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P19157 (GSTP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1

Short name=Gst P1
EC=2.5.1.18
Alternative name(s):
GST YF-YF
GST class-pi
GST-piB
Preadipocyte growth factor
Gene names
Name:Gstp1
Synonyms:Gstpib
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Can metabolize 1-chloro-2,4-dinitrobenzene. 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

Ubiquitously expressed.

Sequence similarities

Belongs to the GST superfamily. Pi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Mass spectrometry

Molecular mass is 23478.8±2 Da from positions 2 - 210. Determined by ESI. Ref.8

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Molecular functionTransferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to cell-matrix adhesion

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

cellular response to epidermal growth factor stimulus

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

cellular response to glucocorticoid stimulus

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

cellular response to insulin stimulus

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

cellular response to lipopolysaccharide

Inferred from direct assay PubMed 16023107. Source: BHF-UCL

common myeloid progenitor cell proliferation

Inferred from mutant phenotype PubMed 11408560. Source: BHF-UCL

glutathione metabolic process

Inferred from direct assay Ref.3. Source: MGI

negative regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 16023107. Source: BHF-UCL

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

Inferred from direct assay PubMed 16023107. Source: BHF-UCL

negative regulation of JUN kinase activity

Inferred from direct assay PubMed 10945608PubMed 16023107. Source: BHF-UCL

negative regulation of MAP kinase activity

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

negative regulation of acute inflammatory response

Non-traceable author statement PubMed 18962899. Source: BHF-UCL

negative regulation of apoptotic process

Traceable author statement PubMed 18962899. Source: BHF-UCL

negative regulation of biosynthetic process

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway

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

negative regulation of fibroblast proliferation

Inferred from mutant phenotype PubMed 11408560. Source: BHF-UCL

negative regulation of interleukin-1 beta production

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

negative regulation of leukocyte proliferation

Inferred from mutant phenotype PubMed 11408560. Source: BHF-UCL

negative regulation of monocyte chemotactic protein-1 production

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

negative regulation of neutrophil aggregation

Non-traceable author statement PubMed 18962899. Source: BHF-UCL

negative regulation of nitric-oxide synthase biosynthetic process

Inferred from direct assay PubMed 16023107PubMed 18962899. Source: BHF-UCL

negative regulation of peroxidase activity

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

negative regulation of stress-activated MAPK cascade

Inferred from direct assay PubMed 16023107. Source: BHF-UCL

negative regulation of tumor necrosis factor production

Inferred from direct assay PubMed 16023107PubMed 18962899. Source: BHF-UCL

oligodendrocyte development

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

organ regeneration

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

positive regulation of superoxide anion generation

Inferred from mutant phenotype PubMed 11408560. Source: BHF-UCL

regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 10945608. Source: BHF-UCL

regulation of stress-activated MAPK cascade

Inferred from direct assay PubMed 10945608. Source: BHF-UCL

response to L-ascorbic acid

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

response to amino acid

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

response to estradiol

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

response to ethanol

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

response to nutrient levels

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

response to reactive oxygen species

Inferred from direct assay PubMed 10945608. Source: BHF-UCL

response to toxic substance

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

xenobiotic metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

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

cytosol

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

intracellular

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

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

plasma membrane

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

protein complex

Inferred from direct assay PubMed 11279197. Source: BHF-UCL

   Molecular_functionJUN kinase binding

Inferred from physical interaction PubMed 11279197. Source: BHF-UCL

drug binding

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

glutathione transferase activity

Inferred from direct assay Ref.3. Source: MGI

kinase regulator activity

Inferred from mutant phenotype PubMed 12646564. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 210209Glutathione S-transferase P 1
PRO_0000185903

Regions

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

Sites

Binding site81Glutathione
Binding site141Glutathione
Binding site391Glutathione
Binding site451Glutathione

Amino acid modifications

Modified residue41Phosphotyrosine; by EGFR By similarity
Modified residue1031N6-succinyllysine Ref.9
Modified residue1161N6-succinyllysine Ref.9
Modified residue1281N6-acetyllysine By similarity

Secondary structure

......................................... 210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19157 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DAC7762F4E34FF27

FASTA21023,609
        10         20         30         40         50         60 
MPPYTIVYFP VRGRCEAMRM LLADQGQSWK EEVVTIDTWM QGLLKPTCLY GQLPKFEDGD 

