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Glutathione synthetase (GSH synthetase) (GSH-S) (EC 6.3.2.3) (Glutathione synthase)

 GSHB_HUMAN              Reviewed;         474 AA.
P48637; B2R697; B6F210; E1P5P9; Q4TTD9;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
27-SEP-2017, entry version 180.
RecName: Full=Glutathione synthetase;
Short=GSH synthetase;
Short=GSH-S;
EC=6.3.2.3;
AltName: Full=Glutathione synthase;
Name=GSS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=7646467; DOI=10.1042/bj3100353;
Gali R.R., Board P.G.;
"Sequencing and expression of a cDNA for human glutathione
synthetase.";
Biochem. J. 310:353-358(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=19672693; DOI=10.1007/s11033-009-9675-3;
Uchida M., Sugaya M., Kanamaru T., Hisatomi H.;
"Alternative RNA splicing in expression of the glutathione synthetase
gene in human cells.";
Mol. Biol. Rep. 37:2105-2109(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
Shi Z.-Z., Galang R.L., Habib G.M., Lebovitz R.M., Lieberman M.W.;
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLU-437.
TISSUE=Substantia nigra;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-236 AND GLU-437.
NIEHS SNPs program;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 26-34; 113-125; 142-158; 222-230; 254-267;
274-283; 294-305; 419-434 AND 453-474, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-474 IN COMPLEX WITH ADP
AND GLUTATHIONE, COFACTOR, AND SUBUNIT.
PubMed=10369661; DOI=10.1093/emboj/18.12.3204;
Polekhina G., Board P.G., Gali R.R., Rossjohn J., Parker M.W.;
"Molecular basis of glutathione synthetase deficiency and a rare gene
permutation event.";
EMBO J. 18:3204-3213(1999).
[16]
VARIANTS GSS DEFICIENCY GLY-219; TRP-267 AND CYS-283.
PubMed=8896573; DOI=10.1038/ng1196-361;
Shi Z.-Z., Habib G.M., Rhead W.J., Gahl W.A., He X., Sazer S.,
Lieberman M.W.;
"Mutations in the glutathione synthetase gene cause 5-oxoprolinuria.";
Nat. Genet. 14:361-365(1996).
[17]
VARIANTS GSS DEFICIENCY.
PubMed=9215686; DOI=10.1093/hmg/6.7.1147;
Dahl N., Pigg M., Ristoff E., Gali R., Carlsson B., Mannervik B.,
Larsson A., Board P.;
"Missense mutations in the human glutathione synthetase gene result in
severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and
neurological dysfunction.";
Hum. Mol. Genet. 6:1147-1152(1997).
[18]
VARIANTS GSS DEFICIENCY GLY-219 AND PRO-301.
PubMed=27581854; DOI=10.1542/peds.2015-4324;
Signolet I., Chenouard R., Oca F., Barth M., Reynier P., Denis M.C.,
Simard G.;
"Recurrent isolated neonatal hemolytic anemia: think about glutathione
synthetase deficiency.";
Pediatrics 138:0-0(2016).
-!- CATALYTIC ACTIVITY: ATP + gamma-L-glutamyl-L-cysteine + glycine =
ADP + phosphate + glutathione.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10369661};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000269|PubMed:10369661};
-!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
from L-cysteine and L-glutamate: step 2/2.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10369661}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-2969145, EBI-2969145;
P54274:TERF1; NbExp=2; IntAct=EBI-2969145, EBI-710997;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P48637-1; Sequence=Displayed;
Name=2;
IsoId=P48637-2; Sequence=VSP_047617;
Note=Detected in colon, kidney, lung, liver, placenta,
peripheral blood and uterus, but not in heart, skeletal muscle
and spleen.;
-!- DISEASE: Glutathione synthetase deficiency (GSS deficiency)
[MIM:266130]: Severe form characterized by an increased rate of
hemolysis and defective function of the central nervous system.
{ECO:0000269|PubMed:27581854, ECO:0000269|PubMed:8896573,
ECO:0000269|PubMed:9215686}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Glutathione synthetase deficiency of erythrocytes
(GLUSYNDE) [MIM:231900]: Mild form causing hemolytic anemia.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the eukaryotic GSH synthase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/gss/";
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EMBL; L42531; AAA69492.1; -; mRNA.
