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Microsomal glutathione S-transferase 1 (Microsomal GST-1) (EC 2.5.1.18) (Microsomal GST-I)

 MGST1_HUMAN             Reviewed;         155 AA.
P10620; A8K533; G5EA53;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
25-OCT-2017, entry version 158.
RecName: Full=Microsomal glutathione S-transferase 1;
Short=Microsomal GST-1;
EC=2.5.1.18;
AltName: Full=Microsomal GST-I;
Name=MGST1; Synonyms=GST12, MGST;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=3372534;
Dejong J.L., Morgenstern R., Joernvall H., Depierre J.W., Tu C.-P.D.;
"Gene expression of rat and human microsomal glutathione S-
transferases.";
J. Biol. Chem. 263:8430-8436(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Foreskin;
PubMed=8812420; DOI=10.1006/geno.1996.0429;
Kelner M.J., Stokely M.N., Stovall N.E., Montoya M.A.;
"Structural organization of the human microsomal glutathione S-
transferase gene (GST12).";
Genomics 36:100-103(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10524215; DOI=10.1016/S0167-4781(99)00112-8;
Lee S.H., DeJong J.;
"Microsomal GST-I: genomic organization, expression, and alternative
splicing of the human gene.";
Biochim. Biophys. Acta 1446:389-396(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles. Has a wide
substrate specificity.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- ENZYME REGULATION: Can be activated by reagents that attack Cys-50
sulfhydryl, such as N-ethylmaleimide. Activation also occurs via
nitration of Tyr-93 by peroxynitrite (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Homotrimer; The trimer binds only one molecule of
glutathione. {ECO:0000250}.
-!- INTERACTION:
Q8WX92:NELFB; NbExp=2; IntAct=EBI-2691601, EBI-347721;
-!- SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Mitochondrion outer
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P10620-1; Sequence=Displayed;
Name=2;
IsoId=P10620-2; Sequence=VSP_046160;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in liver.
-!- PTM: Peroxynitrite induces nitration at Tyr-93 which activates the
enzyme. {ECO:0000250}.
-!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mgst1/";
-----------------------------------------------------------------------
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EMBL; J03746; AAA35934.1; -; mRNA.
EMBL; U46498; AAC50711.1; -; Genomic_DNA.
EMBL; AF092926; AAC50711.1; JOINED; Genomic_DNA.
EMBL; U46497; AAC50711.1; JOINED; Genomic_DNA.
EMBL; U71213; AAB17184.1; -; Genomic_DNA.
EMBL; U71211; AAB17184.1; JOINED; Genomic_DNA.
EMBL; U71212; AAB17184.1; JOINED; Genomic_DNA.
EMBL; BT006982; AAP35628.1; -; mRNA.
EMBL; AY368173; AAQ55111.1; -; Genomic_DNA.
EMBL; AK291148; BAF83837.1; -; mRNA.
EMBL; AC007528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471094; EAW96362.1; -; Genomic_DNA.
EMBL; CH471094; EAW96367.1; -; Genomic_DNA.
EMBL; BC005923; AAH05923.1; -; mRNA.
EMBL; BC056863; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS58209.1; -. [P10620-2]
CCDS; CCDS8677.1; -. [P10620-1]
PIR; B28083; B28083.
RefSeq; NP_001247440.1; NM_001260511.1. [P10620-1]
RefSeq; NP_001247441.1; NM_001260512.1.
RefSeq; NP_001254527.1; NM_001267598.1. [P10620-2]
RefSeq; NP_064696.1; NM_020300.4. [P10620-1]
RefSeq; NP_665707.1; NM_145764.2. [P10620-1]
RefSeq; NP_665734.1; NM_145791.2. [P10620-1]
RefSeq; NP_665735.1; NM_145792.2. [P10620-1]
UniGene; Hs.389700; -.
ProteinModelPortal; P10620; -.
BioGrid; 110413; 6.
IntAct; P10620; 8.
STRING; 9606.ENSP00000010404; -.
ChEMBL; CHEMBL1743184; -.
DrugBank; DB00143; Glutathione.
iPTMnet; P10620; -.
PhosphoSitePlus; P10620; -.
SwissPalm; P10620; -.
BioMuta; MGST1; -.
DMDM; 121740; -.
EPD; P10620; -.
MaxQB; P10620; -.
PaxDb; P10620; -.
PeptideAtlas; P10620; -.
PRIDE; P10620; -.
TopDownProteomics; P10620-1; -. [P10620-1]
DNASU; 4257; -.
