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Q9DCM2 (GSTK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase kappa 1

EC=2.5.1.18
Alternative name(s):
GST 13-13
GST class-kappa
GSTK1-1
Short name=mGSTK1
Glutathione S-transferase subunit 13
Gene names
Name:Gstk1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion Ref.1.

Tissue specificity

Predominantly expressed in heart, kidney, liver and skeletal muscle. Ref.1

Post-translational modification

Acetylation of Lys-93 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the GST superfamily. Kappa family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 226225Glutathione S-transferase kappa 1
PRO_0000185892

Regions

Region16 – 183Glutathione binding By similarity
Region200 – 2012Glutathione binding By similarity

Sites

Binding site531Glutathione By similarity
Binding site1831Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue361N6-succinyllysine Ref.5
Modified residue491N6-succinyllysine Ref.5
Modified residue681N6-acetyllysine; alternate Ref.6
Modified residue681N6-succinyllysine; alternate Ref.5
Modified residue741N6-acetyllysine; alternate Ref.6
Modified residue741N6-succinyllysine; alternate Ref.5
Modified residue851N6-acetyllysine Ref.6
Modified residue931N6-acetyllysine; alternate Ref.6
Modified residue931N6-succinyllysine; alternate Ref.5
Modified residue1161N6-acetyllysine; alternate Ref.6
Modified residue1161N6-succinyllysine; alternate Ref.5
Modified residue1441N6-succinyllysine Ref.5
Modified residue1581N6-acetyllysine; alternate Ref.6
Modified residue1581N6-succinyllysine; alternate Ref.5
Modified residue1651N6-acetyllysine Ref.6
Modified residue1671N6-acetyllysine; alternate Ref.6
Modified residue1671N6-succinyllysine; alternate Ref.5
Modified residue1771N6-acetyllysine; alternate Ref.6
Modified residue1771N6-succinyllysine; alternate Ref.5
Modified residue1931N6-succinyllysine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9DCM2 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 480332FD618ABCDD

FASTA22625,704
        10         20         30         40         50         60 
MGPAPRILEL FYDVLSPYSW LGFEVLCRYQ HLWNIKLQLR PTLIAGIMKD SGNQPPAMVP 

        70         80         90        100        110        120 
RKGQYIFKEI PLLKQFFQVP LNIPKDFFGE TVKKGSINAM RFLTTVSMEQ PEMLEKVSRE 

       130        140        150        160        170        180 
IWMRVWSRDE DITEYQSILA AAVKAGMSTA QAQHFLEKIS TQQVKNKLIE NTDAACKYGA 

       190        200        210        220 
FGLPTTVAHV DGKTYMLFGS DRLELLAYLL GEKWMGPVPP TANARL 

« Hide

References

« Hide 'large scale' references
[1]"Biochemical and genetic characterization of a murine class Kappa glutathione S-transferase."
Jowsey I.R., Thomson R.E., Orton T.C., Elcombe C.R., Hayes J.D.
Biochem. J. 373:559-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: FVB/N.
Tissue: Kidney.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[3]"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].
Strain: FVB/N.
Tissue: Liver.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 203-213, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-49; LYS-68; LYS-74; LYS-93; LYS-116; LYS-144; LYS-158; LYS-167; LYS-177 AND LYS-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-74; LYS-85; LYS-93; LYS-116; LYS-158; LYS-165; LYS-167 AND LYS-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002661 mRNA. Translation: BAB22268.1.
AY279096 mRNA. Translation: AAP20655.1.
BC058163 mRNA. Translation: AAH58163.1.
CCDSCCDS20063.1.
RefSeqNP_083831.1. NM_029555.2.
UniGeneMm.267014.

3D structure databases

ProteinModelPortalQ9DCM2.
SMRQ9DCM2. Positions 2-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48623N.
IntActQ9DCM2. 2 interactions.
MINTMINT-1860526.
STRING10090.ENSMUSP00000031897.

PTM databases

PhosphoSiteQ9DCM2.

Proteomic databases

MaxQBQ9DCM2.
PaxDbQ9DCM2.
PRIDEQ9DCM2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031897; ENSMUSP00000031897; ENSMUSG00000029864.
GeneID76263.
KEGGmmu:76263.
UCSCuc009bqo.1. mouse.

Organism-specific databases

CTD373156.
MGIMGI:1923513. Gstk1.

Phylogenomic databases

eggNOGCOG3917.
GeneTreeENSGT00440000033697.
HOGENOMHOG000219769.
HOVERGENHBG051852.
InParanoidQ9DCM2.
KOK13299.
OMAELWRRIW.
OrthoDBEOG793B9B.
PhylomeDBQ9DCM2.
TreeFamTF105323.

Gene expression databases

BgeeQ9DCM2.
CleanExMM_GSTK1.
GenevestigatorQ9DCM2.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR001853. DSBA-like_thioredoxin_dom.
IPR014440. HCCAis_GSTk.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF01323. DSBA. 1 hit.
[Graphical view]
PIRSFPIRSF006386. HCCAis_GSTk. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
ProtoNetSearch...

Other

NextBio344879.
PROQ9DCM2.
SOURCESearch...

Entry information

Entry nameGSTK1_MOUSE
AccessionPrimary (citable) accession number: Q9DCM2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot