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Human Metabolome Database Version 2.5

 

Showing metabocard for Ureidopropionic acid (HMDB00026)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-09-09 10:07:34
Accession Number HMDB00026
Secondary Accession Numbers Not Available
Common Name Ureidopropionic acid
Description Ureidopropionic acid is an intermediate in the metabolism of uracil. More specifically it is a breakdown product of dihydrouracil and is produced by the enzyme dihydropyrimidase. It is further decomposed to beta-alanine via the enzyme beta-ureidopropionase. Ureidopropionic acid is essentially a urea derivative of beta-alanine. High levels of Ureidopropionic acid are found in individuals with beta-ureidopropionase (UP) deficiency [PMID: 11675655]. Enzyme deficiencies in pyrimidine metabolism are associated with a risk for severe toxicity against the antineoplastic agent 5-fluorouracil.
Synonyms
  1. 3-Ureido-propionate
  2. 3-Ureidopropionate
  3. 3-Ureidopropionic acid
  4. Carbamoyl-b-Ala-OH
  5. N-(aminocarbonyl)-'b-Alanine
  6. N-(aminocarbonyl)-beta-Alanine
  7. N-Carbamoyl-beta-alanine
  8. Ureidopropionate
  9. Ureidopropionic acid
  10. beta-Ureidopropionate
  11. beta-Ureidopropionic acid
  12. Carbamoyl-beta-Ala-OH
  13. 3-ureidopropanoate
  14. 3-ureidopropanoic acid
  15. N-carbamoyl-b-alanine
  16. 3-(carbamoylamino)propanoic acid
  17. N-(aminocarbonyl)-b-alanine
  18. 3-(carbamoylamino)propanoate
  19. N-Carbamyl-b-alanine
  20. N-Carbamyl-beta-alanine
Chemical IUPAC Name 3-carbamoylaminopropanoic acid
Chemical Formula C4H8N2O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • urea
Biofunction
  • Component of beta-Alanine metabolism
  • Component of Pantothenate and CoA biosynthesis
  • Component of Pyrimidine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 132.118
Monoisotopic Molecular Weight 132.053497
Isomeric SMILES NC(=O)NCCC(O)=O
Canonical SMILES NC(=O)NCCC(O)=O
KEGG Compound ID C02642 Link Image
BioCyc ID 3-UREIDO-PROPIONATE Link Image
BiGG ID 40270 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00026 Link Image
Metagene Link HMDB00026 Link Image
METLIN ID 5097 Link Image
PubChem Compound 111 Link Image
PubChem Substance 10322862 Link Image
ChEBI ID 18261 Link Image
CAS Registry Number 462-88-4
InChI Identifier InChI=1/C4H8N2O3/c5-4(9)6-2-1-3(7)8/h1-2H2,(H,7,8)(H3,5,6,9)
Synthesis Reference w-Ureido carboxylic acids. (1962), 3 pp. GB 913713 19621228 CAN 58:72975 AN 1963:72975
Melting Point (Experimental) 170 oC
Experimental Water Solubility 20.9 mg/mL [BEILSTEIN] Source: PhysProp
Predicted Water Solubility 52.7 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.98 [Predicted by ALOGPS]; -1.6 [Predicted by PubChem via XLOGP]; -1.34 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location
  • Cerebrospinal Fluid
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid CSF
Value 0.0 - 0.5 uM
Age Children:1-13 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • van Kuilenburg AB, Meijer J, Dobritzsch D, Meinsma R, Duran M, Lohkamp B, Zoetekouw L, Abeling NG, van Tinteren HL, Bosch AM: Clinical, biochemical and genetic findings in two siblings with a dihydropyrimidinase deficiency. Mol Genet Metab. 2007 Jun;91(2):157-64. Epub 2007 Mar 26. [PubMed Link Image]
Biofluid Urine
