Home

GSS (human)

Overview GSS Defects in GSS are the cause of glutathione synthetase deficiency (GSS deficiency); also known as 5- oxoprolinuria or pyroglutamic aciduria. It is a severe form characterized by an increased rate of hemolysis and defective function of the central nervous system. Defects in GSS are the cause of glutathione synthetase deficiency of erythrocytes (GLUSYNDE)[MIM:231900]. Glutathione synthetase deficiency of erythrocytes is a mild form causing hemolytic anemia. Belongs to the eukaryotic GSH synthase family. Note: This description may include information from UniProtKB. Protein type: Other Amino Acids Metabolism - glutathione; Ligase; EC 6.3.2.3 Cellular Component: cytosol Molecular Function: protein homodimerization activity; glutathione binding; glycine binding; magnesium ion binding; glutathione synthase activity; ATP binding Biological Process: amino acid metabolic process; response to nutrient levels; nervous system development; response to cadmium ion; xenobiotic metabolic process; glutathione biosynthetic process; response to oxidative stress; response to amino acid stimulus; aging Reference #:  P48637 (UniProtKB) Alt. Names/Synonyms: Glutathione synthase; Glutathione synthetase; GSH synthetase; GSH-S; GSHB; GSHS; GSS; MGC14098 Gene Symbols: GSS Molecular weight: 52,385 Da Basal Isoelectric point: 5.67  Predict pI for various phosphorylation states

Select Structure to View Below GSS 2HGS - A=1-474 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  DISEASE 231900 266130 601002  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		R20	QQLEELARQAVDRAL
0	2		K108-u	ARLFDIHkQVLkEGI
0	4		K112-u	DIHkQVLkEGIAQTV
0	1		P138	QRSADGSPALkQIEI
0	11		K141-u	ADGSPALkQIEINtI
0	1		T147-p	LkQIEINtISASFGG
0	1		K172	HVLSVLSKTKEAGKI
0	1		K178	SKTKEAGKILSNNPS
0	10		K186-a	ILSNNPSkGLALGIA
0	2		K186-u	ILSNNPSkGLALGIA
0	1		K213-u	VLLIAQEkERNIFDQ
0	2		T238-p	NIHVIRRtFEDISEk
0	1		K245-u	tFEDISEkGSLDQDR
0	24		Y270-p	VVYFRDGyMPRQYSL
0	1		Y339	RATFAGLYSLDVGEE
0	1		K384-u	EEMVQALkQLKDSEE
0	1		K387	VQALkQLKDSEERAS
0	1		K400	ASYILMEKIEPEPFE
0	7		S415-p	NCLLRPGsPARVVQC
0	1		K452	VGHLLRTKAIEHADG

	mouse
K20-u	KQLEELAkQAIDRAL
K108-u	ARLFDIYkQVLkEGI
K112-u	DIYkQVLkEGIAQTV
K138-u	QCGADGSkALkQIEI
K141-u	ADGSkALkQIEINTI
T147	LkQIEINTISASFGG
K172-u	HVLNVLNkTKEASkI
K178-u	NkTKEASkILSNNPS
K186	ILSNNPSKGLALGIA
K186-u	ILSNNPSkGLALGIA
K213	VLLIAQEKERNIFDQ
R238	KIHVIRGRFEDVSER
R245	RFEDVSERGSLDQNR
Y270	VVYFRDGYMPSQYNS
Y339	RATFAGLYSLDMGEE
E384	EEMVQALEQLkDSEE
K387-u	VQALEQLkDSEERAS
K400-u	ASYILMEkIEPEPFR
S415-p	NCLLRPGsPAQVVQC
K452-u	VGHLLRTkAVEHADG

	rat
Q20	KQLEELAQQAIDRAL
K108	ARLFDIYKQVLKEGI
K112	DIYKQVLKEGIAQTV
K138	QCSADGSKALKQIEI
K141	ADGSKALKQIEINTI
T147	LKQIEINTISASFGG
K172	HVLNVLNKTNEASKI
K178	NKTNEASKILSNNPS
K186	ILSNNPSKGLALGIA
K186	ILSNNPSKGLALGIA
K213	VLLIAQEKERNIFDQ
R238	KIHVIRRRFEDVSER
R245	RFEDVSERGSLDQNR
Y270	VVYFRDGYMPSQYNA
Y339-p	RATFAGLySLDMGEE
E384	EEMVHALEQLKDSEE
K387	VHALEQLKDSEERAS
K400	ASYILMEKIEPEPFR
S415	NCLLRPGSPAQVVQC
K452	VGHLLRTKAIEHADG

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.