Full text data of GMPS
GMPS
[Confidence: low (only semi-automatic identification from reviews)]
GMP synthase [glutamine-hydrolyzing]; 6.3.5.2 (GMP synthetase; Glutamine amidotransferase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
GMP synthase [glutamine-hydrolyzing]; 6.3.5.2 (GMP synthetase; Glutamine amidotransferase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P49915
ID GUAA_HUMAN Reviewed; 693 AA.
AC P49915;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
DE AltName: Full=Glutamine amidotransferase;
GN Name=GMPS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8089153;
RA Hirst M., Haliday E., Nakamura J., Lou L.;
RT "Human GMP synthetase. Protein purification, cloning, and functional
RT expression of cDNA.";
RL J. Biol. Chem. 269:23830-23837(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
RX PubMed=11110714;
RA Pegram L.D., Megonigal M.D., Lange B.J., Nowell P.C., Rowley J.D.,
RA Rappaport E.F., Felix C.A.;
RT "t(3;11) translocation in treatment-related acute myeloid leukemia
RT fuses MLL with the GMPS (guanosine 5-prime monophosphate synthetase)
RT gene.";
RL Blood 96:4360-4362(2000).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-9, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318 AND SER-332, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Involved in the de novo synthesis of guanine nucleotides
CC which are not only essential for DNA and RNA synthesis, but also
CC provide GTP, which is involved in a number of cellular processes
CC important for cell division.
CC -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP +
CC diphosphate + GMP + L-glutamate.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISEASE: Note=A chromosomal aberration involving GMPS is found in
CC acute myeloid leukemias. Translocation t(3,11)(q25,q23) with
CC KMT2A/MLL1.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC -!- SIMILARITY: Contains 1 GMPS ATP-PPase (ATP pyrophosphatase)
CC domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GMPSID229.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U10860; AAA60331.1; -; mRNA.
DR EMBL; BC012178; AAH12178.1; -; mRNA.
DR PIR; A54847; A54847.
DR RefSeq; NP_003866.1; NM_003875.2.
DR UniGene; Hs.591314; -.
DR PDB; 2VPI; X-ray; 2.40 A; A/B=25-219.
DR PDB; 2VXO; X-ray; 2.50 A; A/B=20-693.
DR PDBsum; 2VPI; -.
DR PDBsum; 2VXO; -.
DR ProteinModelPortal; P49915; -.
DR SMR; P49915; 23-693.
DR IntAct; P49915; 13.
DR MINT; MINT-5004310; -.
DR STRING; 9606.ENSP00000419851; -.
DR ChEMBL; CHEMBL5721; -.
DR DrugBank; DB00142; L-Glutamic Acid.
DR DrugBank; DB00130; L-Glutamine.
DR MEROPS; C26.950; -.
DR PhosphoSite; P49915; -.
DR DMDM; 1708072; -.
DR REPRODUCTION-2DPAGE; IPI00029079; -.
DR PaxDb; P49915; -.
DR PeptideAtlas; P49915; -.
DR PRIDE; P49915; -.
DR DNASU; 8833; -.
DR Ensembl; ENST00000496455; ENSP00000419851; ENSG00000163655.
DR GeneID; 8833; -.
DR KEGG; hsa:8833; -.
DR UCSC; uc003faq.3; human.
DR CTD; 8833; -.
DR GeneCards; GC03P155588; -.
DR HGNC; HGNC:4378; GMPS.
DR HPA; HPA050682; -.
DR MIM; 600358; gene.
DR neXtProt; NX_P49915; -.
DR PharmGKB; PA28763; -.
DR eggNOG; COG0519; -.
DR HOGENOM; HOG000223965; -.
DR HOVERGEN; HBG005929; -.
DR InParanoid; P49915; -.
DR KO; K01951; -.
DR OMA; EIKKEYC; -.
DR OrthoDB; EOG7J17Z9; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00189; UER00296.
DR ChiTaRS; GMPS; human.
DR EvolutionaryTrace; P49915; -.
DR GeneWiki; GMP_synthase; -.
DR GenomeRNAi; 8833; -.
DR NextBio; 33152; -.
DR PRO; PR:P49915; -.
DR ArrayExpress; P49915; -.
DR Bgee; P49915; -.
DR CleanEx; HS_GMPS; -.
