CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040775
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 GMP synthase [glutamine-hydrolyzing] 
Protein Synonyms/Alias
  
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
46SLFRGLQKEEVVLLTubiquitination[1, 2]
66DKVADGFKVVARSGNubiquitination[1, 2, 3]
83AGIANESKKLYGAQFubiquitination[1, 3, 4, 5, 6]
84GIANESKKLYGAQFHubiquitination[1, 2, 7]
101VGLTENGKVILKNFLubiquitination[1]
105ENGKVILKNFLYDIAubiquitination[1]
190SVEEALKKLGIQVKVubiquitination[1, 2]
226TPRKRISKTLNMTTSubiquitination[1, 2]
237MTTSPEEKRKIIGDTubiquitination[1]
239TSPEEKRKIIGDTFVubiquitination[1]
290SGKAELIKTHHNDTEacetylation[2]
290SGKAELIKTHHNDTEubiquitination[1, 2, 5, 7]
313GKVIEPLKDFHKDEVubiquitination[1, 7]
317EPLKDFHKDEVRILGacetylation[2, 8, 9]
317EPLKDFHKDEVRILGubiquitination[1]
358AEEPYICKDFPETNNubiquitination[1, 2, 4, 5, 7, 10]
378ADFSASVKKPHTLLQubiquitination[1]
379DFSASVKKPHTLLQRubiquitination[2]
436YVCGISSKDEPDWESubiquitination[4]
470YIFGPPVKEPPTDVTubiquitination[1]
508RESGYAGKISQMPVIubiquitination[1, 2]
528FDRDPLQKQPSCQRSubiquitination[1]
586IMYDLTSKPPGTTEWubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [10] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 594 AA 
Protein Sequence
MALCNGDSKM MNKVFGGTVH KKSVREDGVF NISVDNTCSL FRGLQKEEVV LLTHGDSVDK 60
VADGFKVVAR SGNIVAGIAN ESKKLYGAQF HPEVGLTENG KVILKNFLYD IAGCSGTFTV 120
QNRELECIRE IKERVGTSKV LVLLSGGVDS TVCTALLNRA LNQEQVIAVH IDNGFMRKRE 180
SQSVEEALKK LGIQVKVINA AHSFYNGTTT LPISDEDRTP RKRISKTLNM TTSPEEKRKI 240
IGDTFVKIAN EVIGEMNLKP EEVFLAQGTL RPDLIESASL VASGKAELIK THHNDTELIR 300
KLREEGKVIE PLKDFHKDEV RILGRELGLP EELVSRHPFP GPGLAIRVIC AEEPYICKDF 360
PETNNILKIV ADFSASVKKP HTLLQRVKAC TTEEDQEKLM QITSLHSLNA FLLPIKTVGV 420
QGDCRSYSYV CGISSKDEPD WESLIFLARL IPRMCHNVNR VVYIFGPPVK EPPTDVTPTF 480
LTTGVLSTLR QADFEAHNIL RESGYAGKIS QMPVILTPLH FDRDPLQKQP SCQRSVVIRT 540
FITSDFMTGI PATPGNEIPV EVVLKMVTEI KKIPGISRIM YDLTSKPPGT TEWE 594 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
 GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
 GO:0006177; P:GMP biosynthetic process; IEA:InterPro. 
Interpro
 IPR017926; GATASE.
 IPR001674; GMP_synth_C.
 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