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Protein

Glutathione S-transferase Mu 4

Gene

GSTM4

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. Active on 1-chloro-2,4-dinitrobenzene.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. glutathione derivative biosynthetic process Source: Reactome
  2. glutathione metabolic process Source: BHF-UCL
  3. nitrobenzene metabolic process Source: Ensembl
  4. small molecule metabolic process Source: Reactome
  5. xenobiotic catabolic process Source: BHF-UCL
  6. 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-RKQ03013.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 4 (EC:2.5.1.18)
Alternative name(s):
GST class-mu 4
GST-Mu2
GSTM4-4
Gene namesi
Name:GSTM4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4636. GSTM4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29026.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 218217Glutathione S-transferase Mu 4PRO_0000185824Add
BLAST

Proteomic databases

MaxQBiQ03013.
PaxDbiQ03013.
PRIDEiQ03013.

2D gel databases

REPRODUCTION-2DPAGEIPI00008770.

PTM databases

PhosphoSiteiQ03013.

Expressioni

Tissue specificityi

Expressed in a wide variety of tissues.

Gene expression databases

BgeeiQ03013.
CleanExiHS_GSTM4.
ExpressionAtlasiQ03013. baseline and differential.
GenevestigatoriQ03013.

Organism-specific databases

HPAiHPA055972.
HPA055973.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi109203. 15 interactions.
IntActiQ03013. 9 interactions.
MINTiMINT-1368381.
STRINGi9606.ENSP00000358851.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi14 – 2310Combined sources
Beta strandi28 – 336Combined sources
Turni38 – 414Combined sources
Helixi44 – 507Combined sources
Helixi51 – 533Combined sources
Beta strandi60 – 645Combined sources
Beta strandi69 – 724Combined sources
Helixi73 – 8311Combined sources
Helixi91 – 11424Combined sources
Helixi120 – 14223Combined sources
Beta strandi150 – 1523Combined sources
Helixi155 – 17016Combined sources
Helixi179 – 19012Combined sources
Helixi192 – 1987Combined sources
Turni214 – 2163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GTUX-ray3.30A/B/C/D/E/F/G/H2-218[»]
ProteinModelPortaliQ03013.
SMRiQ03013. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03013.

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 bindingBy similarity
Regioni46 – 505Glutathione bindingBy similarity
Regioni59 – 602Glutathione bindingBy similarity
Regioni72 – 732Glutathione bindingBy similarity

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.
InParanoidiQ03013.
KOiK00799.
OMAiTKIAVWG.
OrthoDBiEOG7KH9M3.
PhylomeDBiQ03013.
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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q03013-1) [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
MSMTLGYWDI RGLAHAIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK
60 70 80 90 100
FKLGLDFPNL PYLIDGAHKI TQSNAILCYI ARKHNLCGET EEEKIRVDIL
110 120 130 140 150
ENQAMDVSNQ LARVCYSPDF EKLKPEYLEE LPTMMQHFSQ FLGKRPWFVG
160 170 180 190 200
DKITFVDFLA YDVLDLHRIF EPNCLDAFPN LKDFISRFEG LEKISAYMKS
210
SRFLPKPLYT RVAVWGNK
Length:218
Mass (Da):25,561
Last modified:January 23, 2007 - v3
Checksum:i35E96FA54D566B1E
GO
Isoform 2 (identifier: Q03013-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     190-195: GLEKIS → VSCGIM
     196-218: Missing.

Show »
Length:195
Mass (Da):22,829
Checksum:i32F3BEF15BB378D3
GO
Isoform 3 (identifier: Q03013-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     60-120: Missing.

Show »
Length:157
Mass (Da):18,627
Checksum:i095AFD32871D3B4A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 43SMT → PMI in CAA48637 (PubMed:8471052).Curated
Sequence conflicti17 – 171I → M in AAA57346 (PubMed:8349586).Curated
Sequence conflicti37 – 371D → G in CAA48637 (PubMed:8471052).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21S → P.
Corresponds to variant rs3211190 [ dbSNP | Ensembl ].
VAR_033979
Natural varianti160 – 1601A → V.
Corresponds to variant rs17838158 [ dbSNP | Ensembl ].
VAR_033980
Natural varianti208 – 2081L → V.
Corresponds to variant rs2229052 [ dbSNP | Ensembl ].
VAR_049487
Natural varianti209 – 2091Y → F.
Corresponds to variant rs2229053 [ dbSNP | Ensembl ].
VAR_049488
Natural varianti211 – 2111R → K.
Corresponds to variant rs2229054 [ dbSNP | Ensembl ].
VAR_049489
Natural varianti212 – 2121V → M.1 Publication
Corresponds to variant rs1051113 [ dbSNP | Ensembl ].
VAR_049490

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei60 – 12061Missing in isoform 3. 1 PublicationVSP_047688Add
BLAST
Alternative sequencei190 – 1956GLEKIS → VSCGIM in isoform 2. 1 PublicationVSP_011773
Alternative sequencei196 – 21823Missing in isoform 2. 1 PublicationVSP_011774Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96234 mRNA. Translation: AAA57347.1.
M96233 Genomic DNA. Translation: AAA57346.1.
X68677 Genomic DNA. Translation: CAA48637.1.
M99422 mRNA. Translation: AAA58623.1.
DQ062813 mRNA. Translation: AAY98515.1.
CR541869 mRNA. Translation: CAG46667.1.
AK291880 mRNA. Translation: BAF84569.1.
AC000031 Genomic DNA. No translation available.
CH471122 Genomic DNA. Translation: EAW56405.1.
BC015513 mRNA. Translation: AAH15513.1.
BC108729 mRNA. Translation: AAI08730.1.
X56837 Genomic DNA. Translation: CAA40167.1.
CCDSiCCDS806.1. [Q03013-2]
CCDS807.1. [Q03013-1]
PIRiA47486.
S32425.
RefSeqiNP_000841.1. NM_000850.4. [Q03013-1]
NP_671489.1. NM_147148.2. [Q03013-2]
UniGeneiHs.348387.