DR Genevestigator; P49915; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0003921; F:GMP synthase activity; TAS:ProtInc.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; TAS:ProtInc.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR004739; GMP_synth_N.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chromosomal rearrangement;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene;
KW Purine biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 693 GMP synthase [glutamine-hydrolyzing].
FT /FTId=PRO_0000140257.
FT DOMAIN 27 216 Glutamine amidotransferase type-1.
FT DOMAIN 217 435 GMPS ATP-PPase.
FT NP_BIND 244 250 ATP (By similarity).
FT ACT_SITE 104 104 For GATase activity (By similarity).
FT ACT_SITE 190 190 For GATase activity (By similarity).
FT ACT_SITE 192 192 For GATase activity (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 9 9 N6-acetyllysine.
FT MOD_RES 318 318 Phosphothreonine.
FT MOD_RES 332 332 Phosphoserine.
FT CONFLICT 415 415 H -> I (in Ref. 1; AA sequence).
FT STRAND 28 32
FT TURN 35 38
FT HELIX 39 47
FT STRAND 52 54
FT HELIX 61 67
FT STRAND 70 76
FT HELIX 91 94
FT STRAND 100 104
FT HELIX 105 113
FT STRAND 118 123
FT STRAND 127 133
FT HELIX 138 140
FT STRAND 145 151
FT STRAND 153 159
FT STRAND 165 170
FT STRAND 173 179
FT TURN 180 183
FT STRAND 184 189
FT STRAND 193 196
FT HELIX 199 207
FT TURN 208 211
FT HELIX 219 234
FT STRAND 238 242
FT HELIX 247 259
FT HELIX 262 264
FT STRAND 265 271
FT HELIX 281 289
FT STRAND 294 298
FT HELIX 300 304
FT HELIX 327 329
FT HELIX 333 354
FT STRAND 361 365
FT HELIX 377 382
FT HELIX 387 389
FT HELIX 396 403
FT HELIX 410 413
FT HELIX 416 425
FT HELIX 430 433
FT HELIX 442 446
FT STRAND 450 452
FT HELIX 459 470
FT HELIX 472 475
FT HELIX 481 489
FT HELIX 492 504
FT STRAND 507 520
FT STRAND 523 536
FT HELIX 540 553
FT STRAND 557 563
FT HELIX 582 601
FT HELIX 605 607
FT STRAND 613 617
FT HELIX 624 626
FT STRAND 633 637
FT STRAND 643 649
FT TURN 654 656
FT HELIX 659 671
FT STRAND 675 681
SQ SEQUENCE 693 AA; 76715 MW; 1CDA0DD3B244728D CRC64;
MALCNGDSKL ENAGGDLKDG HHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP
AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPV LGICYGMQMM NKVFGGTVHK
KSVREDGVFN ISVDNTCSLF RGLQKEEVVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE
SKKLYGAQFH PEVGLTENGK VILKNFLYDI AGCSGTFTVQ NRELECIREI KERVGTSKVL
VLLSGGVDST VCTALLNRAL NQEQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA
HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMNLKPE
EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR
ILGRELGLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH
TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW
ESLIFLARLI PRMCHNVNRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR
ESGYAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIP ATPGNEIPVE
VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE
//
ID GUAA_HUMAN Reviewed; 693 AA.
AC P49915;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
DE AltName: Full=Glutamine amidotransferase;
GN Name=GMPS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8089153;
RA Hirst M., Haliday E., Nakamura J., Lou L.;
RT "Human GMP synthetase. Protein purification, cloning, and functional
RT expression of cDNA.";
RL J. Biol. Chem. 269:23830-23837(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
RX PubMed=11110714;
RA Pegram L.D., Megonigal M.D., Lange B.J., Nowell P.C., Rowley J.D.,
RA Rappaport E.F., Felix C.A.;
RT "t(3;11) translocation in treatment-related acute myeloid leukemia
RT fuses MLL with the GMPS (guanosine 5-prime monophosphate synthetase)
RT gene.";
RL Blood 96:4360-4362(2000).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-9, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318 AND SER-332, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Involved in the de novo synthesis of guanine nucleotides
CC which are not only essential for DNA and RNA synthesis, but also
CC provide GTP, which is involved in a number of cellular processes
CC important for cell division.
