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P48429 (GST2_ASCSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase 2

EC=2.5.1.18
Alternative name(s):
GST class-sigma
Gene names
Name:GST2
OrganismAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier6253 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Sequence similarities

Belongs to the GST superfamily. Sigma family.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Molecular functionTransferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›20Glutathione S-transferase 2
PRO_0000185924

Regions

Domain1 – ›20›20GST N-terminal

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P48429 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: A506D5F2B144FB20

FASTA202,249
        10         20 
GYKVTYFAIR GLAEPIXLLL 

« Hide

References

[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.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR012336. Thioredoxin-like_fold.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGST2_ASCSU
AccessionPrimary (citable) accession number: P48429
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families