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P46439 (GSTM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. 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 Mu 5

EC=2.5.1.18
Alternative name(s):
GST class-mu 5
GSTM5-5
Gene names
Name:GSTM5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Ref.4

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.4

Subunit structure

Homodimer. Ref.4

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

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

Traceable author statement. Source: Reactome

glutathione metabolic process

Inferred from direct assay Ref.4. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionglutathione transferase activity

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 218218Glutathione S-transferase Mu 5
PRO_0000185825

Regions

Domain2 – 8887GST N-terminal
Domain90 – 207118GST C-terminal
Region7 – 82Glutathione binding By similarity
Region46 – 505Glutathione binding By similarity
Region59 – 602Glutathione binding By similarity
Region72 – 732Glutathione binding By similarity

Sites

Binding site1161Substrate By similarity

Natural variations

Natural variant671A → T. Ref.2 Ref.3
Corresponds to variant rs17854972 [ dbSNP | Ensembl ].
VAR_065098
Natural variant1791L → P.
Corresponds to variant rs2227963 [ dbSNP | Ensembl ].
VAR_049491

Experimental info

Sequence conflict351L → M in AAA20040. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P46439 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 62B03FCD960FB4AB

FASTA21825,675
        10         20         30         40         50         60 
MPMTLGYWDI RGLAHAIRLL LEYTDSSYVE KKYTLGDAPD YDRSQWLNEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGAHKI TQSNAILRYI ARKHNLCGET EEEKIRVDIL ENQVMDNHME LVRLCYDPDF 

       130        140        150        160        170        180 
EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG DKITFVDFLA YDVLDMKRIF EPKCLDAFLN 

       190        200        210 
LKDFISRFEG LKKISAYMKS SQFLRGLLFG KSATWNSK 

« Hide

References

« Hide 'large scale' references
[1]"A basis for differentiating among the multiple human Mu-glutathione S-transferases and molecular cloning of brain GSTM5."
Takahashi Y., Campbell E.A., Hirata Y., Takayama T., Listowsky I.
J. Biol. Chem. 268:8893-8898(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-67.
Tissue: Amygdala.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-67.
Tissue: PNS.
[4]"An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases."
Patskovsky Y.V., Patskovska L.N., Listowsky I.
Biochemistry 38:16187-16194(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02321 mRNA. Translation: AAA20040.1.
AK289673 mRNA. Translation: BAF82362.1.
BC058881 mRNA. Translation: AAH58881.1.
PIRA46048.
RefSeqNP_000842.2. NM_000851.3.
XP_005270841.1. XM_005270784.2.
UniGeneHs.75652.

3D structure databases

ProteinModelPortalP46439.
SMRP46439. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109204. 2 interactions.
IntActP46439. 1 interaction.
STRING9606.ENSP00000256593.

Chemistry

ChEMBLCHEMBL2819.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteP46439.

Polymorphism databases

DMDM67476963.

Proteomic databases

PaxDbP46439.
PRIDEP46439.

Protocols and materials databases

DNASU2949.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256593; ENSP00000256593; ENSG00000134201.
GeneID2949.
KEGGhsa:2949.
UCSCuc001dyn.3. human.

Organism-specific databases

CTD2949.
GeneCardsGC01P110256.
HGNCHGNC:4637. GSTM5.
MIM138385. gene.
neXtProtNX_P46439.
PharmGKBPA29027.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300089.
HOGENOMHOG000115735.
HOVERGENHBG106842.
KOK00799.
OrthoDBEOG7KH9M3.
PhylomeDBP46439.
TreeFamTF353040.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP46439.
BgeeP46439.
CleanExHS_GSTM5.
GenevestigatorP46439.

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.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01267. GSTRNSFRASEM.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi2949.
NextBio11688.
PROP46439.
SOURCESearch...

Entry information

Entry nameGSTM5_HUMAN
AccessionPrimary (citable) accession number: P46439
Secondary accession number(s): A8K0V8, Q6PD78
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 119 of the entry and version 3 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 1

Human chromosome 1: entries, gene names and cross-references to MIM