HUMAN:GSTP1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	GSTP1 (synonyms: FAEES3, GST3)
Protein Name(s)	Glutathione S-transferase P GST class-pi GSTP1-1
External Links
UniProt	P09211
EMBL	X06547 M24485 X08058 X08094 X08095 X08096 X15480 U12472 U30897 U62589 U21689 BT019949 BT019950 CR450361 AY324387 BC010915
CCDS	CCDS41679.1
PIR	A41177 JS0153
RefSeq	NP_000843.1
UniGene	Hs.523836
PDB	10GS 11GS 12GS 13GS 14GS 16GS 17GS 18GS 19GS 1AQV 1AQW 1AQX 1EOG 1EOH 1GSS 1KBN 1LBK 1MD3 1MD4 1PGT 1PX6 1PX7 1ZGN 20GS 22GS 2A2R 2A2S 2GSS 2J9H 2PGT 3CSH 3CSI 3CSJ 3DD3 3DGQ 3GSS 3GUS 3HJM 3HJO 3HKR 3IE3 3KM6 3KMN 3KMO 3N9J 3PGT 4GSS 4PGT 5GSS 6GSS 7GSS 8GSS 9GSS
PDBsum	10GS 11GS 12GS 13GS 14GS 16GS 17GS 18GS 19GS 1AQV 1AQW 1AQX 1EOG 1EOH 1GSS 1KBN 1LBK 1MD3 1MD4 1PGT 1PX6 1PX7 1ZGN 20GS 22GS 2A2R 2A2S 2GSS 2J9H 2PGT 3CSH 3CSI 3CSJ 3DD3 3DGQ 3GSS 3GUS 3HJM 3HJO 3HKR 3IE3 3KM6 3KMN 3KMO 3N9J 3PGT 4GSS 4PGT 5GSS 6GSS 7GSS 8GSS 9GSS
ProteinModelPortal	P09211
SMR	P09211
BioGrid	109205
IntAct	P09211
MINT	MINT-4998983
STRING	9606.ENSP00000381607
BindingDB	P09211
ChEMBL	CHEMBL3902
DrugBank	DB01008 DB00958 DB00291 DB00515 DB01242 DB00773 DB00143 DB00526 DB00163
PhosphoSite	P09211
DOSAC-COBS-2DPAGE	P09211
OGP	P09211
REPRODUCTION-2DPAGE	IPI00219757
SWISS-2DPAGE	P09211
UCD-2DPAGE	P09211
MaxQB	P09211
PaxDb	P09211
PRIDE	P09211
DNASU	2950
Ensembl	ENST00000398606
GeneID	2950
KEGG	hsa:2950
UCSC	uc001omf.3
CTD	2950
GeneCards	GC11P067351
HGNC	HGNC:4638
HPA	CAB019298 HPA019779 HPA019869
MIM	134660
neXtProt	NX_P09211
PharmGKB	PA29028
eggNOG	KOG1695
HOGENOM	HOG000115733
HOVERGEN	HBG108324
InParanoid	P09211
KO	K00799
OMA	LRCKYAT
OrthoDB	EOG7KH9M3
PhylomeDB	P09211
TreeFam	TF105321
Reactome	REACT_172715 REACT_6926
SABIO-RK	P09211
ChiTaRS	GSTP1
EvolutionaryTrace	P09211
GeneWiki	GSTP1
GenomeRNAi	2950
NextBio	11692
PMAP-CutDB	P09211
PRO	PR:P09211
Proteomes	UP000005640
Bgee	P09211
CleanEx	HS_GSTP1
ExpressionAtlas	P09211
Genevestigator	P09211
GO	GO:0005737 GO:0005829 GO:0005615 GO:0070062 GO:0005622 GO:0005739 GO:0005634 GO:0005886 GO:0097057 GO:0031982 GO:0035731 GO:0004364 GO:0008432 GO:0019207 GO:0070026 GO:0035730 GO:0071222 GO:0007417 GO:0035726 GO:1901687 GO:0006749 GO:0002674 GO:0043066 GO:0009890 GO:0070373 GO:2001237 GO:0048147 GO:0043124 GO:0032691 GO:0043508 GO:0070664 GO:0043407 GO:0043409 GO:0071638 GO:0051771 GO:0006469 GO:0032873 GO:0032720 GO:0010804 GO:0035732 GO:0032930 GO:0070372 GO:0032872 GO:0000302 GO:0044281 GO:0006805
Gene3D	1.20.1050.10 3.40.30.10
InterPro	IPR010987 IPR004045 IPR004046 IPR003082 IPR012336
Pfam	PF00043 PF02798
PRINTS	PR01268
SUPFAM	SSF47616 SSF52833
PROSITE	PS50405 PS50404

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0043651	linoleic acid metabolic process	PMID:16624487^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004602	glutathione peroxidase activity	PMID:16624487^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(CHEBI:91272) has_output:(CHEBI:72639)\|part_of(GO:0043651)\|inhibited_by(CHEBI:72639)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031982	vesicle	PMID:19190083^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002202)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:23580065^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:22664934^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
involved_in	GO:2001237	negative regulation of extrinsic apoptotic signaling pathway	PMID:16636664^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0097057	TRAF2-GSTP1 complex	PMID:16636664^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071638	negative regulation of monocyte chemotactic protein-1 production	PMID:18962899^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071222	cellular response to lipopolysaccharide	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	P		Seeded From UniProt	complete
involved_in	GO:0070664	negative regulation of leukocyte proliferation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	P		Seeded From UniProt	complete
involved_in	GO:0070373	negative regulation of ERK1 and ERK2 cascade	PMID:11408560^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070372	regulation of ERK1 and ERK2 cascade	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	P		Seeded From UniProt	complete
enables	GO:0070026	nitric oxide binding	PMID:11533048^[11]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051771	negative regulation of nitric-oxide synthase biosynthetic process	PMID:18962899^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048147	negative regulation of fibroblast proliferation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	P		Seeded From UniProt	complete
involved_in	GO:0043508	negative regulation of JUN kinase activity	PMID:16636664^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043409	negative regulation of MAPK cascade	PMID:18962899^[9]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043407	negative regulation of MAP kinase activity	PMID:11408560^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043124	negative regulation of I-kappaB kinase/NF-kappaB signaling	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	P		Seeded From UniProt	complete
involved_in	GO:0035732	nitric oxide storage	PMID:12871931^[12]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0035731	dinitrosyl-iron complex binding	PMID:11533048^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0035731	dinitrosyl-iron complex binding	PMID:12871945^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0035730	S-nitrosoglutathione binding	PMID:11533048^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0035726	common myeloid progenitor cell proliferation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	P		Seeded From UniProt	complete
involved_in	GO:0032930	positive regulation of superoxide anion generation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	P		Seeded From UniProt	complete
involved_in	GO:0032873	negative regulation of stress-activated MAPK cascade	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	P		Seeded From UniProt	complete
involved_in	GO:0032872	regulation of stress-activated MAPK cascade	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	P		Seeded From UniProt	complete
involved_in	GO:0032720	negative regulation of tumor necrosis factor production	PMID:18962899^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032691	negative regulation of interleukin-1 beta production	PMID:18962899^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019207	kinase regulator activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	F		Seeded From UniProt	complete
involved_in	GO:0010804	negative regulation of tumor necrosis factor-mediated signaling pathway	PMID:16636664^[8]	ECO:0000305	curator inference used in manual assertion	GO:0005515	P		Seeded From UniProt	complete
involved_in	GO:0009890	negative regulation of biosynthetic process	PMID:18962899^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008432	JUN kinase binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	F		Seeded From UniProt	complete
involved_in	GO:0006469	negative regulation of protein kinase activity	PMID:16636664^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0002674	negative regulation of acute inflammatory response	PMID:18962899^[9]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000302	response to reactive oxygen species	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P19157	P		Seeded From UniProt	complete
involved_in	GO:0006805	xenobiotic metabolic process	PMID:1540159^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006749	glutathione metabolic process	PMID:1540159^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004364	glutathione transferase activity	PMID:1540159^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0098869	cellular oxidant detoxification	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004602	P		Seeded From UniProt	complete
involved_in	GO:1904706	negative regulation of vascular smooth muscle cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0071672	negative regulation of smooth muscle cell chemotaxis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0071460	cellular response to cell-matrix adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0071385	cellular response to glucocorticoid stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0071364	cellular response to epidermal growth factor stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0045471	response to ethanol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
enables	GO:0043295	glutathione binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	F		Seeded From UniProt	complete
involved_in	GO:0043200	response to amino acid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0033591	response to L-ascorbic acid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0032869	cellular response to insulin stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0032355	response to estradiol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0031667	response to nutrient levels	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0031100	animal organ regeneration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	F		Seeded From UniProt	complete
involved_in	GO:0014003	oligodendrocyte development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0009636	response to toxic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
enables	GO:0008144	drug binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	F		Seeded From UniProt	complete
involved_in	GO:0006805	xenobiotic metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
involved_in	GO:0006469	negative regulation of protein kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	C		Seeded From UniProt	complete
enables	GO:0004364	glutathione transferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P04906 ensembl:ENSRNOP00000024601	F		Seeded From UniProt	complete
enables	GO:0004364	glutathione transferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003082	F		Seeded From UniProt	complete
enables	GO:0004364	glutathione transferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.5.1.18	F		Seeded From UniProt	complete
involved_in	GO:0007417	central nervous system development	PMID:9802272^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:16130169^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16130169^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1904813	ficolin-1-rich granule lumen	Reactome:R-HSA-6800434	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901687	glutathione derivative biosynthetic process	Reactome:R-HSA-156590	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0034774	secretory granule lumen	Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	Reactome:R-HSA-3299685	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-3343700 Reactome:R-HSA-176054	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6800434 Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Seeley, SK et al. (2006) Metabolism of oxidized linoleic acid by glutathione transferases: peroxidase activity toward 13-hydroperoxyoctadecadienoic acid. Biochim. Biophys. Acta 1760 1064-70 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ ^5.0 ^5.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page
↑ Böhm, D et al. (2012) Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Oncol. Rep. 28 429-38 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 Wu, Y et al. (2006) Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals. Oncogene 25 5787-800 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 Luo, L et al. (2009) Recombinant protein glutathione S-transferases P1 attenuates inflammation in mice. Mol. Immunol. 46 848-57 PubMed GONUTS page
↑ ^10.0 ^10.1 Ruscoe, JE et al. (2001) Pharmacologic or genetic manipulation of glutathione S-transferase P1-1 (GSTpi) influences cell proliferation pathways. J. Pharmacol. Exp. Ther. 298 339-45 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Lo Bello, M et al. (2001) Human glutathione transferase P1-1 and nitric oxide carriers; a new role for an old enzyme. J. Biol. Chem. 276 42138-45 PubMed GONUTS page
↑ Turella, P et al. (2003) Glutathione transferase superfamily behaves like storage proteins for dinitrosyl-diglutathionyl-iron complex in heterogeneous systems. J. Biol. Chem. 278 42294-9 PubMed GONUTS page
↑ De Maria, F et al. (2003) The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily: suggestion for an evolutionary pressure in the direction of the storage of nitric oxide. J. Biol. Chem. 278 42283-93 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Kong, KH et al. (1992) Tyrosine-7 is an essential residue for the catalytic activity of human class PI glutathione S-transferase: chemical modification and site-directed mutagenesis studies. Biochem. Biophys. Res. Commun. 182 1122-9 PubMed GONUTS page
↑ Menegon, A et al. (1998) Parkinson's disease, pesticides, and glutathione transferase polymorphisms. Lancet 352 1344-6 PubMed GONUTS page
↑ ^16.0 ^16.1 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

