UniProt Accession

 GSTP1_HUMAN; P09211; O00460; Q15690; Q5TZY3 

Genbank Protein ID

 X06547; M24485; X08058; X08094; X08095; X08096; X15480; U12472; U30897; U62589; U21689; BT019949; BT019950; CR450361; AY324387; BC010915 

Genbank Nucleotide ID

 CAA29794.1; AAA56823.1; CAA30847.1; CAA30894.1; CAA30894.1; CAA30894.1; CAA33508.1; AAA64919.1; AAC51280.1; AAC51237.1; AAC13869.1; AAV38752.1; AAV38753.1; CAG29357.1; AAP72967.1; AAH10915.1 

Protein Name

 Glutathione S-transferase P 

Protein Synonyms/Alias

 GST class-pi; GSTP1-1 

Gene Name

 GSTP1 

Gene Synonyms/Alias

 FAEES3; GST3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
55	CLYGQLPKFQDGDLT	ubiquitination	[1]
82	RTLGLYGKDQQEAAL	ubiquitination	[1, 2, 3]
103	GVEDLRCKYISLIYT	ubiquitination	[1, 3, 4]
116	YTNYEAGKDDYVKAL	acetylation	[5]
121	AGKDDYVKALPGQLK	acetylation	[6]
121	AGKDDYVKALPGQLK	ubiquitination	[1, 7]
128	KALPGQLKPFETLLS	acetylation	[4, 6, 8, 9]
128	KALPGQLKPFETLLS	ubiquitination	[1, 2, 3, 4, 7, 10, 11, 12, 13]
189	GRLSARPKLKAFLAS	ubiquitination	[1]
191	LSARPKLKAFLASPE	ubiquitination	[1, 3, 7, 12, 13]
209	LPINGNGKQ******	ubiquitination	[1]

Reference

 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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] 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]
 [10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [11] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [12] 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]
 [13] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

Functional Description

 Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. 

Sequence Annotation

 DOMAIN 2 81 GST N-terminal.
 DOMAIN 83 204 GST C-terminal.
 REGION 52 53 Glutathione binding.
 REGION 65 66 Glutathione binding.
 BINDING 8 8 Glutathione.
 BINDING 14 14 Glutathione.
 BINDING 39 39 Glutathione.
 BINDING 45 45 Glutathione (By similarity).
 MOD_RES 4 4 Phosphotyrosine; by EGFR.
 MOD_RES 109 109 Phosphotyrosine (By similarity).
 MOD_RES 128 128 N6-acetyllysine.
 MOD_RES 199 199 Phosphotyrosine; by EGFR.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 210 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0097057; C:TRAF2-GSTP1 complex; IDA:BHF-UCL.
 GO:0035731; F:dinitrosyl-iron complex binding; IDA:BHF-UCL.
 GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
 GO:0008432; F:JUN kinase binding; ISS:BHF-UCL.
 GO:0019207; F:kinase regulator activity; ISS:BHF-UCL.
 GO:0070026; F:nitric oxide binding; NAS:BHF-UCL.
 GO:0035730; F:S-nitrosoglutathione binding; IDA:BHF-UCL.
 GO:0071222; P:cellular response to lipopolysaccharide; ISS:BHF-UCL.
 GO:0007417; P:central nervous system development; TAS:ProtInc.
 GO:0035726; P:common myeloid progenitor cell proliferation; ISS:BHF-UCL.
 GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
 GO:0002674; P:negative regulation of acute inflammatory response; NAS:BHF-UCL.
 GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
 GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
 GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
 GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB cascade; ISS:BHF-UCL.
 GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:BHF-UCL.
 GO:0043508; P:negative regulation of JUN kinase activity; IDA:BHF-UCL.
 GO:0070664; P:negative regulation of leukocyte proliferation; ISS:BHF-UCL.
 GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IDA:BHF-UCL.
 GO:0060547; P:negative regulation of necrotic cell death; ISS:BHF-UCL.
 GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
 GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISS:BHF-UCL.
 GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
 GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IC:BHF-UCL.
 GO:0035732; P:nitric oxide storage; NAS:BHF-UCL.
 GO:0032930; P:positive regulation of superoxide anion generation; ISS:BHF-UCL.
 GO:0000302; P:response to reactive oxygen species; ISS:BHF-UCL.
 GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB. 

Interpro

 IPR010987; Glutathione-S-Trfase_C-like.
 IPR004045; Glutathione_S-Trfase_N.
 IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
 IPR004046; GST_C.
 IPR003082; GST_pi.
 IPR012336; Thioredoxin-like_fold. 

Pfam

 PF00043; GST_C
 PF02798; GST_N 

SMART

  

PROSITE

 PS50405; GST_CTER
 PS50404; GST_NTER 

PRINTS

 PR01268; GSTRNSFRASEP.