GSTP1
entrez
2950
canonical
uniprot
P09211
canonical
ensembl
ENSG00000084207
resolver
ensp
ENSP00000381607
resolver
enst
ENST00000398606
resolver
genesymbol
GSTP1
resolver
genesymbol
HEL-S-22
resolver
genesymbol_syn
FAEES3
resolver
genesymbol_syn
GST3
resolver
genesymbol_syn
GSTP1
resolver
hgnc
HGNC:4638
resolver
uniprot
O00460
resolver
uniprot
Q15690
resolver
uniprot
Q5TZY3
resolver
uniprot
V9HWE9
resolver
uniprot_entry
GSTP1_HUMAN
resolver
uniprot_entry
V9HWE9_HUMAN
resolver
uniprot_sec
O00460
resolver
uniprot_sec
Q15690
resolver
uniprot_sec
Q5TZY3
resolver
amino_acid_sequence
MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ
uniprot
proteins
ec_number
2.5.1.18
uniprot
proteins
function
FUNCTION: Catalyzes conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:1540159, PubMed:1567427, PubMed:8433974). Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubMed:9084911). Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276). Acts as a negative regulator of ferroptosis by mediating glutathione conjugation and detoxification of 4-hydroxynonenal (4-HNE) reactive aldehyde (PubMed:38016474). Negatively regulates CDK5 activity via p25/p35 translocation to prevent neurodegeneration (PubMed:21668448). {ECO:0000269|PubMed:1540159, ECO:0000269|PubMed:1567427, ECO:0000269|PubMed:21046276, ECO:0000269|PubMed:21668448, ECO:0000269|PubMed:38016474, ECO:0000269|PubMed:8433974, ECO:0000269|PubMed:9084911}.
uniprot
proteins
mass_dalton
23356
uniprot
proteins
mutagenesis
MUTAGEN 8; /note="Y->F: Reduces catalytic activity about 50-fold."; /evidence="ECO:0000269|PubMed:1540159, ECO:0000269|PubMed:1567427, ECO:0000269|PubMed:38016474"; MUTAGEN 52..53; /note="QL->AA: Impaired ability to inhibit ferroptosis."; /evidence="ECO:0000269|PubMed:38016474"; MUTAGEN 55; /note="K->R: Decreased ubiquitination. In 3R; abolished ubiquitination, preventing its degradation; when associated with R-121 and R-191."; /evidence="ECO:0000269|PubMed:38016474"; MUTAGEN 99; /note="D->A: Reduces affinity for glutathione. Slightly reduced catalytic activity."; /evidence="ECO:0000269|PubMed:8433974"; MUTAGEN 105; /note="I->A: Impaired ability to inhibit ferroptosis."; /evidence="ECO:0000269|PubMed:38016474"; MUTAGEN 109; /note="Y->A: Impaired ability to inhibit ferroptosis."; /evidence="ECO:0000269|PubMed:38016474"; MUTAGEN 121; /note="K->R: Decreased ubiquitination. In 3R; abolished ubiquitination, preventing its degradation; when associated with R-55 and R-191."; /evidence="ECO:0000269|PubMed:38016474"; MUTAGEN 191; /note="K->R: Strongly decreased ubiquitination. In 3R; abolished ubiquitination, preventing its degradation; when associated with R-55 and R-121."; /evidence="ECO:0000269|PubMed:38016474
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated at Lys-55, Lys-121 and Lys-191 by SMURF2, leading to its degradation and initiation of ferroptosis. {ECO:0000269|PubMed:38016474}.
uniprot
proteins
protein_family
GST superfamily
uniprot
proteins
protein_family
Pi family
uniprot
proteins
pubmed
10441116
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
1522586
uniprot
proteins
pubmed
1540159
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1567427
uniprot
proteins
pubmed
19254954
uniprot
proteins
pubmed
19269317
uniprot
proteins
pubmed
19396894
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19808963
uniprot
proteins
pubmed
21046276
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21668448
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
2327795
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2466554
uniprot
proteins
pubmed
2542132
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
3196325
uniprot
proteins
pubmed
3395118
uniprot
proteins
pubmed
3664469
uniprot
proteins
pubmed
38016474
uniprot
proteins
pubmed
3864155
uniprot
proteins
pubmed
3979555
uniprot
proteins
pubmed
8433974
uniprot
proteins
pubmed
9012673
uniprot
proteins
pubmed
9084911
uniprot
proteins
pubmed
9092542
uniprot
proteins
pubmed
9150948
uniprot
proteins
pubmed
9245401
uniprot
proteins
pubmed
9351803
uniprot
proteins
pubmed
9398518
uniprot
proteins
pubmed
9485454
uniprot
proteins
sequence_length
210
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19269317}. Mitochondrion {ECO:0000269|PubMed:19269317}. Nucleus {ECO:0000269|PubMed:19269317}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. {ECO:0000269|PubMed:19269317}.
uniprot
proteins