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P46439

- GSTM5_HUMAN

UniProt

P46439 - GSTM5_HUMAN

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Protein

Glutathione S-transferase Mu 5

Gene

GSTM5

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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: 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.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109204. 7 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L02321 mRNA. Translation: AAA20040.1 .
AK289673 mRNA. Translation: BAF82362.1 .
BC058881 mRNA. Translation: AAH58881.1 .
CCDSi CCDS811.1.
PIRi A46048.
RefSeqi NP_000842.2. NM_000851.3.
XP_005270841.1. XM_005270784.2.
UniGenei Hs.75652.

3D structure databases

ProteinModelPortali P46439.
SMRi P46439. Positions 2-218.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109204. 7 interactions.
IntActi P46439. 1 interaction.
STRINGi 9606.ENSP00000256593.

Chemistry

ChEMBLi CHEMBL2819.
DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei P46439.

Polymorphism databases

DMDMi 67476963.

Proteomic databases

PaxDbi P46439.
PRIDEi P46439.

Protocols and materials databases

DNASUi 2949.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256593 ; ENSP00000256593 ; ENSG00000134201 .
GeneIDi 2949.
KEGGi hsa:2949.
UCSCi uc001dyn.3. human.

Organism-specific databases

CTDi 2949.
GeneCardsi GC01P110256.
HGNCi HGNC:4637. GSTM5.
MIMi 138385. gene.
neXtProti NX_P46439.
PharmGKBi PA29027.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300089.
HOGENOMi HOG000115735.
HOVERGENi HBG106842.
InParanoidi P46439.
KOi K00799.
OrthoDBi EOG7KH9M3.
PhylomeDBi P46439.
TreeFami TF353040.

Enzyme and pathway databases

Reactomei REACT_6926. Glutathione conjugation.

Miscellaneous databases

GenomeRNAii 2949.
NextBioi 11688.
PROi P46439.
SOURCEi Search...

Gene expression databases

Bgeei P46439.
CleanExi HS_GSTM5.
ExpressionAtlasi P46439. baseline and differential.
Genevestigatori P46439.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01267. GSTRNSFRASEM.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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.

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: October 29, 2014
This is version 123 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