CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008232
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GMP synthase [glutamine-hydrolyzing] 
Protein Synonyms/Alias
 GMP synthetase; Glutamine amidotransferase 
Gene Name
 GMPS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9ALCNGDSKLENAGGDacetylation[1]
9ALCNGDSKLENAGGDubiquitination[2]
65ETPAFAIKEQGFRAIubiquitination[2, 3, 4, 5]
145SLFRGLQKEEVVLLTubiquitination[6]
165DKVADGFKVVARSGNubiquitination[2, 6]
182AGIANESKKLYGAQFubiquitination[2, 4, 6, 7]
183GIANESKKLYGAQFHubiquitination[6, 8]
200VGLTENGKVILKNFLubiquitination[6]
204ENGKVILKNFLYDIAubiquitination[6]
289SVEEALKKLGIQVKVubiquitination[6]
325TPRKRISKTLNMTTSubiquitination[6]
336MTTSPEEKRKIIGDTubiquitination[6]
338TSPEEKRKIIGDTFVubiquitination[6]
389SGKAELIKTHHNDTEubiquitination[6, 7, 8]
412GKVIEPLKDFHKDEVubiquitination[6, 8]
416EPLKDFHKDEVRILGacetylation[1]
416EPLKDFHKDEVRILGubiquitination[6]
457AEEPYICKDFPETNNubiquitination[6, 7, 8, 9]
477ADFSASVKKPHTLLQubiquitination[6]
569YIFGPPVKEPPTDVTubiquitination[6]
607RESGYAGKISQMPVIubiquitination[6]
627FDRDPLQKQPSCQRSubiquitination[6]
685IMYDLTSKPPGTTEWubiquitination[6]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931
Functional Description
 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. 
Sequence Annotation
 DOMAIN 27 216 Glutamine amidotransferase type-1.
 DOMAIN 217 435 GMPS ATP-PPase.
 NP_BIND 244 250 ATP (By similarity).
 ACT_SITE 104 104 For GATase activity (By similarity).
 ACT_SITE 190 190 For GATase activity (By similarity).
 ACT_SITE 192 192 For GATase activity (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 9 9 N6-acetyllysine.
 MOD_RES 318 318 Phosphothreonine.
 MOD_RES 332 332 Phosphoserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Chromosomal rearrangement; Complete proteome; Cytoplasm; Direct protein sequencing; Glutamine amidotransferase; GMP biosynthesis; Ligase; Nucleotide-binding; Phosphoprotein; Proto-oncogene; Purine biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 693 AA 
Protein Sequence
MALCNGDSKL ENAGGDLKDG HHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP 60
AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPV LGICYGMQMM NKVFGGTVHK 120
KSVREDGVFN ISVDNTCSLF RGLQKEEVVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE 180
SKKLYGAQFH PEVGLTENGK VILKNFLYDI AGCSGTFTVQ NRELECIREI KERVGTSKVL 240
VLLSGGVDST VCTALLNRAL NQEQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA 300
HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMNLKPE 360
EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR 420
ILGRELGLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH 480
TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW 540
ESLIFLARLI PRMCHNVNRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR 600
ESGYAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIP ATPGNEIPVE 660
VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE 693 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:EC.
 GO:0003921; F:GMP synthase activity; TAS:ProtInc.
 GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
 GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
 GO:0009113; P:purine nucleobase biosynthetic process; TAS:ProtInc. 
Interpro
 IPR017926; GATASE.
 IPR001674; GMP_synth_C.
 IPR004739; GMP_synth_N.
 IPR025777; GMPS_ATP_PPase_dom.
 IPR022310; NAD/GMP_synthase.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00117; GATase
 PF00958; GMP_synt_C
 PF02540; NAD_synthase 
SMART
  
PROSITE
 PS51273; GATASE_TYPE_1
 PS51553; GMPS_ATP_PPASE 
PRINTS