CPLM-010423

Genbank Nucleotide ID

Glutathione S-transferase omega-1

Protein Synonyms/Alias

GSTO-1; Glutathione S-transferase omega 1-1; GSTO 1-1; Glutathione-dependent dehydroascorbate reductase; Monomethylarsonic acid reductase; MMA(V) reductase; S-(Phenacyl)glutathione reductase; SPG-R

Homo sapiens (Human)

Position	Peptide	Type	References
11	ESARSLGKGSAPPGP	ubiquitination	[1, 2, 3, 4, 5, 6]
57	EVININLKNKPEWFF	acetylation	[6, 7, 8]
57	EVININLKNKPEWFF	ubiquitination	[4]
59	ININLKNKPEWFFKK	acetylation	[6]
59	ININLKNKPEWFFKK	ubiquitination	[4, 6]
65	NKPEWFFKKNPFGLV	acetylation	[7]
65	NKPEWFFKKNPFGLV	ubiquitination	[1, 2, 5, 9, 10]
66	KPEWFFKKNPFGLVP	ubiquitination	[4]
122	MILELFSKVPSLVGS	acetylation	[7]
136	SFIRSQNKEDYAGLK	acetylation	[11]
136	SFIRSQNKEDYAGLK	ubiquitination	[1, 5]
143	KEDYAGLKEEFRKEF	acetylation	[7]
148	GLKEEFRKEFTKLEE	acetylation	[7]
152	EFRKEFTKLEEVLTN	acetylation	[6, 7, 8, 11, 12]
152	EFRKEFTKLEEVLTN	ubiquitination	[4]
160	LEEVLTNKKTTFFGG	acetylation	[6, 11]
160	LEEVLTNKKTTFFGG	ubiquitination	[2]
188	FERLEAMKLNECVDH	ubiquitination	[2, 6]
207	KLWMAAMKEDPTVSA	ubiquitination	[2]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] 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]
[3] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[4] 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]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] 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]
[7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[10] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[11] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[12] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]

Functional Description

Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.

DOMAIN 22 101 GST N-terminal.
DOMAIN 106 230 GST C-terminal.
REGION 85 86 Glutathione binding.
ACT_SITE 32 32 Nucleophile.
BINDING 59 59 Glutathione.
BINDING 72 72 Glutathione; via amide nitrogen and
MOD_RES 2 2 N-acetylserine.
MOD_RES 57 57 N6-acetyllysine.
MOD_RES 143 143 N6-acetyllysine.
MOD_RES 148 148 N6-acetyllysine.
MOD_RES 152 152 N6-acetyllysine.

3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Oxidoreductase; Polymorphism; Reference proteome; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:UniProtKB.
GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
GO:0050610; F:methylarsonate reductase activity; IEA:EC.
GO:0071243; P:cellular response to arsenic-containing substance; IDA:UniProtKB.
GO:0019852; P:L-ascorbic acid metabolic process; IDA:UniProtKB.
GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO:0014810; P:positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; IC:BHF-UCL.
GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL.
GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.

IPR010987; Glutathione-S-Trfase_C-like.
IPR004045; Glutathione_S-Trfase_N.
IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
IPR004046; GST_C.
IPR005442; GST_omega.
IPR012336; Thioredoxin-like_fold.

PS50405; GST_CTER
PS50404; GST_NTER

PR01625; GSTRNSFRASEO.