CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004777
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
81VLETLQEKGERTNPNacetylation[1]
182FPDEAINKHPRFGTLacetylation[1]
209VINVPIFKDKNTPSPacetylation[1]
211NVPIFKDKNTPSPFVacetylation[1]
318ERGLEPLKNNRFKISacetylation[1]
412NWQTMRFKPPPPNSDacetylation[1]
465DFLIPLSKVDENMKVacetylation[1]
471SKVDENMKVAQERDAacetylation[1]
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] 
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; Direct protein sequencing; 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
EDNMRKRRKE ATSVLGEHQA LCTITSFPRL GCPGFTLPEH RPNPEEGGAS KSLFFPDEAI 180
NKHPRFGTLT RNIRHRRGEK VVINVPIFKD KNTPSPFVET FPEDEEASKA SKPDHIYMDA 240
MGFGMGNCCL QVTFQACSIS EARYLYDQLA TICPIVMALS AASPFYRGYV SDIDCRWGVI 300
SASVDDRTRE ERGLEPLKNN RFKISKSRYD SIDSYLSKCG EKYNDIDLTI DTEIYEQLLE 360
EGIDHLLAQH VAHLFIRDPL TLFEEKIHLD DANESDHFEN IQSTNWQTMR FKPPPPNSDI 420
GWRVEFRPME VQLTDFENSA YVVFVVLLTR VILSYKLDFL IPLSKVDENM KVAQERDAVL 480
QGMFYFRKDI CKGGNAVVDG CSKAQTSSEP SAEEYTLMSI DTIINGKEGV FPGLIPILNS 540
YLENMEVDVD TRCSILNYLK LIKKRASGEL MTVARWMREF IANHPDYKQD SVITDEINYS 600
LILKCNQIAN ELCECPELLG SGFRKAKYSG GKSDPSD 637 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0017109; C:glutamate-cysteine ligase complex; IDA:RGD.
 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:0046982; F:protein heterodimerization activity; IDA:RGD.
 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; IEA:Compara.
 GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
 GO:0031397; P:negative regulation of protein ubiquitination; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Compara.
 GO:0050880; P:regulation of blood vessel size; ISS:UniProtKB.
 GO:0051900; P:regulation of mitochondrial depolarization; IEA:Compara.
 GO:0046685; P:response to arsenic-containing substance; IEA:Compara.
 GO:0009408; P:response to heat; ISS:UniProtKB.
 GO:0009725; P:response to hormone stimulus; ISS:UniProtKB.
 GO:0051409; P:response to nitrosative stress; IMP:RGD.
 GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
 GO:0009410; P:response to xenobiotic stimulus; IEA:Compara. 
Interpro
 IPR004308; GCS. 
Pfam
 PF03074; GCS 
SMART
  
PROSITE
  
PRINTS