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P28161

- GSTM2_HUMAN

UniProt

P28161 - GSTM2_HUMAN

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Protein
Glutathione S-transferase Mu 2
Gene
GSTM2, GST4
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 1161Substrate By 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
Complete GO annotation...

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

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: 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: UniProt
  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 – 11Removed By similarity
Chaini2 – 218217Glutathione S-transferase Mu 2
PRO_0000185818Add
BLAST

Proteomic databases

MaxQBiP28161.
PaxDbiP28161.
PRIDEiP28161.

2D gel databases

OGPiP28161.
REPRODUCTION-2DPAGEP28161.

PTM databases

PhosphoSiteiP28161.

Expressioni

Tissue specificityi

Muscle.

Gene expression databases

ArrayExpressiP28161.
BgeeiP28161.
CleanExiHS_GSTM2.
GenevestigatoriP28161.

Organism-specific databases

HPAiCAB040547.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109201. 3 interactions.
DIPiDIP-129N.
STRINGi9606.ENSP00000241337.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP28161.

Family & Domainsi

Domains and Repeats

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

Phylogenomic databases

eggNOGiNOG300089.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
KOiK00799.
OMAiWASGMAF.
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. Align

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

MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK    50
FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL 100
ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG 150
DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS 200
SRFLPRPVFT KMAVWGNK 218
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

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.
VSP_045614Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21P → S in AAV38750. 1 Publication
Sequence conflicti9 – 91N → D in AAV38750. 1 Publication
Sequence conflicti51 – 511F → L in BAG61446. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS44192.1. [P28161-2 ]
CCDS808.1. [P28161-1 ]
PIRi A39375.
RefSeqi NP_000839.1. NM_000848.3. [P28161-1 ]
NP_001135840.1. NM_001142368.1. [P28161-2 ]
UniGenei Hs.279837.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HNA X-ray 1.85 A 2-218 [» ]
1HNB X-ray 3.50 A/B 2-218 [» ]
1HNC X-ray 3.00 A/B/C/D 2-218 [» ]
1XW5 X-ray 1.80 A/B 2-218 [» ]
1YKC X-ray 2.10 A/B 2-218 [» ]
2AB6 X-ray 2.50 A/B/C/D 2-218 [» ]
2C4J X-ray 1.35 A/B/C/D 2-218 [» ]
2GTU X-ray 2.55 A/B 2-218 [» ]
3GTU X-ray 2.80 A/C 2-218 [» ]
3GUR X-ray 2.50 A/B/C/D 2-218 [» ]
ProteinModelPortali P28161.
SMRi P28161. Positions 2-218.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109201. 3 interactions.
DIPi DIP-129N.
STRINGi 9606.ENSP00000241337.

Chemistry

BindingDBi P28161.
ChEMBLi CHEMBL4589.
DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei P28161.

Polymorphism databases

DMDMi 232204.

2D gel databases

OGPi P28161.
REPRODUCTION-2DPAGE P28161.

Proteomic databases

MaxQBi P28161.
PaxDbi P28161.
PRIDEi P28161.

Protocols and materials databases

DNASUi 2946.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000241337 ; ENSP00000241337 ; ENSG00000213366 . [P28161-1 ]
ENST00000442650 ; ENSP00000416883 ; ENSG00000213366 . [P28161-2 ]
ENST00000460717 ; ENSP00000435910 ; ENSG00000213366 . [P28161-2 ]
GeneIDi 2946.
KEGGi hsa:2946.
UCSCi uc001dyi.3. human. [P28161-1 ]
uc010ovt.2. human.

Organism-specific databases

CTDi 2946.
GeneCardsi GC01P110210.
HGNCi HGNC:4634. GSTM2.
HPAi CAB040547.
MIMi 138380. gene.
neXtProti NX_P28161.
PharmGKBi PA29023.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300089.
HOGENOMi HOG000115735.
HOVERGENi HBG106842.
KOi K00799.
OMAi WASGMAF.
PhylomeDBi P28161.
TreeFami TF353040.

Enzyme and pathway databases

Reactomei REACT_6926. Glutathione conjugation.
SABIO-RK P28161.

Miscellaneous databases

ChiTaRSi GSTM2. human.
EvolutionaryTracei P28161.
GeneWikii GSTM2.
GenomeRNAii 2946.
NextBioi 11674.
PROi P28161.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28161.
Bgeei P28161.
CleanExi HS_GSTM2.
Genevestigatori P28161.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01267. GSTRNSFRASEM.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1991) [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(2004) [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 (OCT-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(2006) [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(2004) [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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
    Tissue: Testis.
  7. Lubec G., Vishwanath V.
    Submitted (MAR-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(1994) [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(2006) [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(2009) [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: September 3, 2014
This is version 151 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

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