAAGACCGAGAAGCCAAATTGGCAGAGAATGCTTGTACCCTGGCTGAC
CTGACAGAGGGTCAGGTTGGCAAGCTACTCATCCGCAAGTCTGGAAGGGTGCAACTCCTC
TTGGGCAAGGTGACTCTGGACGTGACCATGGGAACTGCCTGCTCCTTCCTGCAGGAGCTG
GTGTCCGTGGGCCTTGGAGACAGTAGGACAGGGGAGATGACAGTCCTGGGACACGTGAAG
CACAAACTTGTATGTTCCCCTGATTTTGAATCCCTCTTGGATCACAAACACCGGTAA
Enzyme 13 GenBank Gene ID NM_001722.2 Link Image
Enzyme 13 GeneCard ID POLR3D Link Image
Enzyme 13 GenAtlas ID POLR3D Link Image
Enzyme 13 HGNC ID HGNC:1080 Link Image
Enzyme 13 Chromosome Location 8
Enzyme 13 Locus 8q21
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  6. Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed Link Image]
  7. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6014
Enzyme 14 Name DNA-directed RNA polymerase II subunit RPB1
Enzyme 14 Synonyms
  1. RNA polymerase II subunit B1
  2. DNA-directed RNA polymerase II subunit A
  3. DNA-directed RNA polymerase III largest subunit
  4. RNA-directed RNA polymerase II subunit RPB1
Enzyme 14 Gene Name POLR2A
Enzyme 14 Protein Sequence >DNA-directed RNA polymerase II subunit RPB1
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
SPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPASPKYTPTSPSYSPSSPEYTPTSPKY
SPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTS
PKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN
Enzyme 14 Number of Residues 1970
Enzyme 14 Molecular Weight 217174.2
Enzyme 14 Theoretical pI 7.38
Enzyme 14 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
  • transcription from RNA polymerase II promoter
  • transcription, DNA-dependent
Component
  • DNA-directed RNA polymerase II, core complex
  • intracellular organelle part
  • nuclear part
  • nucleoplasm part
  • organelle part
Enzyme 14 General Function Involved in DNA binding
Enzyme 14 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II 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. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Acts as a RNA- dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome
Enzyme 14 Pathways
Enzyme 14 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 36124 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P24928 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name RPB1_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID X63564 Link Image
Enzyme 14 GeneCard ID POLR2A Link Image
Enzyme 14 GenAtlas ID POLR2A Link Image
Enzyme 14 HGNC ID HGNC:9187 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 17p13.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Kershnar E, Wu SY, Chiang CM: Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes. J Biol Chem. 1998 Dec 18;273(51):34444-53. [PubMed Link Image]
  6. 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]
  7. Parada CA, Roeder RG: A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription. EMBO J. 1999 Jul 1;18(13):3688-701. [PubMed Link Image]
  8. Kim JB, Yamaguchi Y, Wada T, Handa H, Sharp PA: Tat-SF1 protein associates with RAP30 and human SPT5 proteins. Mol Cell Biol. 1999 Sep;19(9):5960-8. [PubMed Link Image]
  9. 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]
  10. Carty SM, Greenleaf AL: Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing. Mol Cell Proteomics. 2002 Aug;1(8):598-610. [PubMed Link Image]
  11. Yang L, Li N, Wang C, Yu Y, Yuan L, Zhang M, Cao X: Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells. J Biol Chem. 2004 Mar 19;279(12):11639-48. Epub 2003 Dec 17. [PubMed Link Image]
  12. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  13. Katsarou ME, Papakyriakou A, Katsaros N, Scorilas A: Expression of the C-terminal domain of novel human SR-A1 protein: interaction with the CTD domain of RNA polymerase II. Biochem Biophys Res Commun. 2005 Aug 19;334(1):61-8. [PubMed Link Image]
  14. Sun XJ, Wei J, Wu XY, Hu M, Wang L, Wang HH, Zhang QH, Chen SJ, Huang QH, Chen Z: Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase. J Biol Chem. 2005 Oct 21;280(42):35261-71. Epub 2005 Aug 22. [PubMed Link Image]
  15. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  16. Li M, Phatnani HP, Guan Z, Sage H, Greenleaf AL, Zhou P: Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1. Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17636-41. Epub 2005 Nov 28. [PubMed Link Image]
  17. Moniaux N, Nemos C, Schmied BM, Chauhan SC, Deb S, Morikane K, Choudhury A, Vanlith M, Sutherlin M, Sikela JM, Hollingsworth MA, Batra SK: The human homologue of the RNA polymerase II-associated factor 1 (hPaf1), localized on the 19q13 amplicon, is associated with tumorigenesis. Oncogene. 2006 Jun 1;25(23):3247-57. Epub 2006 Feb 20. [PubMed Link Image]
  18. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  19. Haline-Vaz T, Silva TC, Zanchin NI: The human interferon-regulated ISG95 protein interacts with RNA polymerase II and shows methyltransferase activity. Biochem Biophys Res Commun. 2008 Aug 8;372(4):719-24. Epub 2008 Jun 3. [PubMed Link Image]
  20. Becker R, Loll B, Meinhart A: Snapshots of the RNA processing factor SCAF8 bound to different phosphorylated forms of the carboxyl-terminal domain of RNA polymerase II. J Biol Chem. 2008 Aug 15;283(33):22659-69. Epub 2008 Jun 11. [PubMed Link Image]
  21. Chang J, Nie X, Chang HE, Han Z, Taylor J: Transcription of hepatitis delta virus RNA by RNA polymerase II. J Virol. 2008 Feb;82(3):1118-27. Epub 2007 Nov 21. [PubMed Link Image]
  22. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  23. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  24. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  25. Zhang Y, Kim Y, Genoud N, Gao J, Kelly JW, Pfaff SL, Gill GN, Dixon JE, Noel JP: Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1. Mol Cell. 2006 Dec 8;24(5):759-70. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6017
Enzyme 15 Name DNA-directed RNA polymerase, mitochondrial
Enzyme 15 Synonyms
  1. MtRPOL
Enzyme 15 Gene Name POLRMT
Enzyme 15 Protein Sequence >DNA-directed RNA polymerase, mitochondrial
MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHV
ELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCG
RWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTR
QAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLP
LAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYA
AALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSL
PPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKP
TLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVV
RMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASD
AEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSS
RLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHS
GAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQL
FQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEAL
YRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDW
LKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCME
VANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVA
AQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDF
PQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQ
PYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCY
RKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILE
ASQLKETLQAVPKPGAFDLEQVKRSTYFFS
Enzyme 15 Number of Residues 1230
Enzyme 15 Molecular Weight 138619.3
Enzyme 15 Theoretical pI 9.25
Enzyme 15 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 15 General Function Involved in DNA binding
Enzyme 15 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 15 Pathways
Enzyme 15 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 2979529 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O00411 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name RPOM_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >3693 bp
ATGTCGGCACTTTGCTGGGGCCGCGGAGCGGCGGGGCTCAAACGAGCCCTACGGCCTTGC
GGCCGCCCGGGACTCCCCGGCAAAGAAGGGACCGCCGGTGGCGTCTGCGGCCCCAGGAGG
AGCTCGTCCGCCAGCCCCCAGGAGCAAGACCAAGACCGCAGGAAGGACTGGGGCCACGTG
GAGCTGCTGGAGGTGCTCCAGGCGCGGGTGCGGCAGCTGCAGGCTGAGAGCGTGTCGGAG
GTGGTGGTGAACAGGGTGGATGTGGCGCGGCTCCCAGAATGTGGCAGTGGAGATGGTAGC
CTCCAGCCACCCAGGAAGGTCCAGATGGGGGCCAAGGATGCCACCCCGGTGCCCTGTGGC
CGCTGGGCAAAGATACTGGAGAAGGATAAGCGGACCCAGCAGATGCGTATGCAGCGGTTG
AAGGCGAAGCTGCAGATGCCATTCCAGAGCGGGGAGTTCAAGGCGCTGACCAGGCGCCTG
CAGGTGGAGCCCCGGCTCCTGAGCAAGCAGATGGCCGGGTGCCTGGAGGACTGCACGCGC
CAGGCCCCCGAGAGCCCCTGGGAGGAGCAGCTGGCCCGGCTGCTGCAGGAGGCCCCTGGG
AAGCTGAGCCTCGATGTGGAGCAGGCCCCGTCGGGGCAGCACTCGCAGGCCCAGCTCTCA
GGTCAGCAGCAGAGGCTCCTGGCCTTCTTCAAGTGCTGCCTGCTCACTGACCAGCTGCCC
CTCGCCCACCACCTGCTGGTCGTCCACCACGGCCAGCGGCAGAAGCGGAAGCTGCTCACG
CTGGACATGTACAACGCCGTGATGCTTGGCTGGGCGCGGCAGGGTGCCTTCAAGGAGCTG
GTATATGTGTTATTCATGGTGAAGGATGCCGGCTTGACTCCGGACCTGCTGTCCTATGCG
GCTGCCCTCCAGTGCATGGGGAGGCAGGACCAGGACGCCGGGACCATCGAAAGGTGTCTG
GAACAGATGAGCCAGGAGGGGCTGAAGCTGCAGGCACTCTTCACCGCCGTTCTGCTGTCT
GAGGAGGATCGGGCCACTGTTCTGAAGGCCGTGCACAAGGTGAAGCCCACCTTCAGCCTC
CCGCCGCAGCTGCCGCCCCCGGTCAACACCTCCAAGCTGCTCAGGGACGTGTATGCCAAG
GATGGGCGTGTGTCCTACCCGAAGCTGCACCTGCCCTTGAAGACCCTGCAGTGCCTCTTT
GAGAAGCAGCTCCACATGGAGCTGGCCAGCAGGGTGTGCGTGGTGTCCGTGGAGAAGCCC
ACGTTGCCAAGCAAGGAGGTCAAGCACGCGCGGAAGACCCTGAAGACCCTGCGGGACCAA
TGGGAGAAAGCACTGTGCCGGGCGCTGCGGGAGACCAAGAACCGCCTAGAGCGCGAGGTG
TACGAGGGCCGGTTCTCACTTTACCCCTTCCTGTGCCTGCTGGACGAGCGCGAGGTGGTG
CGGATGCTCCTGCAGGTCCTGCAGGCGCTGCCCGCCCAAGGTGAGTCCTTCACCACCCTG
GCCCGGGAGCTGAGTGCGCGCACTTTCAGCCGGCACGTGGTGCAGAGGCAGCGGGTCAGT
GGCCAGGTGCAGGCGCTGCAGAACCACTACAGGAAGTACCTCTGCTTGCTGGCCTCCGAC
GCCGAGGTGCCCGAGCCCTGCCTGCCGCGGCAGTACTGGGAGGAGCTGGGGGCGCCCGAG
GCCCTGCGGGAGCAGCCCTGGCCCCTGCCAGTGCAGATGGAGCTGGGCAAGCTGCTGGCG
GAGATGCTGGTGCAGGCTACGCAGATGCCATGCAGCCTGGACAAGCCGCATCGTTCCTCT
CGGCTTGTCCCCGTGCTCTACCACGTGTATTCCTTCCGCAACGTCCAGCAGATCGGCATC
CTGAAGCCGCACCCGGCCTACGTGCAGCTGCTGGAGAAGGCCGCGGAGCCCACGCTGACC
TTCGAGGCGGTGGATGTACCCATGCTTTGCCCCCCGCTGCCCTGGACATCGCCGCACTCT
GGTGCTTTCCTGCTCAGCCCCACCAAGCTGATGCGCACGGTGGAAGGCGCCACGCAGCAC
CAGGAGCTGCTGGAAACCTGCCCGCCCACCGCGCTGCATGGCGCACTGGACGCCCTCACC
CAACTGGGCAACTGCGCCTGGCGCGTCAACGGGCGCGTGCTGGACCTGGTGCTGCAGCTC
TTCCAGGCCAAGGGCTGCCCCCAGCTAGGCGTGCCGGCCCCGCCCTCCGAGGCGCCCCAG
CCGCCCGAGGCCCACCTGCCGCACAGCGCCGCGCCCGCCCGCAAGGCCGAGCTGCGCCGT
GAGCTGGCGCACTGCCAGAAGGTGGCCCGGGAGATGCACAGCCTGCGGGCGGAGGCGCTG
TACCGCCTCTCGCTGGCGCAGCACCTGCGGGACCGCGTCTTCTGGCTGCCGCACAACATG
GACTTCCGCGGCCGCACCTACCCCTGCCCGCCGCACTTCAACCACCTGGGCAGCGACGTG
GCGCGGGCCCTGCTGGAGTTCGCCCAGGGCCGCCCGCTCGGCCCGCACGGCCTGGATTGG
CTCAAGATCCACCTGGTCAATCTCACGGGGTTGAAGAAGCGGGAGCCGCTGCGGAAGCGC
CTGGCCTTTGCGGAGGAGGTGATGGATGACATCCTGGACTCCGCGGACCAACCCTTGACG
GGCCGAAAGTGGTGGATGGGCGCGGAGGAACCCTGGCAGACGCTGGCCTGCTGTATGGAG
GTGGCGAACGCTGTGCGCGCCTCCGACCCTGCCGCCTATGTCTCCCACCTCCCCGTCCAT
CAGGACGGCTCTTGCAACGGCCTGCAGCATTATGCTGCTCTGGGCCGCGACAGCGTGGGC
GCCGCCTCCGTCAACCTGGAGCCCTCGGATGTGCCGCAGGACGTGTACAGCGGCGTGGCC
GCGCAGGTGGAGGTGTTCCGTAGGCAGGACGCCCAGCGGGGCATGCGGGTGGCACAGGTG
CTGGAAGGTTTCATCACCCGCAAGGTGGTGAAGCAGACGGTGATGACGGTGGTGTACGGG
GTCACGCGCTATGGCGGGCGCCTGCAGATTGAGAAGCGCCTCCGGGAGCTGAGCGACTTT
CCCCAGGAGTTCGTGTGGGAGGCCTCTCACTATCTCGTACGCCAGGTCTTCAAGAGTCTA
CAGGAGATGTTCTCGGGGACCCGGGCCATCCAGCACTGGCTGACCGAGAGTGCCCGCCTC
ATCTCCCACATGGGCTCTGTGGTGGAGTGGGTCACACCCCTGGGCGTCCCCGTCATCCAG
CCCTATCGCCTGGACTCCAAGGTCAAGCAAATAGGAGGTGGAATTCAGAGCATCACCTAC
ACCCACAACGGAGACATCAGCCGAAAGCCCAACACACGTAAGCAGAAGAACGGCTTCCCG
CCCAACTTCATCCACTCGCTGGACTCCTCCCACATGATGCTCACCGCCCTGCACTGCTAC
AGGAAGGGCCTGACCTTCGTCTCTGTGCACGACTGTTACTGGACTCACGCAGCTGATGTC
TCCGTCATGAACCAGGTGTGCCGGGAGCAGTTTGTCCGCTTGCACAGCGAGCCCATCCTG
CAGGACCTGTCCAGATTCCTGGTCAAGCGGTTCTGCTCTGAGCCCCAGAAGATCTTGGAG
GCCAGCCAGCTGAAGGAGACACTGCAGGCGGTGCCCAAGCCAGGGGCCTTCGACCTGGAG
CAGGTGAAGCGTTCCACCTACTTCTTCAGCTGA
Enzyme 15 GenBank Gene ID AC004449 Link Image
Enzyme 15 GeneCard ID POLRMT Link Image
Enzyme 15 GenAtlas ID POLRMT Link Image
Enzyme 15 HGNC ID HGNC:9200 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 19p13.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Falkenberg M, Gaspari M, Rantanen A, Trifunovic A, Larsson NG, Gustafsson CM: Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA. Nat Genet. 2002 Jul;31(3):289-94. Epub 2002 Jun 17. [PubMed Link Image]
  4. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6018
Enzyme 16 Name DNA-directed RNA polymerase I subunit RPA2
Enzyme 16 Synonyms
  1. RNA polymerase I subunit 2
  2. DNA-directed RNA polymerase I 135 kDa polypeptide
  3. RPA135
Enzyme 16 Gene Name POLR1B
Enzyme 16 Protein Sequence >DNA-directed RNA polymerase I subunit RPA2
MDPGSRWRNLPSGPSLKHLTDPSYGIPREQQKAALQELTRAHVESFNYAVHEGLGLAVQA
IPPFEFAFKDERISFTILDAVISPPTVPKGTICKEANVYPAECRGRRSTYRGKLTADINW
AVNGISKGIIKQFLGYVPIMVKSKLCNLRNLPPQALIEHHEEAEEMGGYFIINGIEKVIR
MLIMPRRNFPIAMIRPKWKTRGPGYTQYGVSMHCVREEHSAVNMNLHYLENGTVMLNFIY
RKELFFLPLGFALKALVSFSDYQIFQELIKGKEDDSFLRNSVSQMLRIVMEEGCSTQKQV
LNYLGECFRVKLNVPDWYPNEQAAEFLFNQCICIHLKSNTEKFYMLCLMTRKLFALAKGE
CMEDNPDSLVNQEVLTPGQLFLMFLKEKLEGWLVSIKIAFDKKAQKTSVSMNTDNLMRIF
TMGIDLTKPFEYLFATGNLRSKTGLGLLQDSGLCVVADKLNFIRYLSHFRCVHRGADFAK
MRTTTVRRLLPESWGFLCPVHTPDGEPCGLMNHLTAVCEVVTQFVYTASIPALLCNLGVT
PIDGAPHRSYSECYPVLLDGVMVGWVDKDLAPGIADSLRHFKVLREKRIPPWMEVVLIPM
TGKPSLYPGLFLFTTPCRLVRPVQNLALGKEELIGTMEQIFMNVAIFEDEVFAGVTTHQE
LFPHSLLSVIANFIPFSDHNQSPRNMYQCQMGKQTMGFPLLTYQDRSDNKLYRLQTPQSP
LVRPSMYDYYDMDNYPIGTNAIVAVISYTGYDMEDAMIVNKASWERGFAHGSVYKSEFID
LSEKIKQGDSSLVFGIKPGDPRVLQKLDDDGLPFIGAKLQYGDPYYSYLNLNTGESFVMY
YKSKENCVVDNIKVCSNDTGSGKFKCVCITMRVPRNPTIGDKFASRHGQKGILSRLWPAE
DMPFTESGMVPDILFNPHGFPSRMTIGMLIESMAGKSAALHGLCHDATPFIFSEENSALE
YFGEMLKAAGYNFYGTERLYSGISGLELEADIFIGVVYYQRLRHMVSDKFQVRTTGARDR
VTNQPIGGRNVQGGIRFGEMERDALLAHGTSFLLHDRLFNCSDRSVAHVCVKCGSLLSPL
LEKPPPSWSAMRNRKYNCTLCSRSDTIDTVSVPYVFRYFVAELAAMNIKVKLDVV
Enzyme 16 Number of Residues 1135
Enzyme 16 Molecular Weight 128228.4
Enzyme 16 Theoretical pI 7.88
Enzyme 16 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleoside binding
  • nucleotidyltransferase activity
  • ribonucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 16 General Function Involved in DNA-directed RNA polymerase activity
Enzyme 16 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft
Enzyme 16 Pathways
Enzyme 16 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 62420281 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9H9Y6 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name RPA2_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >3408 bp
ATGGATCCTGGCAGCCGGTGGCGGAACCTGCCCAGCGGGCCTAGCCTAAAGCACTTGACT
GACCCCTCTTATGGAATCCCGCGGGAACAGCAAAAGGCAGCGTTGCAGGAGCTGACGCGG
GCGCACGTGGAGTCCTTCAACTACGCTGTGCACGAGGGTCTCGGCCTCGCGGTGCAGGCT
ATACCTCCCTTTGAATTTGCTTTCAAAGATGAGCGTATCTCTTTTACTATTCTGGATGCT
GTTATCAGTCCACCTACAGTTCCAAAAGGGACCATCTGCAAAGAGGCCAATGTTTATCCA
GCAGAATGCCGGGGCCGAAGGAGTACCTACCGTGGGAAGTTGACAGCTGATATCAACTGG
GCAGTGAATGGAATCTCAAAAGGAATCATTAAGCAGTTTCTTGGCTATGTTCCCATCATG
GTGAAATCCAAGCTTTGCAACTTACGTAACCTTCCCCCACAAGCCCTCATTGAGCACCAT
GAGGAGGCAGAGGAAATGGGGGGCTATTTTATAATCAATGGCATTGAAAAAGTCATCCGA
ATGTTGATTATGCCTCGGAGAAATTTTCCCATTGCAATGATAAGACCAAAATGGAAAACC
AGAGGGCCTGGTTATACTCAGTATGGAGTTTCAATGCACTGTGTGAGGGAAGAACATTCC
GCTGTCAATATGAACCTCCACTACTTGGAAAATGGCACTGTTATGTTGAACTTTATTTAC
CGAAAAGAACTGTTCTTTCTTCCTTTGGGATTTGCACTTAAGGCACTTGTCAGCTTTTCT
GATTATCAGATCTTTCAGGAGCTCATCAAAGGAAAAGAGGATGATTCTTTCCTTAGGAAC
TCTGTTTCTCAGATGTTAAGGATTGTAATGGAAGAGGGTTGTTCGACACAAAAACAGGTC
CTTAACTACCTAGGTGAATGCTTCAGAGTAAAACTCAATGTTCCTGACTGGTACCCAAAT
GAGCAAGCTGCGGAGTTCCTGTTTAACCAGTGCATCTGTATCCACTTGAAATCCAATACT
GAAAAGTTTTATATGCTTTGTCTCATGACGCGAAAGCTCTTTGCTTTAGCCAAAGGAGAG
TGCATGGAGGACAATCCTGATAGTTTGGTGAACCAGGAAGTCCTCACACCGGGTCAGCTC
TTCCTTATGTTCCTGAAGGAAAAACTGGAAGGTTGGTTAGTGTCTATTAAAATAGCTTTT
GATAAGAAGGCTCAGAAGACCAGTGTTTCCATGAACACTGACAATTTGATGAGGATTTTT
ACAATGGGCATAGACCTTACAAAACCATTTGAATACCTTTTTGCTACTGGGAATCTGCGT
TCTAAAACAGGTCTTGGCCTCCTACAAGATTCTGGACTTTGTGTTGTGGCTGACAAGCTG
AACTTCATACGCTACCTCTCCCATTTCCGCTGCGTGCACAGAGGGGCTGATTTTGCCAAG
ATGAGGACCACCACAGTACGCAGGCTGCTGCCAGAGTCCTGGGGCTTCCTTTGTCCCGTG
CATACCCCAGACGGGGAGCCCTGTGGCCTGATGAACCACCTAACTGCCGTATGTGAGGTT
GTCACACAGTTTGTGTATACGGCATCTATTCCAGCTTTACTGTGCAACTTGGGGGTCACT
CCCATTGATGGAGCTCCCCACCGATCATACAGTGAGTGCTACCCTGTCCTGCTGGACGGT
GTCATGGTTGGCTGGGTGGATAAGGATCTTGCTCCAGGCATCGCAGATTCTCTTCGTCAT
TTTAAGGTGTTGAGAGAGAAAAGAATTCCTCCCTGGATGGAAGTGGTCCTTATACCCATG
ACAGGAAAACCAAGTCTGTACCCAGGATTGTTCCTTTTTACCACTCCTTGTAGACTGGTA
CGGCCTGTGCAGAACTTAGCATTGGGCAAAGAAGAGCTAATTGGAACTATGGAACAGATC
TTCATGAATGTCGCTATCTTTGAGGATGAAGTTTTTGCTGGAGTTACCACACACCAGGAA
CTCTTTCCACACAGCCTGCTGAGTGTGATTGCCAACTTCATCCCTTTCTCTGATCACAAC
CAGAGTCCACGGAACATGTACCAATGCCAGATGGGTAAGCAAACTATGGGCTTTCCACTT
CTCACTTATCAAGACCGATCGGATAACAAACTGTATCGTCTTCAGACTCCTCAGAGTCCC
TTGGTGAGACCCTCCATGTATGATTATTATGACATGGATAACTATCCAATTGGGACCAAT
GCCATCGTTGCTGTGATTTCTTACACTGGCTATGATATGGAAGATGCCATGATTGTGAAT
AAGGCCTCTTGGGAACGAGGCTTTGCCCATGGAAGTGTCTACAAGTCTGAGTTCATAGAC
CTCTCTGAAAAAATTAAACAAGGAGATAGTAGCCTGGTGTTTGGCATCAAACCTGGTGAC
CCACGCGTTCTGCAGAAGTTAGATGACGATGGATTGCCGTTTATAGGAGCAAAACTGCAG
TACGGAGATCCGTATTACAGCTACCTCAACCTCAACACCGGGGAAAGTTTTGTGATGTAC
TATAAGAGTAAAGAAAATTGTGTTGTGGATAACATCAAAGTGTGCAGTAATGACACTGGG
AGTGGAAAATTCAAGTGTGTTTGCATCACTATGAGAGTGCCTCGGAACCCAACTATCGGA
GATAAATTTGCCAGTCGCCATGGGCAGAAGGGCATTTTAAGCAGATTGTGGCCGGCTGAG
GACATGCCTTTTACTGAGAGTGGGATGGTCCCAGACATTCTGTTCAATCCCCATGGTTTT
CCATCCCGCATGACCATTGGGATGTTAATTGAGAGTATGGCCGGGAAGTCTGCAGCTTTG
CATGGTCTCTGCCATGATGCTACACCCTTCATCTTCTCAGAGGAGAACTCGGCCTTAGAA
TACTTTGGTGAGATGTTAAAGGCTGCTGGCTACAATTTCTATGGCACCGAGAGGTTATAT
AGTGGCATCAGTGGGCTAGAACTGGAAGCAGACATCTTCATAGGAGTGGTTTATTATCAG
CGCTTACGCCATATGGTCTCAGACAAATTTCAAGTAAGGACAACTGGAGCCCGAGACAGA
GTCACCAACCAGCCTATTGGGGGAAGAAATGTCCAGGGTGGAATCCGTTTTGGGGAGATG
GAACGGGATGCGCTTTTAGCTCATGGTACATCTTTTCTCCTTCATGACCGCCTCTTCAAC
TGCTCAGATCGGTCGGTAGCCCATGTGTGTGTGAAGTGTGGCAGTTTACTCTCTCCACTG
TTGGAGAAGCCACCCCCTTCTTGGTCTGCCATGCGCAACAGAAAATACAACTGTACTCTG
TGTAGTCGCAGTGACACTATCGATACTGTTTCTGTGCCTTATGTTTTTCGGTATTTTGTA
GCTGAACTGGCAGCTATGAACATCAAAGTGAAACTGGATGTTGTTTAA
Enzyme 16 GenBank Gene ID AC012442 Link Image
Enzyme 16 GeneCard ID POLR1B Link Image
Enzyme 16 GenAtlas ID POLR1B Link Image
Enzyme 16 HGNC ID HGNC:20454 Link Image
Enzyme 16 Chromosome Location 2
Enzyme 16 Locus 2q13
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Miller G, Panov KI, Friedrich JK, Trinkle-Mulcahy L, Lamond AI, Zomerdijk JC: hRRN3 is essential in the SL1-mediated recruitment of RNA Polymerase I to rRNA gene promoters. EMBO J. 2001 Mar 15;20(6):1373-82. [PubMed Link Image]
  4. Panov KI, Panova TB, Gadal O, Nishiyama K, Saito T, Russell J, Zomerdijk JC: RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor. Mol Cell Biol. 2006 Jul;26(14):5436-48. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6019
Enzyme 17 Name DNA-directed RNA polymerase III subunit RPC7
Enzyme 17 Synonyms
  1. RNA polymerase III subunit C7
  2. DNA-directed RNA polymerase III subunit G
  3. RNA polymerase III 32 kDa subunit
  4. RPC32
Enzyme 17 Gene Name POLR3G
Enzyme 17 Protein Sequence >DNA-directed RNA polymerase III subunit RPC7
MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLAL
KQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAG
PKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDD
DAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDEATY
Enzyme 17 Number of Residues 223
Enzyme 17 Molecular Weight 25914.3
Enzyme 17 Theoretical pI 4.26
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Involved in DNA-directed RNA polymerase activity
Enzyme 17 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the RPC3/POLR3C-RPC6/POLR3F- RPC7/POLR3G subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway
Enzyme 17 Pathways
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function Not Available
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 115529475 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O15318 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name RPC7_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >672 bp
ATGGCTGGGAATAAAGGAAGAGGACGTGCTGCTTATACCTTTAATATTGAGGCTGTTGGA
TTTAGCAAAGGTGAAAAGTTACCTGATGTAGTGTTGAAACCACCCCCACTATTTCCTGAT
ACAGATTATAAACCAGTGCCACTGAAAACAGGAGAAGGTGAAGAATATATGCTGGCTTTG
AAACAGGAGTTGAGAGAAACAATGAAAAGAATGCCTTATTTTATTGAAACACCTGAAGAA
AGACAAGATATTGAAAGGTATAGTAAAAGATACATGAAGGTATACAAGGAAGAATGGATA
CCAGATTGGAGAAGACTTCCAAGAGAGATGATGCCAAGAAATAAATGTAAAAAAGCAGGC
CCAAAACCCAAAAAGGCAAAAGACGCAGGCAAAGGCACACCACTCACTAATACTGAAGAT
GTGTTGAAAAAAATGGAGGAATTGGAAAAAAGAGGTGATGGTGAAAAATCAGATGAGGAA
AATGAAGAGAAAGAAGGAAGCAAAGAGAAAAGTAAAGAAGGTGATGATGACGATGACGAT
GATGCCGCAGAACAGGAGGAATATGATGAAGAAGAGCAAGAAGAGGAAAATGACTACATT
AATTCATACTTTGAAGATGGAGATGATTTTGGCGCAGACAGTGATGACAACATGGATGAG
GCAACCTATTAG
Enzyme 17 GenBank Gene ID NM_006467.2 Link Image
Enzyme 17 GeneCard ID POLR3G Link Image
Enzyme 17 GenAtlas ID POLR3G Link Image
Enzyme 17 HGNC ID HGNC:30075 Link Image
Enzyme 17 Chromosome Location 5
Enzyme 17 Locus 5q14.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Wang Z, Roeder RG: Three human RNA polymerase III-specific subunits form a subcomplex with a selective function in specific transcription initiation. Genes Dev. 1997 May 15;11(10):1315-26. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  4. 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]
  5. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed Link Image]
  8. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6031
Enzyme 18 Name DNA-directed RNA polymerase I subunit RPA49
Enzyme 18 Synonyms
  1. RNA polymerase I subunit A49
  2. DNA-directed RNA polymerase I subunit E
  3. RNA polymerase I-associated factor 1
  4. RNA polymerase I-associated factor 53
Enzyme 18 Gene Name POLR1E
Enzyme 18 Protein Sequence >DNA-directed RNA polymerase I subunit RPA49
MYQASAVSLLPRDIPSCHSPSPGFSHLPTSSSQLAPDLLQFPLGQDPSFLAIPILTLPPS
DSLVPPYIVWYIVWPSALISFLGCTLTVQFSNGKLQSPGNMRFTLYENKDSTNPRKRNQR
ILAAETDRLSYVGNNFGTGALKCNTLCRHFVGILNKTSGQMEVYDAELFNMQPLFSDVSV
ESELALESQTKTYREKMDSCIEAFGTTKQKRALNTRRMNRVGNESLNRAVAKAAETIIDT
KGVTALVSDAIHNDLQDDSLYLPPCYDDAAKPEDVYKFEDLLSPAEYEALQSPSEAFRNV
TSEEILKMIEENSHCTFVIEALKSLPSDVESRDRQARCIWFLDTLIKFRAHRVVKRKSAL
GPGVPHIINTKLLKHFTCLTYNNGRLRNLISDSMKAKITAYVIILALHIHDFQIDLTVLQ
RDLKLSEKRMMEIAKAMRLKISKRRVSVAAGSEEDHKLGTLSLPLPPAQTSDRLAKRRKI
T
Enzyme 18 Number of Residues 481
Enzyme 18 Molecular Weight 53961.4
Enzyme 18 Theoretical pI 8.74
Enzyme 18 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 18 General Function Involved in DNA binding
Enzyme 18 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Appears to be involved in the formation of the initiation complex at the promoter by mediating the interaction between Pol I and UBTF/UBF
Enzyme 18 Pathways
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 21749630 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9GZS1 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name RPA49_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1446 bp
ATGTACCAGGCCTCTGCTGTCAGCCTCCTTCCGCGAGACATTCCCTCCTGTCACAGCCCC
TCCCCAGGGTTCTCCCACCTCCCTACCTCCTCTTCTCAGCTGGCCCCGGATCTCCTCCAG
TTCCCTTTGGGTCAGGACCCGAGCTTCCTTGCCATCCCCATTCTGGCACTCCCTCCCAGT
GACAGTCTAGTCCCACCGTACATTGTGTGGTACATTGTGTGGCCTTCTGCTCTCATCTCA
TTCTTGGGCTGCACTCTTACAGTCCAGTTCTCCAACGGGAAGCTACAGAGTCCAGGCAAC
ATGCGCTTTACCTTGTATGAGAACAAAGATTCCACCAACCCCAGGAAGAGGAATCAACGG
ATCCTGGCAGCTGAAACAGATAGGCTCTCCTATGTGGGAAACAATTTTGGGACTGGAGCC
CTCAAATGCAACACTTTGTGCAGGCACTTTGTGGGAATTTTGAACAAGACCTCTGGCCAA
ATGGAAGTATATGATGCTGAATTGTTCAACATGCAGCCACTATTTTCAGATGTATCAGTC
GAGAGTGAACTGGCGCTAGAGAGTCAGACCAAAACTTACAGAGAAAAGATGGATTCTTGT
ATTGAAGCCTTTGGTACCACCAAACAGAAGCGAGCTCTGAACACCAGGAGAATGAACAGA
GTTGGCAATGAATCTTTGAATCGTGCAGTGGCTAAAGCTGCAGAGACTATCATTGATACG
AAGGGTGTGACTGCTCTGGTCAGCGATGCTATCCACAATGACTTGCAAGATGACTCCCTC
TACCTTCCTCCCTGCTATGATGATGCAGCCAAGCCTGAAGACGTGTATAAATTTGAAGAT
CTTCTTTCCCCTGCGGAGTATGAAGCTCTTCAGAGCCCATCTGAAGCTTTCAGGAACGTC
ACGTCAGAAGAAATACTGAAGATGATTGAGGAGAACAGCCATTGCACCTTTGTCATAGAA
GCGTTGAAGTCTTTGCCATCAGATGTGGAGAGCCGAGACCGCCAGGCCCGATGCATATGG
TTTCTGGATACCCTCATCAAATTTCGAGCTCATAGGGTAGTTAAGCGGAAAAGTGCTCTG
GGACCTGGAGTTCCCCACATCATCAACACCAAACTGCTGAAGCACTTTACTTGCTTGACC
TACAACAATGGCAGATTACGGAACTTAATTTCGGATTCTATGAAGGCGAAGATTACCGCA
TATGTGATCATACTTGCCTTGCACATACATGACTTCCAAATTGACCTGACAGTGTTACAG
AGGGACTTGAAGCTCAGTGAGAAAAGGATGATGGAGATAGCCAAAGCCATGAGGCTGAAG
ATCTCCAAAAGAAGGGTGTCTGTGGCCGCCGGCAGTGAAGAAGATCACAAACTGGGCACC
CTGTCCCTCCCGCTGCCTCCAGCCCAGACCTCAGACCGCCTGGCAAAGCGGAGGAAGATT
ACCTAG
Enzyme 18 GenBank Gene ID AK091294 Link Image
Enzyme 18 GeneCard ID POLR1E Link Image
Enzyme 18 GenAtlas ID POLR1E Link Image
Enzyme 18 HGNC ID HGNC:17631 Link Image
Enzyme 18 Chromosome Location 9
Enzyme 18 Locus 9p13.2
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Panov KI, Panova TB, Gadal O, Nishiyama K, Saito T, Russell J, Zomerdijk JC: RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor. Mol Cell Biol. 2006 Jul;26(14):5436-48. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6033
Enzyme 19 Name 6-phosphofructokinase, liver type
Enzyme 19 Synonyms
  1. Phosphofructo-1-kinase isozyme B
  2. PFK-B
  3. Phosphofructokinase 1
  4. Phosphohexokinase
Enzyme 19 Gene Name PFKL
Enzyme 19 Protein Sequence >6-phosphofructokinase, liver type
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVE
GGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDG
SLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDS
ALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWE
NFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQ
RGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQK
AMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRS
AVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESI
VENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLG
SDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFN
IHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGH
LQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFS
PVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
Enzyme 19 Number of Residues 780
Enzyme 19 Molecular Weight 85017.8
Enzyme 19 Theoretical pI 7.54
Enzyme 19 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 metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • 6-phosphofructokinase complex
  • cell part
  • cytoplasm
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 19 General Function Involved in 6-phosphofructokinase activity
Enzyme 19 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 19 Pathways
Enzyme 19 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 35431 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P17858 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name K6PL_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 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 19 GenBank Gene ID X15573 Link Image
Enzyme 19 GeneCard ID PFKL Link Image
Enzyme 19 GenAtlas ID PFKL Link Image
Enzyme 19 HGNC ID HGNC:8876 Link Image
Enzyme 19 Chromosome Location 2
Enzyme 19 Locus 21q22.3
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6035
Enzyme 20 Name DNA-directed RNA polymerase III subunit RPC8
Enzyme 20 Synonyms
  1. RNA polymerase III subunit C8
  2. DNA-directed RNA polymerase III subunit H
  3. RNA polymerase III subunit 22.9 kDa subunit
  4. RPC22.9
Enzyme 20 Gene Name POLR3H
Enzyme 20 Protein Sequence >DNA-directed RNA polymerase III subunit RPC8
MFVLVEMVDTVRIPPWQFERKLNDSIAEELNKKLANKVVYNVGLCICLFDITKLEDAYVF
PGDGASHTKVHFRCVVFHPFLDEILIGKIKGCSPEGVHVSLGFFDDILIPPESLQQPAKF
DEAEQVWVWEYETEEGAHDLYMDTGEEIRFRVVDESFVDTSPTGPSSADATTSSEELPKK
EAPYTLVGSISEPGLGLLSWWTSN
Enzyme 20 Number of Residues 204
Enzyme 20 Molecular Weight 22917.7
Enzyme 20 Theoretical pI 4.21
Enzyme 20 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 20 General Function Involved in DNA-directed RNA polymerase activity
Enzyme 20 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway
Enzyme 20 Pathways
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 65301161 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9Y535 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name RPC8_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >615 bp
ATGTTCGTCCTGGTGGAAATGGTGGACACCGTCCGGATCCCCCCTTGGCAGTTTGAGAGG
AAGCTCAACGACTCCATTGCCGAGGAGCTGAACAAGAAGTTGGCCAACAAGGTCGTGTAC
AACGTGGGACTCTGCATTTGTCTGTTTGATATCACCAAACTGGAGGATGCCTATGTATTC
CCTGGGGATGGCGCATCACACACCAAAGTCCATTTTCGCTGCGTGGTGTTTCATCCATTC
CTAGATGAGATTCTCATTGGGAAGATCAAAGGCTGCAGCCCAGAAGGAGTGCACGTCTCT
CTAGGCTTCTTCGATGACATTCTCATCCCCCCAGAGTCACTGCAGCAGCCAGCCAAGTTC
GACGAAGCGGAGCAGGTGTGGGTGTGGGAGTACGAGACGGAGGAAGGAGCACACGACCTC
TACATGGACACCGGCGAGGAGATCCGCTTCCGGGTGGTGGACGAGAGCTTTGTTGACACG
TCCCCCACAGGGCCCAGCTCAGCAGATGCCACCACTTCCAGTGAGGAGCTGCCAAAGAAG
GAGGCTCCGTACACGCTTGTGGGATCCATCAGTGAGCCAGGCCTGGGCCTTCTCTCCTGG
TGGACCAGCAACTAG
Enzyme 20 GenBank Gene ID NM_001018050.2 Link Image
Enzyme 20 GeneCard ID POLR3H Link Image
Enzyme 20 GenAtlas ID POLR3H Link Image
Enzyme 20 HGNC ID HGNC:30349 Link Image
Enzyme 20 Chromosome Location 2
Enzyme 20 Locus 22q13.2
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  4. 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed Link Image]
  7. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6036
Enzyme 21 Name DNA-directed RNA polymerase III subunit RPC10
Enzyme 21 Synonyms
  1. RNA polymerase III subunit C10
  2. DNA-directed RNA polymerase III subunit K
  3. RNA polymerase III 12.5 kDa subunit
  4. RPC12.5
  5. RNA polymerase III subunit C11
  6. HsC11p
  7. RPC11
  8. hRPC11
Enzyme 21 Gene Name POLR3K
Enzyme 21 Protein Sequence >DNA-directed RNA polymerase III subunit RPC10
MLLFCPGCGNGLIVEEGQRCHRFSCNTCPYVHNITRKVTNRKYPKLKEVDDVLGGAAAWE
NVDSTAESCPKCEHPRAYFMQLQTRSADEPMTTFYKCCNAQCGHRWRD
Enzyme 21 Number of Residues 108
Enzyme 21 Molecular Weight 12336.0
Enzyme 21 Theoretical pI 7.89
Enzyme 21 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transcription regulator activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • transcription
Component
Enzyme 21 General Function Involved in DNA binding
Enzyme 21 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway
Enzyme 21 Pathways
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 14336676 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9Y2Y1 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name RPC10_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >327 bp
ATGCTGCTGTTCTGCCCCGGCTGCGGGAACGGGCTGATCGTGGAGGAGGGACAACGCTGC
CACCGCTTCTCCTGCAACACGTGCCCCTACGTGCACAACATCACCCGCAAGGTAACAAAT
CGGAAGTACCCAAAACTGAAAGAAGTGGATGATGTGCTTGGTGGAGCAGCTGCCTGGGAG
AATGTTGACTCTACTGCAGAGTCGTGTCCCAAATGCGAACATCCTCGTGCTTACTTCATG
CAGCTTCAGACCCGCTCTGCAGATGAGCCGATGACCACCTTCTACAAGTGCTGCAATGCT
CAGTGTGGACACCGCTGGAGGGATTAG
Enzyme 21 GenBank Gene ID AE006462 Link Image
Enzyme 21 GeneCard ID POLR3K Link Image
Enzyme 21 GenAtlas ID POLR3K Link Image
Enzyme 21 HGNC ID HGNC:14121 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 16p13.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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. De Gobbi M, Viprakasit V, Hughes JR, Fisher C, Buckle VJ, Ayyub H, Gibbons RJ, Vernimmen D, Yoshinaga Y, de Jong P, Cheng JF, Rubin EM, Wood WG, Bowden D, Higgs DR: A regulatory SNP causes a human genetic disease by creating a new transcriptional promoter. Science. 2006 May 26;312(5777):1215-7. [PubMed Link Image]
  4. 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]
  5. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. 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]
  8. Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed Link Image]
  9. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6037
Enzyme 22 Name 6-phosphofructokinase, muscle type
Enzyme 22 Synonyms
  1. Phosphofructo-1-kinase isozyme A
  2. PFK-A
  3. Phosphofructokinase-M
  4. Phosphofructokinase 1
  5. Phosphohexokinase
Enzyme 22 Gene Name PFKM
Enzyme 22 Protein Sequence >6-phosphofructokinase, muscle type
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVD
GGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDG
SLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDS
ALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWE
EHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQ
RGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTK
AMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVR
STVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQ
ISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSV
GADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPF
TIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLG
HMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVF
QPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
Enzyme 22 Number of Residues 780
Enzyme 22 Molecular Weight 85181.9
Enzyme 22 Theoretical pI 8.07
Enzyme 22 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 metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • 6-phosphofructokinase complex
  • cell part
  • cytoplasm
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 22 General Function Involved in 6-phosphofructokinase activity
Enzyme 22 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 22 Pathways
Enzyme 22 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 189855 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P08237 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name K6PF_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >2343 bp
ATGACCCATGAAGAGCACCATGCAGCCAAAACCCTGGGGATTGGCAAAGCCATTGCTGTC
TTAACCTCTGGTGGAGATGCCCAAGGTATGAATGCTGCTGTCAGGGCTGTGGTTCGAGTT
GGTATCTTCACCGGTGCCCGTGTCTTCTTTGTCCATGAGGGTTATCAAGGCCTGGTGGAT
GGTGGAGATCACATCAAGGAAGCCACCTGGGAGAGCGTTTCGATGATGCTTCAGCTGGGA
GGCACGGTGATTGGAAGTGCCCGGTGCAAGGACTTTCGGGAACGAGAAGGACGACTCCGA
GCTGCCTACAACCTGGTGAAGCGTGGGATCACCAATCTCTGTGTCATTGGGGGTGATGGC
AGCCTCACTGGGGCTGACACCTTCCGTTCTGAGTGGAGTGACTTGTTGAGTGACCTCCAG
AAAGCAGGTAAGATCACAGATGAGGAGGCTACGAAGTCCAGCTACCTGAACATTGTGGGC
CTGGTTGGGTCAATTGACAATGACTTCTGTGGCACCGATATGACCATTGGCACTGACTCT
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 22 GenBank Gene ID M26066 Link Image
Enzyme 22 GeneCard ID PFKM Link Image
Enzyme 22 GenAtlas ID PFKM Link Image
Enzyme 22 HGNC ID HGNC:8877 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 12q13.3
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. 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]
  7. Raben N, Sherman JB: Mutations in muscle phosphofructokinase gene. Hum Mutat. 1995;6(1):1-6. [PubMed Link Image]
  8. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6039
Enzyme 23 Name Pyruvate kinase isozymes M1/M2
Enzyme 23 Synonyms
  1. Cytosolic thyroid hormone-binding protein
  2. CTHBP
  3. Opa-interacting protein 3
  4. OIP-3
  5. Pyruvate kinase 2/3
  6. Pyruvate kinase muscle isozyme
  7. Thyroid hormone-binding protein 1
  8. THBP1
  9. Tumor M2-PK
  10. p58
Enzyme 23 Gene Name PKM2
Enzyme 23 Protein Sequence >Pyruvate kinase isozymes M1/M2
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
Enzyme 23 Number of Residues 531
Enzyme 23 Molecular Weight 57936.4
Enzyme 23 Theoretical pI 7.94
Enzyme 23 GO Classification
Function
  • alkali metal ion binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • magnesium ion binding
  • metal ion binding
  • potassium ion binding
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 23 General Function Involved in magnesium ion binding
Enzyme 23 Specific Function Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival
Enzyme 23 Pathways
Enzyme 23 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 33286418 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID P14618 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name KPYM_HUMAN Link Image
Enzyme 23 PDB ID 1F3X Link Image
Enzyme 23 PDB File Show
Enzyme 23 3D Structure
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1596 bp
ATGTCGAAGCCCCATAGTGAAGCCGGGACTGCCTTCATTCAGACCCAGCAGCTGCACGCA
GCCATGGCTGACACATTCCTGGAGCACATGTGCCGCCTGGACATTGATTCACCACCCATC
ACAGCCCGGAACACTGGCATCATCTGTACCATTGGCCCAGCTTCCCGATCAGTGGAGACG
TTGAAGGAGATGATTAAGTCTGGAATGAATGTGGCTCGTCTGAACTTCTCTCATGGAACT
CATGAGTACCATGCGGAGACCATCAAGAATGTGCGCACAGCCACGGAAAGCTTTGCTTCT
GACCCCATCCTCTACCGGCCCGTTGCTGTGGCTCTAGACACTAAAGGACCTGAGATCCGA
ACTGGGCTCATCAAGGGCAGCGGCACTGCAGAGGTGGAGCTGAAGAAGGGAGCCACTCTC
AAAATCACGCTGGATAACGCCTACATGGAAAAGTGTGACGAGAACATCCTGTGGCTGGAC
TACAAGAACATCTGCAAGGTGGTGGAAGTGGGCAGCAAGATCTACGTGGATGATGGGCTT
ATTTCTCTCCAGGTGAAGCAGAAAGGTGCCGACTTCCTGGTGACGGAGGTGGAAAATGGT
GGCTCCTTGGGCAGCAAGAAGGGTGTGAACCTTCCTGGGGCTGCTGTGGACTTGCCTGCT
GTGTCGGAGAAGGACATCCAGGATCTGAAGTTTGGGGTCGAGCAGGATGTTGATATGGTG
TTTGCGTCATTCATCCGCAAGGCATCTGATGTCCATGAAGTTAGGAAGGTCCTGGGAGAG
AAGGGAAAGAACATCAAGATTATCAGCAAAATCGAGAATCATGAGGGGGTTCGGAGGTTT
GATGAAATCCTGGAGGCCAGTGATGGGATCATGGTGGCTCGTGGTGATCTAGGCATTGAG
ATTCCTGCAGAGAAGGTCTTCCTTGCTCAGAAGATGATGATTGGACGGTGCAACCGAGCT
GGGAAGCCTGTCATCTGTGCTACTCAGATGCTGGAGAGCATGATCAAGAAGCCCCGCCCC
ACTCGGGCTGAAGGCAGTGATGTGGCCAATGCAGTCCTGGATGGAGCCGACTGCATCATG
CTGTCTGGAGAAACAGCCAAAGGGGACTATCCTCTGGAGGCTGTGCGCATGCAGCACCTG
ATTGCCCGTGAGGCAGAGGCTGCCATCTACCACTTGCAATTATTTGAGGAACTCCGCCGC
CTGGCGCCCATTACCAGCGACCCCACAGAAGCCACCGCCGTGGGTGCCGTGGAGGCCTCC
TTCAAGTGCTGCAGTGGGGCCATAATCGTCCTCACCAAGTCTGGCAGGTCTGCTCACCAG
GTGGCCAGATACCGCCCACGTGCCCCCATCATTGCTGTGACCCGGAATCCCCAGACAGCT
CGTCAGGCCCACCTGTACCGTGGCATCTTCCCTGTGCTGTGCAAGGACCCAGTCCAGGAG
GCCTGGGCTGAGGACGTGGACCTCCGGGTGAACTTTGCCATGAATGTTGGCAAGGCCCGA
GGCTTCTTCAAGAAGGGAGATGTGGTCATTGTGCTGACCGGATGGCGCCCTGGCTCCGGC
TTCACCAACACCATGCGTGTTGTTCCTGTGCCGTGA
Enzyme 23 GenBank Gene ID NM_002654.3 Link Image
Enzyme 23 GeneCard ID PKM2 Link Image
Enzyme 23 GenAtlas ID PKM2 Link Image
Enzyme 23 HGNC ID HGNC:9021 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 15q22
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Tani K, Yoshida MC, Satoh H, Mitamura K, Noguchi T, Tanaka T, Fujii H, Miwa S: Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma. Gene. 1988 Dec 20;73(2):509-16. [PubMed Link Image]
  2. Kato H, Fukuda T, Parkison C, McPhie P, Cheng SY: Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7861-5. [PubMed Link Image]
  3. Takenaka M, Noguchi T, Sadahiro S, Hirai H, Yamada K, Matsuda T, Imai E, Tanaka T: Isolation and characterization of the human pyruvate kinase M gene. Eur J Biochem. 1991 May 23;198(1):101-6. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Ashizawa K, McPhie P, Lin KH, Cheng SY: An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate. Biochemistry. 1991 Jul 23;30(29):7105-11. [PubMed Link Image]
  8. 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]
  9. Williams JM, Chen GC, Zhu L, Rest RF: Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. Mol Microbiol. 1998 Jan;27(1):171-86. [PubMed Link Image]
  10. Garcia-Gonzalo FR, Cruz C, Munoz P, Mazurek S, Eigenbrodt E, Ventura F, Bartrons R, Rosa JL: Interaction between HERC1 and M2-type pyruvate kinase. FEBS Lett. 2003 Mar 27;539(1-3):78-84. [PubMed Link Image]
  11. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  12. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  13. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  14. Stetak A, Veress R, Ovadi J, Csermely P, Keri G, Ullrich A: Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death. Cancer Res. 2007 Feb 15;67(4):1602-8. [PubMed Link Image]
  15. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  16. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  17. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  18. Shimada N, Shinagawa T, Ishii S: Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein. Genes Cells. 2008 Mar;13(3):245-54. [PubMed Link Image]
  19. Lee J, Kim HK, Han YM, Kim J: Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription. Int J Biochem Cell Biol. 2008;40(5):1043-54. Epub 2007 Nov 29. [PubMed Link Image]
  20. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  21. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  22. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  23. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  24. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  25. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  26. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  27. Dombrauckas JD, Santarsiero BD, Mesecar AD: Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis. Biochemistry. 2005 Jul 12;44(27):9417-29. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6041
Enzyme 24 Name Pyruvate kinase isozymes R/L
Enzyme 24 Synonyms
  1. Pyruvate kinase 1
  2. R-type/L-type pyruvate kinase
  3. Red cell/liver pyruvate kinase
Enzyme 24 Gene Name PKLR
Enzyme 24 Protein Sequence >Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Enzyme 24 Number of Residues 574
Enzyme 24 Molecular Weight 61829.6
Enzyme 24 Theoretical pI 7.83
Enzyme 24 GO Classification
Function
  • alkali metal ion binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • magnesium ion binding
  • metal ion binding
  • potassium ion binding
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 24 General Function Involved in magnesium ion binding
Enzyme 24 Specific Function Plays a key role in glycolysis
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID P30613 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name KPYR_HUMAN Link Image
Enzyme 24 PDB ID 1LIU Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 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 24 GenBank Gene ID AB015983 Link Image
Enzyme 24 GeneCard ID PKLR Link Image
Enzyme 24 GenAtlas ID PKLR Link Image
Enzyme 24 HGNC ID HGNC:9020 Link Image
Enzyme 24 Chromosome Location 1
Enzyme 24 Locus 1q21
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. 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]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed Link Image]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  13. Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A: Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. J Biol Chem. 2002 Jun 28;277(26):23807-14. Epub 2002 Apr 17. [PubMed Link Image]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]
  22. 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]
  23. 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]
  24. 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]
  25. 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]
  26. van Wijk R, Huizinga EG, van Wesel AC, van Oirschot BA, Hadders MA, van Solinge WW: Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: structural implications of amino acid substitutions in PK. Hum Mutat. 2009 Mar;30(3):446-53. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6363
Enzyme 25 Name UTP--glucose-1-phosphate uridylyltransferase
Enzyme 25 Synonyms
  1. UDP-glucose pyrophosphorylase
  2. UDPGP
  3. UGPase
Enzyme 25 Gene Name UGP2
Enzyme 25 Protein Sequence >UTP--glucose-1-phosphate uridylyltransferase
MSRFVQDLSKAMSQDGASQFQEVIRQELELSVKKELEKILTTASSHEFEHTKKDLDGFRK
LFHRFLQEKGPSVDWGKIQRPPEDSIQPYEKIKARGLPDNISSVLNKLVVVKLNGGLGTS
MGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNH
CRVKIYTFNQSRYPRINKESLLPVAKDVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFI
GEGKEYIFVSNIDNLGATVDLYILNHLMNPPNGKRCEFVMEVTNKTRADVKGGTLTQYEG
KLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLD
GGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSE
KREFPTVPLVKLGSSFTKVQDYLRRFESIPDMLELDHLTVSGDVTFGKNVSLKGTVIIIA
NHGDRIDIPPGAVLENKIVSGNLRILDH
Enzyme 25 Number of Residues 508
Enzyme 25 Molecular Weight 56939.8
Enzyme 25 Theoretical pI 8.40
Enzyme 25 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 25 General Function Involved in nucleotidyltransferase activity
Enzyme 25 Specific Function Plays a central role as a glucosyl donor in cellular metabolic pathways
Enzyme 25 Pathways
Enzyme 25 Reactions
  • UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose [RN:R00289]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 112180805 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q16851 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name UGPA_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1527 bp
ATGTCGAGATTTGTACAAGATCTTAGCAAAGCAATGTCTCAAGATGGTGCTTCTCAGTTC
CAAGAAGTCATTCGGCAAGAGCTAGAATTATCTGTGAAGAAGGAACTAGAAAAAATACTC
ACCACAGCATCATCACATGAATTTGAGCACACCAAAAAAGACCTGGATGGATTTCGGAAG
CTATTTCATAGATTTTTGCAAGAAAAGGGGCCTTCTGTGGATTGGGGAAAAATCCAGAGA
CCCCCTGAAGATTCGATTCAACCCTATGAAAAGATAAAGGCCAGGGGCTTGCCTGATAAT
ATATCTTCCGTGTTGAACAAACTAGTGGTGGTGAAACTCAATGGTGGTTTGGGAACCAGC
ATGGGCTGCAAAGGCCCTAAAAGTCTGATTGGTGTGAGGAATGAGAATACCTTTCTGGAT
CTGACTGTTCAGCAAATTGAACATTTGAATAAAACCTACAATACAGATGTTCCTCTTGTT
TTAATGAACTCTTTTAACACGGATGAAGATACCAAAAAAATACTACAGAAGTACAATCAT
TGTCGTGTGAAAATCTACACTTTCAATCAAAGCAGGTACCCGAGGATTAATAAAGAATCT
TTACTTCCTGTAGCAAAGGACGTGTCTTACTCAGGGGAAAATACAGAAGCTTGGTACCCT
CCAGGTCATGGTGATATTTACGCCAGTTTCTACAACTCTGGATTGCTTGATACCTTTATA
GGAGAAGGCAAAGAGTATATTTTTGTGTCTAACATAGATAATCTGGGTGCCACAGTGGAT
CTGTATATTCTTAATCATCTAATGAACCCACCCAATGGAAAACGCTGTGAATTTGTCATG
GAAGTCACAAATAAAACACGTGCAGATGTAAAGGGCGGGACACTCACTCAATATGAAGGC
AAACTGAGACTGGTGGAAATTGCTCAAGTGCCAAAAGCACATGTAGACGAGTTCAAGTCT
GTATCAAAGTTCAAAATATTTAATACAAACAACCTATGGATTTCTCTTGCAGCAGTTAAA
AGACTGCAGGAGCAAAATGCCATTGACATGGAAATCATTGTGAATGCAAAGACTTTGGAT
GGAGGCCTGAATGTCATTCAATTAGAAACTGCAGTAGGGGCTGCCATCAAAAGTTTTGAG
AATTCTCTAGGTATTAATGTGCCAAGGAGCCGTTTTCTGCCTGTCAAAACCACATCAGAT
CTCTTGCTGGTGATGTCAAACCTCTATAGTCTTAATGCAGGATCTCTGACAATGAGTGAA
AAGCGGGAATTTCCTACAGTGCCCTTGGTTAAATTAGGCAGTTCTTTTACGAAGGTTCAA
GATTATCTAAGAAGATTTGAAAGTATACCAGATATGCTTGAATTGGATCACCTCACAGTT
TCAGGAGATGTGACATTTGGAAAAAATGTTTCATTAAAGGGAACGGTTATCATCATTGCA
AATCATGGTGACAGAATTGATATCCCACCTGGAGCAGTATTAGAGAACAAGATTGTGTCT
GGAAACCTTCGCATCTTGGACCACTGA
Enzyme 25 GenBank Gene ID BC000173 Link Image
Enzyme 25 GeneCard ID UGP2 Link Image
Enzyme 25 GenAtlas ID UGP2 Link Image
Enzyme 25 HGNC ID HGNC:12527 Link Image
Enzyme 25 Chromosome Location 2
Enzyme 25 Locus 2p14-p13
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Peng HL, Chang HY: Cloning of a human liver UDP-glucose pyrophosphorylase cDNA by complementation of the bacterial galU mutation. FEBS Lett. 1993 Aug 23;329(1-2):153-8. [PubMed Link Image]
  2. 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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Chang HY, Peng HL, Chao YC, Duggleby RG: The importance of conserved residues in human liver UDPglucose pyrophosphorylase. Eur J Biochem. 1996 Mar 1;236(2):723-8. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6368
Enzyme 26 Name UDP-N-acetylhexosamine pyrophosphorylase
Enzyme 26 Synonyms
  1. Antigen X
  2. AGX
  3. Sperm-associated antigen 2
  4. UDP-N-acetylgalactosamine pyrophosphorylase
  5. AGX-1
  6. UDP-N-acetylglucosamine pyrophosphorylase
  7. AGX-2
Enzyme 26 Gene Name UAP1
Enzyme 26 Protein Sequence >UDP-N-acetylhexosamine pyrophosphorylase
MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSS
HQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAY
PKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTK
HKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDME
QRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQ
VVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPY
VDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTT
ARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRSATNGKSETITADVNHNLKDANDVPIQ
CEISPLISYAGEGLESYVADKEFHAPLIIDENGVHELVKNGI
Enzyme 26 Number of Residues 522
Enzyme 26 Molecular Weight 58768.7
Enzyme 26 Theoretical pI 6.29
Enzyme 26 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 26 General Function Involved in nucleotidyltransferase activity
Enzyme 26 Specific Function Converts UDP and GlcNAc-1-P into UDP-GlcNAc, and UDP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P
Enzyme 26 Pathways
Enzyme 26 Reactions
  • UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine [RN:R00416]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 156627575 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q16222 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name UAP1_HUMAN Link Image
Enzyme 26 PDB ID 1JVG Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1518 bp
ATGAACATTAATGACCTCAAACTCACGTTGTCCAAAGCTGGGCAAGAGCACCTACTACGT
TTCTGGAATGAGCTTGAAGAAGCCCAACAGGTAGAACTTTATGCAGAGCTCCAGGCCATG
AACTTTGAGGAGCTGAACTTCTTTTTCCAAAAGGCCATTGAAGGTTTTAACCAGTCTTCT
CACCAAAAGAATGTGGATGCACGAATGGAACCTGTGCCTCGAGAGGTATTAGGCAGTGCT
ACAAGGGATCAAGATCAGCTCCAGGCCTGGGAAAGTGAAGGACTTTTCCAGATTTCTCAG
AATAAAGTAGCAGTTCTTCTTCTAGCTGGTGGGCAGGGGACAAGACTCGGCGTTGCATAT
CCTAAGGGGATGTATGATGTTGGTTTGCCATCCCGTAAGACACTTTTTCAGATTCAAGCA
GAGCGTATCCTGAAGCTACAGCAGGTTGCTGAAAAATATTATGGCAACAAATGCATTATT
CCATGGTATATAATGACCAGTGGCAGAACAATGGAATCTACAAAGGAGTTCTTCACCAAG
CACAAGTACTTTGGTTTAAAAAAAGAGAATGTAATCTTTTTTCAGCAAGGAATGCTCCCC
GCCATGAGTTTTGATGGGAAAATTATTTTGGAAGAGAAGAACAAAGTTTCTATGGCTCCA
GATGGGAATGGTGGTCTTTATCGGGCACTTGCAGCCCAGAATATTGTGGAGGATATGGAG
CAAAGAGGCATTTGGAGCATTCATGTCTATTGTGTTGACAACATATTAGTAAAAGTGGCA
GACCCACGGTTCATTGGATTTTGCATTCAGAAAGGAGCAGACTGTGGAGCAAAGGTGGTA
GAGAAAACGAACCCTACAGAACCAGTTGGAGTGGTTTGCCGAGTGGATGGAGTTTACCAG
GTGGTAGAATATAGTGAGATTTCCCTGGCAACAGCTCAAAAACGAAGCTCAGACGGACGA
CTGCTGTTCAATGCGGGGAACATTGCCAACCATTTCTTCACTGTACCATTTCTGAGAGAT
GTTGTCAATGTTTATGAACCTCAGTTGCAGCACCATGTGGCTCAAAAGAAGATTCCTTAT
GTGGATACCCAAGGACAGTTAATTAAGCCAGACAAACCCAATGGAATAAAGATGGAAAAA
TTTGTCTTTGACATCTTCCAGTTTGCAAAGAAGTTTGTGGTATATGAAGTATTGCGAGAA
GATGAGTTTTCCCCACTAAAGAATGCTGATAGTCAGAATGGGAAAGACAACCCTACTACT
GCAAGGCATGCTTTGATGTCCCTTCATCATTGCTGGGTCCTCAATGCAGGGGGCCATTTC
ATAGATGAAAATGGCTCTCGCCTTCCAGCAATTCCCCGCTTGAAGGATGCCAATGATGTA
CCAATCCAATGTGAAATCTCTCCTCTTATCTCCTATGCTGGAGAAGGATTAGAAAGTTAT
GTGGCAGATAAAGAATTCCATGCACCTCTAATCATCGATGAGAATGGAGTTCATGAGCTG
GTGAAAAATGGTATTTGA
Enzyme 26 GenBank Gene ID NM_003115 Link Image
Enzyme 26 GeneCard ID UAP1 Link Image
Enzyme 26 GenAtlas ID UAP1 Link Image
Enzyme 26 HGNC ID HGNC:12457 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 1q23.3
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Diekman AB, Goldberg E: Characterization of a human antigen with sera from infertile patients. Biol Reprod. 1994 May;50(5):1087-93. [PubMed Link Image]
  2. Mio T, Yabe T, Arisawa M, Yamada-Okabe H: The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism. J Biol Chem. 1998 Jun 5;273(23):14392-7. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Wang-Gillam A, Pastuszak I, Elbein AD: A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc. J Biol Chem. 1998 Oct 16;273(42):27055-7. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y: Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. EMBO J. 2001 Nov 15;20(22):6191-202. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 8075
Enzyme 27 Name Uridine-cytidine kinase 2
Enzyme 27 Synonyms
  1. UCK 2
  2. Cytidine monophosphokinase 2
  3. Testis-specific protein TSA903
  4. Uridine monophosphokinase 2
Enzyme 27 Gene Name UCK2
Enzyme 27 Protein Sequence >Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
Enzyme 27 Number of Residues 261
Enzyme 27 Molecular Weight 29298.9
Enzyme 27 Theoretical pI 6.68
Enzyme 27 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 27 General Function Involved in ATP binding
Enzyme 27 Specific Function Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine
Enzyme 27 Pathways
Enzyme 27 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 18699734 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q9BZX2 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name UCK2_HUMAN Link Image
Enzyme 27 PDB ID 1XRJ Link Image
Enzyme 27 PDB File Show
Enzyme 27 3D Structure
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >786 bp
ATGGCCGGGGACAGCGAGCAGACCCTGCAGAACCACCAGCAGCCCAACGGCGGCGAGCCC
TTCCTTATAGGCGTCAGCGGGGGAACAGCTAGCGGCAAGTCTTCCGTGTGTGCTAAGATC
GTGCAGCTCCTGGGGCAGAATGAGGTGGACTATCGCCAGAAGCAGGTGGTCATCCTGAGC
CAGGATAGCTTCTACCGTGTCCTTACCTCGGAGCAGAAGGCCAAAGCCCTGAAGGGCCAG
TTCAACTTTGACCACCCGGATGCCTTTGACAATGAACTCATTCTCAAAACACTCAAAGAA
ATCACTGAAGGGAAAACAGTCCAGATCCCCGTGTATGACTTTGTCTCCCATTCCCGGAAG
GAGGAGACAGTTACTGTCTATCCCGCAGACGTGGTGCTCTTTGAAGGGATCCTGGCCTTC
TACTCCCAGGAGGTACGAGACCTGTTCCAGATGAAGCTTTTTGTGGATACAGATGCGGAC
ACCCGGCTCTCACGCAGAGTATTAAGGGACATCAGCGAGAGAGGCAGGGATCTTGAGCAG
ATTTTATCTCAGTACATTACGTTCGTCAAGCCTGCCTTTGAGGAATTCTGCTTGCCAACA
AAGAAGTATGCTGATGTGATCATCCCTAGAGGTGCAGATAATCTGGTGGCCATCAACCTC
ATCGTGCAGCACATCCAGGACATCCTGAATGGAGGGCCCTCCAAACGGCAGACCAATGGC
TGTCTCAACGGCTACACCCCTTCACGCAAGAGGCAGGCATCGGAGTCCAGCAGCAGGCCG
CATTGA
Enzyme 27 GenBank Gene ID NM_012474.3 Link Image
Enzyme 27 GeneCard ID UCK2 Link Image
Enzyme 27 GenAtlas ID UCK2 Link Image
Enzyme 27 HGNC ID HGNC:12562 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 1q23
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 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. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F: Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase. Structure. 2004 May;12(5):751-64. [PubMed Link Image]
  9. Appleby TC, Larson G, Cheney IW, Walker H, Wu JZ, Zhong W, Hong Z, Yao N: Structure of human uridine-cytidine kinase 2 determined by SIRAS using a rotating-anode X-ray generator and a single samarium derivative. Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):278-84. Epub 2005 Feb 24. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 8876
Enzyme 28 Name CAD protein
Enzyme 28 Synonyms
  1. Glutamine-dependent carbamoyl-phosphate synthase
  2. Aspartate carbamoyltransferase
  3. Dihydroorotase
Enzyme 28 Gene Name CAD
Enzyme 28 Protein Sequence >CAD protein
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 28 Number of Residues 2225
Enzyme 28 Molecular Weight 242981.7
Enzyme 28 Theoretical pI 6.42
Enzyme 28 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • amino acid binding
  • aspartate carbamoyltransferase activity
  • binding
  • carbamoyl-phosphate synthase activity
  • carboxyl- or carbamoyltransferase activity
  • carboxylic acid binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • 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
  • nucleoside binding
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • 'de novo' pyrimidine base biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • glutamine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase metabolic process
  • pyrimidine base biosynthetic process
  • pyrimidine base metabolic process
Component
Enzyme 28 General Function Involved in hydrolase activity
Enzyme 28 Specific Function This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase)
Enzyme 28 Pathways
Enzyme 28 Reactions
  • (1) 2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate [RN:R00575]
  • (2) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
  • (3) 2 ATP + HCO3- = 2 ADP + phosphate + carbamoyl phosphate [RN:R07641]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 1228049 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P27708 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PYR1_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 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 28 GenBank Gene ID D78586 Link Image
Enzyme 28 GeneCard ID CAD Link Image
Enzyme 28 GenAtlas ID CAD Link Image
Enzyme 28 HGNC ID HGNC:1424 Link Image
Enzyme 28 Chromosome Location 2
Enzyme 28 Locus 2p22-p21
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. 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]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  5. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  6. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  13. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 9663
Enzyme 29 Name CTP synthase 2
Enzyme 29 Synonyms
  1. CTP synthetase 2
  2. UTP--ammonia ligase 2
Enzyme 29 Gene Name CTPS2
Enzyme 29 Protein Sequence >CTP synthase 2
MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFV
LNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDA
VQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFVEAFRQFQFKAKRENFCNIHV
SLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ
VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLFKWRNMADRYERLQKICS
IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQK
LCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDAD
STEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH
RFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPY
LGLLLAATGNLNAYLQQGCKLSSSDRYSDASDDSFSEPRIAELEIS
Enzyme 29 Number of Residues 586
Enzyme 29 Molecular Weight 65677.0
Enzyme 29 Theoretical pI 6.91
Enzyme 29 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
Component
Enzyme 29 General Function Involved in CTP synthase activity
Enzyme 29 Specific Function Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides
Enzyme 29 Pathways
Enzyme 29 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 9651727 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q9NRF8 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PYRG2_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1761 bp
ATGAAGTACATCCTGGTCACGGGTGGGGTCATCTCAGGCATTGGTAAAGGGATCATTGCC
AGCAGCATTGGAACGATTCTAAAATCATGTGGACTCCGAGTTACTGCCATAAAAATCGAC
CCCTATATTAACATCGATGCTGGCACTTTTTCACCTTATGAACACGGTGAAGTCTTCGTC
TTAAATGATGGTGGAGAAGTTGATTTAGACCTTGGAAATTATGAAAGATTTTTGGATATT
AATCTTTATAAAGACAACAATATCACCACGGGGAAGATATATCAGCATGTGATCAATAAA
GAGAGGCGTGGTGATTACCTGGGGAAAACAGTGCAAGTTGTCCCTCACATTACTGATGCT
GTCCAGGAGTGGGTTATGAATCAAGCCAAGGTGCCGGTGGATGGTAATAAGGAAGAGCCC
CAAATATGCGTTATTGAGCTGGGAGGCACCATTGGAGACATCGAAGGAATGCCGTTTGTG
GAGGCGTTTAGACAATTCCAGTTTAAGGCGAAAAGAGAGAATTTCTGTAATATCCACGTT
AGCCTTGTCCCACAGCTCAGTGCTACCGGAGAACAAAAAACCAAACCCACCCAAAACAGC
GTCCGCGCACTGAGGGGTTTAGGCCTGTCTCCAGATCTGATTGTCTGCCGAAGTTCAACG
CCCATTGAGATGGCCGTGAAGGAGAAGATTTCTATGTTTTGTCACGTGAACCCTGAACAG
GTCATATGTATCCATGATGTTTCTTCCACATACCGAGTTCCTGTGCTTTTAGAGGAACAA
AGCATTGTGAAATATTTTAAGGAGAGATTGCACCTGCCCATCGGTGATTCTGCAAGTAAT
TTGCTTTTTAAGTGGAGAAATATGGCTGACAGGTATGAAAGGTTACAGAAAATATGCTCC
ATAGCCCTGGTTGGCAAATACACCAAGCTCAGAGACTGCTACGCCTCTGTGTTCAAAGCC
CTGGAACACTCAGCCCTGGCCATCAACCACAAGTTGAATCTGATGTACATAGACTCCATT
GATCTGGAGAAGATCACTGAAACCGAGGACCCTGTGAAATTTCATGAAGCTTGGCAGAAG
CTATGCAAAGCTGATGGTATTCTTGTGCCTGGAGGCTTTGGAATCAGAGGAACATTGGGA
AAACTCCAGGCGATTTCTTGGGCAAGGACAAAGAAGATTCCTTTTCTGGGAGTTTGTCTT
GGGATGCAACTAGCAGTGATAGAGTTTGCAAGAAACTGCCTTAACTTGAAAGATGCTGAT
TCCACAGAGTTTAGGCCAAATGCCCCAGTTCCTCTGGTGATTGATATGCCCGAGCACAAC
CCTGGCAATTTGGGAGGAACAATGAGACTGGGAATAAGAAGAACTGTTTTCAAAACTGAA
AATTCAATATTAAGGAAACTTTATGGTGATGTTCCTTTTATAGAAGAAAGACACAGACAT
CGGTTCGAGGTAAACCCTAACCTGATCAAACAATTTGAGCAGAATGACTTAAGTTTTGTA
GGTCAGGATGTTGATGGAGACAGGATGGAAATCATTGAACTGGCAAATCATCCTTATTTT
GTTGGTGTCCAGTTCCATCCTGAGTTTTCTTCTAGGCCGATGAAGCCTTCCCCTCCGTAT
CTGGGGCTGTTACTTGCAGCAACTGGGAACCTGAATGCCTACTTGCAACAGGGTTGCAAA
CTGTCTTCCAGTGATAGATACAGTGATGCCAGTGATGACAGCTTTTCAGAGCCAAGGATA
GCTGAGTTGGAAATAAGCTGA
Enzyme 29 GenBank Gene ID AF226667 Link Image
Enzyme 29 GeneCard ID CTPS2 Link Image
Enzyme 29 GenAtlas ID CTPS2 Link Image
Enzyme 29 HGNC ID HGNC:2520 Link Image
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. van Kuilenburg AB, Meinsma R, Vreken P, Waterham HR, van Gennip AH: Identification of a cDNA encoding an isoform of human CTP synthetase. Biochim Biophys Acta. 2000 Jul 24;1492(2-3):548-52. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Han GS, Sreenivas A, Choi MG, Chang YF, Martin SS, Baldwin EP, Carman GM: Expression of Human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A. J Biol Chem. 2005 Nov 18;280(46):38328-36. Epub 2005 Sep 22. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 13093
Enzyme 30 Name Uncharacterized protein POLR3G
Enzyme 30 Synonyms
  1. Polymerase
  2. RNAIII
  3. DNA directedpolypeptide G
  4. 32kD, isoform CRA_a
Enzyme 30 Gene Name POLR3G
Enzyme 30 Protein Sequence >Uncharacterized protein POLR3G
MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLAL
KQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAG
PKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDD
DAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDEATY
Enzyme 30 Number of Residues 223
Enzyme 30 Molecular Weight 25915
Enzyme 30 Theoretical pI 4.26
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Not Available
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function Not Available
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein Not Available