[PMID:16624487-1] 1.0 ^1.1 Seeley, SK et al. (2006) Metabolism of oxidized linoleic acid by glutathione transferases: peroxidase activity toward 13-hydroperoxyoctadecadienoic acid. Biochim. Biophys. Acta 1760 1064-70 PubMed GONUTS page

[PMID:23533145-2] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19190083-3] Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page

[PMID:19056867-4] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-5] 5.0 ^5.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:23580065-6] Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page

[PMID:22664934-7] Böhm, D et al. (2012) Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Oncol. Rep. 28 429-38 PubMed GONUTS page

[PMID:16636664-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 Wu, Y et al. (2006) Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals. Oncogene 25 5787-800 PubMed GONUTS page

[PMID:18962899-9] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 Luo, L et al. (2009) Recombinant protein glutathione S-transferases P1 attenuates inflammation in mice. Mol. Immunol. 46 848-57 PubMed GONUTS page

[PMID:11408560-10] 10.0 ^10.1 Ruscoe, JE et al. (2001) Pharmacologic or genetic manipulation of glutathione S-transferase P1-1 (GSTpi) influences cell proliferation pathways. J. Pharmacol. Exp. Ther. 298 339-45 PubMed GONUTS page

[PMID:11533048-11] 11.0 ^11.1 ^11.2 Lo Bello, M et al. (2001) Human glutathione transferase P1-1 and nitric oxide carriers; a new role for an old enzyme. J. Biol. Chem. 276 42138-45 PubMed GONUTS page

[PMID:12871931-12] Turella, P et al. (2003) Glutathione transferase superfamily behaves like storage proteins for dinitrosyl-diglutathionyl-iron complex in heterogeneous systems. J. Biol. Chem. 278 42294-9 PubMed GONUTS page

[PMID:12871945-13] De Maria, F et al. (2003) The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily: suggestion for an evolutionary pressure in the direction of the storage of nitric oxide. J. Biol. Chem. 278 42283-93 PubMed GONUTS page

[PMID:1540159-14] 14.0 ^14.1 ^14.2 Kong, KH et al. (1992) Tyrosine-7 is an essential residue for the catalytic activity of human class PI glutathione S-transferase: chemical modification and site-directed mutagenesis studies. Biochem. Biophys. Res. Commun. 182 1122-9 PubMed GONUTS page

[PMID:9802272-15] Menegon, A et al. (1998) Parkinson's disease, pesticides, and glutathione transferase polymorphisms. Lancet 352 1344-6 PubMed GONUTS page

[PMID:16130169-16] 16.0 ^16.1 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

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