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Reviewed, UniProtKB/Swiss-Prot P49915 (GUAA_HUMAN)

Last modified June 16, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    GMP synthase [glutamine-hydrolyzing]
    EC=6.3.5.2
Alternative name(s):
    Glutamine amidotransferase
    GMP synthetase
Gene names
Name: GMPS
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division.

Catalytic activity

ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate.

Pathway

Purine metabolism; GMP biosynthesis; GMP from XMP (glutamine route): step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Involvement in disease

A chromosomal aberration involving GMPS is found in acute myeloid leukemias. Translocation t(3,11)(q25,q23) with MLL.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Contains 1 GMP-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 693693GMP synthase [glutamine-hydrolyzing]
PRO_0000140257

Regions

Domain27 – 216190Glutamine amidotransferase type-1
Nucleotide binding244 – 2507ATP By similarity

Sites

Active site1041For GATase activity By similarity
Active site1901For GATase activity By similarity
Active site1921For GATase activity By similarity

Amino acid modifications

Modified residue3181Phosphothreonine Ref.4
Modified residue3321Phosphoserine Ref.5

Experimental info

Sequence conflict4151H → I AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49915-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 1CDA0DD3B244728D

FASTA69376,715
        10         20         30         40         50         60 
MALCNGDSKL ENAGGDLKDG HHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP 

        70         80         90        100        110        120 
AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPV LGICYGMQMM NKVFGGTVHK 

       130        140        150        160        170        180 
KSVREDGVFN ISVDNTCSLF RGLQKEEVVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE 

       190        200        210        220        230        240 
SKKLYGAQFH PEVGLTENGK VILKNFLYDI AGCSGTFTVQ NRELECIREI KERVGTSKVL 

       250        260        270        280        290        300 
VLLSGGVDST VCTALLNRAL NQEQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA 

       310        320        330        340        350        360 
HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMNLKPE 

       370        380        390        400        410        420 
EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR 

       430        440        450        460        470        480 
ILGRELGLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH 

       490        500        510        520        530        540 
TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW 

       550        560        570        580        590        600 
ESLIFLARLI PRMCHNVNRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR 

       610        620        630        640        650        660 
ESGYAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIP ATPGNEIPVE 

       670        680        690 
VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE 

« Hide

References

« Hide 'large scale' references
[1]"Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA."
Hirst M., Haliday E., Nakamura J., Lou L.
J. Biol. Chem. 269:23830-23837(1994) [PubMed: 8089153] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[3]"t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (guanosine 5-prime monophosphate synthetase) gene."
Pegram L.D., Megonigal M.D., Lange B.J., Nowell P.C., Rowley J.D., Rappaport E.F., Felix C.A.
Blood 96:4360-4362(2000) [PubMed: 11110714] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH MLL.
[4]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, MASS SPECTROMETRY.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

U10860 mRNA. Translation: AAA60331.1.
BC012178 mRNA. Translation: AAH12178.1.
IPIIPI00029079.
PIRA54847.
RefSeqNP_003866.1.
UniGeneHs.591314

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2VPIX-ray2.40A/B25-219[»]
2VXOX-ray2.50A/B20-693[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP49915. 4 interactions.

Protein family/group databases

MEROPSC26.950.

PTM databases

PhosphoSiteP49915.

2-D gel databases

REPRODUCTION-2DPAGEIPI00029079.

Proteomic databases

PeptideAtlasP49915.
PRIDEP49915.

Genome annotation databases

EnsemblENSG00000163655. Homo sapiens. [Contig view]
GeneID8833.
KEGGhsa:8833.

Organism-specific databases

GeneCardsGC03P157071.
H-InvDBHIX0018176.
HGNCHGNC:4378. GMPS.
MIM600358. gene.
PharmGKBPA28763.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP49915.
HOVERGENP49915.

Enzyme and pathway databases

BRENDA6.3.5.2. 247.
ReactomeREACT_1698. Nucleotide metabolism.

Gene expression databases

ArrayExpressP49915.
BgeeP49915.
CleanExHS_GMPS.
GermOnlineENSG00000163655. Homo sapiens.

Family and domain databases

InterProIPR006220. Anth_synthII.
IPR011702. GATASE.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
IPR001674. GMP_synth_C.
IPR004739. GMP_synth_N.
IPR018317. Queuosine_synth-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF06508. ExsB. 1 hit.
PF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
[Graphical view]
PRINTSPR00097. ANTSNTHASEII.
PR00096. GATASE.
TIGRFAMsTIGR00888. guaA_Nterm. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00142. L-Glutamic Acid.
DB00130. L-Glutamine.
NextBio33152.
SOURCESearch...

Entry information

Entry nameGUAA_HUMAN
AccessionPrimary (citable) accession number: P49915
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents