CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010658
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamate--cysteine ligase catalytic subunit 
Protein Synonyms/Alias
 GCS heavy chain; Gamma-ECS; Gamma-glutamylcysteine synthetase 
Gene Name
 Gclc 
Gene Synonyms/Alias
 Glclc 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
64SFDHENRKVQLLLNGubiquitination[1]
81VLETLQEKGERTNPNubiquitination[1]
209VINVPIFKDKNTPSPubiquitination[1]
211NVPIFKDKNTPSPFVubiquitination[1]
318ERGLEPLKNNRFRISubiquitination[1]
338SIDSYLSKCGEKYNDubiquitination[1]
412NWQTMRFKPPPPNSDubiquitination[1]
492YFRKDICKGGNAVVDacetylation[2, 3]
Reference
 [1] 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]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
Functional Description
  
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 5 5 Phosphoserine (By similarity).
 MOD_RES 8 8 Phosphoserine (By similarity).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 637 AA 
Protein Sequence
MGLLSQGSPL SWEETQRHAD HVRRHGILQF LHIYHAVKDR HKDVLKWGDE VEYMLVSFDH 60
ENRKVQLLLN GGDVLETLQE KGERTNPNHP TLWRPEYGSY MIEGTPGQPY GGTMSEFNTV 120
EANMRKRRKE ATSVLGEHQA LCTITSFPRL GCPGFTLPEH RPNPEEGGAS KSLFFPDEAI 180
NKHPRFGTLT RNIRHRRGEK VVINVPIFKD KNTPSPFVET FPEDAEASKA SQPDHIYMDA 240
MGFGMGNCCL QVTFQACSIS EARYLYDQLA TICPIVMALS AASPFYRGYV SDIDCRWGVI 300
SASVDDRTRE ERGLEPLKNN RFRISKSRYD SIDSYLSKCG EKYNDIDLTI DKEIYEQLLE 360
EGIDHLLAQH VAHLFIRDPL TLFEEKIHLD DANESDHFEN IQSTNWQTMR FKPPPPNSDI 420
GWRVEFRPME VQLTDFENSA YVVFVVLLTR VILSYKLDFL IPLSKVDENM KVAQKRDAVL 480
QGMFYFRKDI CKGGNAVVDG CSKAQSSSEP AAEEYTLMSI DTIINGKEGV FPGLIPILNS 540
YLENMEVDVD TRCSILNYLK LIKKRASGEL MTVARWMREF IANHPDYKQD SVITDEINYS 600
LIWKCNQIAD ELCECPELLG SGFRKAKYSG GKSDPSA 637 
Gene Ontology
 GO:0005829; C:cytosol; IDA:MGI.
 GO:0017109; C:glutamate-cysteine ligase complex; IDA:MGI.
 GO:0043531; F:ADP binding; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0050662; F:coenzyme binding; ISS:UniProtKB.
 GO:0016595; F:glutamate binding; ISS:UniProtKB.
 GO:0004357; F:glutamate-cysteine ligase activity; ISS:UniProtKB.
 GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
 GO:0045454; P:cell redox homeostasis; ISS:UniProtKB.
 GO:0006534; P:cysteine metabolic process; ISS:UniProtKB.
 GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
 GO:0006750; P:glutathione biosynthetic process; ISS:UniProtKB.
 GO:0019852; P:L-ascorbic acid metabolic process; IMP:MGI.
 GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0031397; P:negative regulation of protein ubiquitination; IMP:MGI.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
 GO:0050880; P:regulation of blood vessel size; ISS:UniProtKB.
 GO:0051900; P:regulation of mitochondrial depolarization; IGI:MGI.
 GO:0046685; P:response to arsenic-containing substance; IMP:MGI.
 GO:0009408; P:response to heat; ISS:UniProtKB.
 GO:0009725; P:response to hormone stimulus; ISS:UniProtKB.
 GO:0051409; P:response to nitrosative stress; IEA:Compara.
 GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
 GO:0009410; P:response to xenobiotic stimulus; IMP:MGI. 
Interpro
 IPR004308; GCS. 
Pfam
 PF03074; GCS 
SMART
  
PROSITE
  
PRINTS