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GMPS (guanine monphosphate synthetase)

Identity

Other namesGMPS-PEN
HGNC (Hugo) GMPS
Location 3q24
Location_base_pair Starts at 157071019 and ends at 157138214 bp from pter ( according to hg18-Mar_2006)  [Mapping]

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
HGNC (Hugo)GMPS   4378
Entrez_Gene (NCBI)GMPS  8833  guanine monphosphate synthetase
Cards
AtlasGMPSID229
GeneCards (Weizmann)GMPS
Ensembl (Hinxton)ENSG00000066294 [Gene_View]  GMPS [Vega]
AceView (NCBI)GMPS
Genatlas (Paris)GMPS
euGene (Indiana)8833
SOURCE (Stanford)NM_003875
Genomic and cartography
GoldenPath (UCSC)GMPS  -  3q24   chr3:157071019-157138214 +  3q24   [Description]    (hg18-Mar_2006)
EnsemblGMPS - 3q24 [CytoView]
Mapping of homologs : NCBIGMPS [Mapview]
OMIM600358   601626   
Gene and transcription
Gene : Genbank (Entrez)AK223399 AK291504 AK300787 AK302148 AK315832
Reference sequence (RefSeq transcript) :SRSNM_003875
Reference transcript : EntrezNM_003875
RefSeq genomic : SRSAC_000046 AC_000135 NC_000003 NT_005612 NW_001838884 NW_921807
RefSeq genomic : EntrezAC_000046 AC_000135 NC_000003 NT_005612 NW_001838884 NW_921807
Consensus coding sequences : CCDS NCBIGMPS
Cluster EST : UnigeneHs.591314 [ SRS ] Hs.591314 [ NCBI ]
Alternative Splicing : Fast-db (Paris)14188
Protein : pattern, domain, 3D structure
Protein : UniProt/SwissProtP49915 (SRS) P49915 (Expasy) P49915 (Uniprot)
With graphics : InterProP49915
Splice isoforms : VarSplice FASTAP49915(VarSplice FASTA)
Domaine pattern : Prosite (SRS)GATASE_TYPE_1 (PS51273)   
Domain pattern : Prosite (Expaxy)GATASE_TYPE_1 (PS51273)   
Domains : Interpro (SRS)Anth_synthII    ExsB/QueC    GATASE    GATase_1_AS    GATase_class1_C    GMP_synth_C    GMP_synth_N    Rossmann-like_a/b/a_fold   
Domains : Interpro (EBI)Anth_synthII    ExsB/QueC    GATASE    GATase_1_AS    GATase_class1_C    GMP_synth_C    GMP_synth_N    Rossmann-like_a/b/a_fold   
Related proteins : CluSTrP49915
Domain families : Pfam SRSExsB (PF06508)    GATase (PF00117)    GMP_synt_C (PF00958)   
Domain families : Pfam SangerExsB (PF06508)    GATase (PF00117)    GMP_synt_C (PF00958)   
Domain families : Pfam NCBIpfam06508    pfam00117    pfam00958   
Blocks (Seattle)P49915
Crystal structure of protein : PDB SRS2VPI    2VXO   
Crystal structure of protein : PDBSum2VPI    2VXO   
Crystal structure of protein : IMB2VPI    2VXO   
Crystal structure of protein : PDB RSDB2VPI    2VXO   
HPRD10927
Protein Interaction databases
DIP (DOE-UCLA)P49915
IntAct (EBI)P49915
Polymorphism : SNP, mutations, diseases
Single Nucleotide Polymorphism (SNP) : dbSNP NCBIGMPS
SNP : GeneSNP UtahGMPS
SNP : HGBaseGMPS
Genetic variants : HAPMAPGMPS
Somatic Mutations in Cancer : COSMICGMPS 
Translocation Breakpoints in Cancer : TICdbGMPS 
Mutations and Diseases : HGMDGMPS
Hereditary diseases : OMIM600358    601626   
Hereditary diseases : GENETests600358    601626   
Diseases : Genetic AssociationGMPS
General knowledge
Homologs : HomoloGeneGMPS
Homology/Alignments : Family Browser UCSCGMPS
Phylogenetic Trees/Animal Genes : TreeFamGMPS
Catalytic activity : 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 ]   
Chemical/Protein Interactions : CTD8833
Keywords Ontology : AmiGOnucleotide binding  GMP synthase activity  GMP synthase (glutamine-hydrolyzing) activity  ATP binding  cytoplasm  purine nucleotide biosynthetic process  GMP biosynthetic process  glutamine metabolic process  biosynthetic process  purine base biosynthetic process  ligase activity  
Keywords Ontology : EGO-EBInucleotide binding  GMP synthase activity  GMP synthase (glutamine-hydrolyzing) activity  ATP binding  cytoplasm  purine nucleotide biosynthetic process  GMP biosynthetic process  glutamine metabolic process  biosynthetic process  purine base biosynthetic process  ligase activity  
Pathways : BIOCARTA
Pathways : KEGGPurine metabolismGlutamate metabolism
Other databases
Probes
Probes : ImagenesGMPS Related clones (RZPD - Berlin)
Literature
PubMed11 Pubmed reference(s) in Entrez
PubGeneGMPS

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

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indexed on : Sat Jun 27 16:36:44 CEST 2009

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