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Protein

Glutathione S-transferase Mu 2

Gene

GSTM2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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
Sitei210 – 2101Important for substrate specificity

GO - Molecular functioni

  1. enzyme binding Source: BHF-UCL
  2. glutathione binding Source: BHF-UCL
  3. glutathione transferase activity Source: UniProtKB
  4. protein homodimerization activity Source: BHF-UCL
  5. receptor binding Source: BHF-UCL

GO - Biological processi

  1. cellular detoxification of nitrogen compound Source: BHF-UCL
  2. cellular response to caffeine Source: BHF-UCL
  3. glutathione derivative biosynthetic process Source: Reactome
  4. glutathione metabolic process Source: UniProtKB
  5. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  6. nitrobenzene metabolic process Source: BHF-UCL
  7. positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  8. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  9. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  10. regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion Source: BHF-UCL
  11. relaxation of cardiac muscle Source: BHF-UCL
  12. small molecule metabolic process Source: Reactome
  13. xenobiotic catabolic process Source: UniProtKB
  14. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 2681.
ReactomeiREACT_6926. Glutathione conjugation.
SABIO-RKP28161.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 2 (EC:2.5.1.18)
Alternative name(s):
GST class-mu 2
GSTM2-2
Gene namesi
Name:GSTM2
Synonyms:GST4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4634. GSTM2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. sarcoplasmic reticulum Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi210 – 2101T → C, F, H, I, K, L, R, Y or W: Reduced enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA29023.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 218217Glutathione S-transferase Mu 2PRO_0000185818Add
BLAST

Proteomic databases

MaxQBiP28161.
PaxDbiP28161.
PRIDEiP28161.

2D gel databases

OGPiP28161.
REPRODUCTION-2DPAGEP28161.

PTM databases

PhosphoSiteiP28161.

Expressioni

Tissue specificityi

Muscle.

Gene expression databases

BgeeiP28161.
CleanExiHS_GSTM2.
ExpressionAtlasiP28161. baseline and differential.
GenevestigatoriP28161.

Organism-specific databases

HPAiCAB040547.
HPA055972.
HPA055973.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi109201. 6 interactions.
DIPiDIP-129N.
STRINGi9606.ENSP00000241337.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Helixi12 – 143Combined sources
Helixi15 – 239Combined sources
Beta strandi28 – 336Combined sources
Turni38 – 414Combined sources
Helixi44 – 474Combined sources
Turni48 – 514Combined sources
Beta strandi60 – 656Combined sources
Beta strandi68 – 725Combined sources
Helixi73 – 8311Combined sources
Helixi91 – 11626Combined sources
Helixi120 – 14223Combined sources
Beta strandi150 – 1523Combined sources
Helixi155 – 17016Combined sources
Turni172 – 1776Combined sources
Helixi179 – 19012Combined sources
Helixi192 – 1998Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi205 – 2073Combined sources
Turni208 – 2125Combined sources
Beta strandi214 – 2163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HNAX-ray1.85A2-218[»]
1HNBX-ray3.50A/B2-218[»]
1HNCX-ray3.00A/B/C/D2-218[»]
1XW5X-ray1.80A/B2-218[»]
1YKCX-ray2.10A/B2-218[»]
2AB6X-ray2.50A/B/C/D2-218[»]
2C4JX-ray1.35A/B/C/D2-218[»]
2GTUX-ray2.55A/B2-218[»]
3GTUX-ray2.80A/C2-218[»]
3GURX-ray2.50A/B/C/D2-218[»]
ProteinModelPortaliP28161.
SMRiP28161. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28161.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8887GST N-terminalAdd
BLAST
Domaini90 – 208119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Glutathione binding
Regioni46 – 505Glutathione binding
Regioni59 – 602Glutathione binding
Regioni72 – 732Glutathione binding

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.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP28161.
KOiK00799.
OMAiMAIWGSK.
PhylomeDBiP28161.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P28161-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK
60 70 80 90 100
FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL
110 120 130 140 150
ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG
160 170 180 190 200
DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS
210
SRFLPRPVFT KMAVWGNK
Length:218
Mass (Da):25,745
Last modified:January 23, 2007 - v2
Checksum:i15203709D4A63789
GO
Isoform 2 (identifier: P28161-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     190-218: GLEKISAYMKSSRFLPRPVFTKMAVWGNK → HS

Note: No experimental confirmation available.

Show »
Length:191
Mass (Da):22,644
Checksum:i9267243C014F878F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21P → S in AAV38750 (Ref. 3) Curated
Sequence conflicti9 – 91N → D in AAV38750 (Ref. 3) Curated
Sequence conflicti51 – 511F → L in BAG61446 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti173 – 1731S → N.
Corresponds to variant rs2229050 [ dbSNP | Ensembl ].
VAR_049486

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei190 – 21829GLEKI…VWGNK → HS in isoform 2. CuratedVSP_045614Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63509 mRNA. Translation: AAA60963.1.
AK299482 mRNA. Translation: BAG61446.1.
BT019947 mRNA. Translation: AAV38750.1.
AC000031 Genomic DNA. No translation available.
AC000032 Genomic DNA. No translation available.
BC105038 mRNA. Translation: AAI05039.1.
BC105066 mRNA. Translation: AAI05067.1.
CCDSiCCDS44192.1. [P28161-2]
CCDS808.1. [P28161-1]
PIRiA39375.
RefSeqiNP_000839.1. NM_000848.3. [P28161-1]
NP_001135840.1. NM_001142368.1. [P28161-2]
UniGeneiHs.279837.

Genome annotation databases

EnsembliENST00000241337; ENSP00000241337; ENSG00000213366. [P28161-1]
ENST00000442650; ENSP00000416883; ENSG00000213366. [P28161-2]
ENST00000460717; ENSP00000435910; ENSG00000213366. [P28161-2]
GeneIDi2946.
KEGGihsa:2946.
UCSCiuc001dyi.3. human. [P28161-1]
uc010ovt.2. human.

Polymorphism databases

DMDMi232204.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63509 mRNA. Translation: AAA60963.1.
AK299482 mRNA. Translation: BAG61446.1.
BT019947 mRNA. Translation: AAV38750.1.
AC000031 Genomic DNA. No translation available.
AC000032 Genomic DNA. No translation available.
BC105038 mRNA. Translation: AAI05039.1.
BC105066 mRNA. Translation: AAI05067.1.
CCDSiCCDS44192.1. [P28161-2]
CCDS808.1. [P28161-1]
PIRiA39375.
RefSeqiNP_000839.1. NM_000848.3. [P28161-1]
NP_001135840.1. NM_001142368.1. [P28161-2]
UniGeneiHs.279837.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HNAX-ray1.85A2-218[»]
1HNBX-ray3.50A/B2-218[»]
1HNCX-ray3.00A/B/C/D2-218[»]
1XW5X-ray1.80A/B2-218[»]
1YKCX-ray2.10A/B2-218[»]
2AB6X-ray2.50A/B/C/D2-218[»]
2C4JX-ray1.35A/B/C/D2-218[»]
2GTUX-ray2.55A/B2-218[»]
3GTUX-ray2.80A/C2-218[»]
3GURX-ray2.50A/B/C/D2-218[»]
ProteinModelPortaliP28161.
SMRiP28161. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109201. 6 interactions.
DIPiDIP-129N.
STRINGi9606.ENSP00000241337.

Chemistry

BindingDBiP28161.
ChEMBLiCHEMBL4589.
DrugBankiDB00143. Glutathione.

PTM databases

PhosphoSiteiP28161.

Polymorphism databases

DMDMi232204.

2D gel databases

OGPiP28161.
REPRODUCTION-2DPAGEP28161.

Proteomic databases

MaxQBiP28161.
PaxDbiP28161.
PRIDEiP28161.

Protocols and materials databases

DNASUi2946.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000241337; ENSP00000241337; ENSG00000213366. [P28161-1]
ENST00000442650; ENSP00000416883; ENSG00000213366. [P28161-2]
ENST00000460717; ENSP00000435910; ENSG00000213366. [P28161-2]
GeneIDi2946.
KEGGihsa:2946.
UCSCiuc001dyi.3. human. [P28161-1]
uc010ovt.2. human.

Organism-specific databases

CTDi2946.
GeneCardsiGC01P110210.
HGNCiHGNC:4634. GSTM2.
HPAiCAB040547.
HPA055972.
HPA055973.
MIMi138380. gene.
neXtProtiNX_P28161.
PharmGKBiPA29023.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP28161.
KOiK00799.
OMAiMAIWGSK.
PhylomeDBiP28161.
TreeFamiTF353040.

Enzyme and pathway databases

BRENDAi2.5.1.18. 2681.
ReactomeiREACT_6926. Glutathione conjugation.
SABIO-RKP28161.

Miscellaneous databases

ChiTaRSiGSTM2. human.
EvolutionaryTraceiP28161.
GeneWikiiGSTM2.
GenomeRNAii2946.
NextBioi11674.
PROiP28161.
SOURCEiSearch...

Gene expression databases

BgeeiP28161.
CleanExiHS_GSTM2.
ExpressionAtlasiP28161. baseline and differential.
GenevestigatoriP28161.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus."
    Vorachek W.R., Pearson W.R., Rule G.S.
    Proc. Natl. Acad. Sci. U.S.A. 88:4443-4447(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Muscle.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "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 (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. "Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript."
    Ross V.L., Board P.G.
    Biochem. J. 294:373-380(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
    Tissue: Testis.
  7. Lubec G., Vishwanath V.
    Submitted (FEB-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 53-69 AND 153-182, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity."
    Raghunathan S., Chandross R.J., Kretsinger R.H., Allison T.J., Penington C.J., Rule G.S.
    J. Mol. Biol. 238:815-832(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.
  10. "Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution."
    Norrgard M.A., Ivarsson Y., Tars K., Mannervik B.
    Proc. Natl. Acad. Sci. U.S.A. 103:4876-4881(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, MUTAGENESIS OF THR-210, CATALYTIC ACTIVITY.
  11. "Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases."
    Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F., Federici G., Caccuri A.M.
    Cancer Res. 69:8025-8034(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NBDHEX.

Entry informationi

Entry nameiGSTM2_HUMAN
AccessioniPrimary (citable) accession number: P28161
Secondary accession number(s): B4DRY4
, E9PEM9, Q2M318, Q5TZY5, Q8WWE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 158 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.