        70         80         90        100        110        120 
LTLYQSNAIL RHLGRSLGLY GKNQREAAQM DMVNDGVEDL RGKYVTLIYT NYENGKNDYV 

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

       190        200        210 
VARLSARPKI KAFLSSPEHV NRPINGNGKQ 

« Hide

References

« Hide 'large scale' references
[1]"A cDNA sequence coding a class pi glutathione S-transferase of mouse."
Hatayama I., Satoh K., Sato K.
Nucleic Acids Res. 18:4606-4606(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"Isolation and characterization of two mouse PI class glutathione S-transferase genes."
Bammler T.K., Smith C.A.D., Wolf R.C.
Biochem. J. 298:385-390(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Two murine GSTpi genes are arranged in tandem and are differentially expressed."
Xu X., Stambrook P.J.
J. Biol. Chem. 269:30268-30273(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
Tissue: Liver.
[4]"Molecular cloning of mouse preadipocyte growth factor."
Kawada T., Aoki N., Kamei Y., Sugimoto E.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"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].
[6]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12; 56-71; 122-141 AND 192-209, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[7]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-210.
Strain: C57BL/6J.
Tissue: Embryo.
[8]"Purification, mass spectrometric characterization, and covalent modification of murine glutathione S-transferases."
Mitchell A.E., Morin D., Lame M.W., Jones A.D.
Chem. Res. Toxicol. 8:1054-1062(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MASS SPECTROMETRY.
Strain: CD-1.
Tissue: Liver.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-103 AND LYS-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors."
Garcia-Saez I., Parraga A., Phillips M.F., Mantle T.J., Coll M.
J. Mol. Biol. 237:298-314(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOGS.
[11]"The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region."
Vega M.C., Walsh S.B., Mantle T.J., Coll M.
J. Biol. Chem. 273:2844-2850(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53451 mRNA. Translation: CAA37529.1.
X76143 Genomic DNA. No translation available.
U15654 Genomic DNA. Translation: AAA64837.1.
D30687 mRNA. Translation: BAA06349.1.
BC002048 mRNA. Translation: AAH02048.1.
BC061109 mRNA. Translation: AAH61109.1.
AK079144 mRNA. Translation: BAC37560.1.
PIRB55140. S12709.
RefSeqNP_038569.1. NM_013541.1.
UniGeneMm.299292.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAYX-ray2.00A/B2-210[»]
1GLPX-ray1.90A/B2-210[»]
1GLQX-ray1.80A/B2-210[»]
1GSYX-ray2.44A/B2-209[»]
1GTIX-ray3.00A/B/C/D/E/F2-210[»]
2GLRX-ray2.20A/B2-210[»]
2OA7X-ray2.20A/B2-209[»]
2OACX-ray2.20A/B2-209[»]
2OADX-ray2.50A/B2-209[»]
3O76X-ray1.77A/B2-210[»]
ProteinModelPortalP19157.
SMRP19157. Positions 2-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200101. 1 interaction.
IntActP19157. 4 interactions.
MINTMINT-1869068.
STRING10090.ENSMUSP00000047790.

PTM databases

PhosphoSiteP19157.

2D gel databases

REPRODUCTION-2DPAGEP19157.
SWISS-2DPAGEP19157.

Proteomic databases

PaxDbP19157.
PRIDEP19157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000169613; ENSMUSP00000129565; ENSMUSG00000060803.
ENSMUST00000180480; ENSMUSP00000138073; ENSMUSG00000097830.
GeneID14870.
KEGGmmu:14870.
UCSCuc008fyf.1. mouse.

Organism-specific databases

CTD2950.
MGIMGI:95865. Gstp1.

Phylogenomic databases

eggNOGNOG05174.
GeneTreeENSGT00550000074559.
HOGENOMHOG000115733.
HOVERGENHBG108324.
InParanoidP19157.
KOK00799.
OMADLRCKYV.
OrthoDBEOG7KH9M3.
PhylomeDBP19157.
TreeFamTF105321.

Gene expression databases

BgeeP19157.
CleanExMM_GSTP1.
GenevestigatorP19157.

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

EvolutionaryTraceP19157.
NextBio287133.
PROP19157.
SOURCESearch...

Entry information

Entry nameGSTP1_MOUSE
AccessionPrimary (citable) accession number: P19157
Secondary accession number(s): Q8BNY4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 146 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot