Inosine monophosphate synthase

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

1P4R, 1PKX, 1PL0

Identifiers
AliasesATIC, AICAR, AICARFT, HEL-S-70p, IMPCHASE, PURH, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
External IDsOMIM: 601731; MGI: 1351352; HomoloGene: 2983; GeneCards: ATIC; OMA:ATIC - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for ATIC
Genomic location for ATIC
Band2q35Start215,311,956 bp[1]
End215,349,773 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for ATIC
Genomic location for ATIC
Band1|1 C3Start71,596,309 bp[2]
End71,618,790 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • stromal cell of endometrium

  • rectum

  • anterior pituitary

  • body of pancreas

  • ganglionic eminence

  • caudate nucleus

  • left coronary artery

  • spleen

  • right coronary artery

  • islet of Langerhans
Top expressed in
  • hand

  • condyle

  • maxillary prominence

  • abdominal wall

  • primitive streak

  • foot

  • fossa

  • Paneth cell

  • yolk sac

  • calvaria
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • protein homodimerization activity
  • IMP cyclohydrolase activity
  • catalytic activity
  • phosphoribosylaminoimidazolecarboxamide formyltransferase activity
  • hydrolase activity
  • cadherin binding
Cellular component
  • cytosol
  • membrane
  • mitochondrion
  • extracellular exosome
  • plasma membrane
Biological process
  • purine nucleotide biosynthetic process
  • dihydrofolate metabolic process
  • 'de novo' IMP biosynthetic process
  • brainstem development
  • ribonucleotide metabolic process
  • cerebellum development
  • nucleoside metabolic process
  • tetrahydrofolate biosynthetic process
  • animal organ regeneration
  • response to inorganic substance
  • cerebral cortex development
  • purine ribonucleoside monophosphate biosynthetic process
  • metabolism
  • nucleobase-containing compound metabolic process
  • cellular response to interleukin-7
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

471

108147

Ensembl

ENSG00000138363

ENSMUSG00000026192

UniProt

P31939

Q9CWJ9

RefSeq (mRNA)

NM_004044

NM_026195

RefSeq (protein)

NP_004035

NP_080471

Location (UCSC)Chr 2: 215.31 – 215.35 MbChr 1: 71.6 – 71.62 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Bifunctional purine biosynthesis protein PURH is a protein that in humans is encoded by the ATIC gene.[5][6][7]

ATIC encodes an enzyme which generates inosine monophosphate from aminoimidazole carboxamide ribonucleotide.

It has two functions:

  • EC 2.1.2.3 - 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
  • EC 3.5.4.10 - IMP cyclohydrolase

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000138363 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026192 – 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. ^ Rayl EA, Moroson BA, Beardsley GP (Mar 1996). "The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping". J Biol Chem. 271 (4): 2225–33. doi:10.1074/jbc.271.4.2225. PMID 8567683.
  6. ^ Sugita T, Aya H, Ueno M, Ishizuka T, Kawashima K (Nov 1997). "Characterization of molecularly cloned human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase". J Biochem. 122 (2): 309–13. doi:10.1093/oxfordjournals.jbchem.a021754. PMID 9378707.
  7. ^ "Entrez Gene: ATIC 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase".

Further reading

  • Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667. S2CID 41855774.
  • Yamauchi M, Seki N, Mita K, Saito T, Tsuji S, Hongo E, Morimyo M, Shiomi T, Koyama H (1996). "Isolation of human purH gene expressed in the rodent transformant cells by subtractive enrichment of 3'-untranslated region of human transcript". DNA Res. 2 (6): 269–75. doi:10.1093/dnares/2.6.269. PMID 8867801.
  • Beardsley GP, Rayl EA, Gunn K, Moroson BA, Seow H, Anderson KS, Vergis J, Fleming K, Worland S (1998). "Structure and Functional Relationships in Human pur H". Purine and Pyrimidine Metabolism in Man IX. Advances in Experimental Medicine and Biology. Vol. 431. pp. 221–6. doi:10.1007/978-1-4615-5381-6_43. ISBN 978-0-306-45778-4. PMID 9598063.
  • Vergis JM, Bulock KG, Fleming KG, Beardsley GP (2001). "Human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase. A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity". J. Biol. Chem. 276 (11): 7727–33. doi:10.1074/jbc.M009940200. PMID 11096114.
  • Bulock KG, Beardsley GP, Anderson KS (2002). "The kinetic mechanism of the human bifunctional enzyme ATIC (5-amino-4-imidazolecarboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase). A surprising lack of substrate channeling". J. Biol. Chem. 277 (25): 22168–74. doi:10.1074/jbc.M111964200. PMID 11948179.
  • Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (2003). "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.
  • Cheong CG, Wolan DW, Greasley SE, Horton PA, Beardsley GP, Wilson IA (2004). "Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates". J. Biol. Chem. 279 (17): 18034–45. doi:10.1074/jbc.M313691200. PMID 14966129.
  • Marie S, Heron B, Bitoun P, Timmerman T, Van Den Berghe G, Vincent MF (2004). "AICA-Ribosiduria: A Novel, Neurologically Devastating Inborn Error of Purine Biosynthesis Caused by Mutation of ATIC". Am. J. Hum. Genet. 74 (6): 1276–81. doi:10.1086/421475. PMC 1182092. PMID 15114530.
  • Dervieux T, Furst D, Lein DO, Capps R, Smith K, Walsh M, Kremer J (2004). "Polyglutamation of methotrexate with common polymorphisms in reduced folate carrier, aminoimidazole carboxamide ribonucleotide transformylase, and thymidylate synthase are associated with methotrexate effects in rheumatoid arthritis". Arthritis Rheum. 50 (9): 2766–74. doi:10.1002/art.20460. PMID 15457444.
  • Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R (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.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L (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.

External links

  • Inosine+monophosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • Overview of all the structural information available in the PDB for UniProt: P31939 (Human Bifunctional purine biosynthesis protein PURH (Inosine monophosphate synthase)) at the PDBe-KB.


  • v
  • t
  • e
  • 1p4r: Crystal Structure of Human ATIC in complex with folate-based inhibitor BW1540U88UD
    1p4r: Crystal Structure of Human ATIC in complex with folate-based inhibitor BW1540U88UD
  • 1pkx: Crystal Structure of human ATIC in complex with XMP
    1pkx: Crystal Structure of human ATIC in complex with XMP
  • 1pl0: Crystal structure of human ATIC in complex with folate-based inhibitor, BW2315U89UC
    1pl0: Crystal structure of human ATIC in complex with folate-based inhibitor, BW2315U89UC
  • 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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