CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004296
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamine synthetase 
Protein Synonyms/Alias
 GS; Glutamate decarboxylase; Glutamate--ammonia ligase 
Gene Name
 GLUL 
Gene Synonyms/Alias
 GLNS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11SASSHLNKGIKQVYMubiquitination[1, 2, 3, 4]
14SHLNKGIKQVYMSLPubiquitination[1, 2, 3, 4, 5, 6]
25MSLPQGEKVQAMYIWubiquitination[5]
91MFRDPFRKDPNKLVLubiquitination[1, 2, 3, 4]
95PFRKDPNKLVLCEVFubiquitination[1, 2, 3, 4]
103LVLCEVFKYNRRPAEubiquitination[1, 3, 7]
241VIATFDPKPIPGNWNubiquitination[3]
259CHTNFSTKAMREENGubiquitination[1, 3, 4, 8]
268MREENGLKYIEEAIEubiquitination[1, 2, 3, 4, 5, 6, 8, 9]
276YIEEAIEKLSKRHQYubiquitination[1, 2, 3, 4, 5, 6]
291HIRAYDPKGGLDNARubiquitination[2, 3, 5, 6, 9]
333PRTVGQEKKGYFEDRubiquitination[5]
334RTVGQEKKGYFEDRRubiquitination[3, 4, 5]
372GDEPFQYKN******ubiquitination[1, 2, 3, 4, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] 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]
 [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
 This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity). Essential for proliferation of fetal skin fibroblasts. 
Sequence Annotation
 MOD_RES 2 2 N-acetylthreonine.
 MOD_RES 104 104 Phosphotyrosine (By similarity).
 MOD_RES 180 180 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Disease mutation; Ligase; Lyase; Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 373 AA 
Protein Sequence
MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW 60
NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI 120
MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY 180
RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP 240
KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL 300
TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL 360
LNETGDEPFQ YKN 373 
Gene Ontology
 GO:0043679; C:axon terminus; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0043204; C:perikaryon; IEA:Compara.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0005791; C:rough endoplasmic reticulum; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016595; F:glutamate binding; IEA:Compara.
 GO:0004351; F:glutamate decarboxylase activity; IEA:EC.
 GO:0004356; F:glutamate-ammonia ligase activity; EXP:Reactome.
 GO:0000287; F:magnesium ion binding; IEA:Compara.
 GO:0030145; F:manganese ion binding; IEA:Compara.
 GO:0008283; P:cell proliferation; IDA:UniProtKB.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0006538; P:glutamate catabolic process; TAS:BHF-UCL.
 GO:0006542; P:glutamine biosynthetic process; TAS:BHF-UCL.
 GO:0001504; P:neurotransmitter uptake; TAS:Reactome.
 GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Compara.
 GO:0032024; P:positive regulation of insulin secretion; IEA:Compara.
 GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Compara.
 GO:0051260; P:protein homooligomerization; IEA:Compara.
 GO:0009749; P:response to glucose stimulus; IEA:Compara. 
Interpro
 IPR008147; Gln_synt_beta.
 IPR014746; Gln_synth/guanido_kin_cat_dom.
 IPR008146; Gln_synth_cat_dom.
 IPR027303; Gln_synth_gly_rich_site.
 IPR027302; Gln_synth_N_conserv_site. 
Pfam
 PF00120; Gln-synt_C
 PF03951; Gln-synt_N 
SMART
  
PROSITE
 PS00180; GLNA_1
 PS00181; GLNA_ATP 
PRINTS