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Protein

Glutathione S-transferase P 1

Gene

Gstp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (By similarity).By similarity

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei8Glutathione1 Publication1
Binding sitei14Glutathione1 Publication1
Binding sitei39Glutathione1 Publication1
Binding sitei45Glutathione1 Publication1

GO - Molecular functioni

  • dinitrosyl-iron complex binding Source: MGI
  • drug binding Source: BHF-UCL
  • glutathione peroxidase activity Source: MGI
  • glutathione transferase activity Source: MGI
  • JUN kinase binding Source: BHF-UCL
  • kinase regulator activity Source: BHF-UCL
  • S-nitrosoglutathione binding Source: MGI

GO - Biological processi

  • animal organ regeneration Source: BHF-UCL
  • cellular response to cell-matrix adhesion Source: BHF-UCL
  • cellular response to epidermal growth factor stimulus Source: BHF-UCL
  • cellular response to glucocorticoid stimulus Source: BHF-UCL
  • cellular response to insulin stimulus Source: BHF-UCL
  • cellular response to lipopolysaccharide Source: BHF-UCL
  • common myeloid progenitor cell proliferation Source: BHF-UCL
  • glutathione metabolic process Source: MGI
  • negative regulation of acute inflammatory response Source: BHF-UCL
  • negative regulation of apoptotic process Source: BHF-UCL
  • negative regulation of biosynthetic process Source: BHF-UCL
  • negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  • negative regulation of fibroblast proliferation Source: BHF-UCL
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  • negative regulation of interleukin-1 beta production Source: BHF-UCL
  • negative regulation of JUN kinase activity Source: BHF-UCL
  • negative regulation of leukocyte proliferation Source: BHF-UCL
  • negative regulation of MAP kinase activity Source: BHF-UCL
  • negative regulation of monocyte chemotactic protein-1 production Source: BHF-UCL
  • negative regulation of neutrophil aggregation Source: BHF-UCL
  • negative regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  • negative regulation of peroxidase activity Source: BHF-UCL
  • negative regulation of stress-activated MAPK cascade Source: BHF-UCL
  • negative regulation of tumor necrosis factor production Source: BHF-UCL
  • oligodendrocyte development Source: BHF-UCL
  • positive regulation of superoxide anion generation Source: BHF-UCL
  • regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • regulation of stress-activated MAPK cascade Source: BHF-UCL
  • response to amino acid Source: BHF-UCL
  • response to estradiol Source: BHF-UCL
  • response to ethanol Source: BHF-UCL
  • response to L-ascorbic acid Source: BHF-UCL
  • response to nutrient levels Source: BHF-UCL
  • response to reactive oxygen species Source: BHF-UCL
  • response to toxic substance Source: BHF-UCL
  • xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 3474.
ReactomeiR-MMU-156590. Glutathione conjugation.
R-MMU-3299685. Detoxification of Reactive Oxygen Species.
R-MMU-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase P 1 (EC:2.5.1.18)
Short name:
Gst P1
Alternative name(s):
GST YF-YF
GST class-pi
GST-piB
Preadipocyte growth factor
Gene namesi
Name:Gstp1
Synonyms:Gstpib
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:95865. Gstp1.

Subcellular locationi

  • Cytoplasm By similarity
  • Mitochondrion By similarity
  • Nucleus By similarity

  • Note: The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.By similarity

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytosol Source: BHF-UCL
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • intracellular Source: BHF-UCL
  • mitochondrion Source: MGI
  • nucleus Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
  • protein complex Source: BHF-UCL
  • TRAF2-GSTP1 complex Source: MGI
  • vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001859032 – 210Glutathione S-transferase P 1Add BLAST209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4Phosphotyrosine; by EGFRBy similarity1
Modified residuei62PhosphothreonineBy similarity1
Modified residuei103N6-succinyllysineCombined sources1
Modified residuei116N6-succinyllysineCombined sources1
Modified residuei128N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP19157.
MaxQBiP19157.
PaxDbiP19157.
PeptideAtlasiP19157.
PRIDEiP19157.
TopDownProteomicsiP19157.

2D gel databases

REPRODUCTION-2DPAGEP19157.
SWISS-2DPAGEP19157.

PTM databases

iPTMnetiP19157.
PhosphoSitePlusiP19157.
SwissPalmiP19157.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiENSMUSG00000060803.
CleanExiMM_GSTP1.
GenevisibleiP19157. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with CDK5 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Prdx6O087092EBI-2309446,EBI-444895

GO - Molecular functioni

  • JUN kinase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi200101. 3 interactors.
IntActiP19157. 6 interactors.
MINTiMINT-1869068.
STRINGi10090.ENSMUSP00000129565.

Structurei

Secondary structure

1210
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi10 – 12Combined sources3
Helixi13 – 15Combined sources3
Helixi16 – 24Combined sources9
Beta strandi29 – 33Combined sources5
Helixi36 – 40Combined sources5
Beta strandi42 – 44Combined sources3
Helixi45 – 47Combined sources3
Beta strandi49 – 51Combined sources3
Beta strandi55 – 58Combined sources4
Beta strandi61 – 65Combined sources5
Helixi66 – 77Combined sources12
Helixi84 – 110Combined sources27
Helixi112 – 135Combined sources24
Helixi138 – 140Combined sources3
Beta strandi144 – 148Combined sources5
Helixi151 – 166Combined sources16
Turni168 – 173Combined sources6
Helixi175 – 186Combined sources12
Helixi188 – 195Combined sources8
Helixi197 – 200Combined sources4
Beta strandi204 – 208Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BAYX-ray2.00A/B2-210[»]
1GLPX-ray1.90A/B2-210[»]
1GLQX-ray1.80A/B2-210[»]
1GSYX-ray2.44A/B2-210[»]
1GTIX-ray3.00A/B/C/D/E/F2-210[»]
2GLRX-ray2.20A/B2-210[»]
2OA7X-ray2.20A/B2-210[»]
2OACX-ray2.20A/B2-210[»]
2OADX-ray2.50A/B2-210[»]
3O76X-ray1.77A/B2-210[»]
ProteinModelPortaliP19157.
SMRiP19157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19157.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 81GST N-terminalAdd BLAST80
Domaini83 – 204GST C-terminalAdd BLAST122

