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Protein

Glutathione S-transferase 2

Gene

GST2

Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 2 (EC:2.5.1.18)
Alternative name(s):
GST class-sigma
Gene namesi
Name:GST2
OrganismiAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifieri6253 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›20›20Glutathione S-transferase 2PRO_0000185924Add
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – ›20›20GST N-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the GST superfamily. Sigma family.Curated
Contains 1 GST N-terminal domain.Curated

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P48429-1 [UniParc]FASTAAdd to basket

« Hide

        10         20
GYKVTYFAIR GLAEPIXLLL
Length:20
Mass (Da):2,249
Last modified:February 1, 1996 - v1
Checksum:iA506D5F2B144FB20
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei20 – 201

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of a cDNA encoding glutathione S-transferase from Ascaris suum."
    Liebau E., Schoenberger O.L., Walter R.D., Henkle-Duehrsen K.J.
    Mol. Biochem. Parasitol. 63:167-170(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

Entry informationi

Entry nameiGST2_ASCSU
AccessioniPrimary (citable) accession number: P48429
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 1, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.