Enzyme 30 UniProtKB/Swiss-Prot ID A8MTH0 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name A8MTH0_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence Not Available
Enzyme 30 GenBank Gene ID AC027323 Link Image
Enzyme 30 GeneCard ID A8MTH0 Link Image
Enzyme 30 GenAtlas ID POLR3G Link Image
Enzyme 30 HGNC ID HGNC:30075 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 13098
Enzyme 31 Name Uridine-cytidine kinase-like 1
Enzyme 31 Synonyms Not Available
Enzyme 31 Gene Name UCKL1
Enzyme 31 Protein Sequence >Uridine-cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
Enzyme 31 Number of Residues 548
Enzyme 31 Molecular Weight 61140.4
Enzyme 31 Theoretical pI 7.40
Enzyme 31 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 31 General Function Involved in ATP binding
Enzyme 31 Specific Function May contribute to UTP accumulation needed for blast transformation and proliferation
Enzyme 31 Pathways
Enzyme 31 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 57863312 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q9NWZ5 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name UCKL1_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1647 bp
ATGGCTGCGCCCCCGGCCCGCGCGGACGCTGATCCTTCGCCCACGTCGCCACCTACGGCC
CGAGACACACCAGGCCGGCAGGCTGAGAAAAGCGAGACCGCGTGCGAGGACCGCAGCAAT
GCAGAGTCCCTGGACAGGCTCCTGCCACCTGTGGGCACTGGGCGCTCTCCCCGGAAGCGG
ACCACCAGCCAGTGCAAGTCAGAGCCTCCCCTGCTGCGTACAAGCAAGCGTACCATCTAC
ACCGCCGGGCGGCCGCCCTGGTACAATGAACACGGCACGCAATCCAAAGAGGCCTTCGCC
ATCGGCTTGGGAGGCGGCAGTGCCTCTGGGAAGACCACTGTGGCCAGAATGATCATCGAG
GCCCTGGATGTGCCCTGGGTGGTCTTGCTGTCCATGGACTCCTTCTACAAGGTGCTGACT
GAGCAGCAGCAGGAACAGGCCGCACACAACAACTTCAACTTCGACCACCCAGATGCCTTT
GACTTCGACCTCATCATTTCCACCCTCAAGAAGCTGAAGCAGGGGAAGAGTGTCAAGGTG
CCCATTTATGACTTCACCACGCACAGCCGGAAGAAGGACTGGAAAACACTGTATGGTGCA
AACGTCATCATCTTTGAGGGCATCATGGCCTTTGCTGACAAGACACTGTTGGAGCTCCTG
GACATGAAGATCTTTGTGGACACAGACTCCGACATCCGCCTGGTACGGCGGCTGCGCCGG
GACATCAGTGAGCGCGGCCGGGACATCGAGGGTGTCATCAAGCAGTACAACAAGTTTGTC
AAGCCCTCCTTCGACCAGTACATCCAGCCCACCATGCGCCTGGCAGACATCGTGGTCCCC
AGAGGGAGCGGCAACACGGTGGCCATCGACCTGATTGTGCAGCACGTGCACAGCCAGCTG
GAGGAGCGTGAACTCAGCGTCAGGGCTGCGCTGGCCTCGGCACACCAGTGCCACCCGCTG
CCCCGGACGCTGAGCGTCCTGAAGAGCACGCCGCAGGTACGGGGCATGCACACCATCATC
AGGGACAAGGAGACCAGTCGCGACGAGTTCATCTTCTACTCCAAGAGACTGATGCGGCTG
CTCATCGAGCACGCGCTCTCCTTCCTGCCCTTTCAGGACTGCGTCGTACAGACCCCGCAG
GGGCAGGACTATGCGGGCAAGTGCTATGCGGGGAAGCAGATCACCGGTGTGTCCATTCTG
CGCGCCGGTGAAACCATGGAGCCCGCGCTGCGCGCTGTGTGCAAAGACGTGCGCATCGGC
ACCATCCTCATCCAGACCAACCAGCTTACCGGGGAGCCCGAGCTCCACTACCTGAGGCTG
CCCAAGGACATCAGCGATGACCACGTGATCCTCATGGACTGCACCGTGTCCACGGGCGCG
GCGGCCATGATGGCAGTGCGCGTGCTCCTGGACCACGACGTGCCTGAGGACAAGATCTTT
TTGCTGTCGCTGCTCATGGCAGAGATGGGCGTGCACTCAGTGGCCTATGCATTTCCGCGA
GTGAGAATCATCACCACGGCGGTGGACAAGCGGGTCAATGACCTTTTCCGCATCATCCCA
GGCATTGGGAACTTTGGCGACCGCTACTTTGGGACAGACGCGGTCCCCGATGGCAGTGAC
GAGGAGGAAGTGGCCTACACGGGTTAG
Enzyme 31 GenBank Gene ID NM_017859.3 Link Image
Enzyme 31 GeneCard ID UCKL1 Link Image
Enzyme 31 GenAtlas ID UCKL1 Link Image
Enzyme 31 HGNC ID HGNC:15938 Link Image
Enzyme 31 Chromosome Location 2
Enzyme 31 Locus 20q13.33
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Fortier JM, Kornbluth J: NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase. J Immunol. 2006 Jun 1;176(11):6454-63. [PubMed Link Image]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 13379
Enzyme 32 Name Ectonucleoside triphosphate diphosphohydrolase 8
Enzyme 32 Synonyms
  1. E-NTPDase 8
  2. NTPDase 8
  3. NTPDase8
Enzyme 32 Gene Name ENTPD8
Enzyme 32 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
Enzyme 32 Number of Residues 495
Enzyme 32 Molecular Weight 53903.1
Enzyme 32 Theoretical pI 4.96
Enzyme 32 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 32 General Function Involved in hydrolase activity
Enzyme 32 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 32 Pathways
Enzyme 32 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 9-29 472-492
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 110431368 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q5MY95 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name ENTP8_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1488 bp
ATGGGGCTGTCCCGGAAGGAGCAGGTCTTCTTGGCCCTGCTGGGGGCCTCGGGGGTCTCA
GGCCTCACGGCACTCATTCTCCTCCTGGTGGAGGCCACCAGCGTGCTCCTGCCCACAGAC
ATCAAGTTTGGGATCGTGTTTGATGCGGGCTCCTCCCACACGTCCCTCTTCCTGTATCAG
TGGCTGGCGAACAAGGAGAATGGCACGGGTGTGGTCAGCCAGGCCCTGGCCTGCCAGGTG
GAAGGGCCTGGAATCTCCTCCTACACTTCTAATGCTGCACAGGCTGGTGAGAGCCTGCAG
GGCTGCTTGGAGGAGGCGCTGGTGCTGATCCCAGAGGCCCAGCATCGGAAAACACCCACG
TTCCTGGGGGCCACGGCTGGCATGAGGTTGCTCAGCCGGAAGAACAGCTCTCAGGCCAGG
GACATCTTTGCAGCAGTCACCCAGGTCCTGGGCCGGTCTCCCGTGGACTTTTGGGGTGCC
GAGCTCCTGGCCGGGCAGGCCGAAGGTGCCTTTGGTTGGATCACTGTCAACTACGGCTTG
GGGACGCTGGTCAAGTACTCCTTCACTGGAGAATGGATCCAGCCTCCGGAGGAGATGCTG
GTGGGTGCCCTGGACATGGGAGGGGCCTCCACCCAGATCACGTTCGTGCCTGGGGGCCCC
ATCTTGGACAAGAGCACCCAGGCCGATTTTCGCCTCTACGGCTCCGACTACAGCGTCTAC
ACTCACAGCTACCTGTGCTTTGGACGGGACCAGATGCTGAGCAGGCTCCTCGTGGGGCTG
GTACAGAGCCGCCCGGCTGCCCTGCTCCGTCACCCGTGCTACCTCAGCGGCTACCAGACC
ACACTGGCCCTGGGCCCGCTGTATGAGTCACCCTGTGTCCACGCCACGCCCCCGCTGAGC
CTCCCCCAGAACCTCACAGTTGAAGGGACAGGCAACCCTGGAGCCTGCGTCTCAGCCATC
CGGGAACTTTTCAACTTCTCCAGCTGCCAGGGCCAGGAGGACTGCGCCTTTGACGGGGTC
TACCAGCCCCCGCTGCGGGGCCAGTTCTATGCCTTCTCCAACTTCTACTACACCTTCCAC
TTCCTGAACCTCACCTCCAGGCAGCCCCTGAGCACGGTCAACGCCACCATCTGGGAGTTT
TGCCAGAGGCCCTGGAAACTGGTGGAGGCCAGCTACCCTGGGCAGGACCGCTGGCTGCGG
GACTACTGTGCCTCAGGCCTGTACATCCTCACCCTCCTGCACGAGGGCTACGGGTTCAGC
GAGGAGACCTGGCCCAGCCTCGAGTTCCGAAAGCAGGCGGGCGGTGTGGACATTGGCTGG
ACACTGGGCTACATGCTGAACCTGACCGGGATGATCCCGGCCGATGCGCCGGCTCAGTGG
CGGGCAGAGAGCTACGGCGTCTGGGTGGCCAAAGTGGTGTTCATGGTGCTGGCCCTGGTG
GCGGTGGTGGGGGCTGCCTTGGTCCAGCTCTTCTGGTTGCAGGACTAG
Enzyme 32 GenBank Gene ID NM_001033113.1 Link Image
Enzyme 32 GeneCard ID ENTPD8 Link Image
Enzyme 32 GenAtlas ID ENTPD8 Link Image
Enzyme 32 HGNC ID HGNC:24860 Link Image
Enzyme 32 Chromosome Location 9
Enzyme 32 Locus 9q34.3
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Knowles AF, Li C: Molecular cloning and characterization of expressed human ecto-nucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) and its soluble extracellular domain. Biochemistry. 2006 Jun 13;45(23):7323-33. [PubMed Link Image]
  2. Fausther M, Lecka J, Kukulski F, Levesque SA, Pelletier J, Zimmermann H, Dranoff JA, Sevigny J: Cloning, purification, and identification of the liver canalicular ecto-ATPase as NTPDase8. Am J Physiol Gastrointest Liver Physiol. 2007 Mar;292(3):G785-95. Epub 2006 Nov 9. [PubMed Link Image]
  3. 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]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Levesque SA, Lavoie EG, Lecka J, Bigonnesse F, Sevigny J: Specificity of the ecto-ATPase inhibitor ARL 67156 on human and mouse ectonucleotidases. Br J Pharmacol. 2007 Sep;152(1):141-50. Epub 2007 Jul 2. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 15191
Enzyme 33 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 33 Synonyms Not Available
Enzyme 33 Gene Name NME7
Enzyme 33 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 33 Number of Residues 376
Enzyme 33 Molecular Weight 42492
Enzyme 33 Theoretical pI 6.44
Enzyme 33 GO Classification Not Available
Enzyme 33 General Function Nucleotide transport and metabolism
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 158254838 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID A8K3T6 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name A8K3T6_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 33 GenBank Gene ID AK290701 Link Image
Enzyme 33 GeneCard ID A8K3T6 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 15192
Enzyme 34 Name DNA-directed RNA polymerase III subunit RPC1
Enzyme 34 Synonyms
  1. RNA polymerase III subunit C1
  2. DNA-directed RNA polymerase III largest subunit
  3. DNA-directed RNA polymerase III subunit A
  4. RNA polymerase III 155 kDa subunit
  5. RPC155
  6. RNA polymerase III subunit C160
Enzyme 34 Gene Name POLR3A
Enzyme 34 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 34 Number of Residues 1390
Enzyme 34 Molecular Weight 155640.2
Enzyme 34 Theoretical pI 8.62
Enzyme 34 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 34 General Function Involved in DNA binding
Enzyme 34 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. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 39725938 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID O14802 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name RPC1_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >4173 bp
ATGGTGAAGGAGCAGTTCCGGGAGACGGATGTGGCCAAGAAAATAAGCCACATCTGTTTT
GGAATGAAGTCACCTGAGGAGATGCGCCAGCAGGCGCACATCCAAGTTGTGAGTAAGAAC
CTGTACAGCCAGGACAACCAACATGCCCCCTTGCTATATGGGGTGCTCGACCATAGGATG
GGTACGAGTGAGAAGGATCGTCCATGTGAAACCTGTGGGAAAAACTTGGCTGACTGTCTA
GGCCACTATGGGTATATCGACCTGGAGTTGCCGTGTTTTCATGTAGGGTACTTCAGAGCA
GTCATAGGCATCTTACAGATGATCTGCAAAACCTGCTGCCACATCATGCTGTCCCAAGAG
GAGAAGAAGCAGTTTCTGGACTATCTAAAGAGGCCCGGCCTGACCTACCTTCAGAAGCGA
GGACTGAAAAAGAAAATCTCTGACAAGTGCCGGAAGAAAAACATCTGCCATCACTGTGGC
GCTTTTAATGGTACCGTAAAGAAGTGTGGACTGCTGAAAATAATTCATGAGAAATACAAG
ACCAACAAAAAAGTGGTGGATCCCATTGTATCAAATTTCCTTCAGTCTTTTGAAACAGCC
ATTGAACATAATAAAGAAGTGGAGCCTCTGCTGGGAAGGGCACAGGAAAACTTGAATCCC
TTAGTAGTTCTGAATTTATTTAAACGAATCCCAGCTGAAGATGTTCCTCTACTTCTGATG
AACCCAGAAGCCGGAAAGCCGTCTGATTTGATTCTCACACGACTTTTGGTGCCTCCTTTG
TGTATCAGACCCTCCGTTGTGAGTGATTTGAAGTCTGGCACCAATGAAGATGATCTGACA
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
ATTGGTGAGCCAGGCACCCAGATGACCCTGAAGACTTTCCACTTTGCAGGTGTGGCCTCC
ATGAACATCACCCTGGGCGTGCCCCGGATTAAAGAGATCATCAACGCTTCCAAGGCCATC
AGCACTCCAATTATCACAGCACAGCTAGACAAGGATGACGACGCGGATTATGCTCGCCTC
GTGAAAGGGAGAATTGAGAAAACCCTCTTGGGAGAGATTTCCGAGTATATTGAAGAAGTG
TTTCTTCCTGATGACTGCTTTATTCTCGTCAAGCTCTCCCTGGAACGGATTAGGCTTCTG
AGACTGGAAGTGAACGCTGAGACAGTGAGATATTCCATCTGCACATCCAAGCTCCGTGTG
AAGCCCGGTGATGTGGCTGTTCATGGTGAGGCTGTGGTGTGTGTCACCCCCAGAGAGAAC
AGCAAGAGCTCCATGTACTACGTGCTGCAGTTCCTGAAAGAGGATCTCCCCAAGGTGGTG
GTGCAGGGCATTCCAGAGGTGTCCAGAGCTGTCATCCACATTGACGAGCAGAGTGGAAAG
GAGAAGTACAAGCTTCTGGTGGAAGGTGATAACCTGCGGGCAGTCATGGCCACACACGGT
GTGAAGGGCACCCGAACCACCTCCAATAACACCTATGAGGTGGAGAAAACTCTGGGCATC
GAGGCCGCCCGGACAACGATCATCAATGAAATCCAGTACACCATGGTGAACCACGGCATG
AGCATCGACAGGAGGCACGTGATGCTGCTCTCCGACCTCATGACCTACAAGGGTGAAGTC
CTGGGCATCACTAGGTTTGGCCTGGCCAAGATGAAGGAGAGTGTGCTGATGCTGGCCTCC
TTTGAGAAGACGGCTGACCATCTCTTTGACGCTGCCTACTTCGGGCAGAAGGACTCTGTG
TGTGGGGTGTCTGAGTGCATCATCATGGGAATCCCAATGAACATTGGAACCGGGCTCTTC
AAGCTGCTTCACAAGGCTGACAGGGACCCGAACCCTCCCAAGAGGCCCCTGATCTTCGAC
ACAAATGAATTCCACATCCCCCTTGTCACATAG
Enzyme 34 GenBank Gene ID NM_007055.3 Link Image
Enzyme 34 GeneCard ID POLR3A Link Image
Enzyme 34 GenAtlas ID POLR3A Link Image
Enzyme 34 HGNC ID HGNC:30074 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 10q22-q23
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 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. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. 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]
  6. Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed Link Image]
  7. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 15193
Enzyme 35 Name DNA-directed RNA polymerase I subunit RPA1
Enzyme 35 Synonyms
  1. RNA polymerase I subunit A1
  2. A190
  3. DNA-directed RNA polymerase I largest subunit
  4. DNA-directed RNA polymerase I subunit A
  5. RNA polymerase I 194 kDa subunit
  6. RPA194
Enzyme 35 Gene Name POLR1A
Enzyme 35 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 35 Number of Residues 1720
Enzyme 35 Molecular Weight 194809.6
Enzyme 35 Theoretical pI 7.03
Enzyme 35 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 35 General Function Involved in DNA binding
Enzyme 35 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 35 Pathways Not Available
