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Q7RTV2 (GSTA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 A5

EC=2.5.1.18
Alternative name(s):
GST class-alpha member 5
Glutathione S-transferase A5-5
Gene names
Name:GSTA5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.3

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expression not detected.

Sequence similarities

Belongs to the GST superfamily. Alpha family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Molecular functionTransferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 222221Glutathione S-transferase A5
PRO_0000185787

Regions

Domain3 – 8381GST N-terminal
Domain85 – 208124GST C-terminal
Region54 – 552Glutathione binding By similarity
Region67 – 682Glutathione binding By similarity

Sites

Binding site91Glutathione By similarity
Binding site451Glutathione By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue41N6-succinyllysine By similarity

Natural variations

Natural variant551V → I.
Corresponds to variant rs2397118 [ dbSNP | Ensembl ].
VAR_024483

Sequences

Sequence LengthMass (Da)Tools
Q7RTV2 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 6DFCECF202F2D898

FASTA22225,722
        10         20         30         40         50         60 
MAEKPKLHYS NARGSMESIR WLLAAAGVEL EEKFLESAED LDKLRNDGSL LFQQVPMVEI 

        70         80         90        100        110        120 
DGMKLVQTRA ILNYIASKYN LYGKDMKERA LIDMYTEGIV DLTEMILLLL ICQPEERDAK 

       130        140        150        160        170        180 
TALVKEKIKN RYFPAFEKVL KSHRQDYLVG NKLSWADIHL VELFYYVEEL DSSLISSFPL 

       190        200        210        220 
LKALKTRISN LPTVKKFLQP GSQRKPPMDE KSLEEARKIF RF 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter."
Morel F., Rauch C., Coles B., Ferrec E.L., Guillouzo A.
Pharmacogenetics 12:277-286(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[3]"The human hGSTA5 gene encodes an enzymatically active protein."
Singh S.P., Zimniak L., Zimniak P.
Biochim. Biophys. Acta 1800:16-22(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590363 Genomic DNA. Translation: CAI13814.1.
BK000212 Genomic DNA. Translation: DAA00071.1.
RefSeqNP_714543.1. NM_153699.1.
UniGeneHs.646984.

3D structure databases

ProteinModelPortalQ7RTV2.
SMRQ7RTV2. Positions 2-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000284562.

Chemistry

DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteQ7RTV2.

Polymorphism databases

DMDM50400409.

Proteomic databases

PaxDbQ7RTV2.
PRIDEQ7RTV2.

Protocols and materials databases

DNASU221357.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284562; ENSP00000284562; ENSG00000182793.
ENST00000370989; ENSP00000360028; ENSG00000182793.
GeneID221357.
KEGGhsa:221357.
UCSCuc003pba.1. human.

Organism-specific databases

CTD221357.
GeneCardsGC06M052696.
HGNCHGNC:19662. GSTA5.
HPAHPA004342.
MIM607605. gene.
neXtProtNX_Q7RTV2.
PharmGKBPA134962856.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266414.
HOGENOMHOG000115734.
HOVERGENHBG053749.
InParanoidQ7RTV2.
KOK00799.
OMAICQPEER.
OrthoDBEOG79CZ0K.
PhylomeDBQ7RTV2.
TreeFamTF105321.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ7RTV2.
CleanExHS_GSTA5.
GenevestigatorQ7RTV2.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11571:SF4. PTHR11571:SF4. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01266. GSTRNSFRASEA.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi221357.
NextBio91297.
PROQ7RTV2.
SOURCESearch...

Entry information

Entry nameGSTA5_HUMAN
AccessionPrimary (citable) accession number: Q7RTV2
Secondary accession number(s): Q5SZC2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 15, 2003
Last modified: March 19, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM