Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Glutathione S-transferase P  

UniProtKB / Swiss-Prot ID :  GSTP1_HUMAN

Gene Name (Synonyms) : 
GSTP1, FAEES3, GST3  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Mitochondrion. Nucleus. Note=The 83 N-terminal amino-acids function as un uncleaved transit peptide, and arginine residues within it are crucial for motochondrial localization. 

Protein Function :  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. 

Protein Sequence MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTIL...
Predicted Secondary Structure CCCCEEEEECCCCCHHHHHHHHHHCCCCEEEEEECHHHCCCCCCCCCCCCCCCCEEEECCEEEEHHHHHH...
Protein Variant
LocationDescription
105I -> V (in allele GSTP1*B and alleleGSTP1*C; dbSNP:rs1695).
114A -> V (in allele GSTP1*C;dbSNP:rs1138272).
169G -> D (in dbSNP:rs41462048). VAR_049493
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
4Phosphotyrosine-MPPYTVVY
-CCCCEEEE
13.29Phosphositeplus
Link
4Phosphotyrosine; by EGFR.-MPPYTVVY
-CCCCEEEE
13.29UniProtKB
Link
8PhosphotyrosineYTVVYFPVR
CEEEEECCC
9.60Phosphositeplus
Link
8Phosphotyrosine.YTVVYFPVR
CEEEEECCC
9.60UniProtKB
Link
43PhosphoserineWQEGSLKAS
CCCCCCCCC
26.41HPRD
Link
43PhosphoserineWQEGSLKAS
CCCCCCCCC
26.41Phosphositeplus
Link
48S-nitrosocysteineLKASCLYGQ
CCCCCCCCC
3.97dbSNO
Link
64PhosphotyrosineDLTLYQSNT
CEEEEHHHH
12.50Phosphositeplus
Link
82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GLYGKDQQE
CCCCCCHHH
38.51Phosphositeplus
Link
109PhosphotyrosineISLIYTNYE
HHHHCCCHH
8.33Phosphositeplus
Link
116N6-acetyllysineYEAGKDDYV
HHHHHHHHH
55.25Phosphositeplus
Link
121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DDYVKALPG
HHHHHHHHH
37.67Phosphositeplus
Link
121N6-acetyllysineDDYVKALPG
HHHHHHHHH
37.67HPRD
Link
121N6-acetyllysineDDYVKALPG
HHHHHHHHH
37.67Phosphositeplus
Link
121N6-acetyllysine.DDYVKALPG
HHHHHHHHH
37.67UniProtKB
Link
128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PGQLKPFET
HHHHHHHHH
39.51Phosphositeplus
Link
128N6-acetyllysinePGQLKPFET
HHHHHHHHH
39.51HPRD
Link
128N6-acetyllysinePGQLKPFET
HHHHHHHHH
39.51Phosphositeplus
Link
128N6-acetyllysine.PGQLKPFET
HHHHHHHHH
39.51UniProtKB
Link
185PhosphoserineVGRLSARPK
HHHHHCCHH
22.37Phosphositeplus
Link
191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RPKLKAFLA
CHHHHHHHC
43.13Phosphositeplus
Link
199PhosphotyrosineASPEYVNLP
CCCCCCCCC
9.68Phosphositeplus
Link
199Phosphotyrosine; by EGFR.ASPEYVNLP
CCCCCCCCC
9.68UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TGM2_HUMANphysical interactionMINT-16698MINT9973324
PNO1_HUMANphysical interactionMINT-63446MINT16169070
PTN_HUMANphysical interactionEBI-730096
intact16169070
PNO1_HUMANphysical interactionEBI-732085
intact16169070
GSTP1_HUMANin vitroHPRD:00614HPRD9398518
PTN_HUMANyeast 2-hybridHPRD:00614HPRD16169070
TRAF2_HUMANin vitro
in vivo
HPRD:00614HPRD16636664
PNO1_HUMANyeast 2-hybridHPRD:00614HPRD16169070
CP3A5_HUMANENSP00000196968STRING
GSTT1_HUMANENSP00000196968STRING
HYEP_HUMANENSP00000196968STRING
CHST2_HUMANENSP00000196968STRING
CP3A4_HUMANENSP00000196968STRING
CP3A4_HUMANENSP00000196968STRING
CP1A2_HUMANENSP00000196968STRING
MK08_HUMANENSP00000196968STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB01008Busulfan
DB04339Carbocisteine
DB00958Carboplatin
DB00291Chlorambucil
DB00515Cisplatin
DB01242Clomipramine
DB00773Etoposide
DB00143Glutathione
DB00526Oxaliplatin
DB00163Vitamin E
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-121 AND LYS-128, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylation of the human glutathione S-transferase P1 byepidermal growth factor receptor.";
Okamura T., Singh S., Buolamwini J., Haystead T., Friedman H.,Bigner D., Ali-Osman F.;
J. Biol. Chem. 284:16979-16989(2009).
Cited for: PHOSPHORYLATION AT TYR-4 AND TYR-199.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-8, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures