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Protein

Glutathione S-transferase P

Gene

GSTP1

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei8GlutathioneBy similarity1
Binding sitei14GlutathioneBy similarity1
Binding sitei39GlutathioneBy similarity1
Binding sitei45GlutathioneBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase P (EC:2.5.1.18)
Alternative name(s):
GST class-pi
Gene namesi
Name:GSTP1
OrganismiMacaca mulatta (Rhesus macaque)
Taxonomic identifieri9544 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
Proteomesi
  • UP000006718 Componenti: Unplaced

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001859012 – 210Glutathione S-transferase PAdd BLAST209

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ28514.

Interactioni

Subunit structurei

Homodimer. Interacts with CDK5.By similarity

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LX2model-A1-210[»]
ProteinModelPortaliQ28514.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity2
Regioni65 – 66Glutathione bindingBy similarity2

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

GeneTreeiENSGT00550000074559.
HOVERGENiHBG108324.
InParanoidiQ28514.
KOiK00799.

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.

Q28514-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPYTVVYFP VRGRCAALRM LLADQGQSWK EEVVTMETWQ EGSLKASCLY
60 70 80 90 100
GQLPKFQDGD LTLYQSNTFL RHLGRTLGLY GKDQREAALV DMVNDGVEDL
110 120 130 140 150
RCKYLSLIYT NYEAGKDDYV KALPGQLKPF ETLLSQNQGG KTFIVGDQIS
160 170 180 190 200
FADYNLLDLL LIHEVLAPGC LDAFPLLSAY VARLSARPKL KAFLASPEHV
210
NLPINGNGKQ
Length:210
Mass (Da):23,438
Last modified:January 23, 2007 - v3
Checksum:i4DE128B6A6C45434
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L49501 mRNA. Translation: AAC37605.1.
PIRiJC6529.
RefSeqiNP_001036141.1. NM_001042676.1.
UniGeneiMmu.3442.

Genome annotation databases

EnsembliENSMMUT00000026042; ENSMMUP00000024369; ENSMMUG00000018524.
GeneIDi721704.
KEGGimcc:721704.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L49501 mRNA. Translation: AAC37605.1.
PIRiJC6529.
RefSeqiNP_001036141.1. NM_001042676.1.
UniGeneiMmu.3442.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LX2model-A1-210[»]
ProteinModelPortaliQ28514.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ28514.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMMUT00000026042; ENSMMUP00000024369; ENSMMUG00000018524.
GeneIDi721704.
KEGGimcc:721704.

Organism-specific databases

CTDi2950.

Phylogenomic databases

GeneTreeiENSGT00550000074559.
HOVERGENiHBG108324.
InParanoidiQ28514.
KOiK00799.

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_MACMU
AccessioniPrimary (citable) accession number: Q28514
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.