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P10620 (MGST1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length155 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentEndoplasmic reticulum
Membrane
Microsome
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionTransferase
   PTMAcetylation
Nitration
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processLeydig cell differentiation

Inferred from electronic annotation. Source: Ensembl

cellular response to lipid hydroperoxide

Inferred from direct assay PubMed 20727966. Source: UniProtKB

glutathione derivative biosynthetic process

Traceable author statement. Source: Reactome

glutathione metabolic process

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Inferred from direct assay PubMed 20727966. Source: UniProtKB

protein homotrimerization

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentapical part of cell

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

peroxisomal membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionglutathione binding

Inferred from electronic annotation. Source: Ensembl

glutathione peroxidase activity

Inferred from direct assay PubMed 20727966. Source: UniProtKB

glutathione transferase activity

Inferred from direct assay PubMed 20727966. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20195357. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NELFBQ8WX922EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 155154Microsomal glutathione S-transferase 1
PRO_0000217736

Regions

Topological domain3 – 97Lumenal By similarity
Transmembrane10 – 3324Helical; By similarity
Topological domain34 – 6229Cytoplasmic By similarity
Transmembrane63 – 9634Helical; By similarity
Topological domain97 – 993Lumenal By similarity
Transmembrane100 – 12324Helical; By similarity
Topological domain124 – 1285Cytoplasmic By similarity
Transmembrane129 – 14820Helical; By similarity
Topological domain149 – 1557Lumenal By similarity

Sites

Binding site381Glutathione By similarity
Binding site731Glutathione By similarity
Binding site741Glutathione By similarity
Binding site761Glutathione By similarity
Binding site811Glutathione By similarity
Binding site1211Glutathione By similarity
Site501Activates the enzyme when modified By similarity

Amino acid modifications

Modified residue421N6-acetyllysine By similarity
Modified residue551N6-acetyllysine By similarity
Modified residue601N6-acetyllysine By similarity

Natural variations

Alternative sequence75 – 15581AHLND…SKLYL → IKQTLSIYLASSI in isoform 2.
VSP_046160

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 892A529C97E3C853

FASTA15517,599
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 8F4C9AF76F18EF97
Show »

FASTA879,984

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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

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.
CCDSCCDS58209.1. [P10620-2]
CCDS8677.1. [P10620-1]
PIRB28083.
RefSeqNP_001247440.1. NM_001260511.1. [P10620-1]
NP_001247441.1. NM_001260512.1.
NP_001254527.1. NM_001267598.1. [P10620-2]
NP_064696.1. NM_020300.4. [P10620-1]
NP_665707.1. NM_145764.2. [P10620-1]
NP_665734.1. NM_145791.2. [P10620-1]
NP_665735.1. NM_145792.2. [P10620-1]
UniGeneHs.389700.

3D structure databases

ProteinModelPortalP10620.
SMRP10620. Positions 10-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110413. 2 interactions.
IntActP10620. 2 interactions.
STRING9606.ENSP00000010404.

Chemistry

ChEMBLCHEMBL1743184.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteP10620.

Polymorphism databases

DMDM121740.

Proteomic databases

MaxQBP10620.
PaxDbP10620.
PRIDEP10620.

Protocols and materials databases

DNASU4257.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000010404; ENSP00000010404; ENSG00000008394. [P10620-1]
ENST00000396207; ENSP00000379510; ENSG00000008394. [P10620-1]
ENST00000396209; ENSP00000379512; ENSG00000008394. [P10620-1]
ENST00000396210; ENSP00000379513; ENSG00000008394. [P10620-1]
ENST00000535309; ENSP00000438308; ENSG00000008394. [P10620-2]
GeneID4257.
KEGGhsa:4257.
UCSCuc001rdf.3. human. [P10620-1]
uc031qgm.1. human.

Organism-specific databases

CTD4257.
GeneCardsGC12P016500.
HGNCHGNC:7061. MGST1.
HPAHPA044840.
MIM138330. gene.
neXtProtNX_P10620.
PharmGKBPA30791.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG71159.
HOGENOMHOG000231759.
HOVERGENHBG052470.
InParanoidP10620.
KOK00799.
OMALIHFRIF.
PhylomeDBP10620.
TreeFamTF105327.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP10620.
BgeeP10620.
CleanExHS_MGST1.
GenevestigatorP10620.

Family and domain databases

Gene3D1.20.120.550. 1 hit.
InterProIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamPF01124. MAPEG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMicrosomal_glutathione_S-transferase_1.
GenomeRNAi4257.
NextBio16787.
PROP10620.
SOURCESearch...

Entry information

Entry nameMGST1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM