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Q9DCM2

- GSTK1_MOUSE

UniProt

Q9DCM2 - GSTK1_MOUSE

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Protein
Glutathione S-transferase kappa 1
Gene
Gstk1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 – 531Glutathione By similarity
Binding sitei183 – 1831Glutathione; via amide nitrogen and carbonyl oxygen By similarity

GO - Molecular functioni

  1. glutathione peroxidase activity Source: MGI
  2. glutathione transferase activity Source: MGI
  3. protein disulfide oxidoreductase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. glutathione metabolic process Source: MGI
  2. oxidation-reduction process Source: GOC
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: Chromosome 6

Organism-specific databases

MGIiMGI:1923513. Gstk1.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrial inner membrane Source: MGI
  2. mitochondrial matrix Source: Ensembl
  3. mitochondrion Source: MGI
  4. peroxisome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 226225Glutathione S-transferase kappa 1
PRO_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.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the GST superfamily. Kappa family.

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

MGPAPRILEL FYDVLSPYSW LGFEVLCRYQ HLWNIKLQLR PTLIAGIMKD    50
SGNQPPAMVP RKGQYIFKEI PLLKQFFQVP LNIPKDFFGE TVKKGSINAM 100
RFLTTVSMEQ PEMLEKVSRE IWMRVWSRDE DITEYQSILA AAVKAGMSTA 150
QAQHFLEKIS TQQVKNKLIE NTDAACKYGA FGLPTTVAHV DGKTYMLFGS 200
DRLELLAYLL GEKWMGPVPP TANARL 226
Length:226
Mass (Da):25,704
Last modified:January 23, 2007 - v3
Checksum:i480332FD618ABCDD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK002661 mRNA. Translation: BAB22268.1 .
AY279096 mRNA. Translation: AAP20655.1 .
BC058163 mRNA. Translation: AAH58163.1 .
CCDSi CCDS20063.1.
RefSeqi NP_083831.1. NM_029555.2.
UniGenei Mm.267014.

3D structure databases

ProteinModelPortali Q9DCM2.
SMRi Q9DCM2. Positions 2-221.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-48623N.
IntActi Q9DCM2. 2 interactions.
MINTi MINT-1860526.
STRINGi 10090.ENSMUSP00000031897.

PTM databases

PhosphoSitei Q9DCM2.

Proteomic databases

MaxQBi Q9DCM2.
PaxDbi Q9DCM2.
PRIDEi Q9DCM2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031897 ; ENSMUSP00000031897 ; ENSMUSG00000029864 .
GeneIDi 76263.
KEGGi mmu:76263.
UCSCi uc009bqo.1. mouse.

Organism-specific databases

CTDi 373156.
MGIi MGI:1923513. Gstk1.

Phylogenomic databases

eggNOGi COG3917.
GeneTreei ENSGT00440000033697.
HOGENOMi HOG000219769.
HOVERGENi HBG051852.
InParanoidi Q9DCM2.
KOi K13299.
OMAi ELWRRIW.
OrthoDBi EOG793B9B.
PhylomeDBi Q9DCM2.
TreeFami TF105323.

Miscellaneous databases

NextBioi 344879.
PROi Q9DCM2.
SOURCEi Search...

Gene expression databases

Bgeei Q9DCM2.
CleanExi MM_GSTK1.
Genevestigatori Q9DCM2.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR001853. DSBA-like_thioredoxin_dom.
IPR014440. HCCAis_GSTk.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF01323. DSBA. 1 hit.
[Graphical view ]
PIRSFi PIRSF006386. HCCAis_GSTk. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
ProtoNeti Search...

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: July 9, 2014
This is version 96 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