Enzyme 35 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 221044078 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID O95602 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name RPA1_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >5163 bp
ATGTTGATCTCCAAGAACATGCCCTGGCGGCGGCTGCAGGGCATTTCCTTCGGGATGTAT
TCGGCTGAAGAGCTCAAGAAATTAAGTGTTAAATCCATTACGAACCCTCGATACCTGGAC
AGCCTGGGGAACCCATCGGCAAACGGCCTGTACGATTTAGCTTTGGGCCCTGCAGATTCC
AAAGAGGTGTGCTCCACCTGCGTGCAGGACTTCAGCAACTGTTCTGGGCACCTGGGCCAC
ATTGAGCTCCCACTCACAGTGTATAACCCTCTCCTCTTCGATAAGCTGTACCTGCTGCTT
CGGGGCTCTTGTTTAAACTGCCACATGCTGACTTGTCCCCGGGCCGTGATTCACCTCTTA
CTCTGCCAGCTGAGGGTTCTGGAAGTCGGGGCCCTACAAGCAGTCTACGAGCTTGAGAGA
ATTCTGAACAGGTTTCTGGAAGAAAATCCCGATCCCTCTGCCTCTGAAATTCGGGAGGAA
TTAGAACAATACACAACTGAAATTGTGCAGAACAACCTCCTGGGGTCCCAGGGCGCACAT
GTAAAGAACGTGTGTGAGAGCAAGAGCAAGCTCATTGCTCTCTTCTGGAAGGCACATATG
AATGCTAAGCGCTGTCCCCACTGCAAGACCGGGCGATCCGTTGTCCGAAAGGAACACAAC
AGCAAGTTGACTATCACGTTTCCAGCCATGGTGCACAGGACAGCTGGCCAGAAGGACTCT
GAGCCCCTGGGAATTGAGGAAGCTCAGATAGGAAAACGAGGATACTTAACACCCACCAGT
GCCCGCGAACACCTTTCTGCCCTGTGGAAGAATGAAGGATTCTTTCTGAACTACCTTTTT
TCGGGAATGGATGATGATGGTATGGAATCCAGATTCAATCCCAGTGTGTTCTTTCTAGAT
TTCTTGGTGGTGCCGCCCTCAAGGTATCGCCCAGTCAGTCGCCTAGGAGACCAGATGTTT
ACTAATGGCCAGACGGTGAACTTGCAGGCTGTCATGAAGGATGTAGTTCTGATTCGAAAA
CTTCTGGCATTGATGGCCCAAGAACAGAAGTTGCCAGAGGAAGTGGCCACACCCACTACA
GATGAGGAAAAAGACTCTTTGATTGCTATTGACCGATCCTTTTTGAGTACACTTCCAGGC
CAGTCCCTCATAGACAAACTTTACAACATTTGGATTCGCCTTCAGAGCCACGTCAATATT
GTGTTTGATAGCGAGATGGACAAACTAATGATGGACAAGTACCCAGGCATTAGGCAGATC
CTGGAGAAGAAAGAAGGCCTGTTCCGAAAACACATGATGGGAAAGCGAGTGGACTACGCT
GCGCGCTCAGTCATCTGCCCAGACATGTACATCAACACCAACGAAATTGGAATTCCCATG
GTGTTTGCCACAAAACTGACCTACCCACAGCCAGTTACCCCATGGAATGTTCAGGAACTT
AGGCAAGCGGTCATCAACGGCCCTAATGTGCACCCAGGAGCCTCCATGGTCATCAATGAG
GACGGCAGCCGCACAGCCCTGAGCGCTGTGGACATGACCCAGCGAGAGGCCGTGGCCAAG
CAGCTTCTGACCCCAGCCACGGGGGCACCTAAGCCCCAGGGGACAAAAATTGTGTGCCGG
CATGTGAAGAATGGGGACATTCTGCTACTGAACCGACAGCCCACACTGCACAGACCCTCC
ATCCAGGCCCACCGTGCCCGCATCCTGCCTGAAGAGAAAGTGCTGCGGCTCCACTATGCC
AACTGCAAGGCCTATAATGCCGACTTTGATGGAGACGAGATGAATGCCCATTTCCCCCAG
AGTGAGCTGGGCCGGGCCGAGGCCTACGTCCTGGCCTGCACTGATCAGCAGTACCTTGTT
CCCAAGGATGGCCAACCATTGGCGGGACTGATCCAGGATCACATGGTTTCAGGGGCAAGC
ATGACTACTCGGGGTTGCTTTTTCACCCGGGAGCACTATATGGAGCTGGTGTACCGAGGA
CTCACGGACAAAGTGGGGCGCGTGAAGCTCCTTTCTCCTTCCATCCTGAAGCCCTTTCCG
CTGTGGACAGGAAAACAGGTTGTGTCAACGCTGCTCATAAATATAATCCCAGAGGACCAC
ATCCCACTGAACTTATCTGGAAAGGCGAAAATCACTGGGAAAGCCTGGGTGAAGGAAACT
CCTCGATCCGTTCCTGGCTTTAACCCTGACTCGATGTGCGAGTCCCAGGTGATCATCAGG
GAAGGGGAGCTGCTCTGCGGAGTGCTGGACAAGGCGCACTATGGGAGCTCCGCCTACGGC
CTGGTCCACTGCTGCTATGAGATCTATGGAGGCGAGACCAGCGGCAAGGTTCTAACCTGC
CTGGCCCGCCTCTTCACCGCCTACCTGCAGCTCTACAGAGGCTTCACCTTGGGCGTGGAA
GACATTTTGGTGAAGCCAAAGGCAGATGTCAAGAGGCAACGTATCATTGAAGAATCCACC
CACTGCGGGCCCCAGGCTGTCAGGGCTGCATTAAACCTGCCAGAAGCCGCATCATATGAT
GAGGTCCGAGGAAAATGGCAGGATGCCCATCTGGGCAAGGACCAGAGGGATTTTAACATG
ATTGATCTGAAGTTCAAGGAGGAAGTGAACCATTACAGCAATGAGATTAACAAGGCATGC
ATGCCTTTTGGCCTACACAGACAGTTCCCAGAGAACAGCCTGCAGATGATGGTGCAGTCG
GGAGCCAAAGGTTCAACTGTGAACACGATGCAGATCTCGTGCCTGCTGGGCCAGATTGAA
CTGGAAGGTCGGAGACCCCCGCTGATGGCGTCTGGCAAGTCACTGCCCTGCTTTGAGCCT
TATGAGTTCACCCCCAGGGCTGGTGGCTTTGTCACTGGCAGGTTCCTTACCGGCATCAAA
CCTCCTGAGTTCTTCTTCCACTGCATGGCAGGACGAGAAGGCCTGGTGGACACTGCTGTG
AAAACCAGCCGCTCAGGCTATCTCCAAAGGTGCATCATCAAGCACCTAGAGGGGCTGGTC
GTGCAGTATGATCTCACGGTCCGTGACAGTGACGGCAGTGTGGTGCAGTTCCTGTATGGG
GAGGATGGCCTGGACATCCCCAAGACACAGTTCCTGCAGCCCAAGCAGTTCCCCTTCCTG
GCCAGCAACTACGAGGTGATAATGAAATCACAGCATCTCCATGAAGTTTTATCCAGAGCA
GATCCCAAAAAAGCTCTCCACCACTTCAGAGCTATCAAAAAATGGCAAAGCAAGCACCCC
AACACCCTGCTGAGAAGAGGCGCCTTCTTGAGTTATTCCCAGAAAATTCAGGAAGCTGTG
AAAGCCCTGAAACTTGAGAGTGAAAACCGCAATGGCCGCAGCCCTGGGACTCAGGAGATG
CTGAGGATGTGGTATGAGTTGGATGAGGAAAGCCGAAGGAAATACCAGAAGAAGGCGGCC
GCTTGTCCTGACCCCAGTCTGTCTGTCTGGCGTCCTGACATCTACTTTGCATCAGTGTCA
GAAACATTTGAAACAAAGGTTGATGACTACAGTCAAGAGTGGGCAGCTCAAACAGAGAAG
AGTTATGAGAAATCAGAGCTTTCTCTCGACAGGTTGAGGACCTTGCTGCAGCTGAAGTGG
CAGCGCTCACTGTGTGAGCCGGGCGAGGCTGTGGGCCTGCTGGCTGCCCAGAGCATCGGA
GAGCCCTCCACCCAGATGACCCTCAACACCTTCCACTTTGCAGGCAGAGGCGAGATGAAC
GTCACCCTGGGCATTCCAAGGTTGCGGGAGATTCTCATGGTGGCCAGCGCCAACATCAAG
ACACCCATGATGAGCGTGCCCGTGCTCAACACCAAGAAAGCCCTGAAGAGAGTGAAAAGC
CTGAAGAAGCAACTCACCAGGGTGTGCTTGGGGGAGGTGTTGCAGAAAATTGACGTCCAG
GAGTCCTTCTGTATGGAAGAAAAACAGAACAAATTCCAGGTGTACCAGCTGCGGTTTCAG
TTCCTGCCACATGCATATTACCAGCAGGAGAAGTGCCTGAGACCCGAGGACATCCTGCGC
TTCATGGAAACAAGATTCTTTAAACTTCTGATGGAATCCATCAAAAAGAAGAATAATAAA
GCATCAGCTTTCAGGAACGTAAACACTCGAAGAGCTACACAGCGGGATCTGGACAACGCT
GGGGAGTTGGGGAGGAGTCGGGGAGAGCAGGAGGGTGATGAGGAAGAGGAGGGGCACATT
GTGGATGCTGAAGCTGAGGAGGGAGACGCCGATGCCTCTGATGCCAAACGCAAGGAGAAG
CAGGAGGAGGAGGTTGATTATGAGAGTGAGGAAGAGGAGGAGAGGGAGGGCGAGGAGAAC
GACGATGAAGACATGCAGGAGGAACGAAATCCCCACAGGGAAGGTGCTCGAAAGACCCAA
GAGCAAGATGAAGAGGTGGGCTTAGGCACTGAGGAGGACCCGTCCCTTCCCGCCCTCCTG
ACGCAGCCCCGGAAACCCACCCACAGCCAGGAGCCCCAGGGGCCCGAGGCCATGGAGCGC
CGGGTCCAGGCTGTGCGTGAGATCCACCCGTTCATAGATGACTACCAGTACGACACCGAG
GAGAGCCTGTGGTGCCAGGTGACAGTGAAGCTCCCTCTGATGAAGATCAACTTTGACATG
AGCTCCCTGGTAGTATCTTTGGCCCATGGTGCCGTCATCTATGCGACCAAGGGCATCACT
CGGTGCCTCCTGAATGAAACAACCAACAATAAGAACGAGAAGGAGCTTGTGCTAAACACA
GAAGGAATCAACCTCCCAGAGCTATTCAAGTATGCAGAGGTCCTGGATCTGCGCCGCCTC
TACTCCAACGACATCCACGCCATAGCCAACACGTATGGCATTGAGGCCGCGCTGCGGGTG
ATCGAGAAGGAGATCAAGGATGTGTTTGCCGTGTATGGCATCGCGGTCGACCCTCGCCAT
CTCTCCCTGGTTGCTGATTATATGTGCTTCGAGGGTGTTTACAAGCCACTGAATCGCTTT
GGGATCCGGTCAAACTCTTCCCCGCTACAGCAGATGACATTTGAAACCAGCTTCCAGTTT
CTGAAGCAAGCCACCATGCTGGGATCCCACGATGAGCTGAGGTCTCCTTCTGCCTGCCTT
GTGGTCGGGAAGGTCGTCAGGGGCGGGACAGGCCTGTTCGAGCTCAAGCAGCCTCTGAGA
TAG
Enzyme 35 GenBank Gene ID AK302458 Link Image
Enzyme 35 GeneCard ID POLR1A Link Image
Enzyme 35 GenAtlas ID POLR1A Link Image
Enzyme 35 HGNC ID HGNC:17264 Link Image
Enzyme 35 Chromosome Location 2
Enzyme 35 Locus 2p11.2
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Panov KI, Panova TB, Gadal O, Nishiyama K, Saito T, Russell J, Zomerdijk JC: RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor. Mol Cell Biol. 2006 Jul;26(14):5436-48. [PubMed Link Image]
  5. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 15194
Enzyme 36 Name Zinc ribbon domain containing 1
Enzyme 36 Synonyms
  1. SubName: Zinc ribbon domain containing, 1
  2. SubName: Zinc ribbon domain containing, 1, isoform CRA_a
Enzyme 36 Gene Name ZNRD1
Enzyme 36 Protein Sequence >Zinc ribbon domain containing 1
MSVMDLANTCSSFQSDLDFCSDCGSVLPLPGAQDTVTCIRCGFNINVRDFEGKVVKTSVV
FHQLGTAMPMSVEEGPECQGPVVDRRCPRCGHEGMAYHTRQMRSADEGQTVFYTCTNCKF
QEKEDS
Enzyme 36 Number of Residues 126
Enzyme 36 Molecular Weight 13903.6
Enzyme 36 Theoretical pI 4.68
Enzyme 36 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • transcription regulator activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
Component
Enzyme 36 General Function Involved in nucleic acid binding
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 86197925 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q2L6J2 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name Q2L6J2_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >381 bp
ATGTCTGTCATGGACCTCGCCAATACTTGCTCCAGCTTTCAGTCGGACCTGGATTTCTGT
TCAGATTGCGGCTCGGTCCTGCCTCTGCCCGGGGCTCAGGATACGGTCACCTGTATTCGC
TGTGGCTTCAACATCAACGTTCGGGACTTTGAGGGGAAGGTTGTGAAGACTTCGGTTGTG
TTCCACCAACTGGGGACAGCCATGCCTATGTCGGTGGAGGAAGGGCCTGAGTGCCAGGGA
CCTGTGGTTGACAGGCGCTGCCCTCGATGTGGTCATGAAGGAATGGCATACCACACCAGA
CAGATGCGTTCAGCCGATGAAGGGCAAACTGTCTTCTACACCTGTACCAACTGCAAGTTC
CAGGAGAAGGAAGACTCTTGA
Enzyme 36 GenBank Gene ID AB202082 Link Image
Enzyme 36 GeneCard ID ZNRD1 Link Image
Enzyme 36 GenAtlas ID ZNRD1 Link Image
Enzyme 36 HGNC ID HGNC:13182 Link Image
Enzyme 36 Chromosome Location 6
Enzyme 36 Locus 6p21.3
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Shiina T, Ota M, Shimizu S, Katsuyama Y, Hashimoto N, Takasu M, Anzai T, Kulski JK, Kikkawa E, Naruse T, Kimura N, Yanagiya K, Watanabe A, Hosomichi K, Kohara S, Iwamoto C, Umehara Y, Meyer A, Wanner V, Sano K, Macquin C, Ikeo K, Tokunaga K, Gojobori T, Inoko H, Bahram S: Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity. Genetics. 2006 Jul;173(3):1555-70. Epub 2006 May 15. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 15195
Enzyme 37 Name DNA-directed RNA polymerases I and III subunit RPAC2
Enzyme 37 Synonyms
  1. RNA polymerases I and III subunit AC2
  2. AC19
  3. DNA-directed RNA polymerase I subunit D
  4. RNA polymerase I 16 kDa subunit
  5. RPA16
  6. RPC16
  7. hRPA19
Enzyme 37 Gene Name POLR1D
Enzyme 37 Protein Sequence >DNA-directed RNA polymerases I and III subunit RPAC2
MEEDQELERKISGLKTSMAEGERKTALEMVQAAGTDRHCVTFVLHEEDHTLGNSLRYMIM
KNPEVEFCGYTTTHPSESKINLRIQTRGTLPAVEPFQRGLNELMNVCQHVLDKFEASIKD
YKDQKASRNESTF
Enzyme 37 Number of Residues 133
Enzyme 37 Molecular Weight 15237.1
Enzyme 37 Theoretical pI 5.62
Enzyme 37 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • 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
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 37 General Function Involved in DNA-directed RNA polymerase activity
Enzyme 37 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 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 Not Available
Enzyme 37 UniProtKB/Swiss-Prot ID Q9Y2S0 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name RPAC2_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >402 bp
ATGGAAGAGGATCAGGAGCTGGAGAGAAAAATATCTGGATTGAAGACCTCAATGGCTGAA
GGCGAGAGGAAGACAGCCCTGGAAATGGTCCAGGCAGCTGGAACAGATAGACACTGTGTG
ACATTTGTATTGCACGAGGAAGACCATACCCTAGGAAATTCTCTACGTTACATGATCATG
AAGAACCCGGAAGTGGAATTTTGTGGTTACACTACGACCCATCCTTCAGAGAGCAAAATT
AATTTACGCATTCAGACTCGAGGTACCCTTCCAGCTGTTGAGCCATTTCAGAGAGGCCTG
AATGAGCTCATGAATGTCTGCCAACATGTGCTTGACAAGTTTGAGGCCAGCATAAAGGAC
TATAAGGATCAAAAAGCAAGCAGAAATGAATCCACATTCTAG
Enzyme 37 GenBank Gene ID AF077044 Link Image
Enzyme 37 GeneCard ID POLR1D Link Image
Enzyme 37 GenAtlas ID POLR1D Link Image
Enzyme 37 HGNC ID HGNC:20422 Link Image
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 13q12.2
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 15196
Enzyme 38 Name cDNA FLJ75210, highly similar to H.sapiens RNA polymerase II 140 kDa subunit (Polymerase (RNA) II (DNA directed) polypeptide B, 140kDa)
Enzyme 38 Synonyms Not Available
Enzyme 38 Gene Name POLR2B
Enzyme 38 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 38 Number of Residues 1174
Enzyme 38 Molecular Weight 133898
Enzyme 38 Theoretical pI 6.87
Enzyme 38 GO Classification Not Available
Enzyme 38 General Function Transcription
Enzyme 38 Specific Function Not Available
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function Not Available
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 158260669 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID A8K1A8 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name A8K1A8_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 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 38 GenBank Gene ID AK289823 Link Image
Enzyme 38 GeneCard ID A8K1A8 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 15197
Enzyme 39 Name DNA-directed RNA polymerase
Enzyme 39 Synonyms Not Available
Enzyme 39 Gene Name DKFZp686D10173
Enzyme 39 Protein Sequence >DNA-directed RNA polymerase
MDVLAEEFGNLTPEQLAAPIPTVEEKWRLLPAFLKVKGLVKQHIDSFNYFINVEIKKIMK
ANEKVTSDADPMWYLKYLNIYVGLPDVEESFNVTRPVSPHECRLRDMTYSAPITVDIEYT
RGSQRIIRNALPIGRMPIMLRSSNCVLTGKTPAEFAKLNECPLDPGGYFIVKGVEKVILI
QEQLSKNRIIVEADRKGAVGASVTSSTHEKKSRTNMAVKQGRFYLRHNTLSEDIPIVIIF
KAMGVESDQEIVQMIGTEEHVMAAFGPSLEECQKAQIFTQMQALKYIGNKVRRQRMWGGG
PKKTKIEEARELLASTILTHVPVKEFNFRAKCIYTAVMVRRVILAQGDNKVDDRDYYGNK
RLELAGQLLSLLFEDLFKKFNSEMKKIADQVIPKQRAAQFDVVKHMRQDQITNGMVNAIS
TGNWSLKRFKMDRQGVTQVLSRLSYISALGMMTRISSQFEKTRKVSGPRSLQPSQWGMLC
PSDTPEGEACGLVKNLALMTHITTDMEDGPIVKLASNLGVEDVNLLCGEELSYPNVFLVF
LNGNILGVIRDHKKLVNTFRLMRRAGYINEFVSISTNLTDRCVYISSDGGRLCRPYIIVK
KQKPAVTNKHMEELAQGYRNFEDFLHESLVEYLDVNEENDCNIALYEHTINKDTTHLEIE
PFTLLGVCAGLIPYPHHNQSPRNTYQCAMGKQAMGTIGYNQRNRIDTLMYLLAYPQKPMV
KTKTIELIEFEKLPAGQNATVAVMSYSGYDIEDALVLNKASLDRGFGRCLVYKNAKCTLK
RYTNQTFDKVMGPMLDAATRKPIWRHEILDADGICSPGEKVENKQVLVNKSMPTVTQIPL
EGSNVPQQPQYKDVPITYKGATDSYIEKVMISSNAEDAFLIKMLLRQTRRPEIGDKFSSR
