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Q9Y2Q3 (GSTK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 kappa 1

EC=2.5.1.18
Alternative name(s):
GST 13-13
GST class-kappa
GSTK1-1
Short name=hGSTK1
Glutathione S-transferase subunit 13
Gene names
Name:GSTK1
ORF Names:HDCMD47P
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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)

Function

Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).

Catalytic activity

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

Subunit structure

Homodimer. Ref.13

Subcellular location

Peroxisome Ref.2.

Tissue specificity

Ubiquitous. Ref.2

Sequence similarities

Belongs to the GST superfamily. Kappa family.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2Q3-1)

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: Q9Y2Q3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     128-128: R → RVSVGLWESSGRTLDDFLTFPRHVFRVMILPPPGGSTVLPVTPLSPHRLPAVFSSSQ
Isoform 3 (identifier: Q9Y2Q3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     129-140: Missing.
Isoform 4 (identifier: Q9Y2Q3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     52-94: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 226225Glutathione S-transferase kappa 1
PRO_0000185891

Regions

Region16 – 183Glutathione binding
Region200 – 2012Glutathione binding

Sites

Binding site531Glutathione
Binding site1831Glutathione; via amide nitrogen and carbonyl oxygen

Amino acid modifications

Modified residue491N6-succinyllysine By similarity
Modified residue711N6-acetyllysine Ref.11
Modified residue851N6-acetyllysine By similarity
Modified residue1161N6-acetyllysine; alternate By similarity
Modified residue1161N6-succinyllysine; alternate By similarity
Modified residue1441N6-succinyllysine By similarity
Modified residue1581N6-acetyllysine; alternate By similarity
Modified residue1581N6-succinyllysine; alternate By similarity
Modified residue1651N6-acetyllysine By similarity
Modified residue1691N6-acetyllysine Ref.11

Natural variations

Alternative sequence52 – 9443Missing in isoform 4.
VSP_040978
Alternative sequence1281R → RVSVGLWESSGRTLDDFLTF PRHVFRVMILPPPGGSTVLP VTPLSPHRLPAVFSSSQ in isoform 2.
VSP_040025
Alternative sequence129 – 14012Missing in isoform 3.
VSP_040979

Experimental info

Sequence conflict511S → R in BAG61794. Ref.6
Sequence conflict1711T → A in BAG61794. Ref.6
Sequence conflict1791G → R in AAF65506. Ref.4
Sequence conflict2061L → V in AAP97160. Ref.5
Sequence conflict2201P → S in AAF65506. Ref.4

Secondary structure

................................... 226
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: D3FDAFD1533B58A4

FASTA22625,497
        10         20         30         40         50         60 
MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGNKPPGLLP 

        70         80         90        100        110        120 
RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM RFLTAVNLEH PEMLEKASRE 

       130        140        150        160        170        180 
LWMRVWSRNE DITEPQSILA AAEKAGMSAE QAQGLLEKIA TPKVKNQLKE TTEAACRYGA 

       190        200        210        220 
FGLPITVAHV DGQTHMLFGS DRMELLAHLL GEKWMGPIPP AVNARL 

« Hide

Isoform 2 [UniParc].

Checksum: 6F88B28A6081324D
Show »

FASTA28231,566
Isoform 3 [UniParc].

Checksum: FA98AC407CF8FB7B
Show »

FASTA21424,185
Isoform 4 [UniParc].

Checksum: 2AA664FBDBB510C9
Show »

