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Protein

Glutathione S-transferase kappa 1

Gene

Gstk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531GlutathioneBy similarity
Binding sitei183 – 1831Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

  • glutathione peroxidase activity Source: MGI
  • glutathione transferase activity Source: MGI
  • protein disulfide oxidoreductase activity Source: InterPro
  • receptor binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Gstk1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1923513. Gstk1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 226225Glutathione S-transferase kappa 1PRO_0000185892Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6-succinyllysine1 Publication
Modified residuei49 – 491N6-succinyllysine1 Publication
Modified residuei68 – 681N6-acetyllysine; alternate1 Publication
Modified residuei68 – 681N6-succinyllysine; alternate1 Publication
Modified residuei74 – 741N6-acetyllysine; alternate1 Publication
Modified residuei74 – 741N6-succinyllysine; alternate1 Publication
Modified residuei85 – 851N6-acetyllysine1 Publication
Modified residuei93 – 931N6-acetyllysine; alternate1 Publication
Modified residuei93 – 931N6-succinyllysine; alternate1 Publication
Modified residuei116 – 1161N6-acetyllysine; alternate1 Publication
Modified residuei116 – 1161N6-succinyllysine; alternate1 Publication
Modified residuei144 – 1441N6-succinyllysine1 Publication
Modified residuei158 – 1581N6-acetyllysine; alternate1 Publication
Modified residuei158 – 1581N6-succinyllysine; alternate1 Publication
Modified residuei165 – 1651N6-acetyllysine1 Publication
Modified residuei167 – 1671N6-acetyllysine; alternate1 Publication
Modified residuei167 – 1671N6-succinyllysine; alternate1 Publication
Modified residuei177 – 1771N6-acetyllysine; alternate1 Publication
Modified residuei177 – 1771N6-succinyllysine; alternate1 Publication
Modified residuei193 – 1931N6-succinyllysine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9DCM2.
PaxDbiQ9DCM2.
PRIDEiQ9DCM2.

PTM databases

PhosphoSiteiQ9DCM2.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9DCM2.
CleanExiMM_GSTK1.
GenevestigatoriQ9DCM2.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

DIPiDIP-48623N.
IntActiQ9DCM2. 2 interactions.
MINTiMINT-1860526.
STRINGi10090.ENSMUSP00000031897.

Structurei

3D structure databases

ProteinModelPortaliQ9DCM2.
SMRiQ9DCM2. Positions 2-221.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 183Glutathione bindingBy similarity
Regioni200 – 2012Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Kappa family.Curated

Phylogenomic databases

eggNOGiCOG3917.
GeneTreeiENSGT00440000033697.
HOGENOMiHOG000219769.
HOVERGENiHBG051852.
InParanoidiQ9DCM2.
KOiK13299.
OMAiELWRRIW.
OrthoDBiEOG793B9B.
PhylomeDBiQ9DCM2.
TreeFamiTF105323.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR001853. DSBA-like_thioredoxin_dom.
IPR014440. HCCAis_GSTk.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF01323. DSBA. 1 hit.
[Graphical view]
PIRSFiPIRSF006386. HCCAis_GSTk. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9DCM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPAPRILEL FYDVLSPYSW LGFEVLCRYQ HLWNIKLQLR PTLIAGIMKD
60 70 80 90 100
SGNQPPAMVP RKGQYIFKEI PLLKQFFQVP LNIPKDFFGE TVKKGSINAM
110 120 130 140 150
RFLTTVSMEQ PEMLEKVSRE IWMRVWSRDE DITEYQSILA AAVKAGMSTA
160 170 180 190 200
QAQHFLEKIS TQQVKNKLIE NTDAACKYGA FGLPTTVAHV DGKTYMLFGS
210 220
DRLELLAYLL GEKWMGPVPP TANARL
Length:226
Mass (Da):25,704
Last modified:January 23, 2007 - v3
Checksum:i480332FD618ABCDD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002661 mRNA. Translation: BAB22268.1.
AY279096 mRNA. Translation: AAP20655.1.
BC058163 mRNA. Translation: AAH58163.1.
CCDSiCCDS20063.1.
RefSeqiNP_083831.1. NM_029555.2.
UniGeneiMm.267014.

Genome annotation databases

EnsembliENSMUST00000031897; ENSMUSP00000031897; ENSMUSG00000029864.
GeneIDi76263.
KEGGimmu:76263.
UCSCiuc009bqo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002661 mRNA. Translation: BAB22268.1.
AY279096 mRNA. Translation: AAP20655.1.
BC058163 mRNA. Translation: AAH58163.1.
CCDSiCCDS20063.1.
RefSeqiNP_083831.1. NM_029555.2.
UniGeneiMm.267014.

3D structure databases

ProteinModelPortaliQ9DCM2.
SMRiQ9DCM2. Positions 2-221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48623N.
IntActiQ9DCM2. 2 interactions.
MINTiMINT-1860526.
STRINGi10090.ENSMUSP00000031897.

PTM databases

PhosphoSiteiQ9DCM2.

Proteomic databases

MaxQBiQ9DCM2.
PaxDbiQ9DCM2.
PRIDEiQ9DCM2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031897; ENSMUSP00000031897; ENSMUSG00000029864.
GeneIDi76263.
KEGGimmu:76263.
UCSCiuc009bqo.1. mouse.

Organism-specific databases

CTDi373156.
MGIiMGI:1923513. Gstk1.

Phylogenomic databases

eggNOGiCOG3917.
GeneTreeiENSGT00440000033697.
HOGENOMiHOG000219769.
HOVERGENiHBG051852.
InParanoidiQ9DCM2.
KOiK13299.
OMAiELWRRIW.
OrthoDBiEOG793B9B.
PhylomeDBiQ9DCM2.
TreeFamiTF105323.

Miscellaneous databases

NextBioi344879.
PROiQ9DCM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCM2.
CleanExiMM_GSTK1.
GenevestigatoriQ9DCM2.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR001853. DSBA-like_thioredoxin_dom.
IPR014440. HCCAis_GSTk.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF01323. DSBA. 1 hit.
[Graphical view]
PIRSFiPIRSF006386. HCCAis_GSTk. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGSTK1_MOUSE
AccessioniPrimary (citable) accession number: Q9DCM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.