CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000215
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamate--cysteine ligase regulatory subunit 
Protein Synonyms/Alias
 GCS light chain; Gamma-ECS regulatory subunit; Gamma-glutamylcysteine synthetase regulatory subunit; Glutamate--cysteine ligase modifier subunit 
Gene Name
 Gclm 
Gene Synonyms/Alias
 Glclr 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
90PDEREEMKVSAKLFIacetylation[1]
90PDEREEMKVSAKLFIubiquitination[2]
263SRGIIKSKGYILQAKacetylation[3]
263SRGIIKSKGYILQAKphosphoglycerylation[4]
263SRGIIKSKGYILQAKubiquitination[2]
270KGYILQAKRRGS***ubiquitination[2]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237
Functional Description
  
Sequence Annotation
 MOD_RES 263 263 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Glutathione biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 274 AA 
Protein Sequence
MGTDSRAAGA LLARASTLHL QTGNLLNWGR LRKKCPSTHS EELRDCIQKT LNEWSSQISP 60
DLVREFPDVL ECTMSHAVEK INPDEREEMK VSAKLFIVGS NSSSSTRSAV DMACSVLGVA 120
QLDSVIMASP PIEDGVNLSL EHLQPYWEEL ENLVQSKKIV AIGTSDLDKT QLEQLYQWAQ 180
VKPNSNQVNL ASCCVMPPDL TAFAKQFDIQ LLTHNDPKEL LSEASFQEAL QESIPDIEAQ 240
DWVPLWLLRY SVIVKSRGII KSKGYILQAK RRGS 274 
Gene Ontology
 GO:0017109; C:glutamate-cysteine ligase complex; IDA:MGI.
 GO:0004357; F:glutamate-cysteine ligase activity; IEA:Compara.
 GO:0035226; F:glutamate-cysteine ligase catalytic subunit binding; ISS:UniProtKB.
 GO:0006534; P:cysteine metabolic process; IMP:MGI.
 GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
 GO:0006750; P:glutathione biosynthetic process; ISS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0035229; P:positive regulation of glutamate-cysteine ligase activity; IDA:MGI.
 GO:0050880; P:regulation of blood vessel size; ISS:UniProtKB.
 GO:0051900; P:regulation of mitochondrial depolarization; IGI:MGI.
 GO:0042493; P:response to drug; ISS:UniProtKB.
 GO:0051409; P:response to nitrosative stress; IEA:Compara.
 GO:0006979; P:response to oxidative stress; ISS:UniProtKB. 
Interpro
 IPR023210; NADP_OxRdtase_dom. 
Pfam
 PF00248; Aldo_ket_red 
SMART
  
PROSITE
  
PRINTS