P19157 (GSTP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 motochondrial 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 component	Cytoplasm Mitochondrion Nucleus
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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 cascade 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 acute inflammatory response Non-traceable author statement PubMed 18962899. Source: BHF-UCL negative regulation of apoptotic process 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 necrotic cell death Inferred from direct assay PubMed 10945608. 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 response to L-ascorbic acid Inferred from sequence or structural similarity. Source: BHF-UCL response to amino acid stimulus Inferred from sequence or structural similarity. Source: BHF-UCL response to estradiol stimulus Inferred from sequence or structural similarity. Source: BHF-UCL response to ethanol 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 toxin Inferred from sequence or structural similarity. Source: BHF-UCL xenobiotic metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Inferred from sequence or structural similarity. 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_function	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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 210

209

Glutathione S-transferase P 1

PRO_0000185903

Regions

Domain

2 – 81

80

GST N-terminal

Domain

83 – 204

122

GST C-terminal

Region

52 – 53

2

Glutathione binding

Region

65 – 66

2

Glutathione binding

Sites

Binding site

8

1

Glutathione

Binding site

14

1

Glutathione

Binding site

39

1

Glutathione

Binding site

45

1

Glutathione

Amino acid modifications

Modified residue

4

1

Phosphotyrosine; by EGFR By similarity

Modified residue

109

1

Phosphotyrosine Ref.9

Modified residue

128

1

N6-acetyllysine By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

210

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Beta strand

10 – 12

3

Helix

13 – 15

3

Helix

16 – 24

9

Beta strand

29 – 33

5

Helix

36 – 40

5

Beta strand

42 – 44

3

Helix

45 – 47

3

Beta strand

49 – 51

3

Beta strand

55 – 58

4

Beta strand

61 – 65

5

Helix

66 – 77

12

Helix

84 – 110

27

Helix

112 – 135

24

Helix

138 – 140

3

Beta strand

144 – 148

5

Helix

151 – 166

16

Turn

168 – 173

6

Helix

175 – 186

12

Helix

188 – 195

8

Helix

197 – 200

4

Beta strand

204 – 208

5

Sequences

	Sequence		Length	Mass (Da)
	P19157 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: DAC7762F4E34FF27	FASTA	210	23,609
	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

References

	« Hide 'large scale' referencesShow '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, 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. , 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]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-109, MASS SPECTROMETRY. Tissue: Brain.
[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.

IPI

IPI00555023.

PIR

B55140. S12709.

RefSeq

NP_038569.1. NM_013541.1.

UniGene

Mm.299292.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BAY	X-ray	2.00	A/B	2-210	[»]
1GLP	X-ray	1.90	A/B	2-210	[»]
1GLQ	X-ray	1.80	A/B	2-210	[»]
1GSY	X-ray	2.44	A/B	2-209	[»]
1GTI	X-ray	3.00	A/B/C/D/E/F	2-210	[»]
2GLR	X-ray	2.20	A/B	2-210	[»]
2OA7	X-ray	2.20	A/B	2-209	[»]
2OAC	X-ray	2.20	A/B	2-209	[»]
2OAD	X-ray	2.50	A/B	2-209	[»]
3O76	X-ray	1.77	A/B	2-210	[»]

ProteinModelPortal

P19157.

SMR

P19157. Positions 2-210.

ModBase

Search...

Protein-protein interaction databases

IntAct

P19157. 2 interactions.

STRING

10090.ENSMUSP00000047790.

PTM databases

PhosphoSite

P19157.

2D gel databases

REPRODUCTION-2DPAGE

P19157.

SWISS-2DPAGE

P19157.

Proteomic databases

PaxDb

P19157.

PRIDE

P19157.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000169613; ENSMUSP00000129565; ENSMUSG00000060803.
ENSMUST00000180480; ENSMUSP00000138073; ENSMUSG00000097830.

GeneID

14870.

KEGG

mmu:14870.

UCSC

uc008fyf.1. mouse.

Organism-specific databases

CTD

2950.

MGI

MGI:95865. Gstp1.

Phylogenomic databases

eggNOG

NOG05174.

GeneTree

ENSGT00550000074559.

HOGENOM

HOG000115733.

HOVERGEN

HBG108324.

InParanoid

P19157.

KO

K00799.

OMA

YEAGKDD.

OrthoDB

EOG48SGTZ.

Gene expression databases

ArrayExpress

P19157.

Bgee

P19157.

CleanEx

MM_GSTP1.

Genevestigator

P19157.

GermOnline

ENSMUSG00000060803. Mus musculus.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PRINTS

PR01268. GSTRNSFRASEP.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P19157.

NextBio

287133.

SOURCE

Search...

Entry information

Entry name

GSTP1_MOUSE

Accession

Primary (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 3, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program