CPLM-004934

Genbank Nucleotide ID

Glutathione S-transferase Mu 3

Protein Synonyms/Alias

GST class-mu 3; GSTM3-3; hGSTM3-3

Homo sapiens (Human)

Position	Peptide	Type	References
35	TDTSYEEKRYTCGEA	ubiquitination	[1, 2]
54	RSQWLDVKFKLDLDF	ubiquitination	[1, 2, 3, 4]
128	SSDHEKLKPQYLEEL	ubiquitination	[2, 3, 4]
186	LDEFPNLKAFMCRFE	ubiquitination	[5]
197	CRFEALEKIAAYLQS	ubiquitination	[5]
209	LQSDQFCKMPINNKM	ubiquitination	[2]
215	CKMPINNKMAQWGNK	ubiquitination	[1, 2, 5, 6]
222	KMAQWGNKPVC****	ubiquitination	[1, 2, 5]

[1] 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]
[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] 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]
[4] 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]
[5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[6] 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]

Functional Description

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers.

DOMAIN 5 92 GST N-terminal.
DOMAIN 94 212 GST C-terminal.
REGION 11 12 Glutathione binding (By similarity).
REGION 50 54 Glutathione binding (By similarity).
REGION 63 64 Glutathione binding (By similarity).
REGION 76 77 Glutathione binding (By similarity).
BINDING 120 120 Substrate (By similarity).

3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Polymorphism; Reference proteome; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO:0043295; F:glutathione binding; IDA:BHF-UCL.
GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO:0070458; P:cellular detoxification of nitrogen compound; IDA:BHF-UCL.
GO:0008065; P:establishment of blood-nerve barrier; TAS:ProtInc.
GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
GO:0018916; P:nitrobenzene metabolic process; IDA:BHF-UCL.
GO:0043627; P:response to estrogen stimulus; IEP:UniProtKB.
GO:0042178; P:xenobiotic catabolic process; IDA:BHF-UCL.

IPR010987; Glutathione-S-Trfase_C-like.
IPR004045; Glutathione_S-Trfase_N.
IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
IPR004046; GST_C.
IPR003081; GST_mu.
IPR012336; Thioredoxin-like_fold.

PF00043; GST_C
PF02798; GST_N

PS50405; GST_CTER
PS50404; GST_NTER

PR01267; GSTRNSFRASEM.