Value 2.23 (1.48 - 2.81) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Sparidans RW, Bosch TM, Jorger M, Schellens JH, Beijnen JH: Liquid chromatography-tandem mass spectrometric assay for the analysis of uracil, 5,6-dihydrouracil and beta-ureidopropionic acid in urine for the measurement of the activities of the pyrimidine catabolic enzymes. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Jul 24;839(1-2):45-53. Epub 2006 Feb 28. [PubMed Link Image]
Biofluid Urine
Value 0.88 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hofmann U, Schwab M, Seefried S, Marx C, Zanger UM, Eichelbaum M, Murdter TE: Sensitive method for the quantification of urinary pyrimidine metabolites in healthy adults by gas chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 5;791(1-2):371-80. [PubMed Link Image]
Biofluid Urine
Value 0.88 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hofmann U, Schwab M, Seefried S, Marx C, Zanger UM, Eichelbaum M, Murdter TE: Sensitive method for the quantification of urinary pyrimidine metabolites in healthy adults by gas chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 5;791(1-2):371-80. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid CSF
Value 0.5 (0.0-1.0) uM
Age Children:1-13 yrs old
Sex Both
Condition Dihydropyrimidinase deficiency
Comments Not Available
References
  • van Kuilenburg AB, Meijer J, Dobritzsch D, Meinsma R, Duran M, Lohkamp B, Zoetekouw L, Abeling NG, van Tinteren HL, Bosch AM: Clinical, biochemical and genetic findings in two siblings with a dihydropyrimidinase deficiency. Mol Genet Metab. 2007 Jun;91(2):157-64. Epub 2007 Mar 26. [PubMed Link Image]
Associated Disorders
Condition References
Dihydropyrimidinase deficiency
  • van Kuilenburg AB, Meijer J, Dobritzsch D, Meinsma R, Duran M, Lohkamp B, Zoetekouw L, Abeling NG, van Tinteren HL, Bosch AM: Clinical, biochemical and genetic findings in two siblings with a dihydropyrimidinase deficiency. Mol Genet Metab. 2007 Jun;91(2):157-64. Epub 2007 Mar 26. [PubMed Link Image]
OMIM ID
  • 222748 Link Image (Dihydropyrimidinase deficiency)
Pathways
Name SMPDB Link KEGG Link
Beta-Alanine Metabolism SMP00007 Link Image map00410 Link Image
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
General References
  1. Moolenaar SH, Gohlich-Ratmann G, Engelke UF, Spraul M, Humpfer E, Dvortsak P, Voit T, Hoffmann GF, Brautigam C, van Kuilenburg AB, van Gennip A, Vreken P, Wevers RA: beta-Ureidopropionase deficiency: a novel inborn error of metabolism discovered using NMR spectroscopy on urine. Magn Reson Med. 2001 Nov;46(5):1014-7. [PubMed Link Image]
  2. Sparidans RW, Bosch TM, Jorger M, Schellens JH, Beijnen JH: Liquid chromatography-tandem mass spectrometric assay for the analysis of uracil, 5,6-dihydrouracil and beta-ureidopropionic acid in urine for the measurement of the activities of the pyrimidine catabolic enzymes. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Jul 24;839(1-2):45-53. Epub 2006 Feb 28. [PubMed Link Image]
  3. Ito S, Kawamura T, Inada M, Inoue Y, Hirao Y, Koga T, Kunizaki J, Shimizu T, Sato H: Physiologically based pharmacokinetic modelling of the three-step metabolism of pyrimidine using C-uracil as an in vivo probe. Br J Clin Pharmacol. 2005 Dec;60(6):584-93. [PubMed Link Image]
