CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002806
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
14SHLNKGIKQMYMNLPacetylation[1]
95PFRRDPNKLVFCEVFacetylation[1]
103LVFCEVFKYNRKPAEacetylation[1]
107EVFKYNRKPAETNLRacetylation[1]
291HIRAYDPKGGLDNARacetylation[1]
291HIRAYDPKGGLDNARubiquitination[2]
333PRIVGQEKKGYFEDRacetylation[1]
333PRIVGQEKKGYFEDRubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 Essential for proliferation of fetal skin fibroblasts. 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). 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 104 104 Phosphotyrosine (By similarity).
 MOD_RES 180 180 Phosphotyrosine (By similarity).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Lyase; Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 373 AA 
Protein Sequence
MATSASSHLN KGIKQMYMNL PQGEKIQLMY IWVDGTGEGL RCKTRTLDCD PKCVEELPEW 60
NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR RDPNKLVFCE VFKYNRKPAE TNLRHSCKRI 120
MDMVSSQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY 180
RACLYAGIKI TGTNAEVMPA QWEFQIGPCE GIRMGDHLWV ARFILHRVCE DFGVIATFDP 240
KPIPGNWNGA GCHTNFSTKA MREENGLRCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL 300
TGFHETSNIN DFSAGVANRS ASIRIPRIVG QEKKGYFEDR RPSANCDPYA VTEAIVRTCL 360
LNETGDEPFQ YKN 373 
Gene Ontology
 GO:0043679; C:axon terminus; IDA:RGD.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0043204; C:perikaryon; IDA:RGD.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
 GO:0005524; F:ATP binding; IDA:RGD.
 GO:0016595; F:glutamate binding; IDA:RGD.
 GO:0004351; F:glutamate decarboxylase activity; IEA:EC.
 GO:0004356; F:glutamate-ammonia ligase activity; IDA:RGD.
 GO:0000287; F:magnesium ion binding; IDA:RGD.
 GO:0030145; F:manganese ion binding; IDA:RGD.
 GO:0019676; P:ammonia assimilation cycle; IDA:RGD.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0006542; P:glutamine biosynthetic process; IDA:RGD.
 GO:0042133; P:neurotransmitter metabolic process; TAS:RGD.
 GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:RGD.
 GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
 GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:RGD.
 GO:0051260; P:protein homooligomerization; IDA:RGD.
 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