Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00512
Entry Name
UniProt Accession
Theoretical PI
5.74
Molecular Weight
72765.78
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Glutamate--cysteine ligase catalytic subunit
Protein Synonyms/Alias
6.3.2.2; GCS heavy chain; Gamma-ECS; Gamma-glutamylcysteine synthetase;
Gene Name
GCLC
Gene Synonyms/Alias
GLCL; GLCLC;
Created Date
01-FEB-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
500
Canonical
GGNAVVDGCGKAQNS
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Martin DD, Vilas GL, Prescher JA, Rajaiah G, Falck JR, Bertozzi CR, BerthiaumeLG. Rapid detection, discovery, and identification of post-translationallymyristoylated proteins during apoptosis using a bio-orthogonal azidomyristateanalog. FASEB J. 2008 Mar;22(3):797-806. Epub 2007 Oct 10.[PMID:17932026]
Functional Description
Sequence Annotation
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 5 5 Phosphoserine.
Modified residue: 8 8 Phosphoserine.
Protein Length
637 AA.
Protein Sequence
(Canonical)
MGLLSQGSPL SWEETKRHAD HVRRHGILQF LHIYHAVKDR HKDVLKWGDE VEYMLVSFDH  60
ENKKVRLVLS GEKVLETLQE KGERTNPNHP TLWRPEYGSY MIEGTPGQPY GGTMSEFNTV  120
EANMRKRRKE ATSILEENQA LCTITSFPRL GCPGFTLPEV KPNPVEGGAS KSLFFPDEAI  180
NKHPRFSTLT RNIRHRRGEK VVINVPIFKD KNTPSPFIET FTEDDEASRA SKPDHIYMDA  240
MGFGMGNCCL QVTFQACSIS EARYLYDQLA TICPIVMALS AASPFYRGYV SDIDCRWGVI  300
SASVDDRTRE ERGLEPLKNN NYRISKSRYD SIDSYLSKCG EKYNDIDLTI DKEIYEQLLQ  360
EGIDHLLAQH VAHLFIRDPL TLFEEKIHLD DANESDHFEN IQSTNWQTMR FKPPPPNSDI  420
GWRVEFRPME VQLTDFENSA YVVFVVLLTR VILSYKLDFL IPLSKVDENM KVAQKRDAVL  480
QGMFYFRKDI CKGGNAVVDG CGKAQNSTEL AAEEYTLMSI DTIINGKEGV FPGLIPILNS  540
YLENMEVDVD TRCSILNYLK LIKKRASGEL MTVARWMREF IANHPDYKQD SVITDEMNYS  600
LILKCNQIAN ELCECPELLG SAFRKVKYSG SKTDSSN                           637
FASTA
(Canonical)
>LipidDB-9606-00512|P48506
MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDH
ENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTV
EANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAI
NKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDA
MGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVI
SASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQ
EGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDI
GWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVL
QGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNS
YLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYS
LILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN
Gene Ontology
GO:0005737; C:cytoplasm; IBA:RefGenome
GO:0005829; C:cytosol; TAS:Reactome
GO:0017109; C:glutamate-cysteine ligase complex; IEA:Ensembl
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:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl
GO:0045454; P:cell redox homeostasis; IDA:UniProtKB
GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome
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:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome
GO:0019852; P:L-ascorbic acid metabolic process; IEA:Ensembl
GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB
GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl
GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl
GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl
GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB
GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl
GO:0050880; P:regulation of blood vessel size; IMP:UniProtKB
GO:0051900; P:regulation of mitochondrial depolarization; IEA:Ensembl
GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl
GO:0009408; P:response to heat; IDA:UniProtKB
GO:0009725; P:response to hormone; IDA:UniProtKB
GO:0051409; P:response to nitrosative stress; IEA:Ensembl
GO:0006979; P:response to oxidative stress; IDA:UniProtKB
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome
GO:0006805; P:xenobiotic metabolic process; TAS:Reactome
Interpro
InterPro; IPR004308; GCS
Pfam
Pfam; PF03074; GCS;
SMART
PROSITE
PRINTS