  4. Hofmann U, Schwab M, Seefried S, Marx C, Zanger UM, Eichelbaum M, Murdter TE: Sensitive method for the quantification of urinary pyrimidine metabolites in healthy adults by gas chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 5;791(1-2):371-80. [PubMed Link Image]
  5. Malet-Martino MC, Armand JP, Lopez A, Bernadou J, Beteille JP, Bon M, Martino R: Evidence for the importance of 5'-deoxy-5-fluorouridine catabolism in humans from 19F nuclear magnetic resonance spectrometry. Cancer Res. 1986 Apr;46(4 Pt 2):2105-12. [PubMed Link Image]
  6. Desmoulin F, Gilard V, Malet-Martino M, Martino R: Metabolism of capecitabine, an oral fluorouracil prodrug: (19)F NMR studies in animal models and human urine. Drug Metab Dispos. 2002 Nov;30(11):1221-9. [PubMed Link Image]
Metabolic Enzymes
  1. Dihydropyrimidinase
  2. Beta-ureidopropionase
  3. Dihydropyrimidinase-related protein 3
  4. Dihydropyrimidinase-related protein 2
  5. UPB1 protein
Enzyme 1 [top]
Enzyme 1 ID 5814
Enzyme 1 Name Dihydropyrimidinase
Enzyme 1 Synonyms
  1. DHP
  2. DHPase
  3. Dihydropyrimidine amidohydrolase
  4. Hydantoinase
Enzyme 1 Gene Name DPYS
Enzyme 1 Protein Sequence >Dihydropyrimidinase
MAAPSRLLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGAPAGLRVLDAAGKLVL
PGGIDTHTHMQFPFMGSRSIDDFHQGTKAALSGGTTMIIDFAIPQKGGSLIEAFETWRSW
ADPKVCCDYSLHVAVTWWSDQVKEEMKILVQDKGVNSFKMFMAYKDLYMVTDLELYEAFS
RCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAV
NCPLYIVHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDGTHYWNKEWHHAAHHVMGPP
LRPDPSTPDFLMNLLANDDLTTTGTDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIW
EKGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDADIVIWDPKGTRTISAKTHH
QAVNFNIFEGMVCHGVPLVTISRGKVVYEAGVFSVTAGDGKFIPRKPFAEYIYKRIKQRD
RTCTPTPVERAPYKGEVATLKSRVTKEDATAGTRKQAHP
Enzyme 1 Number of Residues 519
Enzyme 1 Molecular Weight 56629.4
Enzyme 1 Theoretical pI 7.28
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Process
Component
Enzyme 1 General Function Involved in hydrolase activity
Enzyme 1 Specific Function Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyzes the ring opening of 5,6- dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 5,6-dihydrouracil + H2O = 3-ureidopropanoate [RN:R02269]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 3608122 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q14117 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DPYS_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1560 bp
ATGGCGGCGCCCTCGCGGCTCCTGATCCGCGGGGGTCGCGTGGTCAACGATGACTTCTCG
GAGGTGGCCGACGTGCTGGTGGAGGACGGCGTGGTGCGGGCACTCGGGCACGACCTGCTG
CCTCCCGGGGGCGCTCCTGCGGGGCTGCGGGTCCTCGACGCCGCCGGCAAGCTCGTCCTG
CCCGGAGGCATCGACACACACACGCACATGCAGTTCCCCTTCATGGGCTCGCGGTCCATC
GACGACTTCCACCAGGGCACCAAGGCTGCTCTCTCAGGAGGCACCACCATGATTATTGAT
TTCGCCATTCCTCAGAAAGGTGGCTCCCTCATTGAGGCCTTCGAGACCTGGCGAAGCTGG
GCTGATCCCAAAGTTTGCTGCGACTACAGCCTTCATGTGGCAGTGACGTGGTGGAGTGAC
CAGGTTAAAGAAGAAATGAAAATCCTTGTGCAAGATAAAGGTGTTAACTCTTTCAAGATG
TTTATGGCCTATAAAGATCTGTACATGGTGACAGACCTGGAGCTGTACGAAGCCTTCTCT
CGGTGCAAGGAAATTGGAGCAATTGCCCAGGTCCATGCGGAAAATGGAGACTTAATTGCA
GAGGGAGCAAAGAAGATGTTGGCTCTGGGGATAACAGGCCCTGAGGGCCACGAGCTGTGC
CGCCCAGAGGCAGTGGAGGCAGAGGCCACGCTGAGAGCCATCACCATAGCCAGCGCTGTG
AACTGTCCTCTCTACATTGTGCATGTGATGAGCAAGTCTGCAGCTAAGGTGATAGCGGAT
GCAAGGAGAGATGGGAAGGTGGTCTATGGTGAACCCATAGCAGCCAGTCTTGGCACAGAT
