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P28801

- GSTP1_BOVIN

UniProt

P28801 - GSTP1_BOVIN

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Protein

Glutathione S-transferase P

Gene

GSTP1

Organism
Bos taurus (Bovine)
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 (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. dinitrosyl-iron complex binding Source: Ensembl
  2. glutathione transferase activity Source: UniProtKB-EC
  3. S-nitrosoglutathione binding Source: Ensembl

GO - Biological processi

  1. glutathione metabolic process Source: Ensembl
  2. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
  3. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  4. negative regulation of interleukin-1 beta production Source: Ensembl
  5. negative regulation of JUN kinase activity Source: Ensembl
  6. negative regulation of monocyte chemotactic protein-1 production Source: Ensembl
  7. negative regulation of nitric-oxide synthase biosynthetic process Source: Ensembl
  8. negative regulation of tumor necrosis factor production Source: Ensembl
  9. xenobiotic metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_204534. Detoxification of Reactive Oxygen Species.
REACT_223659. Glutathione conjugation.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 29

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. extracellular space Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrion Source: UniProtKB-KW
  4. nucleus Source: UniProtKB-KW
  5. plasma membrane Source: Ensembl
  6. TRAF2-GSTP1 complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 210209Glutathione S-transferase PPRO_0000185896Add
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

Proteomic databases

PaxDbiP28801.
PRIDEiP28801.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP28801.
SMRiP28801. Positions 1-210.
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

eggNOGiNOG05174.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115733.
HOVERGENiHBG108324.
InParanoidiP28801.
KOiK00799.
OMAiMNRPING.
OrthoDBiEOG7KH9M3.
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.

P28801-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPYTIVYFP VQGRCEAMRM LLADQGQSWK EEVVAMQSWL QGPLKASCLY
60 70 80 90 100
GQLPKFQDGD LTLYQSNAIL RHLGRTLGLY GKDQQEAALV DMVNDGVEDL
110 120 130 140 150
RCKYVSLIYT NYEAGKEDYV KALPQHLKPF ETLLSQNKGG QAFIVGDQIS
160 170 180 190 200
FADYNLLDLL RIHQVLAPSC LDSFPLLSAY VARLNSRPKL KAFLASPEHM
210
NRPINGNGKQ
Length:210
Mass (Da):23,613
Last modified:January 23, 2007 - v2
Checksum:i79C45DA2031B1EBB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61233 mRNA. Translation: CAA43551.1.
BC102704 mRNA. Translation: AAI02705.1.
PIRiA49180.
RefSeqiNP_803482.1. NM_177516.1.
UniGeneiBt.13949.

Genome annotation databases

EnsembliENSBTAT00000004615; ENSBTAP00000004615; ENSBTAG00000003548.
GeneIDi281806.
KEGGibta:281806.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61233 mRNA. Translation: CAA43551.1 .
BC102704 mRNA. Translation: AAI02705.1 .
PIRi A49180.
RefSeqi NP_803482.1. NM_177516.1.
UniGenei Bt.13949.

3D structure databases

ProteinModelPortali P28801.
SMRi P28801. Positions 1-210.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi P28801.
PRIDEi P28801.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000004615 ; ENSBTAP00000004615 ; ENSBTAG00000003548 .
GeneIDi 281806.
KEGGi bta:281806.

Organism-specific databases

CTDi 2950.

Phylogenomic databases

eggNOGi NOG05174.
GeneTreei ENSGT00550000074559.
HOGENOMi HOG000115733.
HOVERGENi HBG108324.
InParanoidi P28801.
KOi K00799.
OMAi MNRPING.
OrthoDBi EOG7KH9M3.
TreeFami TF105321.

Enzyme and pathway databases

Reactomei REACT_204534. Detoxification of Reactive Oxygen Species.
REACT_223659. Glutathione conjugation.

Miscellaneous databases

NextBioi 20805719.

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. "Isolation of a cDNA encoding a glutathione S-transferase (GST) class-pi from the bovine ocular ciliary epithelium."
    Hernando N., Martin-Alonso J.M., Ghosh S., Coca-Prados M.
    Exp. Eye Res. 55:711-718(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ocular ciliary epithelium.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  3. "Glutathione transferase from bovine placenta. Preparation, biochemical characterization, crystallization, and preliminary crystallographic analysis of a neutral class PI enzyme."
    Schaeffer J., Gallay O., Ladenstein R.
    J. Biol. Chem. 263:17405-17411(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16, SUBUNIT.
    Tissue: Placenta.
  4. "Bovine erythrocyte glutathione S-transferase: purification, inhibition, and complex formation."
    Xu F., Hultquist D.E.
    Biochem. Int. 27:265-274(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-23.
    Tissue: Erythrocyte.

Entry informationi

Entry nameiGSTP1_BOVIN
AccessioniPrimary (citable) accession number: P28801
Secondary accession number(s): Q3SZU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3