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UniProtKB/Swiss-Prot entry Q16772


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GSTA3_HUMAN
Primary accession number Q16772
Secondary accession numbers O43468 Q8WWA8 Q9H415
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on May 27, 2002 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 81)
Name and origin of the protein
Protein name Glutathione S-transferase A3
Synonyms EC 2.5.1.18
Glutathione S-transferase A3-3
GST class-alpha member 3
Gene name
Name: GSTA3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0888-7543(05)80373-8; PubMed=8307579 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki T., Johnston P.N., Board P.G.;
"Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes.";
Genomics 18:680-686(1993).
[2]
NUCLEOTIDE SEQUENCE, AND CHARACTERIZATION.
DOI=10.1074/jbc.M104539200; PubMed=11418619 [NCBI, ExPASy, EBI, Israel, Japan]
Johansson A.-S., Mannervik B.;
"Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones.";
J. Biol. Chem. 276:33061-33065(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-222, AND VARIANT LEU-71.
PubMed=9480897 [NCBI, ExPASy, EBI, Israel, Japan]
Board P.G.;
"Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4.";
Biochem. J. 330:827-831(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L13275; AAA74634.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L13270; AAA74634.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L13271; AAA74634.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L13272; AAA74634.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L13273; AAA74634.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L13274; AAA74634.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF508266; AAM33360.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121969; CAC10389.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020619; AAH20619.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF020919; AAD04712.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A49365; A49365.
RefSeq NP_000838.3; -.
UniGene Hs.102484
3D structure databases
PDB
1TDI; X-ray; 2.40 A; A/B=1-222.[ExPASy / RCSB / EBI]
PDBsum 1TDI; -.
ModBase Q16772.
PTM databases
PhosphoSite Q16772; -.
Enzyme and pathway databases
Reactome REACT_2063; Metabolism of xenobiotics.
Organism-specific databases
GeneCards GC06M052869; -.
H-InvDB HIX0005957; -.
HGNC HGNC:4628; GSTA3.
GenAtlas GSTA3.
HPA HPA004342; -.
MIM 605449; gene. [NCBI / EBI]
PharmGKB PA29018; -.
GeneCards Q16772.
Gene expression databases
ArrayExpress Q16772; -.
CleanEx HS_GSTA3; -.
GermOnline ENSG00000174156; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004364; Molecular function: glutathione transferase activity (traceable author statement from ProtInc).
GO:0008152; Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR010987; Glutathione-S-Trfase_C-like.
IPR003080; GST_alpha.
IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1050.10; GST_C_like; 1.
G3DSA:3.40.30.10; Thioredoxin_fold; 1.
PANTHER PTHR11571:SF4; GST_alpha; 1.
Pfam PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.
PRINTS PR01266; GSTRNSFRASEA.
PROSITE PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q16772; -.
Genome annotation databases
Ensembl ENSG00000174156; Homo sapiens. [Contig view]
GeneID 2940; -.
KEGG hsa:2940; -.
Phylogenomic databases
HOGENOM Q16772; -.
HOVERGEN Q16772; -.
Other
DrugBank DB00143; Glutathione.
LinkHub Q16772; -.
NextBio 11651; -.
SOURCE GSTA3; Homo sapiens.
ProtoNet Q16772.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Polymorphism; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   222  222     Glutathione S-transferase A3. PRO_0000185785
DOMAIN   3    83  81     GST N-terminal. 
DOMAIN   85   207  123     GST C-terminal. 
VARIANT   71    71  1     I -> L (in dbSNP:rs1052661 [NCBI]). VAR_049484 [3D]
VARIANT   73    73  1     N -> D (in dbSNP:rs41273858 [NCBI]). VAR_049485 [3D]
CONFLICT   63    63        M -> I (in Ref. 4; AAH20619). 
CONFLICT   113   114        RP -> PA (in Ref. 1; AAA74634). 
CONFLICT   128   128        T -> I (in Ref. 1; AAA74634). 
STRAND   6     9  4      
TURN   14    16  3      
HELIX   17    25  9      
STRAND   31    34  4      
HELIX   38    46  9      
STRAND   57    60  4      
STRAND   63    67  5      
HELIX   68    78  11      
HELIX   86   108  23      
HELIX   109   111  3      
HELIX   114   130  17      
HELIX   132   143  12      
STRAND   146   149  4      
HELIX   155   170  16      
TURN   172   177  6      
HELIX   179   189  11      
HELIX   192   198  7      
HELIX   210   220  11      
Sequence information
Length: 222 AA [This is the length of the unprocessed precursor] Molecular weight: 25302 Da [This is the MW of the unprocessed precursor] CRC64: 904AA17519B5343C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGKPKLHYF NGRGRMEPIR WLLAAAGVEF EEKFIGSAED LGKLRNDGSL MFQQVPMVEI 

        70         80         90        100        110        120 
DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYTEGMA DLNEMILLLP LCRPEEKDAK 

       130        140        150        160        170        180 
IALIKEKTKS RYFPAFEKVL QSHGQDYLVG NKLSRADISL VELLYYVEEL DSSLISNFPL 

       190        200        210        220 
LKALKTRISN LPTVKKFLQP GSPRKPPADA KALEEARKIF RF 

Q16772 in FASTA format

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