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P09211

- GSTP1_HUMAN

UniProt

P09211 - GSTP1_HUMAN

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Protein

Glutathione S-transferase P

Gene

GSTP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Glutathione1 Publication
Binding sitei14 – 141Glutathione1 Publication
Binding sitei39 – 391Glutathione1 Publication
Binding sitei45 – 451GlutathioneBy similarity

GO - Molecular functioni

  1. dinitrosyl-iron complex binding Source: BHF-UCL
  2. glutathione transferase activity Source: UniProtKB
  3. JUN kinase binding Source: BHF-UCL
  4. kinase regulator activity Source: BHF-UCL
  5. nitric oxide binding Source: BHF-UCL
  6. S-nitrosoglutathione binding Source: BHF-UCL

GO - Biological processi

  1. cellular response to lipopolysaccharide Source: BHF-UCL
  2. central nervous system development Source: ProtInc
  3. common myeloid progenitor cell proliferation Source: BHF-UCL
  4. glutathione derivative biosynthetic process Source: Reactome
  5. glutathione metabolic process Source: UniProtKB
  6. negative regulation of acute inflammatory response Source: BHF-UCL
  7. negative regulation of apoptotic process Source: UniProtKB
  8. negative regulation of biosynthetic process Source: BHF-UCL
  9. negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  10. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  11. negative regulation of fibroblast proliferation Source: BHF-UCL
  12. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  13. negative regulation of interleukin-1 beta production Source: BHF-UCL
  14. negative regulation of JUN kinase activity Source: BHF-UCL
  15. negative regulation of leukocyte proliferation Source: BHF-UCL
  16. negative regulation of MAPK cascade Source: BHF-UCL
  17. negative regulation of MAP kinase activity Source: BHF-UCL
  18. negative regulation of monocyte chemotactic protein-1 production Source: BHF-UCL
  19. negative regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  20. negative regulation of protein kinase activity Source: BHF-UCL
  21. negative regulation of stress-activated MAPK cascade Source: BHF-UCL
  22. negative regulation of tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
  23. negative regulation of tumor necrosis factor production Source: BHF-UCL
  24. nitric oxide storage Source: BHF-UCL
  25. positive regulation of superoxide anion generation Source: BHF-UCL
  26. regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  27. regulation of stress-activated MAPK cascade Source: BHF-UCL
  28. response to reactive oxygen species Source: BHF-UCL
  29. small molecule metabolic process Source: Reactome
  30. xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.
REACT_6926. Glutathione conjugation.
SABIO-RKP09211.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase P (EC:2.5.1.18)
Alternative name(s):
GST class-pi
GSTP1-1
Gene namesi
Name:GSTP1
Synonyms:FAEES3, GST3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:4638. GSTP1.

Subcellular locationi

Cytoplasm 1 Publication. Mitochondrion 1 Publication. Nucleus 1 Publication
Note: The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProtKB
  5. intracellular Source: BHF-UCL
  6. mitochondrion Source: HPA
  7. nucleus Source: UniProtKB-KW
  8. plasma membrane Source: HPA
  9. TRAF2-GSTP1 complex Source: BHF-UCL
  10. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81Y → F: Reduces catalytic activity about 50-fold. 2 Publications
Mutagenesisi99 – 991D → A: Reduces affinity for glutathione. Slightly reduced catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA29028.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 210209Glutathione S-transferase PPRO_0000185900Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41Phosphotyrosine; by EGFR1 Publication
Modified residuei103 – 1031N6-succinyllysineBy similarity
Modified residuei116 – 1161N6-succinyllysineBy similarity
Modified residuei128 – 1281N6-acetyllysine1 Publication
Modified residuei199 – 1991Phosphotyrosine; by EGFR1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP09211.
PaxDbiP09211.
PRIDEiP09211.

2D gel databases

DOSAC-COBS-2DPAGEP09211.
OGPiP09211.
REPRODUCTION-2DPAGEIPI00219757.
SWISS-2DPAGEP09211.
UCD-2DPAGEP09211.

PTM databases

PhosphoSiteiP09211.

