Trifunctional purine biosynthetic protein adenosine-3

Mammalian protein found in Homo sapiens
GART
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1MEJ, 1MEN, 1MEO, 1NJS, 1RBM, 1RBQ, 1RBY, 1RBZ, 1RC0, 1RC1, 1ZLX, 1ZLY, 2QK4, 2V9Y, 4EW1, 4EW2, 4EW3, 4ZZ2, 4ZZ3, 4ZZ1, 4ZYV, 4ZZ0, 4ZYY, 4ZYX, 4ZYZ, 4ZYT, 4ZYU, 4ZYW

Identifiers
AliasesGART, AIRS, GARS, GARTF, PAIS, PGFT, PRGS, phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase
External IDsOMIM: 138440; MGI: 95654; HomoloGene: 637; GeneCards: GART; OMA:GART - orthologs
Gene location (Human)
Chromosome 21 (human)
Chr.Chromosome 21 (human)[1]
Chromosome 21 (human)
Genomic location for GART
Genomic location for GART
Band21q22.11Start33,503,931 bp[1]
End33,543,491 bp[1]
Gene location (Mouse)
Chromosome 16 (mouse)
Chr.Chromosome 16 (mouse)[2]
Chromosome 16 (mouse)
Genomic location for GART
Genomic location for GART
Band16 C3.3|16 53.18 cMStart91,418,074 bp[2]
End91,443,840 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ventricular zone

  • ganglionic eminence

  • rectum

  • smooth muscle tissue

  • epithelium of colon

  • body of pancreas

  • gastric mucosa

  • trabecular bone

  • islet of Langerhans

  • tonsil
Top expressed in
  • Ileal epithelium

  • epiblast

  • primitive streak

  • yolk sac

  • embryo

  • somite

  • extraocular muscle

  • ventricular zone

  • embryo

  • morula
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • transferase activity
  • nucleotide binding
  • phosphoribosylglycinamide formyltransferase activity
  • metal ion binding
  • ligase activity
  • catalytic activity
  • hydroxymethyl-, formyl- and related transferase activity
  • ATP binding
  • phosphoribosylformylglycinamidine cyclo-ligase activity
  • phosphoribosylamine-glycine ligase activity
Cellular component
  • cytoplasm
  • cytosol
  • extracellular exosome
Biological process
  • purine nucleotide biosynthetic process
  • glycine metabolic process
  • 'de novo' IMP biosynthetic process
  • brainstem development
  • biosynthesis
  • response to organic substance
  • cerebellum development
  • ribonucleoside monophosphate biosynthetic process
  • tetrahydrofolate biosynthetic process
  • response to inorganic substance
  • purine ribonucleoside monophosphate biosynthetic process
  • cerebral cortex development
  • metabolism
  • purine nucleobase biosynthetic process
  • adenine biosynthetic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2618

14450

Ensembl

ENSG00000262473
ENSG00000159131

ENSMUSG00000022962

UniProt

P22102

Q64737

RefSeq (mRNA)

NM_000819
NM_001136005
NM_001136006
NM_175085

NM_010256
NM_001357351

RefSeq (protein)

NP_000810
NP_001129477
NP_001129478
NP_780294

NP_034386
NP_001344280

Location (UCSC)Chr 21: 33.5 – 33.54 MbChr 16: 91.42 – 91.44 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Trifunctional purine biosynthetic protein adenosine-3 is an enzyme that in humans is encoded by the GART gene.[5]

This protein is a trifunctional polypeptide. It has phosphoribosylamine—glycine ligase (EC 6.3.4.13), phosphoribosylglycinamide formyltransferase (EC 2.1.2.2), AIR synthetase (FGAM cyclase) (EC 6.3.3.1) activity which is required for de novo purine biosynthesis.

References

  1. ^ a b c ENSG00000159131 GRCh38: Ensembl release 89: ENSG00000262473, ENSG00000159131 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022962 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Gnirke A, Barnes TS, Patterson D, Schild D, Featherstone T, Olson MV (July 1991). "Cloning and in vivo expression of the human GART gene using yeast artificial chromosomes". EMBO J. 10 (7): 1629–34. doi:10.1002/j.1460-2075.1991.tb07685.x. PMC 452831. PMID 2050105.

Further reading

  • Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21". Nature. 405 (6784): 311–9. Bibcode:2000Natur.405..311H. doi:10.1038/35012518. PMID 10830953.
  • Banerjee D, Nandagopal K (2007). "Potential interaction between the GARS-AIRS-GART Gene and CP2/LBP-1c/LSF transcription factor in Down syndrome-related Alzheimer disease". Cell. Mol. Neurobiol. 27 (8): 1117–26. doi:10.1007/s10571-007-9217-2. PMID 17902044. S2CID 5102914.
  • Dahms TE, Sainz G, Giroux EL, et al. (2005). "The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase". Biochemistry. 44 (29): 9841–50. doi:10.1021/bi050307g. PMID 16026156.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Dagle JM, Lepp NT, Cooper ME, et al. (2009). "Determination of genetic predisposition to patent ductus arteriosus in preterm infants". Pediatrics. 123 (4): 1116–23. doi:10.1542/peds.2008-0313. PMC 2734952. PMID 19336370.
  • Franke B, Vermeulen SH, Steegers-Theunissen RP, et al. (2009). "An association study of 45 folate-related genes in spina bifida: Involvement of cubilin (CUBN) and tRNA aspartic acid methyltransferase 1 (TRDMT1)". Birth Defects Research Part A: Clinical and Molecular Teratology. 85 (3): 216–26. doi:10.1002/bdra.20556. PMID 19161160.
  • Barbe L, Lundberg E, Oksvold P, et al. (2008). "Toward a confocal subcellular atlas of the human proteome". Mol. Cell. Proteomics. 7 (3): 499–508. doi:10.1074/mcp.M700325-MCP200. PMID 18029348.
  • Zhang Y, Desharnais J, Marsilje TH, et al. (2003). "Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid". Biochemistry. 42 (20): 6043–56. doi:10.1021/bi034219c. PMID 12755606.
  • Brodsky G, Barnes T, Bleskan J, et al. (1997). "The human GARS-AIRS-GART gene encodes two proteins which are differentially expressed during human brain development and temporally overexpressed in cerebellum of individuals with Down syndrome". Hum. Mol. Genet. 6 (12): 2043–50. doi:10.1093/hmg/6.12.2043. PMID 9328467.
  • Kan JL, Moran RG (1997). "Intronic polyadenylation in the human glycinamide ribonucleotide formyltransferase gene". Nucleic Acids Res. 25 (15): 3118–23. doi:10.1093/nar/25.15.3118. PMC 146841. PMID 9224613.
  • Gomez HL, Santillana SL, Vallejos CS, et al. (2006). "A phase II trial of pemetrexed in advanced breast cancer: clinical response and association with molecular target expression". Clin. Cancer Res. 12 (3 Pt 1): 832–8. doi:10.1158/1078-0432.CCR-05-0295. PMID 16467096.
  • Zhang Y, Desharnais J, Greasley SE, et al. (2002). "Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR". Biochemistry. 41 (48): 14206–15. doi:10.1021/bi020522m. PMID 12450384.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Manieri W, Moore ME, Soellner MB, et al. (2007). "Human glycinamide ribonucleotide transformylase: active site mutants as mechanistic probes". Biochemistry. 46 (1): 156–63. doi:10.1021/bi0619270. PMC 2518408. PMID 17198385.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
  • Zalkin H, Dixon JE (1992). "De novo purine nucleotide biosynthesis". Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic Acid Research and Molecular Biology. 42: 259–87. doi:10.1016/s0079-6603(08)60578-4. ISBN 9780125400428. PMID 1574589.
  • Vieira AR, McHenry TG, Daack-Hirsch S, et al. (2008). "Candidate gene/loci studies in cleft lip/palate and dental anomalies finds novel susceptibility genes for clefts". Genet. Med. 10 (9): 668–74. doi:10.1097/GIM.0b013e3181833793. PMC 2734954. PMID 18978678.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  • Banerjee D, Nandagopal K (2009). "Phylogenetic analysis and in silico characterization of the GARS-AIRS-GART gene which codes for a tri-functional enzyme protein involved in de novo purine biosynthesis". Mol. Biotechnol. 42 (3): 306–19. doi:10.1007/s12033-009-9160-1. PMID 19301155. S2CID 34759623.

External links

  • v
  • t
  • e
  • 1rbm: Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
    1rbm: Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
  • 2qk4: Human glycinamide ribonucleotide synthetase
    2qk4: Human glycinamide ribonucleotide synthetase
  • 1rbz: Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
    1rbz: Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
  • 1zlx: The apo structure of human glycinamide ribonucleotide transformylase
    1zlx: The apo structure of human glycinamide ribonucleotide transformylase
  • 1meo: human glycinamide ribonucleotide Transformylase at pH 4.2
    1meo: human glycinamide ribonucleotide Transformylase at pH 4.2
  • 1rc1: Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
    1rc1: Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
  • 1zly: The structure of human glycinamide ribonucleotide transformylase in complex with alpha,beta-N-(hydroxyacetyl)-D-ribofuranosylamine and 10-formyl-5,8,dideazafolate
    1zly: The structure of human glycinamide ribonucleotide transformylase in complex with alpha,beta-N-(hydroxyacetyl)-D-ribofuranosylamine and 10-formyl-5,8,dideazafolate
  • 1men: complex structure of human GAR Tfase and substrate beta-GAR
    1men: complex structure of human GAR Tfase and substrate beta-GAR
  • 1mej: Human Glycinamide Ribonucleotide Transformylase domain at pH 8.5
    1mej: Human Glycinamide Ribonucleotide Transformylase domain at pH 8.5
  • 1rbq: Human GAR Tfase complex structure with 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
    1rbq: Human GAR Tfase complex structure with 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
  • 1rc0: Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
    1rc0: Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
  • 2v9y: HUMAN AMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE
    2v9y: HUMAN AMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE
  • 1rby: Human GAR Tfase complex structure with 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid and substrate beta-GAR
    1rby: Human GAR Tfase complex structure with 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid and substrate beta-GAR
  • 1njs: human GAR Tfase in complex with hydrolyzed form of 10-trifluoroacetyl-5,10-dideaza-acyclic-5,6,7,8-tetrahydrofolic acid
    1njs: human GAR Tfase in complex with hydrolyzed form of 10-trifluoroacetyl-5,10-dideaza-acyclic-5,6,7,8-tetrahydrofolic acid
  • v
  • t
  • e
Transferase: one carbon transferases (EC 2.1)
2.1.1: Methyl-
N-
O-
Homocysteine
Other
2.1.2: Hydroxymethyl-,
Formyl- and Related
Hydroxymethyltransferase
Formyltransferase
Other
2.1.3: Carboxy-
and Carbamoyl
Carboxy
Carbamoyl
2.1.4: Amidine
  • Arginine:glycine amidinotransferase
  • v
  • t
  • e
Purine metabolism
Anabolism
R5P→IMP:
IMP→AMP:
IMP→GMP:
Nucleotide salvage
Catabolism
Pyrimidine metabolism
Anabolism
Catabolism
Deoxyribonucleotides


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