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P04906 (GSTP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase P

EC=2.5.1.18
Alternative name(s):
Chain 7
GST 7-7
GST class-pi
Gene names
Name:Gstp1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Catalytic activity

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

Subunit structure

Homodimer. Interacts with CDK5 By similarity.

Subcellular location

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.

Tissue specificity

Present in kidney, lung, testis and placenta, very low levels in liver.

Sequence similarities

Belongs to the GST superfamily. Pi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Molecular functionTransferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to cell-matrix adhesion

Inferred from expression pattern PubMed 10793289. Source: RGD

cellular response to epidermal growth factor stimulus

Inferred from expression pattern PubMed 1908848. Source: RGD

cellular response to glucocorticoid stimulus

Inferred from expression pattern PubMed 18349876. Source: RGD

cellular response to insulin stimulus

Inferred from expression pattern PubMed 1908848. Source: RGD

cellular response to lipopolysaccharide

Inferred from sequence or structural similarity. Source: BHF-UCL

common myeloid progenitor cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of JUN kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of interleukin-1 beta production

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of leukocyte proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of monocyte chemotactic protein-1 production

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of nitric-oxide synthase biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of stress-activated MAPK cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of tumor necrosis factor production

Inferred from sequence or structural similarity. Source: BHF-UCL

oligodendrocyte development

Inferred from expression pattern PubMed 17681700. Source: RGD

organ regeneration

Inferred from expression pattern PubMed 7499462. Source: RGD

positive regulation of superoxide anion generation

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of stress-activated MAPK cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

response to L-ascorbic acid

Inferred from expression pattern PubMed 9834927. Source: RGD

response to amino acid

Inferred from expression pattern PubMed 20013880. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 9505896. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 2206462. Source: RGD

response to mercury ion

Inferred from expression pattern PubMed 12730625. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 16317157. Source: RGD

response to reactive oxygen species

Inferred from sequence or structural similarity. Source: BHF-UCL

response to toxic substance

Inferred from expression pattern PubMed 19790251. Source: RGD

xenobiotic metabolic process

Inferred from direct assay PubMed 11018474. Source: RGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18349876. Source: RGD

cytosol

Inferred from direct assay PubMed 3421895. Source: RGD

intracellular

Inferred from sequence or structural similarity. Source: BHF-UCL

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 15942958. Source: RGD

plasma membrane

Inferred from direct assay PubMed 18349876. Source: RGD

protein complex

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionJUN kinase binding

Inferred from sequence or structural similarity. Source: BHF-UCL

drug binding

Inferred from direct assay PubMed 11018474. Source: RGD

glutathione binding

Inferred from direct assay PubMed 11018474. Source: RGD

glutathione transferase activity

Inferred from direct assay PubMed 11018474. Source: RGD

kinase regulator activity

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5 Ref.6
Chain2 – 210209Glutathione S-transferase P
PRO_0000185907

Regions

Domain2 – 8180GST N-terminal
Domain83 – 204122GST C-terminal
Region52 – 532Glutathione binding By similarity
Region65 – 662Glutathione binding By similarity

Sites

Binding site81Glutathione By similarity
Binding site141Glutathione By similarity
Binding site391Glutathione By similarity
Binding site451Glutathione By similarity

Amino acid modifications

Modified residue41Phosphotyrosine; by EGFR By similarity
Modified residue1031N6-succinyllysine By similarity
Modified residue1161N6-succinyllysine By similarity
Modified residue1281N6-acetyllysine By similarity

Experimental info

Sequence conflict151C → Y AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
P04906 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9B71785D1FC28FDB

FASTA21023,439
        10         20         30         40         50         60 
MPPYTIVYFP VRGRCEATRM LLADQGQSWK EEVVTIDVWL QGSLKSTCLY GQLPKFEDGD 

        70         80         90        100        110        120 
LTLYQSNAIL RHLGRSLGLY GKDQKEAALV DMVNDGVEDL RCKYGTLIYT NYENGKDDYV 

       130        140        150        160        170        180 
KALPGHLKPF ETLLSQNQGG KAFIVGNQIS FADYNLLDLL LVHQVLAPGC LDNFPLLSAY 

       190        200        210 
VARLSARPKI KAFLSSPDHL NRPINGNGKQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and the nucleotide sequence of rat glutathione S-transferase P cDNA."
Suguoka Y., Kano T., Okuda A., Sakai M., Kitagawa T., Muramatsu M.
Nucleic Acids Res. 13:6049-6057(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The structure of the rat glutathione S-transferase P gene and related pseudogenes."
Okuda A., Sakai M., Muramatsu M.
J. Biol. Chem. 262:3858-3863(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[4]"Purification and characterization of P-52 (glutathione S-transferase-P or 7-7) from normal liver and putative preneoplastic liver nodules."
Rushmore T.H., Harris L., Nagai M., Sharma R.N., Hayes M.A., Cameron R.G., Murray R.K., Farber E.
Cancer Res. 48:2805-2812(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-27.
[5]Lubec G., Afjehi-Sadat L., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12; 56-71; 122-141 AND 192-209, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
[6]"Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties."
Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H.
Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02904 mRNA. Translation: CAA26664.1.
L29427 Genomic DNA. Translation: AAB59718.1.
BC058439 mRNA. Translation: AAH58439.1.
BC058440 mRNA. Translation: AAH58440.1.
PIRXURTGP. A26546.
S59902.
RefSeqNP_036709.1. NM_012577.2.
UniGeneRn.87063.

3D structure databases

ProteinModelPortalP04906.
SMRP04906. Positions 2-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246591. 1 interaction.
IntActP04906. 1 interaction.

PTM databases

PhosphoSiteP04906.

2D gel databases

World-2DPAGE0004:P04906.

Proteomic databases

PaxDbP04906.
PRIDEP04906.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000024601; ENSRNOP00000024601; ENSRNOG00000018237.
GeneID24426.
KEGGrno:24426.
UCSCRGD:2758. rat.

Organism-specific databases

CTD2950.
RGD2758. Gstp1.

Phylogenomic databases

eggNOGNOG05174.
GeneTreeENSGT00550000074559.
HOGENOMHOG000115733.
HOVERGENHBG108324.
InParanoidP04906.
KOK00799.
OMALRCKYAT.
OrthoDBEOG7KH9M3.
PhylomeDBP04906.
TreeFamTF105321.

Gene expression databases

ArrayExpressP04906.
GenevestigatorP04906.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01268. GSTRNSFRASEP.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603297.
PMAP-CutDBP04906.
PROP04906.

Entry information

Entry nameGSTP1_RAT
AccessionPrimary (citable) accession number: P04906
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families