Miscellaneous databases

PMAP-CutDBP09211.

Expressioni

Gene expression databases

BgeeiP09211.
CleanExiHS_GSTP1.
ExpressionAtlasiP09211. baseline and differential.
GenevestigatoriP09211.

Organism-specific databases

HPAiCAB019298.
HPA019779.
HPA019869.

Interactioni

Subunit structurei

Homodimer. Interacts with CDK5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRDX6P300412EBI-353467,EBI-2255129
TRAF2Q129335EBI-353467,EBI-355744

Protein-protein interaction databases

BioGridi109205. 27 interactions.
IntActiP09211. 25 interactions.
MINTiMINT-4998983.
STRINGi9606.ENSP00000381607.

Structurei

Secondary structure

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Beta strandi10 – 123Combined sources
Helixi13 – 153Combined sources
Helixi16 – 249Combined sources
Beta strandi29 – 335Combined sources
Helixi36 – 416Combined sources
Helixi43 – 475Combined sources
Beta strandi48 – 514Combined sources
Beta strandi55 – 584Combined sources
Beta strandi61 – 644Combined sources
Helixi66 – 7611Combined sources
Helixi84 – 11027Combined sources
Helixi112 – 13524Combined sources
Helixi138 – 1403Combined sources
Beta strandi144 – 1485Combined sources
Helixi151 – 16616Combined sources
Helixi170 – 1734Combined sources
Helixi175 – 18511Combined sources
Helixi188 – 1958Combined sources
Helixi197 – 2004Combined sources
Beta strandi204 – 2085Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
10GSX-ray2.20A/B2-210[»]
11GSX-ray2.30A/B1-210[»]
12GSX-ray2.10A/B1-210[»]
13GSX-ray1.90A/B1-210[»]
14GSX-ray2.80A/B1-210[»]
16GSX-ray1.90A/B1-210[»]
17GSX-ray1.90A/B1-210[»]
18GSX-ray1.90A/B1-210[»]
19GSX-ray1.90A/B2-210[»]
1AQVX-ray1.94A/B2-210[»]
1AQWX-ray1.80A/B/C/D2-210[»]
1AQXX-ray2.00A/B/C/D2-210[»]
1EOGX-ray2.10A/B3-210[»]
1EOHX-ray2.50A/B/C/D/E/F/G/H2-210[»]
1GSSX-ray2.80A/B2-210[»]
1KBNX-ray2.00A/B2-210[»]
1LBKX-ray1.86A/B2-203[»]
1MD3X-ray2.03A/B2-210[»]
1MD4X-ray2.10A/B2-210[»]
1PGTX-ray1.80A/B1-210[»]
1PX6X-ray2.10A/B2-210[»]
1PX7X-ray2.03A/B2-210[»]
1ZGNX-ray2.10A/B2-210[»]
20GSX-ray2.45A/B2-210[»]
22GSX-ray1.90A/B1-210[»]
2A2RX-ray1.40A/B1-210[»]
2A2SX-ray1.70A/B1-210[»]
2GSSX-ray1.90A/B2-210[»]
2J9HX-ray2.40A/B2-210[»]
2PGTX-ray1.90A/B1-210[»]
3CSHX-ray1.55A/B2-210[»]
3CSIX-ray1.90A/B/C/D2-210[»]
3CSJX-ray1.90A/B2-210[»]
3DD3X-ray2.25A/B1-210[»]
3DGQX-ray1.60A/B1-210[»]
3GSSX-ray1.90A/B2-210[»]
3GUSX-ray1.53A/B2-210[»]
3HJMX-ray2.10A/B/C/D2-210[»]
3HJOX-ray1.95A/B2-210[»]
3HKRX-ray1.80A/B2-210[»]
3IE3X-ray1.80A/B2-210[»]
3KM6X-ray2.10A/B2-210[»]
3KMNX-ray1.80A/B2-210[»]
3KMOX-ray2.60A/B2-210[»]
3N9JX-ray1.85A/B1-210[»]
3PGTX-ray2.14A/B1-210[»]
4GSSX-ray2.50A/B2-210[»]
4PGTX-ray2.10A/B1-210[»]
5GSSX-ray1.95A/B2-210[»]
6GSSX-ray1.90A/B2-210[»]
7GSSX-ray2.20A/B2-210[»]
8GSSX-ray1.90A/B/C2-210[»]
9GSSX-ray1.97A/B2-210[»]
ProteinModelPortaliP09211.
SMRiP09211. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09211.

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 binding
Regioni65 – 662Glutathione binding

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

eggNOGiKOG1695.
HOGENOMiHOG000115733.
HOVERGENiHBG108324.
InParanoidiP09211.
KOiK00799.
OMAiANSIYIV.
OrthoDBiEOG7KH9M3.
PhylomeDBiP09211.
TreeFamiTF105321.

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.

P09211-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPYTVVYFP VRGRCAALRM LLADQGQSWK EEVVTVETWQ EGSLKASCLY
60 70 80 90 100
GQLPKFQDGD LTLYQSNTIL RHLGRTLGLY GKDQQEAALV DMVNDGVEDL
110 120 130 140 150
RCKYISLIYT NYEAGKDDYV KALPGQLKPF ETLLSQNQGG KTFIVGDQIS
160 170 180 190 200
FADYNLLDLL LIHEVLAPGC LDAFPLLSAY VGRLSARPKL KAFLASPEYV
210
NLPINGNGKQ
Length:210
Mass (Da):23,356
Last modified:January 23, 2007 - v2
Checksum:i409E33FFAA338396
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861A → P in CAA30894. (PubMed:3196325)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051I → V in allele GSTP1*B and allele GSTP1*C. 3 Publications
Corresponds to variant rs1695 [ dbSNP | Ensembl ].
VAR_014499
Natural varianti114 – 1141A → V in allele GSTP1*C. 2 Publications
Corresponds to variant rs1138272 [ dbSNP | Ensembl ].
VAR_014500
Natural varianti169 – 1691G → D.
Corresponds to variant rs41462048 [ dbSNP | Ensembl ].
VAR_049493

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06547 mRNA. Translation: CAA29794.1.
M24485 Genomic DNA. Translation: AAA56823.1.
X08058 Genomic DNA. Translation: CAA30847.1.
X08094, X08095, X08096 Genomic DNA. Translation: CAA30894.1.
X15480 mRNA. Translation: CAA33508.1.
U12472 Genomic DNA. Translation: AAA64919.1.
U30897 mRNA. Translation: AAC51280.1.
U62589 mRNA. Translation: AAC51237.1.
U21689 Genomic DNA. Translation: AAC13869.1.
BT019949 mRNA. Translation: AAV38752.1.
BT019950 mRNA. Translation: AAV38753.1.
CR450361 mRNA. Translation: CAG29357.1.
AY324387 Genomic DNA. Translation: AAP72967.1.
BC010915 mRNA. Translation: AAH10915.1.
CCDSiCCDS41679.1.
PIRiA41177.
JS0153. A37378.
RefSeqiNP_000843.1. NM_000852.3.
UniGeneiHs.523836.

