UniProt Accession

 GSH1_HUMAN; P48506; Q14399 

Genbank Protein ID

 M90656; AY780794; AL033397; BC022487; BC039894; L39773; AF118846 

Genbank Nucleotide ID

 AAA58499.1; AAV31778.1; AAH22487.1; AAH39894.1; AAC41751.1; AAD18031.1 

Protein Name

 Glutamate--cysteine ligase catalytic subunit 

Protein Synonyms/Alias

 GCS heavy chain; Gamma-ECS; Gamma-glutamylcysteine synthetase 

Gene Name

 GCLC 

Gene Synonyms/Alias

 GLCL; GLCLC 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
81	VLETLQEKGERTNPN	ubiquitination	[1, 2]
209	VINVPIFKDKNTPSP	ubiquitination	[1]
211	NVPIFKDKNTPSPFI	ubiquitination	[1]
318	ERGLEPLKNNNYRIS	ubiquitination	[1, 2]
412	NWQTMRFKPPPPNSD	ubiquitination	[2]
465	DFLIPLSKVDENMKV	ubiquitination	[1]
492	YFRKDICKGGNAVVD	acetylation	[3]

Reference

 [1] 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]
 [2] 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]
 [3] 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] 

Functional Description

  

Sequence Annotation

 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 5 5 Phosphoserine.
 MOD_RES 8 8 Phosphoserine.  

Keyword

 Acetylation; ATP-binding; Complete proteome; Disease mutation; Glutathione biosynthesis; Hereditary hemolytic anemia; Ligase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 637 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0017109; C:glutamate-cysteine ligase complex; IEA:Compara.
 GO:0043531; F:ADP binding; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0050662; F:coenzyme binding; IPI:UniProtKB.
 GO:0016595; F:glutamate binding; IDA:UniProtKB.
 GO:0004357; F:glutamate-cysteine ligase activity; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
 GO:0006534; P:cysteine metabolic process; IDA:UniProtKB.
 GO:0006536; P:glutamate metabolic process; IDA:UniProtKB.
 GO:0006750; P:glutathione biosynthetic process; IDA:UniProtKB.
 GO:0019852; P:L-ascorbic acid metabolic process; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0031397; P:negative regulation of protein ubiquitination; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Compara.
 GO:0050880; P:regulation of blood vessel size; IMP: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; IDA:UniProtKB.
 GO:0009725; P:response to hormone stimulus; IDA:UniProtKB.
 GO:0051409; P:response to nitrosative stress; IEA:Compara.
 GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
 GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. 

Interpro

 IPR004308; GCS. 

Pfam

 PF03074; GCS 

SMART

  

PROSITE

  

PRINTS