GGCACTCACTACTGGAATAAAGAATGGCACCATGCAGCCCACCATGTCATGGGTCCACCT
TTGCGACCAGACCCCTCAACACCCGACTTCCTCATGAATCTGTTGGCTAATGATGATCTA
ACCACAACAGGGACTGATAACTGCACTTTCAACACCTGCCAGAAAGCTCTTGGGAAGGAT
GATTTTACCAAGATCCCCAATGGGGTGAATGGTGTTGAAGATCGGATGTCCGTAATATGG
GAAAAAGGCGTGCATAGTGGTAAAATGGATGAAAACAGATTTGTGGCAGTTACCAGCACA
AATGCAGCCAAAATTTTTAATCTCTATCCAAGAAAAGGAAGAATAGCTGTAGGATCAGAT
GCTGACATTGTTATTTGGGACCCAAAAGGCACAAGGACTATCTCAGCAAAAACTCATCAT
CAGGCTGTTAACTTCAACATTTTCGAGGGCATGGTTTGCCACGGGGTGCCCCTTGTGACT
ATTTCAAGAGGCAAAGTGGTATATGAAGCCGGAGTGTTCAGTGTCACGGCAGGAGATGGG
AAGTTTATTCCTCGAAAACCATTTGCTGAATATATTTACAAACGAATAAAGCAGCGAGAC
CGGACTTGCACACCTACCCCTGTGGAGCGTGCACCCTATAAGGGAGAAGTCGCCACACTG
AAATCCAGAGTGACAAAAGAAGATGCCACAGCAGGGACCAGGAAACAGGCCCACCCCTGA
Enzyme 1 GenBank Gene ID AB004678 Link Image
Enzyme 1 GeneCard ID DPYS Link Image
Enzyme 1 GenAtlas ID DPYS Link Image
Enzyme 1 HGNC ID HGNC:3013 Link Image
Enzyme 1 Chromosome Location 8
Enzyme 1 Locus 8q22
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Hamajima N, Matsuda K, Sakata S, Tamaki N, Sasaki M, Nonaka M: A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution. Gene. 1996 Nov 21;180(1-2):157-63. [PubMed Link Image]
  2. Hamajima N, Kouwaki M, Vreken P, Matsuda K, Sumi S, Imaeda M, Ohba S, Kidouchi K, Nonaka M, Sasaki M, Tamaki N, Endo Y, De Abreu R, Rotteveel J, van Kuilenburg A, van Gennip A, Togari H, Wada Y: Dihydropyrimidinase deficiency: structural organization, chromosomal localization, and mutation analysis of the human dihydropyrimidinase gene. Am J Hum Genet. 1998 Sep;63(3):717-26. [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]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5815
Enzyme 2 Name Beta-ureidopropionase
Enzyme 2 Synonyms
  1. BUP-1
  2. Beta-alanine synthase
  3. N-carbamoyl-beta-alanine amidohydrolase
Enzyme 2 Gene Name UPB1
Enzyme 2 Protein Sequence >Beta-ureidopropionase
MAGAEWKSLEECLEKHLPLPDLQEVKRVLYGKELRKLDLPREAFEAASREDFELQGYAFE
AAEEQLRRPRIVHVGLVQNRIPLPANAPVAEQVSALHRRIKAIVEVAAMCGVNIICFQEA
WTMPFAFCTREKLPWTEFAESAEDGPTTRFCQKLAKNHDMVVVSPILERDSEHGDVLWNT
AVVISNSGAVLGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPL
NWLMYSINGAEIIFNPSATIGALSESLWPIEARNAAIANHCFTCAINRVGTEHFPNEFTS
GDGKKAHQDFGYFYGSSYVAAPDSSRTPGLSRSRDGLLVAKLDLNLCQQVNDVWNFKMTG
RYEMYARELAEAVKSNYSPTIVKE
Enzyme 2 Number of Residues 384
Enzyme 2 Molecular Weight 43165.7
Enzyme 2 Theoretical pI 6.51
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Process
  • metabolic process
  • nitrogen compound metabolic process
Component
Enzyme 2 General Function Involved in hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Enzyme 2 Specific Function Converts N-carbamyl-beta-aminoisobutyric acid and N- carbamyl-beta-alanine to, respectively, beta-aminoisobutyric acid and beta-alanine, ammonia and carbon dioxide
Enzyme 2 Pathways
Enzyme 2 Reactions
  • N-carbamoyl-beta-alanine + H2O = beta-alanine + CO2 + NH3 [RN:R00905]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 6635205 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9UBR1 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name BUP1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1155 bp
ATGGCGGGCGCTGAGTGGAAGTCGCTGGAGGAATGCTTGGAGAAGCACCTGCCGCTCCCC
GACTTGCAGGAAGTGAAGCGCGTTCTCTATGGCAAGGAACTCAGGAAGCTTGATCTGCCC
AGGGAAGCTTTCGAAGCTGCCTCCAGAGAAGACTTTGAACTGCAGGGATATGCCTTTGAA
GCAGCGGAGGAGCAGCTGAGACGACCCCGCATTGTGCACGTGGGGCTGGTTCAGAACAGA
ATCCCCCTCCCCGCAAATGCCCCTGTGGCAGAACAGGTCTCTGCCCTTCATAGACGCATA
AAGGCTATCGTAGAGGTGGCTGCAATGTGTGGAGTCAACATCATCTGTTTCCAGGAAGCA
TGGACTATGCCCTTTGCCTTCTGTACGAGAGAGAAGCTTCCTTGGACAGAATTTGCTGAG
TCAGCAGAGGATGGGCCCACCACCAGATTCTGTCAGAAGCTGGCGAAGAACCATGACATG
GTGGTGGTGTCTCCCATCCTGGAACGAGACAGCGAGCATGGGGATGTTTTGTGGAATACA
GCCGTGGTGATCTCCAATTCCGGAGCAGTCCTGGGAAAGACCAGGAAAAACCACATCCCC
AGAGTGGGTGATTTCAACGAGTCAACTTACTACATGGAGGGAAACCTGGGCCACCCCGTG
TTCCAGACGCAGTTCGGAAGGATCGCGGTGAACATTTGCTACGGGCGGCACCACCCCCTC
AACTGGCTTATGTACAGCATCAACGGGGCTGAGATCATCTTCAACCCCTCGGCCACGATA
GGAGCACTCAGCGAGTCCCTGTGGCCCATCGAGGCCAGAAACGCAGCCATTGCCAATCAC
TGCTTCACCTGCGCCATCAATCGAGTGGGCACCGAGCACTTCCCGAACGAGTTTACCTCG
GGAGATGGAAAGAAAGCTCACCAGGACTTTGGCTACTTTTATGGCTCGAGCTATGTGGCA
GCCCCTGACAGCAGCCGGACTCCTGGGCTGTCCCGTAGCCGGGATGGACTGCTAGTTGCT
AAGCTCGACCTAAACCTCTGCCAGCAGGTGAATGATGTCTGGAACTTCAAGATGACGGGC
AGGTATGAGATGTACGCACGGGAGCTCGCCGAAGCTGTCAAGTCCAACTACAGCCCCACC
ATCGTGAAAGAGTAG
Enzyme 2 GenBank Gene ID AB013885 Link Image
Enzyme 2 GeneCard ID UPB1 Link Image
Enzyme 2 GenAtlas ID UPB1 Link Image
Enzyme 2 HGNC ID HGNC:16297 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 22q11.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Vreken P, van Kuilenburg AB, Hamajima N, Meinsma R, van Lenthe H, Gohlich-Ratmann G, Assmann BE, Wevers RA, van Gennip AH: cDNA cloning, genomic structure and chromosomal localization of the human BUP-1 gene encoding beta-ureidopropionase. Biochim Biophys Acta. 1999 Oct 28;1447(2-3):251-7. [PubMed Link Image]
  2. Sakamoto T, Sakata SF, Matsuda K, Horikawa Y, Tamaki N: Expression and properties of human liver beta-ureidopropionase. J Nutr Sci Vitaminol (Tokyo). 2001 Apr;47(2):132-8. [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. 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. van Kuilenburg AB, Meinsma R, Beke E, Assmann B, Ribes A, Lorente I, Busch R, Mayatepek E, Abeling NG, van Cruchten A, Stroomer AE, van Lenthe H, Zoetekouw L, Kulik W, Hoffmann GF, Voit T, Wevers RA, Rutsch F, van Gennip AH: beta-Ureidopropionase deficiency: an inborn error of pyrimidine degradation associated with neurological abnormalities. Hum Mol Genet. 2004 Nov 15;13(22):2793-801. Epub 2004 Sep 22. [PubMed Link Image]
Enzyme 2 Metabolite References
  1. Moolenaar SH, Gohlich-Ratmann G, Engelke UF, Spraul M, Humpfer E, Dvortsak P, Voit T, Hoffmann GF, Brautigam C, van Kuilenburg AB, van Gennip A, Vreken P, Wevers RA: beta-Ureidopropionase deficiency: a novel inborn error of metabolism discovered using NMR spectroscopy on urine. Magn Reson Med. 2001 Nov;46(5):1014-7. [PubMed Link Image]
Enzyme 3 [top]
Enzyme 3 ID 8498
Enzyme 3 Name Dihydropyrimidinase-related protein 3
Enzyme 3 Synonyms
  1. DRP-3
  2. Collapsin response mediator protein 4
  3. CRMP-4
  4. Unc-33-like phosphoprotein 1
  5. ULIP-1
Enzyme 3 Gene Name DPYSL3
Enzyme 3 Protein Sequence >Dihydropyrimidinase-related protein 3
MSYQGKKNIPRITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEA
NGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAY
EKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYKDLYQVSNTE
LYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAI
TIASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAA
FVTSPPLSPDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEE
RMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDAVKIV
SAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSDYVYK
RIKARRKMADLHAVPRGMYDGPVFDLTTTPKGGTPAGSARGSPTRPNPPVRNLHQSGFSL
SGTQVDEGVRSASKRIVAPPGGRSNITSLS
Enzyme 3 Number of Residues 570
Enzyme 3 Molecular Weight 61962.8
Enzyme 3 Theoretical pI 6.45
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Process
Component
Enzyme 3 General Function Involved in hydrolase activity
Enzyme 3 Specific Function Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1330242 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q14195 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name DPYL3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1713 bp
ATGTCCTACCAAGGCAAGAAGAACATCCCGCGGATCACGAGTGACCGTCTCCTTATCAAG
GGAGGCAGAATCGTCAATGATGATCAGTCCTTTTATGCTGATATTTACATGGAAGATGGC
TTAATAAAACAAATTGGAGACAATCTGATTGTTCCTGGAGGAGTGAAGACCATTGAAGCC
AATGGGAAGATGGTGATCCCTGGAGGCATCGATGTCCATACTCACTTCCAGATGCCATAT
AAGGGAATGACCACAGTAGATGACTTCTTCCAAGGGACAAAGGCGGCCTTAGCAGGTGGC
ACCACCATGATCATTGACCATGTGGTGCCTGAGCCTGAGTCCAGCCTGACTGAGGCCTAT
GAGAAATGGAGAGAGTGGGCTGATGGGAAGAGTTGCTGTGACTATGCCCTGCATGTGGAC
ATCACCCACTGGAATGACAGCGTCAAGCAGGAAGTGCAGAACCTCATCAAGGACAAAGGG
GTTAACTCCTTCATGGTTTATATGGCTTATAAGGATTTGTATCAAGTATCTAACACAGAG
CTCTATGAGATCTTCACCTGCCTGGGAGAGCTGGGGGCCATTGCTCAAGTTCATGCTGAG
AATGGGGATATCATTGCCCAGGAGCAAACCCGCATGTTGGAAATGGGGATAACTGGCCCA
GAAGGCCATGTACTGAGCAGGCCAGAAGAGCTGGAAGCTGAGGCTGTGTTCCGTGCCATC
ACCATTGCCAGCCAAACCAATTGCCCTCTCTACGTCACAAAGGTCATGAGCAAGAGTGCA
GCTGACCTCATCTCACAAGCCAGGAAAAAAGGAAATGTAGTCTTTGGTGAGCCCATCACT
GCCAGCCTCGGCATAGATGGAACCCATTATTGGAGCAAGAACTGGGCCAAGGCGGCTGCA
TTTGTGACATCCCCACCCCTGAGCCCTGACCCAACTACTCCGGACTACATCAACTCCTTG
CTGGCCAGCGGGGATCTGCAGCTATCTGGGAGTGCCCACTGCACCTTCAGCACTGCCCAG
AAAGCAATTGGGAAGGACAACTTCACAGCCATTCCTGAGGGCACCAATGGTGTGGAGGAG
CGGATGTCTGTCATCTGGGACAAGGCTGTGGCCACAGGGAAAATGGACGAAAACCAGTTC
GTGGCTGTGACAAGCACAAACGCTGCCAAGATCTTCAACCTGTATCCCCGCAAGGGAAGA
ATATCTGTGGGTTCTGACAGCGACCTCGTCATCTGGGATCCAGATGCTGTGAAGATCGTC
TCTGCCAAGAACCACCAGTCTGCGGCAGAGTACAACATCTTTGAAGGGATGGAGCTGCGC
GGGGCTCCTCTGGTTGTCATCTGCCAGGGCAAGATCATGCTGGAAGATGGCAACCTGCAC
GTGACCCAGGGGGCTGGCCGCTTCATACCCTGCAGCCCGTTCTCCGACTATGTCTACAAG
CGCATTAAAGCACGGAGGAAGATGGCAGACCTGCATGCCGTCCCAAGGGGCATGTACGAT
GGGCCTGTGTTTGACCTGACCACCACCCCCAAAGGTGGCACCCCCGCAGGCTCTGCTCGG
GGCTCTCCTACTCGGCCGAACCCACCTGTGAGGAATCTTCATCAGTCGGGATTTAGCCTG
TCAGGCACCCAAGTGGATGAGGGGGTTCGCTCAGCCAGCAAGCGCATCGTGGCCCCCCCA
GGCGGCCGTTCTAATATCACATCTCTGAGTTAA
Enzyme 3 GenBank Gene ID D78014 Link Image
Enzyme 3 GeneCard ID DPYSL3 Link Image
Enzyme 3 GenAtlas ID DPYSL3 Link Image
Enzyme 3 HGNC ID HGNC:3015 Link Image
Enzyme 3 Chromosome Location 5
Enzyme 3 Locus 5q32
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Hamajima N, Matsuda K, Sakata S, Tamaki N, Sasaki M, Nonaka M: A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution. Gene. 1996 Nov 21;180(1-2):157-63. [PubMed Link Image]
  2. Gaetano C, Matsuo T, Thiele CJ: Identification and characterization of a retinoic acid-regulated human homologue of the unc-33-like phosphoprotein gene (hUlip) from neuroblastoma cells. J Biol Chem. 1997 May 2;272(18):12195-201. [PubMed Link Image]
  3. 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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 8721
Enzyme 4 Name Dihydropyrimidinase-related protein 2
Enzyme 4 Synonyms
  1. DRP-2
  2. Collapsin response mediator protein 2
  3. CRMP-2
  4. N2A3
  5. Unc-33-like phosphoprotein 2
  6. ULIP-2
Enzyme 4 Gene Name DPYSL2
Enzyme 4 Protein Sequence >Dihydropyrimidinase-related protein 2
MSYQGKKNIPRITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEA
HSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAF
DQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDCQ
IYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAI
TIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAA
FVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEE
RMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTI
SAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFPDFVYK
RIKARSRLAELRGVPRGLYDGPVCEVSVTPKTVTPASSAKTSPAKQQAPPVRNLHQSGFS
LSGAQIDDNIPRRTTQRIVAPPGGRANITSLG
Enzyme 4 Number of Residues 572
Enzyme 4 Molecular Weight 62293.1
Enzyme 4 Theoretical pI 6.33
Enzyme 4 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Process
Component
Enzyme 4 General Function Nucleotide transport and metabolism
Enzyme 4 Specific Function Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 6467213 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q16555 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DPYL2_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1719 bp
ATGTCTTATCAGGGGAAGAAAAATATTCCACGCATCACGAGCGATCGTCTTCTGATCAAA
GGAGGTAAAATTGTTAATGATGACCAGTCGTTCTATGCAGACATATACATGGAAGATGGG
TTGATCAAGCAAATAGGAGAAAATCTGATTGTGCCAGGAGGAGTGAAGACCATCGAGGCC
CACTCCCGGATGGTGATCCCCGGAGGAATTGACGTCCACACTCGTTTCCAGATGCCTGAT
CAGGGAATGACGTCTGCTGATGATTTCTTCCAAGGAACCAAGGCGGCCCTGGCTGGGGGA
ACCACTATGATCATTGACCACGTTGTTCCTGAGCCTGGGACAAGCCTGCTCGCTGCCTTT
GACCAGTGGAGGGAATGGGCCGACAGCAAGTCCTGCTGTGACTACTCTCTGCATGTGGAC
ATCAGCGAGTGGCATAAGGGCATCCAGGAGGAGATGGAAGCGCTTGTGAAGGATCACGGG
GTAAATTCCTTCCTCGTGTACATGGCTTTCAAAGATCGCTTCCAGCTAACGGATTGCCAG
ATTTATGAAGTACTGAGTGTGATCCGGGATATTGGCGCCATAGCCCAAGTCCACGCAGAA
AATGGCGACATCATTGCAGAGGAGCAGCAGAGGATCCTGGATCTGGGCATCACGGGCCCC
GAGGGACATGTGCTGAGCCGACCTGAGGAGGTCGAGGCCGAAGCCGTGAATCGTGCCATC
ACCATCGCCAACCAGACCAACTGCCCGCTGTATATCACCAAGGTGATGAGCAAAAGCTCT
GCTGAGGTCATCGCCCAGGCACGGAAGAAGGGAACTGTGGTGTATGGCGAGCCCATCACT
GCCAGCTTGGGAACGGACGGCTCCCATTACTGGAGCAAGAACTGGGCCAAGGCTGCTGCC
TTTGTCACCTCCCCACCCTTGAGCCCTGATCCAACCACTCCAGACTTTCTCAACTCCTTG
CTGTCCTGTGGAGACCTCCAGGTCACGGGCAGTGCCCATTGCACGTTTAACACTGCCCAG
AAGGCTGTAGGAAAGGACAACTTCACCCTGATTCCGGAGGGCACCAATGGCACTGAGGAG
CGGATGTCCGTCATCTGGGACAAGGCTGTGGTCACTGGGAAGATGGATGAGAACCAGTTT
GTGGCTGTGACCAGCACCAATGCAGCCAAAGTCTTCAACCTTTACCCCCGGAAAGGCCGC
ATTGCTGTGGGATCCGATGCCGACCTGGTCATCTGGGACCCCGACAGCGTTAAAACCATC
TCTGCCAAGACACACAACAGCTCTCTCGAGTACAACATCTTTGAAGGCATGGAGTGCCGC
GGCTCCCCACTGGTGGTCATCAGCCAGGGGAAGATTGTCCTGGAGGACGGCACCCTGCAT
GTCACCGAAGGCTCTGGACGCTACATTCCCCGGAAGCCCTTCCCTGATTTTGTTTACAAG
CGTATCAAGGCAAGGAGCAGGCTGGCTGAGCTGAGAGGGGTTCCTCGTGGCCTGTATGAC
GGACCTGTGTGTGAAGTGTCTGTGACGCCCAAGACAGTCACTCCAGCCTCCTCGGCCAAG
ACGTCTCCTGCCAAGCAGCAGGCCCCACCTGTCCGGAACCTGCACCAGTCTGGATTCAGT
TTGTCTGGTGCTCAGATTGATGACAACATTCCCCGCCGCACCACCCAGCGTATCGTGGCG
CCCCCCGGTGGCCGTGCCAACATCACCAGCCTGGGCTAG
Enzyme 4 GenBank Gene ID AB020777 Link Image
Enzyme 4 GeneCard ID DPYSL2 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location 8
Enzyme 4 Locus 8p22-p21