Genome annotation databases

EnsembliENST00000398606; ENSP00000381607; ENSG00000084207.
GeneIDi2950.
KEGGihsa:2950.
UCSCiuc001omf.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06547 mRNA. Translation: CAA29794.1 .
M24485 Genomic DNA. Translation: AAA56823.1 .
X08058 Genomic DNA. Translation: CAA30847.1 .
X08094 , X08095 , X08096 Genomic DNA. Translation: CAA30894.1 .
X15480 mRNA. Translation: CAA33508.1 .
U12472 Genomic DNA. Translation: AAA64919.1 .
U30897 mRNA. Translation: AAC51280.1 .
U62589 mRNA. Translation: AAC51237.1 .
U21689 Genomic DNA. Translation: AAC13869.1 .
BT019949 mRNA. Translation: AAV38752.1 .
BT019950 mRNA. Translation: AAV38753.1 .
CR450361 mRNA. Translation: CAG29357.1 .
AY324387 Genomic DNA. Translation: AAP72967.1 .
BC010915 mRNA. Translation: AAH10915.1 .
CCDSi CCDS41679.1.
PIRi A41177.
JS0153. A37378.
RefSeqi NP_000843.1. NM_000852.3.
UniGenei Hs.523836.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
10GS X-ray 2.20 A/B 2-210 [» ]
11GS X-ray 2.30 A/B 1-210 [» ]
12GS X-ray 2.10 A/B 1-210 [» ]
13GS X-ray 1.90 A/B 1-210 [» ]
14GS X-ray 2.80 A/B 1-210 [» ]
16GS X-ray 1.90 A/B 1-210 [» ]
17GS X-ray 1.90 A/B 1-210 [» ]
18GS X-ray 1.90 A/B 1-210 [» ]
19GS X-ray 1.90 A/B 2-210 [» ]
1AQV X-ray 1.94 A/B 2-210 [» ]
1AQW X-ray 1.80 A/B/C/D 2-210 [» ]
1AQX X-ray 2.00 A/B/C/D 2-210 [» ]
1EOG X-ray 2.10 A/B 3-210 [» ]
1EOH X-ray 2.50 A/B/C/D/E/F/G/H 2-210 [» ]
1GSS X-ray 2.80 A/B 2-210 [» ]
1KBN X-ray 2.00 A/B 2-210 [» ]
1LBK X-ray 1.86 A/B 2-203 [» ]
1MD3 X-ray 2.03 A/B 2-210 [» ]
1MD4 X-ray 2.10 A/B 2-210 [» ]
1PGT X-ray 1.80 A/B 1-210 [» ]
1PX6 X-ray 2.10 A/B 2-210 [» ]
1PX7 X-ray 2.03 A/B 2-210 [» ]
1ZGN X-ray 2.10 A/B 2-210 [» ]
20GS X-ray 2.45 A/B 2-210 [» ]
22GS X-ray 1.90 A/B 1-210 [» ]
2A2R X-ray 1.40 A/B 1-210 [» ]
2A2S X-ray 1.70 A/B 1-210 [» ]
2GSS X-ray 1.90 A/B 2-210 [» ]
2J9H X-ray 2.40 A/B 2-210 [» ]
2PGT X-ray 1.90 A/B 1-210 [» ]
3CSH X-ray 1.55 A/B 2-210 [» ]
3CSI X-ray 1.90 A/B/C/D 2-210 [» ]
3CSJ X-ray 1.90 A/B 2-210 [» ]
3DD3 X-ray 2.25 A/B 1-210 [» ]
3DGQ X-ray 1.60 A/B 1-210 [» ]
3GSS X-ray 1.90 A/B 2-210 [» ]
3GUS X-ray 1.53 A/B 2-210 [» ]
3HJM X-ray 2.10 A/B/C/D 2-210 [» ]
3HJO X-ray 1.95 A/B 2-210 [» ]
3HKR X-ray 1.80 A/B 2-210 [» ]
3IE3 X-ray 1.80 A/B 2-210 [» ]
3KM6 X-ray 2.10 A/B 2-210 [» ]
3KMN X-ray 1.80 A/B 2-210 [» ]
3KMO X-ray 2.60 A/B 2-210 [» ]
3N9J X-ray 1.85 A/B 1-210 [» ]
3PGT X-ray 2.14 A/B 1-210 [» ]
4GSS X-ray 2.50 A/B 2-210 [» ]
4PGT X-ray 2.10 A/B 1-210 [» ]
5GSS X-ray 1.95 A/B 2-210 [» ]
6GSS X-ray 1.90 A/B 2-210 [» ]
7GSS X-ray 2.20 A/B 2-210 [» ]
8GSS X-ray 1.90 A/B/C 2-210 [» ]
9GSS X-ray 1.97 A/B 2-210 [» ]
ProteinModelPortali P09211.
SMRi P09211. Positions 1-210.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109205. 27 interactions.
IntActi P09211. 25 interactions.
MINTi MINT-4998983.
STRINGi 9606.ENSP00000381607.

