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Showing Protein Multifunctional protein ADE2 (HMDBP00894)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 8 metabolites
Identification
HMDB Protein ID HMDBP00894
Secondary Accession Numbers
  • 6176
  • HMDBP04152
Name Multifunctional protein ADE2
Synonyms
  1. AIR carboxylase
  2. AIRC
  3. Phosphoribosylaminoimidazole carboxylase
  4. Phosphoribosylaminoimidazole-succinocarboxamide synthase
  5. SAICAR synthetase
Gene Name PAICS
Protein Type Enzyme
Biological Properties
General Function Involved in phosphoribosylaminoimidazole carboxylase activity
Specific Function Not Available
Pathways
  • Adenine phosphoribosyltransferase deficiency (APRT)
  • Adenosine Deaminase Deficiency
  • Adenylosuccinate Lyase Deficiency
  • AICA-Ribosiduria
  • Azathioprine Action Pathway
  • Gout or Kelley-Seegmiller Syndrome
  • IMP biosynthesis via de novo pathway
  • Lesch-Nyhan Syndrome (LNS)
  • Mercaptopurine Action Pathway
  • Mitochondrial DNA depletion syndrome
  • Molybdenum Cofactor Deficiency
  • Myoadenylate deaminase deficiency
  • Purine metabolism
  • Purine metabolism
  • Purine Nucleoside Phosphorylase Deficiency
  • Thioguanine Action Pathway
  • Xanthine Dehydrogenase Deficiency (Xanthinuria)
  • Xanthinuria type I
  • Xanthinuria type II
Reactions
Adenosine triphosphate + 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylic acid + L-Aspartic acid → ADP + Phosphate + SAICAR details
5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylic acid → 5-Aminoimidazole ribonucleotide + CO(2) details
5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylic acid → 5-Aminoimidazole ribonucleotide + Carbon dioxide details
Adenosine triphosphate + 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylic acid + L-Aspartic acid → ADP + Phosphate + SAICAR details
GO Classification
Biological Process
'de novo' IMP biosynthetic process
purine nucleobase biosynthetic process
purine ribonucleoside monophosphate biosynthetic process
Cellular Component
cytosol
Function
binding
catalytic activity
phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
phosphoribosylaminoimidazole carboxylase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
lyase activity
carbon-carbon lyase activity
ligase activity
carboxy-lyase activity
ligase activity, forming carbon-nitrogen bonds
acid-amino acid ligase activity
Molecular Function
ATP binding
5-(carboxyamino)imidazole ribonucleotide mutase activity
phosphoribosylaminoimidazole carboxylase activity
phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
Process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
purine nucleoside monophosphate biosynthetic process
purine ribonucleoside monophosphate biosynthetic process
imp biosynthetic process
'de novo' imp biosynthetic process
Cellular Location Not Available
Gene Properties
Chromosome Location 4
Locus 4q12
SNPs PAICS
Gene Sequence 
>1278 bp
ATGGCGACAGCTGAGGTACTGAACATTGGTAAAAAATTATATGAGGGTAAAACAAAAGAA
GTCTACGAATTGTTAGACAGTCCAGGAAAAGTCCTCCTGCAGTCCAAGGACCAGATTACA
GCAGGAAATGCAGCTAGAAAAAACCACCTGGAAGGAAAAGCTGCAATCTCAAATAAAATC
ACCAGTTGTATTTTTCAGTTATTACAGGAAGCAGGTATTAAAACTGCCTTCACCAGAAAA
TGTGGGGAGACAGCTTTCATTGCACCGCAGTGTGAAATGATTCCAATTGAATGGGTTTGC
AGAAGAATAGCAACTGGTTCTTTTCTCAAAAGAAATCCTGGTGTCAAGGAAGGATATAAG
TTTTACCCACCTAAAGTGGAGTTGTTTTTCAAGGATGATGCCAATAATGACCCACAGTGG
TCTGAGGAACAGCTGATTGCTGCAAAATTTTGCTTTGCTGGACTTCTTATAGGCCAGACT
GAAGTGGATATCATGAGTCATGCTACACAGGCTATATTTGAAATACTGGAGAAATCCTGG
TTGCCCCAGAATTGTACACTGGTTGATATGAAGATTGAATTTGGTGTTGATGTAACCACC
AAAGAAATTGTTCTTGCTGATGTTATTGACAATGATTCCTGGAGACTCTGGCCATCAGGA
GATCGAAGCCAACAGAAAGACAAACAGTCTTATCGGGACCTCAAAGAAGTAACTCCTGAA
GGGCTCCAAATGGTAAAGAAAAACTTTGAGTGGGTTGCAGAGAGAGTAGAGTTGCTTTTG
AAATCAGAAAGTCAGTGCAGGGTTGTAGTGTTGATGGGCTCTACTTCTGATCTTGGTCAC
TGTGAAAAAATCAAGAAGGCCTGTGGAAATTTTGGCATTCCATGTGAACTTCGAGTAACA
TCTGCGCATAAAGGACCAGATGAAACTCTGAGGATTAAAGCTGAGTATGAAGGGGATGGC
ATTCCTACTGTATTTGTGGCAGTGGCAGGCAGAAGTAATGGTTTGGGACCAGTGATGTCT
GGGAACACTGCATATCCAGTTATCAGCTGTCCTCCCCTCACACCAGACTGGGGAGTTCAG
GATGTGTGGTCTTCTCTTCGACTACCCAGTGGTCTTGGCTGTTCAACCGTACTTTCTCCA
GAAGGATCAGCTCAATTTGCTGCTCAGATATTTGGGTTAAGCAACCATTTGGTATGGAGC
AAACTGCGAGCAAGCATTTTGAACACATGGATTTCCTTGAAGCAGGCTGACAAGAAAATC
AGAGAATGTAATTTATAA
Protein Properties
Number of Residues 425
Molecular Weight 47078.82
Theoretical pI 7.225
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Multifunctional protein ADE2
MATAEVLNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKI
TSCIFQLLQEAGIKTAFTRKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYK
FYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQTEVDIMSHATQAIFEILEKSW
LPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPE
GLQMVKKNFEWVAERVELLLKSESQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVT
SAHKGPDETLRIKAEYEGDGIPTVFVAVAGRSNGLGPVMSGNTAYPVISCPPLTPDWGVQ
DVWSSLRLPSGLGCSTVLSPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKI
RECNL
GenBank ID Protein 28384
UniProtKB/Swiss-Prot ID P22234
UniProtKB/Swiss-Prot Entry Name PUR6_HUMAN
PDB IDs
GenBank Gene ID X53793
GeneCard ID PAICS
GenAtlas ID PAICS
HGNC ID HGNC:8587
References
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:15489334 ]
  2. 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. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. 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. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. 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. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  5. 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. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  6. 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. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  7. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  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. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  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:16964243 ]
  10. Minet M, Lacroute F: Cloning and sequencing of a human cDNA coding for a multifunctional polypeptide of the purine pathway by complementation of the ade2-101 mutant in Saccharomyces cerevisiae. Curr Genet. 1990 Nov;18(4):287-91. [PubMed:2253271 ]
  11. Li SX, Tong YP, Xie XC, Wang QH, Zhou HN, Han Y, Zhang ZY, Gao W, Li SG, Zhang XC, Bi RC: Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis. J Mol Biol. 2007 Mar 9;366(5):1603-14. Epub 2006 Dec 16. [PubMed:17224163 ]