CC -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP +
CC diphosphate + GMP + L-glutamate.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISEASE: Note=A chromosomal aberration involving GMPS is found in
CC acute myeloid leukemias. Translocation t(3,11)(q25,q23) with
CC KMT2A/MLL1.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC -!- SIMILARITY: Contains 1 GMPS ATP-PPase (ATP pyrophosphatase)
CC domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GMPSID229.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U10860; AAA60331.1; -; mRNA.
DR EMBL; BC012178; AAH12178.1; -; mRNA.
DR PIR; A54847; A54847.
DR RefSeq; NP_003866.1; NM_003875.2.
DR UniGene; Hs.591314; -.
DR PDB; 2VPI; X-ray; 2.40 A; A/B=25-219.
DR PDB; 2VXO; X-ray; 2.50 A; A/B=20-693.
DR PDBsum; 2VPI; -.
DR PDBsum; 2VXO; -.
DR ProteinModelPortal; P49915; -.
DR SMR; P49915; 23-693.
DR IntAct; P49915; 13.
DR MINT; MINT-5004310; -.
DR STRING; 9606.ENSP00000419851; -.
DR ChEMBL; CHEMBL5721; -.
DR DrugBank; DB00142; L-Glutamic Acid.
DR DrugBank; DB00130; L-Glutamine.
DR MEROPS; C26.950; -.
DR PhosphoSite; P49915; -.
DR DMDM; 1708072; -.
DR REPRODUCTION-2DPAGE; IPI00029079; -.
DR PaxDb; P49915; -.
DR PeptideAtlas; P49915; -.
DR PRIDE; P49915; -.
DR DNASU; 8833; -.
DR Ensembl; ENST00000496455; ENSP00000419851; ENSG00000163655.
DR GeneID; 8833; -.
DR KEGG; hsa:8833; -.
DR UCSC; uc003faq.3; human.
DR CTD; 8833; -.
DR GeneCards; GC03P155588; -.
DR HGNC; HGNC:4378; GMPS.
DR HPA; HPA050682; -.
DR MIM; 600358; gene.
DR neXtProt; NX_P49915; -.
DR PharmGKB; PA28763; -.
DR eggNOG; COG0519; -.
DR HOGENOM; HOG000223965; -.
DR HOVERGEN; HBG005929; -.
DR InParanoid; P49915; -.
DR KO; K01951; -.
DR OMA; EIKKEYC; -.
DR OrthoDB; EOG7J17Z9; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00189; UER00296.
DR ChiTaRS; GMPS; human.
DR EvolutionaryTrace; P49915; -.
DR GeneWiki; GMP_synthase; -.
DR GenomeRNAi; 8833; -.
DR NextBio; 33152; -.
DR PRO; PR:P49915; -.
DR ArrayExpress; P49915; -.
DR Bgee; P49915; -.
DR CleanEx; HS_GMPS; -.
DR Genevestigator; P49915; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0003921; F:GMP synthase activity; TAS:ProtInc.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; TAS:ProtInc.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR004739; GMP_synth_N.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chromosomal rearrangement;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene;
KW Purine biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 693 GMP synthase [glutamine-hydrolyzing].
FT /FTId=PRO_0000140257.
FT DOMAIN 27 216 Glutamine amidotransferase type-1.
FT DOMAIN 217 435 GMPS ATP-PPase.
FT NP_BIND 244 250 ATP (By similarity).
FT ACT_SITE 104 104 For GATase activity (By similarity).
FT ACT_SITE 190 190 For GATase activity (By similarity).
FT ACT_SITE 192 192 For GATase activity (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 9 9 N6-acetyllysine.
FT MOD_RES 318 318 Phosphothreonine.
FT MOD_RES 332 332 Phosphoserine.
FT CONFLICT 415 415 H -> I (in Ref. 1; AA sequence).
FT STRAND 28 32
FT TURN 35 38
FT HELIX 39 47
FT STRAND 52 54
FT HELIX 61 67
FT STRAND 70 76
FT HELIX 91 94
FT STRAND 100 104
FT HELIX 105 113
FT STRAND 118 123
FT STRAND 127 133
FT HELIX 138 140
FT STRAND 145 151
FT STRAND 153 159
FT STRAND 165 170
FT STRAND 173 179
FT TURN 180 183
FT STRAND 184 189
FT STRAND 193 196
FT HELIX 199 207
FT TURN 208 211
FT HELIX 219 234
FT STRAND 238 242
FT HELIX 247 259
FT HELIX 262 264
FT STRAND 265 271
FT HELIX 281 289
FT STRAND 294 298
FT HELIX 300 304
FT HELIX 327 329
FT HELIX 333 354
FT STRAND 361 365
FT HELIX 377 382
FT HELIX 387 389
FT HELIX 396 403
FT HELIX 410 413
FT HELIX 416 425
FT HELIX 430 433
FT HELIX 442 446
FT STRAND 450 452
FT HELIX 459 470
FT HELIX 472 475
FT HELIX 481 489
FT HELIX 492 504
FT STRAND 507 520
FT STRAND 523 536
FT HELIX 540 553
FT STRAND 557 563
FT HELIX 582 601
FT HELIX 605 607
FT STRAND 613 617
FT HELIX 624 626
FT STRAND 633 637
FT STRAND 643 649
FT TURN 654 656
FT HELIX 659 671
FT STRAND 675 681
SQ SEQUENCE 693 AA; 76715 MW; 1CDA0DD3B244728D CRC64;
MALCNGDSKL ENAGGDLKDG HHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP
AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPV LGICYGMQMM NKVFGGTVHK
KSVREDGVFN ISVDNTCSLF RGLQKEEVVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE
SKKLYGAQFH PEVGLTENGK VILKNFLYDI AGCSGTFTVQ NRELECIREI KERVGTSKVL
VLLSGGVDST VCTALLNRAL NQEQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA
HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMNLKPE
EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR
ILGRELGLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH
TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW
ESLIFLARLI PRMCHNVNRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR
ESGYAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIP ATPGNEIPVE
VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE
//
MIM
600358
*RECORD*
*FIELD* NO
600358
*FIELD* TI
*600358 GUANINE MONOPHOSPHATE SYNTHETASE; GMPS
;;GMP SYNTHETASE
GMPS/MLL FUSION GENE, INCLUDED
read more*FIELD* TX
DESCRIPTION
In the de novo synthesis of purine nucleotides, IMP is the branch point
metabolite at which point the pathway diverges to the synthesis of
either guanine or adenine nucleotides. In the guanine nucleotide
pathway, there are 2 enzymes involved in converting IMP to GMP, namely
IMP dehydrogenase (IMPD1; 146690), which catalyzes the oxidation of IMP
to XMP, and GMP synthetase (EC 6.3.5.2), which catalyzes the amination
of XMP to GMP. Both IMP dehydrogenase and GMP synthetase exhibit
elevated levels of activity in rapidly proliferating cells such as
neoplastic and regenerating tissues (summary by Hirst et al., 1994).
CLONING
Hirst et al. (1994) purified human GMP synthetase to homogeneity and
isolated a cDNA encoding the enzyme from a T-lymphoblastoma cell line.
The open reading frame encoded a protein of 693 amino acids with a
predicted molecular mass of 76,725. The cDNA complemented a guaA mutant
of Escherichia coli. A single 2.4-kb mRNA was demonstrated. DNA
hybridization analysis suggested that human GMP synthetase is encoded by
1 gene.
MAPPING
By fluorescence in situ hybridization, Fedorova et al. (1997) mapped the
GMPS gene to 3q24.
CYTOGENETICS
In a patient with treatment-related acute myeloid leukemia and the
karyotype t(3;11)(q25;q23), Pegram et al. (2000) identified GMPS to be
the partner gene of MLL (159550). The authors stated that GMPS was the
first partner gene of MLL to be identified on 3q and the first gene of
this type to be found in leukemia-associated translocations.
*FIELD* RF
1. Fedorova, L.; Kost-Alimova, M.; Gizatullin, R. Z.; Alimov, A.;
Zabarovska, V. I.; Szeles, A.; Protopopov, A. I.; Vorobieva, N. V.;
Kashuba, V. I.; Klein, G.; Zelenin, A. V.; Sheer, D.; Zabarovsky,
E. R.: Assignment and ordering of twenty-three unique NotI-linking
clones containing expressed genes including the guanosine 5-prime-monophosphate
synthetase gene to human chromosome 3. Europ. J. Hum. Genet. 5:
110-116, 1997.
2. Hirst, M.; Haliday, E.; Nakamura, J.; Lou, L.: Human GMP synthetase:
protein purification, cloning, and functional expression of cDNA. J.
Biol. Chem. 269: 23830-23837, 1994.
