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Protein

Glutathione S-transferase Mu 5

Gene

GSTM5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161SubstrateBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione derivative biosynthetic process Source: Reactome
  2. glutathione metabolic process Source: UniProtKB
  3. small molecule metabolic process Source: Reactome
  4. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 2681.
ReactomeiREACT_6926. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 5 (EC:2.5.1.18)
Alternative name(s):
GST class-mu 5
GSTM5-5
Gene namesi
Name:GSTM5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4637. GSTM5.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29027.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Glutathione S-transferase Mu 5PRO_0000185825Add
BLAST

Proteomic databases

PaxDbiP46439.
PRIDEiP46439.

PTM databases

PhosphoSiteiP46439.

Expressioni

Gene expression databases

BgeeiP46439.
CleanExiHS_GSTM5.
ExpressionAtlasiP46439. baseline and differential.
GenevestigatoriP46439.

Organism-specific databases

HPAiHPA055972.
HPA055973.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109204. 9 interactions.
IntActiP46439. 1 interaction.
STRINGi9606.ENSP00000256593.

Structurei

3D structure databases

ProteinModelPortaliP46439.
SMRiP46439. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8887GST N-terminalAdd
BLAST
Domaini90 – 207118GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Glutathione bindingBy similarity
Regioni46 – 505Glutathione bindingBy similarity
Regioni59 – 602Glutathione bindingBy similarity
Regioni72 – 732Glutathione bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG300089.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP46439.
KOiK00799.
OrthoDBiEOG7KH9M3.
PhylomeDBiP46439.
TreeFamiTF353040.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46439-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMTLGYWDI RGLAHAIRLL LEYTDSSYVE KKYTLGDAPD YDRSQWLNEK
60 70 80 90 100
FKLGLDFPNL PYLIDGAHKI TQSNAILRYI ARKHNLCGET EEEKIRVDIL
110 120 130 140 150
ENQVMDNHME LVRLCYDPDF EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG
160 170 180 190 200
DKITFVDFLA YDVLDMKRIF EPKCLDAFLN LKDFISRFEG LKKISAYMKS
210
SQFLRGLLFG KSATWNSK
Length:218
Mass (Da):25,675
Last modified:January 23, 2007 - v3
Checksum:i62B03FCD960FB4AB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351L → M in AAA20040 (PubMed:8473333).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671A → T.2 Publications
Corresponds to variant rs17854972 [ dbSNP | Ensembl ].
VAR_065098
Natural varianti179 – 1791L → P.
Corresponds to variant rs2227963 [ dbSNP | Ensembl ].
VAR_049491

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02321 mRNA. Translation: AAA20040.1.
AK289673 mRNA. Translation: BAF82362.1.
BC058881 mRNA. Translation: AAH58881.1.
CCDSiCCDS811.1.
PIRiA46048.
RefSeqiNP_000842.2. NM_000851.3.
XP_005270841.1. XM_005270784.2.
UniGeneiHs.75652.

Genome annotation databases

EnsembliENST00000256593; ENSP00000256593; ENSG00000134201.
GeneIDi2949.
KEGGihsa:2949.
UCSCiuc001dyn.3. human.

Polymorphism databases

DMDMi67476963.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02321 mRNA. Translation: AAA20040.1.
AK289673 mRNA. Translation: BAF82362.1.
BC058881 mRNA. Translation: AAH58881.1.
CCDSiCCDS811.1.
PIRiA46048.
RefSeqiNP_000842.2. NM_000851.3.
XP_005270841.1. XM_005270784.2.
UniGeneiHs.75652.

3D structure databases

ProteinModelPortaliP46439.
SMRiP46439. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109204. 9 interactions.
IntActiP46439. 1 interaction.
STRINGi9606.ENSP00000256593.

Chemistry

ChEMBLiCHEMBL2819.
DrugBankiDB00143. Glutathione.

PTM databases

PhosphoSiteiP46439.

Polymorphism databases

DMDMi67476963.

Proteomic databases

PaxDbiP46439.
PRIDEiP46439.

Protocols and materials databases

DNASUi2949.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256593; ENSP00000256593; ENSG00000134201.
GeneIDi2949.
KEGGihsa:2949.
UCSCiuc001dyn.3. human.

Organism-specific databases

CTDi2949.
GeneCardsiGC01P110256.
HGNCiHGNC:4637. GSTM5.
HPAiHPA055972.
HPA055973.
MIMi138385. gene.
neXtProtiNX_P46439.
PharmGKBiPA29027.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300089.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP46439.
KOiK00799.
OrthoDBiEOG7KH9M3.
PhylomeDBiP46439.
TreeFamiTF353040.

Enzyme and pathway databases

BRENDAi2.5.1.18. 2681.
ReactomeiREACT_6926. Glutathione conjugation.

Miscellaneous databases

ChiTaRSiGSTM5. human.
GenomeRNAii2949.
NextBioi11688.
PROiP46439.
SOURCEiSearch...

Gene expression databases

BgeeiP46439.
CleanExiHS_GSTM5.
ExpressionAtlasiP46439. baseline and differential.
GenevestigatoriP46439.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1992) [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.
    , 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(2003) [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(2003) [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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiGSTM5_HUMAN
AccessioniPrimary (citable) accession number: P46439
Secondary accession number(s): A8K0V8, Q6PD78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.