Ensembl; ENST00000010404; ENSP00000010404; ENSG00000008394. [P10620-1]
Ensembl; ENST00000396207; ENSP00000379510; ENSG00000008394. [P10620-1]
Ensembl; ENST00000396209; ENSP00000379512; ENSG00000008394. [P10620-1]
Ensembl; ENST00000396210; ENSP00000379513; ENSG00000008394. [P10620-1]
Ensembl; ENST00000535309; ENSP00000438308; ENSG00000008394. [P10620-2]
GeneID; 4257; -.
KEGG; hsa:4257; -.
UCSC; uc001rdf.4; human. [P10620-1]
CTD; 4257; -.
DisGeNET; 4257; -.
EuPathDB; HostDB:ENSG00000008394.12; -.
GeneCards; MGST1; -.
HGNC; HGNC:7061; MGST1.
HPA; HPA044840; -.
MIM; 138330; gene.
neXtProt; NX_P10620; -.
OpenTargets; ENSG00000008394; -.
PharmGKB; PA30791; -.
eggNOG; ENOG410IXE1; Eukaryota.
eggNOG; ENOG4111VJG; LUCA.
GeneTree; ENSGT00390000011980; -.
HOGENOM; HOG000231759; -.
HOVERGEN; HBG052470; -.
InParanoid; P10620; -.
KO; K00799; -.
OMA; FYRMTRK; -.
OrthoDB; EOG091G14I4; -.
PhylomeDB; P10620; -.
TreeFam; TF105327; -.
Reactome; R-HSA-156590; Glutathione conjugation.
Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; MGST1; human.
GeneWiki; Microsomal_glutathione_S-transferase_1; -.
GenomeRNAi; 4257; -.
PRO; PR:P10620; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000008394; -.
CleanEx; HS_MGST1; -.
ExpressionAtlas; P10620; baseline and differential.
Genevisible; P10620; HS.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043295; F:glutathione binding; IEA:Ensembl.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:UniProtKB.
GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0071449; P:cellular response to lipid hydroperoxide; IDA:UniProtKB.
GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
Gene3D; 1.20.120.550; -; 1.
InterPro; IPR023352; MAPEG-like_dom.
InterPro; IPR001129; Membr-assoc_MAPEG.
Pfam; PF01124; MAPEG; 1.
SUPFAM; SSF161084; SSF161084; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Endoplasmic reticulum; Membrane; Microsome; Mitochondrion;
Mitochondrion outer membrane; Nitration; Reference proteome;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 155 Microsomal glutathione S-transferase 1.
/FTId=PRO_0000217736.
TOPO_DOM 3 9 Lumenal. {ECO:0000250}.
TRANSMEM 10 33 Helical. {ECO:0000250}.
TOPO_DOM 34 62 Cytoplasmic. {ECO:0000250}.
TRANSMEM 63 96 Helical. {ECO:0000250}.
TOPO_DOM 97 99 Lumenal. {ECO:0000250}.
TRANSMEM 100 123 Helical. {ECO:0000250}.
TOPO_DOM 124 128 Cytoplasmic. {ECO:0000250}.
TRANSMEM 129 148 Helical. {ECO:0000250}.
TOPO_DOM 149 155 Lumenal. {ECO:0000250}.
BINDING 38 38 Glutathione. {ECO:0000250}.
BINDING 73 73 Glutathione. {ECO:0000250}.
BINDING 74 74 Glutathione. {ECO:0000250}.
BINDING 76 76 Glutathione. {ECO:0000250}.
BINDING 81 81 Glutathione. {ECO:0000250}.
BINDING 121 121 Glutathione. {ECO:0000250}.
SITE 50 50 Activates the enzyme when modified.
{ECO:0000250}.
MOD_RES 42 42 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VS7}.
MOD_RES 55 55 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VS7}.
MOD_RES 60 60 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VS7}.
VAR_SEQ 75 155 AHLNDLENIIPFLGIGLLYSLSGPDPSTAILHFRLFVGARI
YHTIAYLTPLPQPNRALSFFVGYGVTLSMAYRLLKSKLYL
-> IKQTLSIYLASSI (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046160.
SEQUENCE 155 AA; 17599 MW; 892A529C97E3C853 CRC64;
MVDLTQVMDD EVFMAFASYA TIILSKMMLM STATAFYRLT RKVFANPEDC VAFGKGENAK
KYLRTDDRVE RVRRAHLNDL ENIIPFLGIG LLYSLSGPDP STAILHFRLF VGARIYHTIA
YLTPLPQPNR ALSFFVGYGV TLSMAYRLLK SKLYL


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