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P47954 (GSTP1_CRIMI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 73. 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):
GST class-pi
Gene names
Name:GSTP1
OrganismCricetulus migratorius (Gray dwarf hamster)
Taxonomic identifier10032 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

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

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
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 210209Glutathione S-transferase P
PRO_0000185899

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

Sequences

Sequence LengthMass (Da)Tools
P47954 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8CF81AEF04779F61

FASTA21023,469
        10         20         30         40         50         60 
MPPYTIVYFP VRGRCEAMRI LLADQGQSWK EEVITGETWG KGSLKSTCLY GQLPKFEDGD 

        70         80         90        100        110        120 
LTLYQSNAIL RHLGRSLGLY GKDQREAALV DMVNDGVEDL RCKYVTLIYT KYEEGKDDYV 

       130        140        150        160        170        180 
KALPGHLKPF ETLLSKNQGG KAFIVGDQIS FADYNLLDLL LIHQVLAPGC LDNFPLLSAY 

       190        200        210 
VARLSARPKI KAFLSSPDHV NRPINGNGKQ 

« Hide

References

[1]"Comparison of the mRNA sequences for Pi class glutathione transferases in different hamster species and the corresponding enzyme activities with anti-benzo[a]pyrene-7,8-dihydrodiol 9,10-epoxide."
Swedmark S., Jernstroem B., Jenssen D.
Biochem. J. 318:533-538(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L46796 mRNA. Translation: AAB39861.1.
PIRS71957.

3D structure databases

ProteinModelPortalP47954.
SMRP47954. Positions 2-210.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG108324.

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...

Entry information

Entry nameGSTP1_CRIMI
AccessionPrimary (citable) accession number: P47954
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 73 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