3. Pegram, L. D.; Megonigal, M. D.; Lange, B. J.; Nowell, P. C.; Rowley,
J. D.; Rappaport, E. F.; Felix, C. A.: t(3;11) translocation in treatment-related
acute myeloid leukemia fuses MLL with the GMPS (guanosine 5-prime
monophosphate synthetase) gene. Blood 96: 4360-4362, 2000.
*FIELD* CN
Victor A. McKusick - updated: 2/14/2001
Victor A. McKusick - updated: 9/10/1997
*FIELD* CD
Victor A. McKusick: 1/30/1995
*FIELD* ED
alopez: 03/08/2012
alopez: 3/19/2010
carol: 4/2/2001
cwells: 2/19/2001
terry: 2/14/2001
carol: 2/26/1999
terry: 9/10/1997
carol: 1/31/1995
carol: 1/30/1995
*RECORD*
*FIELD* NO
600358
*FIELD* TI
*600358 GUANINE MONOPHOSPHATE SYNTHETASE; GMPS
;;GMP SYNTHETASE
GMPS/MLL FUSION GENE, INCLUDED
read more*FIELD* TX
DESCRIPTION
In the de novo synthesis of purine nucleotides, IMP is the branch point
metabolite at which point the pathway diverges to the synthesis of
either guanine or adenine nucleotides. In the guanine nucleotide
pathway, there are 2 enzymes involved in converting IMP to GMP, namely
IMP dehydrogenase (IMPD1; 146690), which catalyzes the oxidation of IMP
to XMP, and GMP synthetase (EC 6.3.5.2), which catalyzes the amination
of XMP to GMP. Both IMP dehydrogenase and GMP synthetase exhibit
elevated levels of activity in rapidly proliferating cells such as
neoplastic and regenerating tissues (summary by Hirst et al., 1994).
CLONING
Hirst et al. (1994) purified human GMP synthetase to homogeneity and
isolated a cDNA encoding the enzyme from a T-lymphoblastoma cell line.
The open reading frame encoded a protein of 693 amino acids with a
predicted molecular mass of 76,725. The cDNA complemented a guaA mutant
of Escherichia coli. A single 2.4-kb mRNA was demonstrated. DNA
hybridization analysis suggested that human GMP synthetase is encoded by
1 gene.
MAPPING
By fluorescence in situ hybridization, Fedorova et al. (1997) mapped the
GMPS gene to 3q24.
CYTOGENETICS
In a patient with treatment-related acute myeloid leukemia and the
karyotype t(3;11)(q25;q23), Pegram et al. (2000) identified GMPS to be
the partner gene of MLL (159550). The authors stated that GMPS was the
first partner gene of MLL to be identified on 3q and the first gene of
this type to be found in leukemia-associated translocations.
*FIELD* RF
1. Fedorova, L.; Kost-Alimova, M.; Gizatullin, R. Z.; Alimov, A.;
Zabarovska, V. I.; Szeles, A.; Protopopov, A. I.; Vorobieva, N. V.;
Kashuba, V. I.; Klein, G.; Zelenin, A. V.; Sheer, D.; Zabarovsky,
E. R.: Assignment and ordering of twenty-three unique NotI-linking
clones containing expressed genes including the guanosine 5-prime-monophosphate
synthetase gene to human chromosome 3. Europ. J. Hum. Genet. 5:
110-116, 1997.
2. Hirst, M.; Haliday, E.; Nakamura, J.; Lou, L.: Human GMP synthetase:
protein purification, cloning, and functional expression of cDNA. J.
Biol. Chem. 269: 23830-23837, 1994.
3. Pegram, L. D.; Megonigal, M. D.; Lange, B. J.; Nowell, P. C.; Rowley,
J. D.; Rappaport, E. F.; Felix, C. A.: t(3;11) translocation in treatment-related
acute myeloid leukemia fuses MLL with the GMPS (guanosine 5-prime
monophosphate synthetase) gene. Blood 96: 4360-4362, 2000.
*FIELD* CN
Victor A. McKusick - updated: 2/14/2001
Victor A. McKusick - updated: 9/10/1997
*FIELD* CD
Victor A. McKusick: 1/30/1995
*FIELD* ED
alopez: 03/08/2012
alopez: 3/19/2010
carol: 4/2/2001
cwells: 2/19/2001
terry: 2/14/2001
carol: 2/26/1999
terry: 9/10/1997
carol: 1/31/1995
carol: 1/30/1995