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P28801 (GSTP1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 102. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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. Ref.3

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
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-1 beta production

Inferred from electronic annotation. Source: Ensembl

negative regulation of monocyte chemotactic protein-1 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of nitric-oxide synthase biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

xenobiotic metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentTRAF2-GSTP1 complex

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionS-nitrosoglutathione binding

Inferred from electronic annotation. Source: Ensembl

dinitrosyl-iron complex binding

Inferred from electronic annotation. Source: Ensembl

glutathione 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 Ref.3
Chain2 – 210209Glutathione S-transferase P
PRO_0000185896

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
P28801 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 79C45DA2031B1EBB

FASTA21023,613
        10         20         30         40         50         60 
MPPYTIVYFP VQGRCEAMRM LLADQGQSWK EEVVAMQSWL QGPLKASCLY GQLPKFQDGD 

        70         80         90        100        110        120 
LTLYQSNAIL RHLGRTLGLY GKDQQEAALV DMVNDGVEDL RCKYVSLIYT NYEAGKEDYV 

       130        140        150        160        170        180 
KALPQHLKPF ETLLSQNKGG QAFIVGDQIS FADYNLLDLL RIHQVLAPSC LDSFPLLSAY 

       190        200        210 
VARLNSRPKL KAFLASPEHM NRPINGNGKQ 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a cDNA encoding a glutathione S-transferase (GST) class-pi from the bovine ocular ciliary epithelium."
Hernando N., Martin-Alonso J.M., Ghosh S., Coca-Prados M.
Exp. Eye Res. 55:711-718(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ocular ciliary epithelium.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[3]"Glutathione transferase from bovine placenta. Preparation, biochemical characterization, crystallization, and preliminary crystallographic analysis of a neutral class PI enzyme."
Schaeffer J., Gallay O., Ladenstein R.
J. Biol. Chem. 263:17405-17411(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16, SUBUNIT.
Tissue: Placenta.
[4]"Bovine erythrocyte glutathione S-transferase: purification, inhibition, and complex formation."
Xu F., Hultquist D.E.
Biochem. Int. 27:265-274(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-23.
Tissue: Erythrocyte.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61233 mRNA. Translation: CAA43551.1.
BC102704 mRNA. Translation: AAI02705.1.
PIRA49180.
RefSeqNP_803482.1. NM_177516.1.
UniGeneBt.13949.

3D structure databases

ProteinModelPortalP28801.
SMRP28801. Positions 1-210.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP28801.
PRIDEP28801.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000004615; ENSBTAP00000004615; ENSBTAG00000003548.
GeneID281806.
KEGGbta:281806.

Organism-specific databases

CTD2950.

Phylogenomic databases

eggNOGNOG05174.
GeneTreeENSGT00550000074559.
HOGENOMHOG000115733.
HOVERGENHBG108324.
InParanoidP28801.
KOK00799.
OMAMNRPING.
OrthoDBEOG7KH9M3.
TreeFamTF105321.

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

NextBio20805719.

Entry information

Entry nameGSTP1_BOVIN
AccessionPrimary (citable) accession number: P28801
Secondary accession number(s): Q3SZU6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 102 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