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Q9TTY8

- GSTP1_CAPHI

UniProt

Q9TTY8 - GSTP1_CAPHI

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Protein
Glutathione S-transferase P
Gene
GSTP1
Organism
Capra hircus (Goat)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Glutathione By similarity
Binding sitei14 – 141Glutathione By similarity
Binding sitei39 – 391Glutathione By similarity
Binding sitei45 – 451Glutathione By similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    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
    OrganismiCapra hircus (Goat)
    Taxonomic identifieri9925 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

    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. mitochondrion Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed By similarity
    Chaini2 – 210209Glutathione S-transferase P
    PRO_0000185897Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41Phosphotyrosine; by EGFR By similarity
    Modified residuei103 – 1031N6-succinyllysine By similarity
    Modified residuei116 – 1161N6-succinyllysine By similarity
    Modified residuei128 – 1281N6-acetyllysine By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiQ9TTY8.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with CDK5 By similarity.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9TTY8.
    SMRiQ9TTY8. Positions 4-210.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8180GST N-terminal
    Add
    BLAST
    Domaini83 – 204122GST C-terminal
    Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 532Glutathione binding By similarity
    Regioni65 – 662Glutathione binding By similarity

    Sequence similaritiesi

    Belongs to the GST superfamily. Pi family.

    Phylogenomic databases

    HOVERGENiHBG108324.

    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.

    Q9TTY8-1 [UniParc]FASTAAdd to Basket

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    MASYTIVYFP VQGRCEAMRM LLADQDQSWK EEVVAMQSWL QGPLKASCLY    50
    GQLPKFQDGD LTLYQSNAIL RHLGRTLGLY GKDQREAALV DMVNDGVEDL 100
    RCKYVSLIYT NYQAGKEDYV KALPQHLKPF ETLLSQNKGG QAFIVGDQIS 150
    FADYNLLDLL RIHQVLAPSC LDSFPLLSAY VARLNSRPKL KAFLASPEHV 200
    NRPINGNGKQ 210
    Length:210
    Mass (Da):23,630
    Last modified:January 23, 2007 - v2
    Checksum:iBDA49F961FA69DBA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF186248 mRNA. Translation: AAF01323.1.
    UniGeneiChi.13313.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF186248 mRNA. Translation: AAF01323.1 .
    UniGenei Chi.13313.

    3D structure databases

    ProteinModelPortali Q9TTY8.
    SMRi Q9TTY8. Positions 4-210.
    ModBasei Search...

    Proteomic databases

    PRIDEi Q9TTY8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG108324.

    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

    1. "Complementary DNA sequence (632 b.p.) of goat germ cell glutathione S-transferase Pi."
      Hemchand T., Shaha C.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.

    Entry informationi

    Entry nameiGSTP1_CAPHI
    AccessioniPrimary (citable) accession number: Q9TTY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 23, 2007
    Last modified: March 19, 2014
    This is version 65 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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