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Q03013 (GSTM4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase Mu 4

EC=2.5.1.18
Alternative name(s):
GST class-mu 4
GST-Mu2
GSTM4-4
Gene names
Name:GSTM4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length218 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. Active on 1-chloro-2,4-dinitrobenzene.

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in a wide variety of tissues.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q03013-1)

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: Q03013-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-195: GLEKIS → VSCGIM
     196-218: Missing.
Isoform 3 (identifier: Q03013-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 218217Glutathione S-transferase Mu 4
PRO_0000185824

Regions

Domain2 – 8887GST N-terminal
Domain90 – 208119GST C-terminal
Region7 – 82Glutathione binding By similarity
Region46 – 505Glutathione binding By similarity
Region59 – 602Glutathione binding By similarity
Region72 – 732Glutathione binding By similarity

Sites

Binding site1161Substrate By similarity

Natural variations

Alternative sequence60 – 12061Missing in isoform 3.
VSP_047688
Alternative sequence190 – 1956GLEKIS → VSCGIM in isoform 2.
VSP_011773
Alternative sequence196 – 21823Missing in isoform 2.
VSP_011774
Natural variant21S → P.
Corresponds to variant rs3211190 [ dbSNP | Ensembl ].
VAR_033979
Natural variant1601A → V.
Corresponds to variant rs17838158 [ dbSNP | Ensembl ].
VAR_033980
Natural variant2081L → V.
Corresponds to variant rs2229052 [ dbSNP | Ensembl ].
VAR_049487
Natural variant2091Y → F.
Corresponds to variant rs2229053 [ dbSNP | Ensembl ].
VAR_049488
Natural variant2111R → K.
Corresponds to variant rs2229054 [ dbSNP | Ensembl ].
VAR_049489
Natural variant2121V → M. Ref.2
Corresponds to variant rs1051113 [ dbSNP | Ensembl ].
VAR_049490

Experimental info

Sequence conflict2 – 43SMT → PMI in CAA48637. Ref.2
Sequence conflict171I → M in AAA57346. Ref.1
Sequence conflict371D → G in CAA48637. Ref.2

Secondary structure

............................... 218
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 35E96FA54D566B1E

FASTA21825,561
        10         20         30         40         50         60 
MSMTLGYWDI RGLAHAIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGAHKI TQSNAILCYI ARKHNLCGET EEEKIRVDIL ENQAMDVSNQ LARVCYSPDF 

       130        140        150        160        170        180 
EKLKPEYLEE LPTMMQHFSQ FLGKRPWFVG DKITFVDFLA YDVLDLHRIF EPNCLDAFPN 

       190        200        210 
LKDFISRFEG LEKISAYMKS SRFLPKPLYT RVAVWGNK 

« Hide

Isoform 2 [UniParc].

Checksum: 32F3BEF15BB378D3
Show »

FASTA19522,829
Isoform 3 [UniParc].

Checksum: 095AFD32871D3B4A
Show »

FASTA15718,627

References

« Hide 'large scale' references
[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(1993) [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(1993) [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(1993) [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(2006) [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 (JUN-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. 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).
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. expand/collapse author list , 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].
[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] (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(1991) [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(1994) [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(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS806.1. [Q03013-2]
CCDS807.1. [Q03013-1]
PIRA47486.
S32425.
RefSeqNP_000841.1. NM_000850.4. [Q03013-1]
NP_671489.1. NM_147148.2. [Q03013-2]
UniGeneHs.348387.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GTUX-ray3.30A/B/C/D/E/F/G/H2-218[»]
ProteinModelPortalQ03013.
SMRQ03013. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109203. 12 interactions.
IntActQ03013. 9 interactions.
MINTMINT-1368381.
STRING9606.ENSP00000358851.

Chemistry

ChEMBLCHEMBL2100.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteQ03013.

Polymorphism databases

DMDM1170096.

2D gel databases

REPRODUCTION-2DPAGEIPI00008770.

Proteomic databases

MaxQBQ03013.
PaxDbQ03013.
PRIDEQ03013.

Protocols and materials databases

DNASU2948.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326729; ENSP00000316471; ENSG00000168765. [Q03013-2]
ENST00000336075; ENSP00000336744; ENSG00000168765. [Q03013-3]
ENST00000369836; ENSP00000358851; ENSG00000168765. [Q03013-1]
GeneID2948.
KEGGhsa:2948.
UCSCuc001dyf.3. human. [Q03013-1]
uc001dyh.2. human. [Q03013-2]

Organism-specific databases

CTD2948.
GeneCardsGC01P110198.
HGNCHGNC:4636. GSTM4.
MIM138333. gene.
neXtProtNX_Q03013.
PharmGKBPA29026.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300089.
HOGENOMHOG000115735.
HOVERGENHBG106842.
InParanoidQ03013.
KOK00799.
OMALFACNIL.
OrthoDBEOG7KH9M3.
PhylomeDBQ03013.
TreeFamTF353040.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKQ03013.

Gene expression databases

ArrayExpressQ03013.
BgeeQ03013.
CleanExHS_GSTM4.
GenevestigatorQ03013.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01267. GSTRNSFRASEM.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ03013.
GeneWikiGSTM4.
GenomeRNAi2948.
NextBio11682.
PROQ03013.
SOURCESearch...

Entry information

Entry nameGSTM4_HUMAN
AccessionPrimary (citable) accession number: Q03013
Secondary accession number(s): A8K765 expand/collapse secondary AC list , Q05465, Q32NC1, Q4JNT8, Q6FH87
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 149 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM