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GMPS (guanine monphosphate synthetase)

Identity

Other namesGMPS-PEN
HGNC GMPS
Location 3q24

DNA/RNA

Transcription 2212 bp mRNA; ORF: 2081 bp

Protein

Description 693 amino acids; 76 kDa;there are two variant forms of human GMP synthetase; homodimerization; GMP synthetase contains two functional domains: a glutamine amidotransferase (glutaminase domain, with a conserved Cys-His-Glu triad), responsible for glutamine hydrolysis, and a synthetase domain; responsible for ATP hydrolysis and GMP formation
Expression higher in proliferating, transformed cells than in nontransformed cells; in normal cells, higher expression in fibroblasts, followed by bone marrow, leukocytes, erythrocytes, placenta, and liver
Localisation cytoplasmic
Function enzyme of the de novo synthesis of guanine nucleotides: amidotransferase that catalyzes the amination of xanthosine 5 prime monophosphate to form GMP in the presence of ATP and glutamine; GTP is also involved in many enzymatic reactions important for cell division.

Implicated in

Entity t(3;11)(q25;q23)
Disease treatment related acute non lymphoblastic leukemia (M4 ANLL)
Hybrid/Mutated Gene fusion of MLL to GMPS
  

External links

Nomenclature
HGNCGMPS   4378
Entrez_GeneGMPS  8833  guanine monphosphate synthetase
Cards
AtlasGMPSID229
GeneCardsGMPS
EnsemblGMPS [Search_View]   ENSG00000066294 [Gene_View]
GenatlasGMPS
GeneLynxGMPS
eGenomeGMPS
euGene8833
Genomic and cartography
GoldenPathGMPS  -  3q24   chr3:157071019-157138214 +  3q24   [Description]    (hg18-Mar_2006)
EnsemblGMPS - 3q24 [CytoView]
NCBIMapview
OMIMDisease map [OMIM]
HomoloGeneGMPS
Gene and transcription
GenbankAK223399 [ ENTREZ ]
GenbankAK291504 [ ENTREZ ]
GenbankAK300787 [ ENTREZ ]
GenbankAK302148 [ ENTREZ ]
GenbankAK315832 [ ENTREZ ]
RefSeqNM_003875 [ SRS ]    NM_003875 [ ENTREZ ]
RefSeqAC_000046 [ SRS ]    AC_000046 [ ENTREZ ]
RefSeqAC_000135 [ SRS ]    AC_000135 [ ENTREZ ]
RefSeqNC_000003 [ SRS ]    NC_000003 [ ENTREZ ]
RefSeqNT_005612 [ SRS ]    NT_005612 [ ENTREZ ]
RefSeqNW_001838884 [ SRS ]    NW_001838884 [ ENTREZ ]
RefSeqNW_921807 [ SRS ]    NW_921807 [ ENTREZ ]
AceViewGMPS AceView - NCBI
UnigeneHs.591314 [ SRS ]    Hs.591314 [ NCBI ]     HS591314 [ spliceNest ]
Fast-db14188 (alternative variants)
Protein : pattern, domain, 3D structure
SwissProtP49915 [ SRS]    P49915 [ EXPASY ]     P49915 [ INTERPRO ]     P49915 [ UNIPROT ]
PrositePS51273 GATASE_TYPE_1 [ SRS ]    PS51273 GATASE_TYPE_1 [ Expasy ]
InterproIPR006220 Anth_synthII [ SRS ]    IPR006220 Anth_synthII [ EBI ]
InterproIPR004479 ExsB/QueC [ SRS ]    IPR004479 ExsB/QueC [ EBI ]
InterproIPR011702 GATASE [ SRS ]    IPR011702 GATASE [ EBI ]
InterproIPR012998 GATase_1_AS [ SRS ]    IPR012998 GATase_1_AS [ EBI ]
InterproIPR000991 GATase_class1_C [ SRS ]    IPR000991 GATase_class1_C [ EBI ]
InterproIPR001674 GMP_synth_C [ SRS ]    IPR001674 GMP_synth_C [ EBI ]
InterproIPR004739 GMP_synth_N [ SRS ]    IPR004739 GMP_synth_N [ EBI ]
InterproIPR014729 Rossmann-like_a/b/a_fold [ SRS ]    IPR014729 Rossmann-like_a/b/a_fold [ EBI ]
CluSTrP49915
PfamPF06508 ExsB [ SRS ]    PF06508 ExsB [ Sanger ]    pfam06508 [ NCBI-CDD ]
PfamPF00117 GATase [ SRS ]    PF00117 GATase [ Sanger ]    pfam00117 [ NCBI-CDD ]
PfamPF00958 GMP_synt_C [ SRS ]    PF00958 GMP_synt_C [ Sanger ]    pfam00958 [ NCBI-CDD ]
BlocksP49915
PDB2VPI [ SRS ]    2VPI [ PdbSum ],   2VPI [ IMB ]   2VPI [ RSDB ]
HPRD10927
Protein Interaction databases
DIPP49915
IntActP49915
Polymorphism : SNP, mutations, diseases
OMIM600358;601626    [ map ]   
GENECLINICS600358;601626
SNPGMPS [dbSNP-NCBI]  
SNPNM_003875 [SNP-NCI]  
SNPGMPS [GeneSNPs - Utah]  GMPS] [HGBASE - SRS]
HAPMAPGMPS [HAPMAP]  
COSMICGMPS [Somatic mutation (COSMIC-CGP-Sanger)]  
TICdbGMPS [Translocation breakpoints In Cancer]  
HGMDGMPS
General knowledge
Family BrowserGMPS [UCSC Family Browser]
SOURCENM_003875
SMDHs.591314
SAGEHs.591314
Enzyme6.3.5.2 [ Enzyme-Expasy ]   6.3.5.2 [ Enzyme-SRS ]   6.3.5.2 [ IntEnz-EBI ]   6.3.5.2 [ BRENDA ]   6.3.5.2 [ KEGG ]   6.3.5.2 [ WIT ]
GOnucleotide binding [Amigo]  nucleotide binding
GOGMP synthase activity [Amigo]  GMP synthase activity
GOGMP synthase (glutamine-hydrolyzing) activity [Amigo]  GMP synthase (glutamine-hydrolyzing) activity
GOATP binding [Amigo]  ATP binding
GOcytoplasm [Amigo]  cytoplasm
GOpurine nucleotide biosynthetic process [Amigo]  purine nucleotide biosynthetic process
GOGMP biosynthetic process [Amigo]  GMP biosynthetic process
GOglutamine metabolic process [Amigo]  glutamine metabolic process
GObiosynthetic process [Amigo]  biosynthetic process
GOpurine base biosynthetic process [Amigo]  purine base biosynthetic process
GOligase activity [Amigo]  ligase activity
KEGGPurine metabolism
KEGGGlutamate metabolism
PubGeneGMPS
TreeFamGMPS
CTD8833 [Comparative ToxicoGenomics Database]
Other databases
Probes
ProbeGMPS Related clones (RZPD - Berlin)
PubMed
PubMed11 Pubmed reference(s) in LocusLink

Bibliography

Human GMP synthetase.
Page T, Bakay B, Nyhan WL
The International journal of biochemistry. 1984 ; 16 (1) : 117-120.
PMID 6698284
 
Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA.
Hirst M, Haliday E, Nakamura J, Lou L
The Journal of biological chemistry. 1994 ; 269 (38) : 23830-23837.
PMID 8089153
 
High-level production from a baculovirus expression system and biochemical characterization of human GMP synthetase.
Lou L, Nakamura J, Tsing S, Nguyen B, Chow J, Straub K, Chan H, Barnett J
Protein expression and purification. 1995 ; 6 (4) : 487-495.
PMID 8527935
 
Biochemical characterization of human GMP synthetase.
Nakamura J, Lou L
The Journal of biological chemistry. 1995 ; 270 (13) : 7347-7353.
PMID 7706277
 
The glutamine hydrolysis function of human GMP synthetase. Identification of an essential active site cysteine.
Nakamura J, Straub K, Wu J, Lou L
The Journal of biological chemistry. 1995 ; 270 (40) : 23450-23455.
PMID 7559506
 
The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL
Nature structural biology. 1996 ; 3 (1) : 74-86.
PMID 8548458
 
Assignment and ordering of twenty-three unique NotI-linking clones containing expressed genes including the guanosine 5'-monophosphate synthetase gene to human chromosome 3.
Fedorova L, Kost-Alimova M, Gizatullin RZ, Alimov A, Zabarovska VI, Szeles A, Protopopov AI, Vorobieva NV, Kashuba VI, Klein G, Zelenin AV, Sheer D, Zabarovsky ER
European journal of human genetics : EJHG. 1997 ; 5 (2) : 110-116.
PMID 9195163
 
t(3;11)(q25;q23) fuses MLL with the GMPS (guanosine 5'-monophosphate synthetase) gene in treatment-related acute myeloid leukemia (AML).
Pegram LD, Megonigal MD, Lange BJ, Nowell PC, Rappaport EF, Felix CA
Blood. 1999 ; 94 (numero Suppl 1).
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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Contributor(s)

Written02-2000Jean-Loup Huret

Citation

This paper should be referenced as such :
Huret JL . GMPS (guanine monphosphate synthetase). Atlas Genet Cytogenet Oncol Haematol. February 2000 .
URL : http://AtlasGeneticsOncology.org/Genes/GMPSID229.html

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Mon Aug 11 21:14:09 2008

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