Genome annotation databases

EnsembliENST00000326729; ENSP00000316471; ENSG00000168765. [Q03013-2]
ENST00000369836; ENSP00000358851; ENSG00000168765. [Q03013-1]
GeneIDi2948.
KEGGihsa:2948.
UCSCiuc001dyf.3. human. [Q03013-1]
uc001dyh.2. human. [Q03013-2]
uc009wfj.3. human.

Polymorphism databases

DMDMi1170096.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96234 mRNA. Translation: AAA57347.1.
M96233 Genomic DNA. Translation: AAA57346.1.
X68677 Genomic DNA. Translation: CAA48637.1.
M99422 mRNA. Translation: AAA58623.1.
DQ062813 mRNA. Translation: AAY98515.1.
CR541869 mRNA. Translation: CAG46667.1.
AK291880 mRNA. Translation: BAF84569.1.
AC000031 Genomic DNA. No translation available.
CH471122 Genomic DNA. Translation: EAW56405.1.
BC015513 mRNA. Translation: AAH15513.1.
BC108729 mRNA. Translation: AAI08730.1.
X56837 Genomic DNA. Translation: CAA40167.1.
CCDSiCCDS806.1. [Q03013-2]
CCDS807.1. [Q03013-1]
PIRiA47486.
S32425.
RefSeqiNP_000841.1. NM_000850.4. [Q03013-1]
NP_671489.1. NM_147148.2. [Q03013-2]
UniGeneiHs.348387.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GTUX-ray3.30A/B/C/D/E/F/G/H2-218[»]
ProteinModelPortaliQ03013.
SMRiQ03013. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109203. 15 interactions.
IntActiQ03013. 9 interactions.
MINTiMINT-1368381.
STRINGi9606.ENSP00000358851.

Chemistry

ChEMBLiCHEMBL2100.
DrugBankiDB00143. Glutathione.

PTM databases

PhosphoSiteiQ03013.

Polymorphism databases

DMDMi1170096.

2D gel databases

REPRODUCTION-2DPAGEIPI00008770.

Proteomic databases

MaxQBiQ03013.
PaxDbiQ03013.
PRIDEiQ03013.

Protocols and materials databases

DNASUi2948.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326729; ENSP00000316471; ENSG00000168765. [Q03013-2]
ENST00000369836; ENSP00000358851; ENSG00000168765. [Q03013-1]
GeneIDi2948.
KEGGihsa:2948.
UCSCiuc001dyf.3. human. [Q03013-1]
uc001dyh.2. human. [Q03013-2]
uc009wfj.3. human.

Organism-specific databases

CTDi2948.
GeneCardsiGC01P110198.
HGNCiHGNC:4636. GSTM4.
HPAiHPA055972.
HPA055973.
MIMi138333. gene.
neXtProtiNX_Q03013.
PharmGKBiPA29026.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiQ03013.
KOiK00799.
OMAiTKIAVWG.
OrthoDBiEOG7KH9M3.
PhylomeDBiQ03013.
TreeFamiTF353040.

Enzyme and pathway databases

BRENDAi2.5.1.18. 2681.
ReactomeiREACT_6926. Glutathione conjugation.
SABIO-RKQ03013.

Miscellaneous databases

ChiTaRSiGSTM4. human.
EvolutionaryTraceiQ03013.
GeneWikiiGSTM4.
GenomeRNAii2948.
NextBioi11682.
PROiQ03013.
SOURCEiSearch...

Gene expression databases

BgeeiQ03013.
CleanExiHS_GSTM4.
ExpressionAtlasiQ03013. baseline and differential.
GenevestigatoriQ03013.

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. "Isolation and analysis of the gene and cDNA for a human Mu class glutathione S-transferase, GSTM4."
    Comstock K.E., Johnson K.J., Rifenbery D., Henner W.D.
    J. Biol. Chem. 268:16958-16965(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  2. "Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4."
    Zhong S., Spurr N.K., Hayes J.D., Wolf C.R.
    Biochem. J. 291:41-50(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-212.
  3. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS.
    Tissue: Testis.
  4. "Screening for inter-individual splicing differences in human GSTM4 and the discovery of a single nucleotide substitution related to the tandem skipping of two exons."
    Denson J., Xi Z., Wu Y., Yang W., Neale G., Zhang J.
    Gene 379:148-155(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  7. "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].
  8. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye and Lung.
  10. "Structure of human glutathione S-transferase class Mu genes."
    Taylor J.B., Oliver J., Sherrington R., Pemble S.E.
    Biochem. J. 274:587-593(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-160.
    Tissue: Lymphocyte.
  11. "A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes."
    Comstock K.E., Widersten M., Hao X.Y., Henner W.D., Mannervik B.
    Arch. Biochem. Biophys. 311:487-495(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  12. "An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases."
    Patskovsky Y.V., Patskovska L.N., Listowsky I.
    Biochemistry 38:16187-16194(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).

Entry informationi

Entry nameiGSTM4_HUMAN
AccessioniPrimary (citable) accession number: Q03013
Secondary accession number(s): A8K765
, Q05465, Q32NC1, Q4JNT8, Q6FH87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 156 of the entry and version 3 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.