P10620 (MGST1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Microsomal glutathione S-transferase 1
Short name=Microsomal GST-1
EC=2.5.1.18

Alternative name(s):
Microsomal GST-I

Gene names

Name:	MGST1
Synonyms:	GST12, MGST

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	155 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	Homotrimer; The trimer binds only one molecule of glutathione By similarity.
Subcellular location	Microsome By similarity. Mitochondrion outer membrane; Peripheral membrane protein By similarity. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Highly expressed in liver.
Post-translational modification	Peroxynitrite induces nitration at Tyr-93 which activates the enzyme By similarity.
Sequence similarities	Belongs to the MAPEG family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Acetylation Nitration
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from electronic annotation. Source: Compara cellular response to lipid hydroperoxide Inferred from direct assay PubMed 20727966. Source: UniProtKB glutathione metabolic process Inferred from electronic annotation. Source: Compara protein homotrimerization Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to organic nitrogen Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	apical part of cell Inferred from electronic annotation. Source: Compara endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 20727966. Source: UniProtKB nucleus Inferred from electronic annotation. Source: Compara peroxisomal membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	glutathione binding Inferred from electronic annotation. Source: Compara glutathione peroxidase activity Inferred from direct assay PubMed 20727966. Source: UniProtKB glutathione transferase activity Inferred from direct assay PubMed 20727966. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NELFB	Q8WX92	2	EBI-2691601,EBI-347721

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P10620-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P10620-2)

The sequence of this isoform differs from the canonical sequence as follows:
     75-155: AHLNDLENII...YRLLKSKLYL → IKQTLSIYLASSI

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 155	154	Microsomal glutathione S-transferase 1		PRO_0000217736
Regions
	Topological domain	3 – 9	7	Lumenal By similarity
	Transmembrane	10 – 33	24	Helical; By similarity
	Topological domain	34 – 62	29	Cytoplasmic By similarity
	Transmembrane	63 – 96	34	Helical; By similarity
	Topological domain	97 – 99	3	Lumenal By similarity
	Transmembrane	100 – 123	24	Helical; By similarity
	Topological domain	124 – 128	5	Cytoplasmic By similarity
	Transmembrane	129 – 148	20	Helical; By similarity
	Topological domain	149 – 155	7	Lumenal By similarity
Sites
	Binding site	38	1	Glutathione By similarity
	Binding site	73	1	Glutathione By similarity
	Binding site	74	1	Glutathione By similarity
	Binding site	76	1	Glutathione By similarity
	Binding site	81	1	Glutathione By similarity
	Binding site	121	1	Glutathione By similarity
	Site	50	1	Activates the enzyme when modified By similarity
Amino acid modifications
	Modified residue	42	1	N6-acetyllysine By similarity
	Modified residue	55	1	N6-acetyllysine By similarity
	Modified residue	93	1	Nitrated tyrosine By similarity
Natural variations
	Alternative sequence	75 – 155	81	AHLND…SKLYL → IKQTLSIYLASSI in isoform 2.		VSP_046160

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 892A529C97E3C853	FASTA	155	17,599
	10 20 30 40 50 60 MVDLTQVMDD EVFMAFASYA TIILSKMMLM STATAFYRLT RKVFANPEDC VAFGKGENAK 70 80 90 100 110 120 KYLRTDDRVE RVRRAHLNDL ENIIPFLGIG LLYSLSGPDP STAILHFRLF VGARIYHTIA 130 140 150 YLTPLPQPNR ALSFFVGYGV TLSMAYRLLK SKLYL
	Isoform 2 [UniParc]. Checksum: 8F4C9AF76F18EF97	FASTA	87	9,984
	10 20 30 40 50 60 MVDLTQVMDD EVFMAFASYA TIILSKMMLM STATAFYRLT RKVFANPEDC VAFGKGENAK 70 80 KYLRTDDRVE RVRRIKQTLS IYLASSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene expression of rat and human microsomal glutathione S-transferases." Dejong J.L., Morgenstern R., Joernvall H., Depierre J.W., Tu C.-P.D. J. Biol. Chem. 263:8430-8436(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[2]	"Structural organization of the human microsomal glutathione S-transferase gene (GST12)." Kelner M.J., Stokely M.N., Stovall N.E., Montoya M.A. Genomics 36:100-103(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Foreskin.
[3]	"Microsomal GST-I: genomic organization, expression, and alternative splicing of the human gene." Lee S.H., DeJong J. Biochim. Biophys. Acta 1446:389-396(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	NIEHS SNPs program Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"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] (ISOFORM 1).
[7]	"The finished DNA sequence of human chromosome 12." 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. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORMS 1 AND 2). Tissue: Brain and Prostate.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03746 mRNA. Translation: AAA35934.1. U46498, AF092926, U46497 Genomic DNA. Translation: AAC50711.1. U71213, U71211, U71212 Genomic DNA. Translation: AAB17184.1. BT006982 mRNA. Translation: AAP35628.1. AY368173 Genomic DNA. Translation: AAQ55111.1. AK291148 mRNA. Translation: BAF83837.1. AC007528 Genomic DNA. No translation available. AC007529 Genomic DNA. No translation available. AC007552 Genomic DNA. No translation available. CH471094 Genomic DNA. Translation: EAW96362.1. CH471094 Genomic DNA. Translation: EAW96367.1. BC005923 mRNA. Translation: AAH05923.1. BC056863 mRNA. No translation available.
IPI	IPI00021805.
PIR	B28083.
RefSeq	NP_001247440.1. NM_001260511.1. NP_001247441.1. NM_001260512.1. NP_001254527.1. NM_001267598.1. NP_064696.1. NM_020300.4. NP_665707.1. NM_145764.2. NP_665734.1. NM_145791.2. NP_665735.1. NM_145792.2.
UniGene	Hs.389700.
3D structure databases
ProteinModelPortal	P10620.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10620. 1 interaction.
STRING	9606.ENSP00000010404.
PTM databases
PhosphoSite	P10620.
Polymorphism databases
DMDM	121740.
Proteomic databases
PaxDb	P10620.
PRIDE	P10620.
Protocols and materials databases
DNASU	4257.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000010404; ENSP00000010404; ENSG00000008394. ENST00000396207; ENSP00000379510; ENSG00000008394. ENST00000396209; ENSP00000379512; ENSG00000008394. ENST00000396210; ENSP00000379513; ENSG00000008394. ENST00000535309; ENSP00000438308; ENSG00000008394.
GeneID	4257.
KEGG	hsa:4257.
UCSC	uc001rdf.3. human.
Organism-specific databases
CTD	4257.
GeneCards	GC12P016500.
HGNC	HGNC:7061. MGST1.
HPA	HPA044840.
MIM	138330. gene.
neXtProt	NX_P10620.
PharmGKB	PA30791.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG71159.
HOGENOM	HOG000231759.
HOVERGEN	HBG052470.
InParanoid	P10620.
KO	K00799.
OMA	ALIHFRI.
OrthoDB	EOG4DJJXQ.
PhylomeDB	P10620.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	P10620.
Bgee	P10620.
CleanEx	HS_MGST1.
Genevestigator	P10620.
GermOnline	ENSG00000008394. Homo sapiens.
Family and domain databases
Gene3D	1.20.120.550. 1 hit.
InterPro	IPR023352. MAPEG-like_dom. IPR001129. Membr-assoc_MAPEG. [Graphical view]
Pfam	PF01124. MAPEG. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1743184.
DrugBank	DB00143. Glutathione.
GenomeRNAi	4257.
NextBio	16787.
SOURCE	Search...

Entry information

Entry name

MGST1_HUMAN

Accession

Primary (citable) accession number: P10620
Secondary accession number(s): A8K533, G5EA53

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 29, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.