EMBL; AB459500; BAG75452.1; -; mRNA.
EMBL; U34683; AAB62390.1; -; mRNA.
EMBL; AK312492; BAG35394.1; -; mRNA.
EMBL; DQ074975; AAY57328.1; -; Genomic_DNA.
EMBL; AL133324; CAB93423.1; -; Genomic_DNA.
EMBL; CH471077; EAW76239.1; -; Genomic_DNA.
EMBL; CH471077; EAW76240.1; -; Genomic_DNA.
EMBL; BC007927; AAH07927.1; -; mRNA.
CCDS; CCDS13245.1; -. [P48637-1]
PIR; S56748; S56748.
RefSeq; NP_000169.1; NM_000178.3. [P48637-1]
RefSeq; NP_001309423.1; NM_001322494.1. [P48637-1]
RefSeq; NP_001309424.1; NM_001322495.1. [P48637-1]
UniGene; Hs.82327; -.
PDB; 2HGS; X-ray; 2.10 A; A=1-474.
PDBsum; 2HGS; -.
ProteinModelPortal; P48637; -.
SMR; P48637; -.
BioGrid; 109192; 27.
IntAct; P48637; 3.
MINT; MINT-5001027; -.
STRING; 9606.ENSP00000216951; -.
DrugBank; DB06151; Acetylcysteine.
DrugBank; DB03408; gamma-Glutamylcysteine.
DrugBank; DB00143; Glutathione.
DrugBank; DB00145; Glycine.
DrugBank; DB00151; L-Cysteine.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
iPTMnet; P48637; -.
PhosphoSitePlus; P48637; -.
BioMuta; GSS; -.
DMDM; 1346191; -.
OGP; P48637; -.
REPRODUCTION-2DPAGE; IPI00010706; -.
EPD; P48637; -.
PaxDb; P48637; -.
PeptideAtlas; P48637; -.
PRIDE; P48637; -.
DNASU; 2937; -.
Ensembl; ENST00000216951; ENSP00000216951; ENSG00000100983. [P48637-1]
Ensembl; ENST00000451957; ENSP00000407517; ENSG00000100983. [P48637-2]
GeneID; 2937; -.
KEGG; hsa:2937; -.
UCSC; uc010zuo.3; human. [P48637-1]
CTD; 2937; -.
DisGeNET; 2937; -.
EuPathDB; HostDB:ENSG00000100983.9; -.
GeneCards; GSS; -.
HGNC; HGNC:4624; GSS.
HPA; HPA054508; -.
HPA; HPA059315; -.
MalaCards; GSS; -.
MIM; 231900; phenotype.
MIM; 266130; phenotype.
MIM; 601002; gene.
neXtProt; NX_P48637; -.
OpenTargets; ENSG00000100983; -.
Orphanet; 289846; Glutathione synthetase deficiency with 5-oxoprolinuria.
Orphanet; 289849; Glutathione synthetase deficiency without 5-oxoprolinuria.
PharmGKB; PA29015; -.
eggNOG; KOG0021; Eukaryota.
eggNOG; ENOG410XPHH; LUCA.
GeneTree; ENSGT00390000013764; -.
HOGENOM; HOG000172641; -.
HOVERGEN; HBG002458; -.
InParanoid; P48637; -.
KO; K21456; -.
OMA; FRSDYMV; -.
OrthoDB; EOG091G05V8; -.
PhylomeDB; P48637; -.
TreeFam; TF105187; -.
BioCyc; MetaCyc:HS02174-MONOMER; -.
BRENDA; 6.3.2.3; 2681.
Reactome; R-HSA-174403; Glutathione synthesis and recycling.
SABIO-RK; P48637; -.
UniPathway; UPA00142; UER00210.
ChiTaRS; GSS; human.
EvolutionaryTrace; P48637; -.
GenomeRNAi; 2937; -.
PRO; PR:P48637; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000100983; -.
CleanEx; HS_GSS; -.
ExpressionAtlas; P48637; baseline and differential.
Genevisible; P48637; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0043295; F:glutathione binding; IDA:UniProtKB.
GO; GO:0004363; F:glutathione synthase activity; IBA:GO_Central.