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Goshima Y, Nakamura F, Strittmatter P, Strittmatter SM: Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33. Nature. 1995 Aug 10;376(6540):509-14. [PubMed Link Image]
  2. Hamajima N, Matsuda K, Sakata S, Tamaki N, Sasaki M, Nonaka M: A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution. Gene. 1996 Nov 21;180(1-2):157-63. [PubMed Link Image]
  3. Kitamura K, Takayama M, Hamajima N, Nakanishi M, Sasaki M, Endo Y, Takemoto T, Kimura H, Iwaki M, Nonaka M: Characterization of the human dihydropyrimidinase-related protein 2 (DRP-2) gene. DNA Res. 1999 Oct 29;6(5):291-7. [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. 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. Gu Y, Hamajima N, Ihara Y: Neurofibrillary tangle-associated collapsin response mediator protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, and Ser-522. Biochemistry. 2000 Apr 18;39(15):4267-75. [PubMed Link Image]
  7. Inagaki N, Chihara K, Arimura N, Menager C, Kawano Y, Matsuo N, Nishimura T, Amano M, Kaibuchi K: CRMP-2 induces axons in cultured hippocampal neurons. Nat Neurosci. 2001 Aug;4(8):781-2. [PubMed Link Image]
  8. Kawano Y, Yoshimura T, Tsuboi D, Kawabata S, Kaneko-Kawano T, Shirataki H, Takenawa T, Kaibuchi K: CRMP-2 is involved in kinesin-1-dependent transport of the Sra-1/WAVE1 complex and axon formation. Mol Cell Biol. 2005 Nov;25(22):9920-35. [PubMed Link Image]
  9. 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]
  10. Deo RC, Schmidt EF, Elhabazi A, Togashi H, Burley SK, Strittmatter SM: Structural bases for CRMP function in plexin-dependent semaphorin3A signaling. EMBO J. 2004 Jan 14;23(1):9-22. Epub 2003 Dec 18. [PubMed Link Image]
  11. 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]
  12. 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]
  13. 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]
  14. Stenmark P, Ogg D, Flodin S, Flores A, Kotenyova T, Nyman T, Nordlund P, Kursula P: The structure of human collapsin response mediator protein 2, a regulator of axonal growth. J Neurochem. 2007 May;101(4):906-17. Epub 2007 Jan 22. [PubMed Link Image]
  15. 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 12999
Enzyme 5 Name UPB1 protein
Enzyme 5 Synonyms
  1. Ureidopropionase, beta, isoform CRA_b
Enzyme 5 Gene Name UPB1
Enzyme 5 Protein Sequence >UPB1 protein
MAGAEWKSLEECLEKHLPLPDLQEVKRVLYGKELRKLDLPREAFEAASREDFELQGYAFE
AAEEQLRRPRIVHVGLVQNRIPLPANAPVAEQVSALHRRIKAIVEVAAMCGVNIICFQEA
WTMPFAFCTREKLPWTEFAESAEDGPTTRFCQKLAKNHDMVVVSPILERDSEHGDVLWNT
AVVISNSGAVLGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPL
NWLMYSINGAEIIFNPSATIGALSESLWPIEARNAAIANHCFTCAINRVGTEHFPNEFTS
GDGKKAHQDFGYFYGSSYVAAPDSSRTPGLSRSRDGLLVAKLDLNLCQQVNDVWNFKMTG
RYEMYARELAEAVKSNYSPTIVKE
Enzyme 5 Number of Residues 384
Enzyme 5 Molecular Weight 43166
Enzyme 5 Theoretical pI 6.51
Enzyme 5 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Process
  • metabolism
  • nitrogen compound metabolism
  • physiological process
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 126153365 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A3KMF8 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A3KMF8_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID BC131703 Link Image
Enzyme 5 GeneCard ID A3KMF8 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available