HGQKGVCGLIVPQEDMPFCDSGICPDIIMNPHGFPSRMTVGKLIELLAGKAGVLDGRFHY
GTAFGGSKVKDVCEDLVRHGYNYLGKDYVTSGITGEPFEAYIYFGPVYYQKLKHMVLDKM
HARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCLIGYGASMLLLERLMISSDAFEVDVC
GQCGLLGYSGWCHYCKSSCHVSSLRIPYACKLLFQELQSMNIIPRLKLSKYNE
Enzyme 39 Number of Residues 1133
Enzyme 39 Molecular Weight 127818.1
Enzyme 39 Theoretical pI 8.64
Enzyme 39 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleoside binding
  • nucleotidyltransferase activity
  • ribonucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 39 General Function Involved in DNA-directed RNA polymerase activity
Enzyme 39 Specific Function Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 31873396 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q7Z3R8 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name Q7Z3R8_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 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 39 GenBank Gene ID BX537447 Link Image
Enzyme 39 GeneCard ID DKFZp686D10173 Link Image
Enzyme 39 GenAtlas ID DKFZp686D10173 Link Image
Enzyme 39 HGNC ID HGNC:30348 Link Image
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 15198
Enzyme 40 Name DNA-directed RNA polymerase III subunit RPC7-like
Enzyme 40 Synonyms
  1. RNA polymerase III subunit C7-like
  2. DNA-directed RNA polymerase III subunit G-like
Enzyme 40 Gene Name POLR3GL
Enzyme 40 Protein Sequence >DNA-directed RNA polymerase III subunit RPC7-like
MASRGGGRGRGRGQLTFNVEAVGIGKGDALPPPTLQPSPLFPPLEFRPVPLPSGEEGEYV
LALKQELRGAMRQLPYFIRPAVPKRDVERYSDKYQMSGPIDNAIDWNPDWRRLPRELKIR
VRKLQKERITILLPKRPPKTTEDKEETIQKLETLEKKEEEVTSEEDEEKEEEEEKEEEEE
EEYDEEEHEEETDYIMSYFDNGEDFGGDSDDNMDEAIY
Enzyme 40 Number of Residues 218
Enzyme 40 Molecular Weight 25333.8
Enzyme 40 Theoretical pI 4.19
Enzyme 40 GO Classification Not Available
Enzyme 40 General Function Transcription
Enzyme 40 Specific Function Not Available
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function Not Available
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 16552536 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q9BT43 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name RPC7L_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >657 bp
ATGGCCAGCCGGGGTGGGGGCCGGGGTCGTGGCCGGGGCCAGTTGACCTTCAACGTGGAG
GCCGTGGGCATTGGGAAAGGGGATGCTTTGCCCCCACCCACCCTGCAGCCTTCTCCACTC
TTCCCTCCCTTGGAGTTCCGCCCAGTACCTTTGCCCTCAGGCGAGGAAGGGGAATATGTC
CTGGCACTGAAGCAAGAGCTACGAGGAGCCATGAGGCAGCTCCCCTACTTCATCCGGCCA
GCTGTCCCCAAGAGAGATGTGGAGCGTTATTCAGACAAATATCAGATGTCAGGTCCGATT
GACAATGCCATCGATTGGAACCCTGATTGGCGGCGTCTACCCCGGGAGCTAAAGATCCGA
GTGCGGAAGCTACAGAAGGAACGGATTACAATTCTGCTCCCCAAGAGGCCCCCTAAGACC
ACAGAAGATAAGGAGGAAACAATACAGAAACTAGAGACCCTGGAGAAGAAGGAAGAAGAA
GTAACTTCAGAGGAGGATGAGGAGAAAGAAGAAGAAGAAGAGAAGGAAGAGGAGGAAGAA
GAAGAGTATGATGAAGAAGAACATGAAGAGGAAACTGATTACATCATGTCATATTTTGAC
AATGGAGAGGACTTTGGTGGTGACAGTGATGACAATATGGACGAGGCTATATACTGA
Enzyme 40 GenBank Gene ID AK056984 Link Image
Enzyme 40 GeneCard ID POLR3GL Link Image
Enzyme 40 GenAtlas ID POLR3GL Link Image
Enzyme 40 HGNC ID HGNC:28466 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 1q21.1
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 15199
Enzyme 41 Name POLR1C protein
Enzyme 41 Synonyms Not Available
Enzyme 41 Gene Name POLR1C
Enzyme 41 Protein Sequence >POLR1C protein
EMRSRVVLGEFGVRNVHTTDFPGNYSGYDDAWDQDRFEKNFRVDVVHMDENSLEFDMVGI
DAAIANAFRRILLAEVPTMAVEKVLVYNNTSIVQDEILAHRLGLIPIHADPRLFEYRNQG
DEEGTEIDTLQFRLQVRCTRNPHAAKDSSDPNELYVNHKVYTRHMTWIPLGNQADLFPEG
TIRPVHDDILIAQLRPGQEIDLLMHCVKGIGKDHAKFSPVATASYRLLPDITLLEPVEGE
AAEELSRCFSPGVIEVQEVQGKKVARVANPRLDTFSREIFRNEKLKKVVRLARVRDHYIF
SVESTGVLPPDVLVSEAIKVLMGKCRRFLDELDAVQMD
Enzyme 41 Number of Residues 338
Enzyme 41 Molecular Weight 38461.5
Enzyme 41 Theoretical pI 5.30
Enzyme 41 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • 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
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 41 General Function Involved in DNA binding
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 14198113 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q96HT3 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name Q96HT3_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1018 bp
GGAAATGCGGAGCCGCGTGGTTCTGGGGGAGTTTGGGGTTCGCAATGTCCATACTACTGA
CTTTCCCGGTAACTATTCCGGTTATGATGATGCCTGGGACCAGGACCGCTTCGAGAAGAA
TTTCCGTGTGGATGTAGTACACATGGATGAAAACTCACTGGAGTTTGACATGGTGGGAAT
TGACGCAGCCATTGCCAATGCTTTTCGACGAATTCTGCTAGCTGAGGTGCCAACTATGGC
TGTGGAGAAGGTCCTGGTGTACAATAATACATCCATTGTTCAGGATGAGATTCTTGCTCA
CCGTCTGGGGCTCATTCCCATTCATGCTGATCCCCGTCTTTTTGAGTATCGGAACCAAGG
AGATGAAGAAGGCACAGAGATAGATACTCTACAGTTTCGTCTCCAGGTCAGATGCACTCG
GAACCCCCATGCTGCTAAAGATTCCTCTGACCCCAACGAACTGTACGTGAACCACAAAGT
GTATACCAGGCATATGACATGGATCCCCCTGGGGAACCAGGCTGATCTCTTTCCAGAGGG
CACTATCCGACCAGTGCATGATGATATCCTCATCGCTCAGCTGCGGCCTGGCCAAGAAAT
TGACCTGCTCATGCACTGTGTCAAGGGCATTGGCAAAGATCATGCCAAGTTTTCACCAGT
GGCAACAGCCAGTTACAGGCTCCTGCCAGACATCACCCTGCTTGAGCCCGTGGAAGGGGA
GGCAGCTGAGGAGTTGAGCAGGTGCTTCTCACCTGGTGTTATTGAGGTGCAGGAAGTCCA
AGGTAAAAAGGTGGCCAGAGTTGCCAACCCCCGGCTGGATACCTTCAGCAGAGAAATCTT
CCGGAATGAGAAGCTAAAGAAGGTTGTGAGGCTTGCCCGGGTTCGAGATCATTATATCTT
CTCTGTTGAGTCAACGGGGGTGTTGCCACCAGATGTGCTGGTGAGTGAAGCCATCAAAGT
ACTGATGGGGAAGTGCCGGCGCTTCTTGGATGAACTAGATGCGGTTCAGATGGACTGA
Enzyme 41 GenBank Gene ID BC008118 Link Image
Enzyme 41 GeneCard ID POLR1C Link Image
Enzyme 41 GenAtlas ID POLR1C Link Image
Enzyme 41 HGNC ID HGNC:20194 Link Image
Enzyme 41 Chromosome Location 6
Enzyme 41 Locus 6p21.1
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 15200
Enzyme 42 Name Uridine kinase
Enzyme 42 Synonyms Not Available
Enzyme 42 Gene Name UCK1
Enzyme 42 Protein Sequence >Uridine kinase
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
Enzyme 42 Number of Residues 201
Enzyme 42 Molecular Weight 22760.4
Enzyme 42 Theoretical pI 6.23
Enzyme 42 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 42 General Function Involved in ATP binding
Enzyme 42 Specific Function ATP + cytidine = ADP + CMP
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964]
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 57162374 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q5JT13 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name Q5JT13_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >606 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGGTGAGCGGCGGCACTGCCAGCGGGAAGTCGACCGTGTGT
GAGAAGATCATGGAGTTGCTGGGACAGAACGAGGTGGAACAGCGGCAGCGGAAGGTGGTC
ATCCTGAGCCAGGACAGGTTCTACAAGGTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTG
AAAGGACAGTACAATTTTGACCATCCAGATGCCTTTGATAATGATTTGATGCACAGGACT
CTGAAGAACATCGTGGAGGGCAAAACGGTGGAGGTGCCGACCTATGATTTTGTGACACAC
TCAAGGTTACCAGAGACCACGGTGGTCTACCCTGCGGACGTGGTTCTGTTTGAGGGCATC
TTGGTGTTCTACAGCCAGGAGATCCGGGACATGTTCCACCTGCGCCTCTTCGTGGACACC
GACTCCGACGTCAGGCTGTCTCGAAGAGACAAAGAAGTATGCCGATGTGATCATCCCGCG
AGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGACATTCTGAA
TGGTGA
Enzyme 42 GenBank Gene ID AL358781 Link Image
Enzyme 42 GeneCard ID UCK1 Link Image
Enzyme 42 GenAtlas ID UCK1 Link Image
Enzyme 42 HGNC ID HGNC:14859 Link Image
Enzyme 42 Chromosome Location 9
Enzyme 42 Locus 9q34.13
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References Not Available
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 16437
Enzyme 43 Name cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
Enzyme 43 Synonyms Not Available
Enzyme 43 Gene Name ENTPD3
Enzyme 43 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 43 Number of Residues 529
Enzyme 43 Molecular Weight 59106
Enzyme 43 Theoretical pI 6.40
Enzyme 43 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 43 General Function Not Available
Enzyme 43 Specific Function Not Available
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein Not Available
Enzyme 43 UniProtKB/Swiss-Prot ID B2R8D0 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name B2R8D0_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence Not Available
Enzyme 43 GenBank Gene ID AK313322 Link Image
Enzyme 43 GeneCard ID B2R8D0 Link Image
Enzyme 43 GenAtlas ID Not Available
Enzyme 43 HGNC ID Not Available
Enzyme 43 Chromosome Location Not Available
Enzyme 43 Locus Not Available
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References Not Available
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 16463
Enzyme 44 Name cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
Enzyme 44 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 44 Gene Name CTPS2
Enzyme 44 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 44 Number of Residues 586
Enzyme 44 Molecular Weight 65678
Enzyme 44 Theoretical pI 6.91
Enzyme 44 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 44 General Function Nucleotide transport and metabolism
Enzyme 44 Specific Function Not Available
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571] ALL_REAC R00571
  • (other) R00573
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein Not Available
Enzyme 44 UniProtKB/Swiss-Prot ID B3KWM2 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name B3KWM2_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence Not Available
Enzyme 44 GenBank Gene ID AK125332 Link Image
Enzyme 44 GeneCard ID B3KWM2 Link Image
Enzyme 44 GenAtlas ID Not Available
Enzyme 44 HGNC ID Not Available
Enzyme 44 Chromosome Location Not Available
Enzyme 44 Locus Not Available
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References Not Available
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 16476
Enzyme 45 Name cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
Enzyme 45 Synonyms Not Available
Enzyme 45 Gene Name PKM2
Enzyme 45 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 45 Number of Residues 531
Enzyme 45 Molecular Weight 57938
Enzyme 45 Theoretical pI 7.94
Enzyme 45 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 45 General Function Carbohydrate transport and metabolism
Enzyme 45 Specific Function Not Available
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein Not Available
Enzyme 45 UniProtKB/Swiss-Prot ID B2R5N8 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name B2R5N8_HUMAN Link Image
Enzyme 45 PDB ID 1F3X Link Image
Enzyme 45 PDB File Show
Enzyme 45 3D Structure
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence Not Available
Enzyme 45 GenBank Gene ID AK312253 Link Image
Enzyme 45 GeneCard ID B2R5N8 Link Image
Enzyme 45 GenAtlas ID Not Available
Enzyme 45 HGNC ID Not Available
Enzyme 45 Chromosome Location 15
Enzyme 45 Locus 15q22
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References Not Available
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 16538
Enzyme 46 Name cDNA, FLJ93080, highly similar to Homo sapiens UDP-N-acteylglucosamine pyrophosphorylase 1 (UAP1), mRNA (UDP-N-acteylglucosamine pyrophosphorylase 1, isoform CRA_a)
Enzyme 46 Synonyms Not Available
Enzyme 46 Gene Name UAP1
Enzyme 46 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 46 Number of Residues 505
Enzyme 46 Molecular Weight 57029
Enzyme 46 Theoretical pI 6.33
Enzyme 46 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolism
  • physiological process
Component
Enzyme 46 General Function Not Available
Enzyme 46 Specific Function Not Available
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein Not Available
Enzyme 46 UniProtKB/Swiss-Prot ID B2R6R8 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name B2R6R8_HUMAN Link Image
Enzyme 46 PDB ID 1JV3 Link Image
Enzyme 46 PDB File Show
Enzyme 46 3D Structure
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence Not Available
Enzyme 46 GenBank Gene ID AK312685 Link Image
Enzyme 46 GeneCard ID B2R6R8 Link Image
Enzyme 46 GenAtlas ID Not Available
Enzyme 46 HGNC ID Not Available
Enzyme 46 Chromosome Location Not Available
Enzyme 46 Locus Not Available
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References Not Available
Enzyme 46 Metabolite References Not Available