GO; GO:0016594; F:glycine binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
GO; GO:0006750; P:glutathione biosynthetic process; TAS:Reactome.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
CDD; cd00228; eu-GS; 1.
Gene3D; 1.10.1080.10; -; 2.
Gene3D; 3.30.1490.50; -; 1.
Gene3D; 3.30.1490.80; -; 1.
Gene3D; 3.40.50.1760; -; 1.
InterPro; IPR004887; Glutathione_synth_subst-bd_euk.
InterPro; IPR005615; Glutathione_synthase.
InterPro; IPR014042; Glutathione_synthase_a-hlx_euk.
InterPro; IPR014709; Glutathione_synthase_dom.
InterPro; IPR014049; Glutathione_synthase_N_euk.
InterPro; IPR016185; PreATP-grasp_dom.
PANTHER; PTHR11130; PTHR11130; 1.
Pfam; PF03917; GSH_synth_ATP; 1.
Pfam; PF03199; GSH_synthase; 1.
PIRSF; PIRSF001558; GSHase; 1.
SUPFAM; SSF52440; SSF52440; 1.
TIGRFAMs; TIGR01986; glut_syn_euk; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Direct protein sequencing; Disease mutation;
Glutathione biosynthesis; Hereditary hemolytic anemia; Ligase;
Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 474 Glutathione synthetase.
/FTId=PRO_0000211260.
NP_BIND 364 373 ATP.
NP_BIND 398 401 ATP.
REGION 148 151 Substrate binding.
REGION 214 216 Substrate binding.
REGION 267 270 Substrate binding.
REGION 461 462 Substrate binding.
METAL 144 144 Magnesium.
METAL 146 146 Magnesium.
METAL 368 368 Magnesium.
BINDING 125 125 Substrate.
BINDING 144 144 ATP.
BINDING 220 220 Substrate.
BINDING 305 305 ATP.
BINDING 375 375 ATP.
BINDING 425 425 ATP.
BINDING 450 450 Substrate.
BINDING 452 452 ATP.
BINDING 458 458 ATP; via carbonyl oxygen.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 93 203 Missing (in isoform 2).
{ECO:0000303|PubMed:19672693}.
/FTId=VSP_047617.
VARIANT 26 26 A -> D (in GSS deficiency;
dbSNP:rs759253242).
/FTId=VAR_003602.
VARIANT 188 188 L -> P (in GSS deficiency; 100-fold
reduction of activity).
/FTId=VAR_003603.
VARIANT 219 219 D -> A (in GSS deficiency).
/FTId=VAR_003604.
VARIANT 219 219 D -> G (in GSS deficiency;
dbSNP:rs28938472).
{ECO:0000269|PubMed:27581854,
ECO:0000269|PubMed:8896573}.
/FTId=VAR_003605.
VARIANT 236 236 R -> Q (in dbSNP:rs34239729).
{ECO:0000269|Ref.5}.
/FTId=VAR_025047.
VARIANT 254 254 L -> R (in GSS deficiency).
/FTId=VAR_003606.
VARIANT 267 267 R -> W (in GSS deficiency;
dbSNP:rs121909308).
{ECO:0000269|PubMed:8896573}.
/FTId=VAR_003607.
VARIANT 270 270 Y -> C (in GSS deficiency; 100-fold
reduction of activity).
/FTId=VAR_003608.
VARIANT 270 270 Y -> H (in GSS deficiency; 100-fold
reduction of activity).
/FTId=VAR_003609.
VARIANT 283 283 R -> C (in GSS deficiency; 10-fold
reduction of activity;
dbSNP:rs121909309).
{ECO:0000269|PubMed:8896573}.
/FTId=VAR_003610.
VARIANT 286 286 L -> Q (in GSS deficiency).
/FTId=VAR_003611.
VARIANT 301 301 L -> P (in GSS deficiency).
{ECO:0000269|PubMed:27581854}.
/FTId=VAR_078567.
VARIANT 330 330 R -> C (in GSS deficiency;
dbSNP:rs148640446).
/FTId=VAR_003612.
VARIANT 437 437 K -> E (in dbSNP:rs34852238).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.5}.
/FTId=VAR_025048.
VARIANT 464 464 G -> V (in GSS deficiency).
/FTId=VAR_003613.