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni52 – 53Glutathione binding1 Publication2
Regioni65 – 66Glutathione binding1 Publication2

Sequence similaritiesi

Belongs to the GST superfamily. Pi family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiKOG1695. Eukaryota.
ENOG4111VAU. LUCA.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115733.
HOVERGENiHBG108324.
InParanoidiP19157.
KOiK00799.
OMAiLRCKYAT.
OrthoDBiEOG091G0K2E.
PhylomeDBiP19157.
TreeFamiTF105321.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19157-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPYTIVYFP VRGRCEAMRM LLADQGQSWK EEVVTIDTWM QGLLKPTCLY
60 70 80 90 100
GQLPKFEDGD LTLYQSNAIL RHLGRSLGLY GKNQREAAQM DMVNDGVEDL
110 120 130 140 150
RGKYVTLIYT NYENGKNDYV KALPGHLKPF ETLLSQNQGG KAFIVGDQIS
160 170 180 190 200
FADYNLLDLL LIHQVLAPGC LDNFPLLSAY VARLSARPKI KAFLSSPEHV
210
NRPINGNGKQ
Length:210
Mass (Da):23,609
Last modified:January 23, 2007 - v2
Checksum:iDAC7762F4E34FF27
GO

Mass spectrometryi

Molecular mass is 23478.8±2 Da from positions 2 - 210. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53451 mRNA. Translation: CAA37529.1.
X76143 Genomic DNA. No translation available.
U15654 Genomic DNA. Translation: AAA64837.1.
D30687 mRNA. Translation: BAA06349.1.
BC002048 mRNA. Translation: AAH02048.1.
BC061109 mRNA. Translation: AAH61109.1.
AK079144 mRNA. Translation: BAC37560.1.
CCDSiCCDS29411.1.
PIRiS12709. B55140.
RefSeqiNP_038569.1. NM_013541.1.
UniGeneiMm.299292.

Genome annotation databases

EnsembliENSMUST00000169613; ENSMUSP00000129565; ENSMUSG00000060803.
ENSMUST00000180480; ENSMUSP00000138073; ENSMUSG00000097830.
GeneIDi14870.
KEGGimmu:14870.
UCSCiuc008fyf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53451 mRNA. Translation: CAA37529.1.
X76143 Genomic DNA. No translation available.
U15654 Genomic DNA. Translation: AAA64837.1.
D30687 mRNA. Translation: BAA06349.1.
BC002048 mRNA. Translation: AAH02048.1.
BC061109 mRNA. Translation: AAH61109.1.
AK079144 mRNA. Translation: BAC37560.1.
CCDSiCCDS29411.1.
PIRiS12709. B55140.
RefSeqiNP_038569.1. NM_013541.1.
UniGeneiMm.299292.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BAYX-ray2.00A/B2-210[»]
1GLPX-ray1.90A/B2-210[»]
1GLQX-ray1.80A/B2-210[»]
1GSYX-ray2.44A/B2-210[»]
1GTIX-ray3.00A/B/C/D/E/F2-210[»]
2GLRX-ray2.20A/B2-210[»]
2OA7X-ray2.20A/B2-210[»]
2OACX-ray2.20A/B2-210[»]
2OADX-ray2.50A/B2-210[»]
3O76X-ray1.77A/B2-210[»]
ProteinModelPortaliP19157.
SMRiP19157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200101. 3 interactors.
IntActiP19157. 6 interactors.
MINTiMINT-1869068.
STRINGi10090.ENSMUSP00000129565.

PTM databases

iPTMnetiP19157.
PhosphoSitePlusiP19157.
SwissPalmiP19157.

2D gel databases

REPRODUCTION-2DPAGEP19157.
SWISS-2DPAGEP19157.

Proteomic databases

EPDiP19157.
MaxQBiP19157.
PaxDbiP19157.
PeptideAtlasiP19157.
PRIDEiP19157.
TopDownProteomicsiP19157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000169613; ENSMUSP00000129565; ENSMUSG00000060803.
ENSMUST00000180480; ENSMUSP00000138073; ENSMUSG00000097830.
GeneIDi14870.
KEGGimmu:14870.
UCSCiuc008fyf.1. mouse.

Organism-specific databases

CTDi2950.
MGIiMGI:95865. Gstp1.

Phylogenomic databases

eggNOGiKOG1695. Eukaryota.
ENOG4111VAU. LUCA.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115733.
HOVERGENiHBG108324.
InParanoidiP19157.
KOiK00799.
OMAiLRCKYAT.
OrthoDBiEOG091G0K2E.
PhylomeDBiP19157.
TreeFamiTF105321.

Enzyme and pathway databases

BRENDAi2.5.1.18. 3474.
ReactomeiR-MMU-156590. Glutathione conjugation.
R-MMU-3299685. Detoxification of Reactive Oxygen Species.
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP19157.
PROiP19157.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000060803.
CleanExiMM_GSTP1.
GenevisibleiP19157. MM.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSTP1_MOUSE
AccessioniPrimary (citable) accession number: P19157
Secondary accession number(s): Q8BNY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 172 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.