GSTM5_HUMAN
ID GSTM5_HUMAN Reviewed; 218 AA.
AC P46439; A8K0V8; Q6PD78;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Glutathione S-transferase Mu 5;
DE EC=2.5.1.18;
DE AltName: Full=GST class-mu 5;
DE AltName: Full=GSTM5-5;
GN Name=GSTM5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8473333; DOI=10.1016/s0021-9258(18)52957-4;
RA Takahashi Y., Campbell E.A., Hirata Y., Takayama T., Listowsky I.;
RT "A basis for differentiating among the multiple human Mu-glutathione S-
RT transferases and molecular cloning of brain GSTM5.";
RL J. Biol. Chem. 268:8893-8898(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-67.
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-67.
RC TISSUE=PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RX PubMed=10587441; DOI=10.1021/bi991714t;
RA Patskovsky Y.V., Patskovska L.N., Listowsky I.;
RT "An asparagine-phenylalanine substitution accounts for catalytic
RT differences between hGSTM3-3 and other human class mu glutathione S-
RT transferases.";
RL Biochemistry 38:16187-16194(1999).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000269|PubMed:10587441}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:10587441};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10587441}.
CC -!- INTERACTION:
CC P46439; Q9Y2J4: AMOTL2; NbExp=4; IntAct=EBI-4312072, EBI-746752;
CC P46439; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-4312072, EBI-10187270;
CC P46439; Q92917: GPKOW; NbExp=3; IntAct=EBI-4312072, EBI-746309;
CC P46439; P28161: GSTM2; NbExp=6; IntAct=EBI-4312072, EBI-9023362;
CC P46439; P21266: GSTM3; NbExp=12; IntAct=EBI-4312072, EBI-350350;
CC P46439; Q6FGJ9: GSTM3; NbExp=3; IntAct=EBI-4312072, EBI-10209603;
CC P46439; Q03013: GSTM4; NbExp=3; IntAct=EBI-4312072, EBI-713363;
CC P46439; P46439: GSTM5; NbExp=8; IntAct=EBI-4312072, EBI-4312072;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; L02321; AAA20040.1; -; mRNA.
DR EMBL; AK289673; BAF82362.1; -; mRNA.
DR EMBL; BC058881; AAH58881.1; -; mRNA.
DR CCDS; CCDS811.1; -.
DR PIR; A46048; A46048.
DR RefSeq; NP_000842.2; NM_000851.3.
DR RefSeq; XP_005270841.1; XM_005270784.4.
DR AlphaFoldDB; P46439; -.
DR SMR; P46439; -.
DR BioGRID; 109204; 15.
DR IntAct; P46439; 9.
DR STRING; 9606.ENSP00000256593; -.
DR ChEMBL; CHEMBL2819; -.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR iPTMnet; P46439; -.
DR PhosphoSitePlus; P46439; -.
DR BioMuta; GSTM5; -.
DR DMDM; 67476963; -.
DR jPOST; P46439; -.
DR MassIVE; P46439; -.
DR PaxDb; P46439; -.
DR PeptideAtlas; P46439; -.
DR PRIDE; P46439; -.
DR ProteomicsDB; 55739; -.
DR Antibodypedia; 20076; 199 antibodies from 30 providers.
DR DNASU; 2949; -.
DR Ensembl; ENST00000256593.8; ENSP00000256593.3; ENSG00000134201.12.
DR GeneID; 2949; -.
DR KEGG; hsa:2949; -.
DR MANE-Select; ENST00000256593.8; ENSP00000256593.3; NM_000851.4; NP_000842.2.
DR CTD; 2949; -.
DR DisGeNET; 2949; -.
DR GeneCards; GSTM5; -.
DR HGNC; HGNC:4637; GSTM5.
DR HPA; ENSG00000134201; Tissue enriched (breast).
DR MIM; 138385; gene.
DR neXtProt; NX_P46439; -.
DR OpenTargets; ENSG00000134201; -.
DR PharmGKB; PA29027; -.
DR VEuPathDB; HostDB:ENSG00000134201; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000155416; -.
DR HOGENOM; CLU_039475_2_0_1; -.
DR InParanoid; P46439; -.
DR OMA; ADFIMYE; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P46439; -.
DR TreeFam; TF353040; -.
DR BRENDA; 2.5.1.18; 2681.
DR PathwayCommons; P46439; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR SABIO-RK; P46439; -.
DR SignaLink; P46439; -.
DR BioGRID-ORCS; 2949; 6 hits in 1063 CRISPR screens.
DR GenomeRNAi; 2949; -.
DR Pharos; P46439; Tbio.
DR PRO; PR:P46439; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P46439; protein.
DR Bgee; ENSG00000134201; Expressed in left ovary and 134 other tissues.
DR ExpressionAtlas; P46439; baseline and differential.
DR Genevisible; P46439; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase Mu 5"
FT /id="PRO_0000185825"
FT DOMAIN 2..88
FT /note="GST N-terminal"
FT DOMAIN 90..207
FT /note="GST C-terminal"
FT BINDING 7..8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 46..50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 59..60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 72..73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VARIANT 67
FT /note="A -> T (in dbSNP:rs17854972)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_065098"
FT VARIANT 179
FT /note="L -> P (in dbSNP:rs2227963)"
FT /id="VAR_049491"
FT CONFLICT 35
FT /note="L -> M (in Ref. 1; AAA20040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 25675 MW; 62B03FCD960FB4AB CRC64;
MPMTLGYWDI RGLAHAIRLL LEYTDSSYVE KKYTLGDAPD YDRSQWLNEK FKLGLDFPNL
PYLIDGAHKI TQSNAILRYI ARKHNLCGET EEEKIRVDIL ENQVMDNHME LVRLCYDPDF
EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG DKITFVDFLA YDVLDMKRIF EPKCLDAFLN
LKDFISRFEG LKKISAYMKS SQFLRGLLFG KSATWNSK