VARIANT 469 469 D -> E (in GSS deficiency).
/FTId=VAR_003614.
HELIX 6 9 {ECO:0000244|PDB:2HGS}.
HELIX 12 28 {ECO:0000244|PDB:2HGS}.
STRAND 32 34 {ECO:0000244|PDB:2HGS}.
STRAND 43 47 {ECO:0000244|PDB:2HGS}.
STRAND 50 53 {ECO:0000244|PDB:2HGS}.
STRAND 56 58 {ECO:0000244|PDB:2HGS}.
HELIX 59 67 {ECO:0000244|PDB:2HGS}.
HELIX 69 81 {ECO:0000244|PDB:2HGS}.
HELIX 83 91 {ECO:0000244|PDB:2HGS}.
HELIX 93 96 {ECO:0000244|PDB:2HGS}.
HELIX 98 113 {ECO:0000244|PDB:2HGS}.
STRAND 119 132 {ECO:0000244|PDB:2HGS}.
STRAND 134 136 {ECO:0000244|PDB:2HGS}.
STRAND 138 146 {ECO:0000244|PDB:2HGS}.
HELIX 153 158 {ECO:0000244|PDB:2HGS}.
HELIX 160 169 {ECO:0000244|PDB:2HGS}.
HELIX 173 176 {ECO:0000244|PDB:2HGS}.
HELIX 184 199 {ECO:0000244|PDB:2HGS}.
STRAND 205 209 {ECO:0000244|PDB:2HGS}.
HELIX 217 228 {ECO:0000244|PDB:2HGS}.
TURN 229 231 {ECO:0000244|PDB:2HGS}.
STRAND 234 237 {ECO:0000244|PDB:2HGS}.
HELIX 239 245 {ECO:0000244|PDB:2HGS}.
STRAND 246 248 {ECO:0000244|PDB:2HGS}.
STRAND 254 256 {ECO:0000244|PDB:2HGS}.
STRAND 259 268 {ECO:0000244|PDB:2HGS}.
HELIX 272 274 {ECO:0000244|PDB:2HGS}.
HELIX 277 288 {ECO:0000244|PDB:2HGS}.
STRAND 289 295 {ECO:0000244|PDB:2HGS}.
HELIX 297 301 {ECO:0000244|PDB:2HGS}.
HELIX 305 310 {ECO:0000244|PDB:2HGS}.
HELIX 316 320 {ECO:0000244|PDB:2HGS}.
HELIX 325 333 {ECO:0000244|PDB:2HGS}.
STRAND 338 340 {ECO:0000244|PDB:2HGS}.
STRAND 342 344 {ECO:0000244|PDB:2HGS}.
HELIX 345 356 {ECO:0000244|PDB:2HGS}.
HELIX 358 360 {ECO:0000244|PDB:2HGS}.
STRAND 361 366 {ECO:0000244|PDB:2HGS}.
STRAND 369 371 {ECO:0000244|PDB:2HGS}.
HELIX 376 386 {ECO:0000244|PDB:2HGS}.
HELIX 390 394 {ECO:0000244|PDB:2HGS}.
STRAND 395 399 {ECO:0000244|PDB:2HGS}.
STRAND 406 411 {ECO:0000244|PDB:2HGS}.
STRAND 418 435 {ECO:0000244|PDB:2HGS}.
STRAND 438 453 {ECO:0000244|PDB:2HGS}.
TURN 461 464 {ECO:0000244|PDB:2HGS}.
STRAND 467 469 {ECO:0000244|PDB:2HGS}.
STRAND 472 474 {ECO:0000244|PDB:2HGS}.
SEQUENCE 474 AA; 52385 MW; 3C25EF7072EFE058 CRC64;
MATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF TLFPSLVPSA
LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT ARLFDIHKQV LKEGIAQTVF
LGLNRSDYMF QRSADGSPAL KQIEINTISA SFGGLASRTP AVHRHVLSVL SKTKEAGKIL
SNNPSKGLAL GIAKAWELYG SPNALVLLIA QEKERNIFDQ RAIENELLAR NIHVIRRTFE
DISEKGSLDQ DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ
LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA IAEALAAPSR
FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK IEPEPFENCL LRPGSPARVV
QCISELGIFG VYVRQEKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV


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