Chemistry

BindingDBi P09211.
ChEMBLi CHEMBL3902.
DrugBanki DB01008. Busulfan.
DB00958. Carboplatin.
DB00291. Chlorambucil.
DB00515. Cisplatin.
DB01242. Clomipramine.
DB00773. Etoposide.
DB00143. Glutathione.
DB00526. Oxaliplatin.
DB00163. Vitamin E.

PTM databases

PhosphoSitei P09211.

2D gel databases

DOSAC-COBS-2DPAGE P09211.
OGPi P09211.
REPRODUCTION-2DPAGE IPI00219757.
SWISS-2DPAGE P09211.
UCD-2DPAGE P09211.

Proteomic databases

MaxQBi P09211.
PaxDbi P09211.
PRIDEi P09211.

Protocols and materials databases

DNASUi 2950.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398606 ; ENSP00000381607 ; ENSG00000084207 .
GeneIDi 2950.
KEGGi hsa:2950.
UCSCi uc001omf.3. human.

Organism-specific databases

CTDi 2950.
GeneCardsi GC11P067351.
HGNCi HGNC:4638. GSTP1.
HPAi CAB019298.
HPA019779.
HPA019869.
MIMi 134660. gene.
neXtProti NX_P09211.
PharmGKBi PA29028.
GenAtlasi Search...

Phylogenomic databases

eggNOGi KOG1695.
HOGENOMi HOG000115733.
HOVERGENi HBG108324.
InParanoidi P09211.
KOi K00799.
OMAi ANSIYIV.
OrthoDBi EOG7KH9M3.
PhylomeDBi P09211.
TreeFami TF105321.

Enzyme and pathway databases

Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.
REACT_6926. Glutathione conjugation.
SABIO-RK P09211.

Miscellaneous databases

ChiTaRSi GSTP1. human.
EvolutionaryTracei P09211.
GeneWikii GSTP1.
GenomeRNAii 2950.
NextBioi 11692.
PMAP-CutDB P09211.
PROi P09211.
SOURCEi Search...

Gene expression databases

Bgeei P09211.
CleanExi HS_GSTP1.
ExpressionAtlasi P09211. baseline and differential.
Genevestigatori P09211.

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

« Hide 'large scale' publications
  1. "Structure and expression of a human class pi glutathione S-transferase messenger RNA."
    Kano T., Sakai M., Muramatsu M.
    Cancer Res. 47:5626-5630(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The structure of the human glutathione S-transferase pi gene."
    Cowell I.G., Dixon K.H., Pemble S.E., Ketterer B., Taylor J.B.
    Biochem. J. 255:79-83(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Structure of the human genomic glutathione S-transferase-pi gene."
    Morrow C.S., Cowan K.H., Goldsmith M.E.
    Gene 75:3-11(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Expression of anionic glutathione-S-transferase and P-glycoprotein genes in human tissues and tumors."
    Moscow J.A., Fairchild C.R., Madden M.J., Ransom D.T., Wieand H.S., O'Brien E.E., Poplack D.G., Cossman J., Myers C.E., Cowan K.H.
    Cancer Res. 49:1422-1428(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Human fatty acid ethyl ester synthase III gene: genomic organization, nucleotide sequence, genetic and chromosomal sublocalization."
    Bora P.S., Smith C., Lange L.G., Bora N.S., Jones C., Gerhard D.S.
    Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins."
    Ali-Osman F., Akande O., Antoun G., Mao J.X., Buolamwini J.
    J. Biol. Chem. 272:10004-10012(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-105 AND VAL-114.
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. NIEHS SNPs program
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-105 AND VAL-114.
  10. "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], VARIANT VAL-105.
    Tissue: Urinary bladder.
  11. "Structural evidence for three different types of glutathione transferase in human tissues."
    Alin P., Mannervik B., Joernvall H.
    FEBS Lett. 182:319-322(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-24.
  12. "Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties."
    Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H.
    Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-24.
  13. "Purification and characterization of unique glutathione S-transferases from human muscle."
    Singh S.V., Ahmad H., Kurosky A., Awasthi Y.C.
    Arch. Biochem. Biophys. 264:13-22(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-14.
  14. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Tissue: Platelet.
  15. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 20-71; 76-101; 104-141; 122-141 AND 192-209, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  16. "A two-dimensional gel database of human colon carcinoma proteins."
    Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
    Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Colon carcinoma.
  17. "Primary and secondary structural analyses of glutathione S-transferase pi from human placenta."
    Ahmad H., Wilson D.E., Fritz R.R., Singh S.V., Medh R.D., Nagle G.T., Awasthi Y.C., Kurosky A.
    Arch. Biochem. Biophys. 278:398-408(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRIMARY AND SECONDARY STRUCTURAL ANALYZES.
  18. "Tyrosine-7 in human class Pi glutathione S-transferase is important for lowering the pKa of the thiol group of glutathione in the enzyme-glutathione complex."
    Kong K.H., Takasu K., Inoue H., Takahashi K.
    Biochem. Biophys. Res. Commun. 184:194-197(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-8.
  19. "Tyrosine-7 is an essential residue for the catalytic activity of human class PI glutathione S-transferase: chemical modification and site-directed mutagenesis studies."
    Kong K.H., Nishida M., Inoue H., Takahashi K.
    Biochem. Biophys. Res. Commun. 182:1122-1129(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-8.
  20. "Site-directed mutagenesis study on the roles of evolutionally conserved aspartic acid residues in human glutathione S-transferase P1-1."
    Kong K.-H., Inoue H., Takahashi K.
    Protein Eng. 6:93-99(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-99, CATALYTIC ACTIVITY.
  21. "Glutathione S-transferase pi localizes in mitochondria and protects against oxidative stress."
    Goto S., Kawakatsu M., Izumi S., Urata Y., Kageyama K., Ihara Y., Koji T., Kondo T.
    Free Radic. Biol. Med. 46:1392-1403(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  22. "Tyrosine phosphorylation of the human glutathione S-transferase P1 by epidermal growth factor receptor."
    Okamura T., Singh S., Buolamwini J., Haystead T., Friedman H., Bigner D., Ali-Osman F.
    J. Biol. Chem. 284:16979-16989(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-4 AND TYR-199.
  23. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase activity."
    Sun K.H., Chang K.H., Clawson S., Ghosh S., Mirzaei H., Regnier F., Shah K.
    J. Neurochem. 118:902-914(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDK5.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8-A resolution."
    Reinemer P., Dirr H.W., Ladenstein R., Huber R., Lo Bello M., Federici G., Parker M.W.
    J. Mol. Biol. 227:214-226(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) COMPLEX WITH S-HEXYLGLUTATHIONE.
  28. "The three-dimensional structure of the human Pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate."
    Oakley A.J., Rossjohn J., Lo Bello M., Caccuri A.M., Federici G., Parker M.W.
    Biochemistry 36:576-585(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR ETHACRYNIC ACID AND GLUTATHIONE.
  29. "Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase."
    Ji X., Tordova M., O'Donnell R., Parsons J.F., Hayden J.B., Gilliland G.L., Zimniak P.
    Biochemistry 36:9690-9702(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND INHIBITOR.
  30. "The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution."
    Oakley A.J., Lo Bello M., Battistoni A., Ricci G., Rossjohn J., Villar H.O., Parker M.W.
    J. Mol. Biol. 274:84-100(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE.
  31. "Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor."
    Prade L., Huber R., Manoharan T.H., Fahl W.E., Reuter W.
    Structure 5:1287-1295(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  32. "Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1."
    Ji X., Blaszczyk J., Xiao B., O'Donnell R., Hu X., Herzog C., Singh S.V., Zimniak P.
    Biochemistry 38:10231-10238(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  33. "Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure."
    Nicotra M., Paci M., Sette M., Oakley A.J., Parker M.W., Lo Bello M., Caccuri A.M., Federici G., Ricci G.
    Biochemistry 37:3020-3027(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  34. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  35. "Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases."
    Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F., Federici G., Caccuri A.M.
    Cancer Res. 69:8025-8034(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 2-210.

Entry informationi

Entry nameiGSTP1_HUMAN
AccessioniPrimary (citable) accession number: P09211
Secondary accession number(s): O00460, Q15690, Q5TZY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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