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P47954

- GSTP1_CRIMI

UniProt

P47954 - GSTP1_CRIMI

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Protein

Glutathione S-transferase P

Gene

GSTP1

Organism
Cricetulus migratorius (Gray dwarf hamster)
Status
Reviewed - Annotation score: 3 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81GlutathioneBy similarity
Binding sitei14 – 141GlutathioneBy similarity
Binding sitei39 – 391GlutathioneBy similarity
Binding sitei45 – 451GlutathioneBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
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
OrganismiCricetulus migratorius (Gray dwarf hamster)
Taxonomic identifieri10032 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

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

  1. mitochondrion Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 210209Glutathione S-transferase PPRO_0000185899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41Phosphotyrosine; by EGFRBy similarity
Modified residuei103 – 1031N6-succinyllysineBy similarity
Modified residuei116 – 1161N6-succinyllysineBy similarity
Modified residuei128 – 1281N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP47954.
SMRiP47954. Positions 2-210.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8180GST N-terminalAdd
BLAST
Domaini83 – 204122GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 532Glutathione bindingBy similarity
Regioni65 – 662Glutathione bindingBy similarity

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

HOVERGENiHBG108324.

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]
PfamiPF00043. GST_C. 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.

P47954-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPYTIVYFP VRGRCEAMRI LLADQGQSWK EEVITGETWG KGSLKSTCLY
60 70 80 90 100
GQLPKFEDGD LTLYQSNAIL RHLGRSLGLY GKDQREAALV DMVNDGVEDL
110 120 130 140 150
RCKYVTLIYT KYEEGKDDYV KALPGHLKPF ETLLSKNQGG KAFIVGDQIS
160 170 180 190 200
FADYNLLDLL LIHQVLAPGC LDNFPLLSAY VARLSARPKI KAFLSSPDHV
210
NRPINGNGKQ
Length:210
Mass (Da):23,469
Last modified:January 23, 2007 - v2
Checksum:i8CF81AEF04779F61
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L46796 mRNA. Translation: AAB39861.1.
PIRiS71957.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L46796 mRNA. Translation: AAB39861.1 .
PIRi S71957.

3D structure databases

ProteinModelPortali P47954.
SMRi P47954. Positions 2-210.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG108324.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01268. GSTRNSFRASEP.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGSTP1_CRIMI
AccessioniPrimary (citable) accession number: P47954
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3