CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008066
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutathione synthetase 
Protein Synonyms/Alias
 GSH synthetase; GSH-S; Glutathione synthase 
Gene Name
 GSS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12WGSLLQDKQQLEELAubiquitination[1, 2]
108ARLFDIHKQVLKEGIubiquitination[1, 2, 3]
112DIHKQVLKEGIAQTVubiquitination[1, 4, 5, 6]
141ADGSPALKQIEINTIubiquitination[1, 3, 7]
172HVLSVLSKTKEAGKIubiquitination[1]
186ILSNNPSKGLALGIAubiquitination[1, 3, 7]
213VLLIAQEKERNIFDQubiquitination[3]
245TFEDISEKGSLDQDRubiquitination[1, 3, 7]
293LERSHAAKCPDIATQubiquitination[1]
305ATQLAGTKKVQQELSubiquitination[8]
306TQLAGTKKVQQELSRubiquitination[1]
364APSRFVLKPQREGGGubiquitination[1]
384EEMVQALKQLKDSEEubiquitination[1, 3, 7]
400ASYILMEKIEPEPFEubiquitination[1]
452VGHLLRTKAIEHADGubiquitination[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] 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]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] 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]
 [8] 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] 
Functional Description
  
Sequence Annotation
 NP_BIND 364 373 ATP.
 NP_BIND 398 401 ATP.
 REGION 148 151 Substrate binding.
 REGION 214 216 Substrate binding.
 REGION 267 270 Substrate binding.
 REGION 461 462 Substrate binding.
 METAL 144 144 Magnesium.
 METAL 146 146 Magnesium.
 METAL 368 368 Magnesium.
 BINDING 125 125 Substrate.
 BINDING 144 144 ATP.
 BINDING 220 220 Substrate.
 BINDING 305 305 ATP.
 BINDING 375 375 ATP.
 BINDING 425 425 ATP.
 BINDING 450 450 Substrate.
 BINDING 452 452 ATP.
 BINDING 458 458 ATP; via carbonyl oxygen.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Direct protein sequencing; Disease mutation; Glutathione biosynthesis; Hereditary hemolytic anemia; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 474 AA 
Protein Sequence
MATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF TLFPSLVPSA 60
LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT ARLFDIHKQV LKEGIAQTVF 120
LGLNRSDYMF QRSADGSPAL KQIEINTISA SFGGLASRTP AVHRHVLSVL SKTKEAGKIL 180
SNNPSKGLAL GIAKAWELYG SPNALVLLIA QEKERNIFDQ RAIENELLAR NIHVIRRTFE 240
DISEKGSLDQ DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ 300
LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA IAEALAAPSR 360
FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK IEPEPFENCL LRPGSPARVV 420
QCISELGIFG VYVRQEKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV 474 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0043295; F:glutathione binding; IDA:UniProtKB.
 GO:0004363; F:glutathione synthase activity; TAS:Reactome.
 GO:0016594; F:glycine binding; IEA:Compara.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0007568; P:aging; IEA:Compara.
 GO:0007399; P:nervous system development; TAS:ProtInc.
 GO:0043200; P:response to amino acid stimulus; IEA:Compara.
 GO:0046686; P:response to cadmium ion; IEA:Compara.
 GO:0031667; P:response to nutrient levels; IEA:Compara.
 GO:0006979; P:response to oxidative stress; TAS:ProtInc.
 GO:0034612; P:response to tumor necrosis factor; IEA:Compara.
 GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. 
Interpro
 IPR004887; Glutathione_synth_subst-bd_euk.
 IPR014042; Glutathione_synthase_a-hlx_euk.
 IPR014709; Glutathione_synthase_dom.
 IPR005615; Glutathione_synthase_euk.
 IPR014049; Glutathione_synthase_N_euk.
 IPR016185; PreATP-grasp_dom. 
Pfam
 PF03917; GSH_synth_ATP
 PF03199; GSH_synthase 
SMART
  
PROSITE
  
PRINTS