FASTA18320,538

References

« Hide 'large scale' references
[1]"Modelling and bioinformatics studies of the human kappa class glutathione transferase predict a novel third glutathione transferase family with homology to prokaryotic 2-hydroxychromene-2-carboxylate (HCCA) isomerases."
Robinson A., Huttley G.A., Booth H.S., Board P.G.
Biochem. J. 379:541-552(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
Tissue: Mammary gland.
[2]"Gene and protein characterization of the human glutathione S-transferase kappa and evidence for a peroxisomal localization."
Morel F., Rauch C., Petit E., Piton A., Theret N., Coles B., Guillouzo A.
J. Biol. Chem. 279:16246-16253(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Umbilical cord blood.
[4]"A novel gene from human dendritic cell."
Zhao Z., Huang X., Li N., Zhu X., Cao X.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Dendritic cell.
[5]"Cloning of a novel human cDNA homologous to rats rGSTK1-1 mRNA."
Zhang M., Yu L., Zhou Y., Hu P.R., Xin Y.R., Zhao S.Y.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [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] (ISOFORMS 2; 3 AND 4).
Tissue: Cerebellum and Hippocampus.
[7]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[10]"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] (ISOFORMS 1 AND 2).
Tissue: Blood, Cervix and Pancreas.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71 AND LYS-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme."
Li J., Xia Z., Ding J.
Protein Sci. 14:2361-2369(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY520571 mRNA. Translation: AAS00610.1.
AY486465 Genomic DNA. Translation: AAS01180.1.
AF070657 mRNA. Translation: AAD20963.1.
AF068287 mRNA. Translation: AAF65506.1.
AF087849 mRNA. Translation: AAP97160.1.
AL136938 mRNA. Translation: CAB66872.1.
AK289570 mRNA. Translation: BAF82259.1.
AK295592 mRNA. Translation: BAG58483.1.
AK299968 mRNA. Translation: BAG61794.1.
AC073342 Genomic DNA. No translation available.
CH471198 Genomic DNA. Translation: EAW51877.1.
BC001231 mRNA. Translation: AAH01231.1.
BC050715 mRNA. Translation: AAH50715.1.
BC063425 mRNA. Translation: AAH63425.1.
RefSeqNP_001137151.1. NM_001143679.1.
NP_001137152.1. NM_001143680.1.
NP_001137153.1. NM_001143681.1.
NP_057001.1. NM_015917.2.
UniGeneHs.390667.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZXX-ray1.93A/B1-226[»]
3RPNX-ray1.90A/B/C/D/E/F1-226[»]
3RPPX-ray1.80A/B/C1-226[»]
ProteinModelPortalQ9Y2Q3.
SMRQ9Y2Q3. Positions 2-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid131875. 35 interactions.
DIPDIP-46924N.
IntActQ9Y2Q3. 7 interactions.
MINTMINT-3084797.
STRING9606.ENSP00000367415.

Chemistry

BindingDBQ9Y2Q3.
ChEMBLCHEMBL4491.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteQ9Y2Q3.

Polymorphism databases

DMDM12643338.

Proteomic databases

PaxDbQ9Y2Q3.
PRIDEQ9Y2Q3.

Protocols and materials databases

DNASU373156.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358406; ENSP00000351181; ENSG00000197448. [Q9Y2Q3-1]
ENST00000409500; ENSP00000386944; ENSG00000197448. [Q9Y2Q3-3]
ENST00000443571; ENSP00000415813; ENSG00000197448. [Q9Y2Q3-4]
ENST00000479303; ENSP00000431049; ENSG00000197448. [Q9Y2Q3-2]
GeneID373156.
KEGGhsa:373156.
UCSCuc003wci.3. human. [Q9Y2Q3-1]
uc003wcj.3. human. [Q9Y2Q3-2]
uc011ksy.2. human. [Q9Y2Q3-4]
uc011ksz.2. human. [Q9Y2Q3-3]

Organism-specific databases

CTD373156.
GeneCardsGC07P142942.
HGNCHGNC:16906. GSTK1.
HPAHPA006311.
HPA022904.
MIM602321. gene.
neXtProtNX_Q9Y2Q3.
PharmGKBPA134948237.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70325.
HOGENOMHOG000219769.
HOVERGENHBG051852.
KOK13299.
OMAELWRRIW.
PhylomeDBQ9Y2Q3.
TreeFamTF105323.

Gene expression databases

ArrayExpressQ9Y2Q3.
BgeeQ9Y2Q3.
CleanExHS_GSTK1.
GenevestigatorQ9Y2Q3.

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

ChiTaRSGSTK1. human.
EvolutionaryTraceQ9Y2Q3.
GeneWikiGSTK1.
GenomeRNAi373156.
NextBio100114.
PROQ9Y2Q3.
SOURCESearch...

Entry information

Entry nameGSTK1_HUMAN
AccessionPrimary (citable) accession number: Q9Y2Q3
Secondary accession number(s): B4DIH1 expand/collapse secondary AC list , B4DSY2, Q6P4H0, Q7Z520, Q9P1S4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 126 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 chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM