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Q9Y2Q3

- GSTK1_HUMAN

UniProt

Q9Y2Q3 - GSTK1_HUMAN

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Protein
Glutathione S-transferase kappa 1
Gene
GSTK1, HDCMD47P
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

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

GO - Molecular functioni

  1. glutathione peroxidase activity Source: UniProtKB
  2. glutathione transferase activity Source: UniProtKB
  3. protein disulfide oxidoreductase activity Source: InterPro
  4. receptor binding Source: UniProtKB

GO - Biological processi

  1. epithelial cell differentiation Source: UniProt
  2. glutathione metabolic process Source: Ensembl
  3. 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:
hGSTK1
Glutathione S-transferase subunit 13
Gene namesi
Name:GSTK1
ORF Names:HDCMD47P
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:16906. GSTK1.

Subcellular locationi

Peroxisome 1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. intracellular Source: LIFEdb
  3. mitochondrial inner membrane Source: Ensembl
  4. mitochondrial matrix Source: Ensembl
  5. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134948237.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 226225Glutathione S-transferase kappa 1
PRO_0000185891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491N6-succinyllysine By similarity
Modified residuei71 – 711N6-acetyllysine1 Publication
Modified residuei85 – 851N6-acetyllysine By similarity
Modified residuei116 – 1161N6-acetyllysine; alternate By similarity
Modified residuei116 – 1161N6-succinyllysine; alternate By similarity
Modified residuei144 – 1441N6-succinyllysine By similarity
Modified residuei158 – 1581N6-acetyllysine; alternate By similarity
Modified residuei158 – 1581N6-succinyllysine; alternate By similarity
Modified residuei165 – 1651N6-acetyllysine By similarity
Modified residuei169 – 1691N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y2Q3.
PaxDbiQ9Y2Q3.
PRIDEiQ9Y2Q3.

PTM databases

PhosphoSiteiQ9Y2Q3.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ArrayExpressiQ9Y2Q3.
BgeeiQ9Y2Q3.
CleanExiHS_GSTK1.
GenevestigatoriQ9Y2Q3.

Organism-specific databases

HPAiHPA006311.
HPA022904.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi131875. 36 interactions.
DIPiDIP-46924N.
IntActiQ9Y2Q3. 7 interactions.
MINTiMINT-3084797.
STRINGi9606.ENSP00000367415.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127
Helixi17 – 2913
Turni30 – 323
Beta strandi33 – 419
Helixi44 – 474
Beta strandi57 – 593
Helixi61 – 7717
Helixi88 – 947
Helixi97 – 10913
Helixi111 – 1133
Helixi114 – 12613
Helixi135 – 14410
Helixi149 – 1568
Turni157 – 1604
Helixi162 – 17716
Beta strandi181 – 1833
Beta strandi185 – 1906
Beta strandi193 – 2019
Helixi203 – 2108

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZXX-ray1.93A/B1-226[»]
3RPNX-ray1.90A/B/C/D/E/F1-226[»]
3RPPX-ray1.80A/B/C1-226[»]
ProteinModelPortaliQ9Y2Q3.
SMRiQ9Y2Q3. Positions 2-221.

Miscellaneous databases

EvolutionaryTraceiQ9Y2Q3.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the GST superfamily. Kappa family.

Phylogenomic databases

eggNOGiNOG70325.
HOGENOMiHOG000219769.
HOVERGENiHBG051852.
KOiK13299.
OMAiELWRRIW.
PhylomeDBiQ9Y2Q3.
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.

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y2Q3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD    50
SGNKPPGLLP RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM 100
RFLTAVNLEH PEMLEKASRE LWMRVWSRNE DITEPQSILA AAEKAGMSAE 150
QAQGLLEKIA TPKVKNQLKE TTEAACRYGA FGLPITVAHV DGQTHMLFGS 200
DRMELLAHLL GEKWMGPIPP AVNARL 226
Length:226
Mass (Da):25,497
Last modified:January 23, 2007 - v3
Checksum:iD3FDAFD1533B58A4
GO
Isoform 2 (identifier: Q9Y2Q3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     128-128: R → RVSVGLWESSGRTLDDFLTFPRHVFRVMILPPPGGSTVLPVTPLSPHRLPAVFSSSQ

Show »
Length:282
Mass (Da):31,566
Checksum:i6F88B28A6081324D
GO
Isoform 3 (identifier: Q9Y2Q3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     129-140: Missing.

Show »
Length:214
Mass (Da):24,185
Checksum:iFA98AC407CF8FB7B
GO
Isoform 4 (identifier: Q9Y2Q3-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:183
Mass (Da):20,538
Checksum:i2AA664FBDBB510C9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei52 – 9443Missing in isoform 4.
VSP_040978Add
BLAST
Alternative sequencei128 – 1281R → RVSVGLWESSGRTLDDFLTF PRHVFRVMILPPPGGSTVLP VTPLSPHRLPAVFSSSQ in isoform 2.
VSP_040025
Alternative sequencei129 – 14012Missing in isoform 3.
VSP_040979Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511S → R in BAG61794. 1 Publication
Sequence conflicti171 – 1711T → A in BAG61794. 1 Publication
Sequence conflicti179 – 1791G → R in AAF65506. 1 Publication
Sequence conflicti206 – 2061L → V in AAP97160. 1 Publication
Sequence conflicti220 – 2201P → S in AAF65506. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS47730.1. [Q9Y2Q3-2]
CCDS47731.1. [Q9Y2Q3-3]
CCDS47732.1. [Q9Y2Q3-4]
CCDS5877.1. [Q9Y2Q3-1]
RefSeqiNP_001137151.1. NM_001143679.1. [Q9Y2Q3-2]
NP_001137152.1. NM_001143680.1. [Q9Y2Q3-3]
NP_001137153.1. NM_001143681.1. [Q9Y2Q3-4]
NP_057001.1. NM_015917.2. [Q9Y2Q3-1]
UniGeneiHs.390667.

Genome annotation databases

EnsembliENST00000358406; ENSP00000351181; ENSG00000197448. [Q9Y2Q3-1]
ENST00000409500; ENSP00000386944; ENSG00000197448. [Q9Y2Q3-3]
ENST00000443571; ENSP00000415813; ENSG00000197448. [Q9Y2Q3-4]
ENST00000479303; ENSP00000431049; ENSG00000197448. [Q9Y2Q3-2]
GeneIDi373156.
KEGGihsa:373156.
UCSCiuc003wci.3. human. [Q9Y2Q3-1]
uc003wcj.3. human. [Q9Y2Q3-2]
uc011ksy.2. human. [Q9Y2Q3-4]
uc011ksz.2. human. [Q9Y2Q3-3]

Polymorphism databases

DMDMi12643338.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS47730.1. [Q9Y2Q3-2 ]
CCDS47731.1. [Q9Y2Q3-3 ]
CCDS47732.1. [Q9Y2Q3-4 ]
CCDS5877.1. [Q9Y2Q3-1 ]
RefSeqi NP_001137151.1. NM_001143679.1. [Q9Y2Q3-2 ]
NP_001137152.1. NM_001143680.1. [Q9Y2Q3-3 ]
NP_001137153.1. NM_001143681.1. [Q9Y2Q3-4 ]
NP_057001.1. NM_015917.2. [Q9Y2Q3-1 ]
UniGenei Hs.390667.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YZX X-ray 1.93 A/B 1-226 [» ]
3RPN X-ray 1.90 A/B/C/D/E/F 1-226 [» ]
3RPP X-ray 1.80 A/B/C 1-226 [» ]
ProteinModelPortali Q9Y2Q3.
SMRi Q9Y2Q3. Positions 2-221.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 131875. 36 interactions.
DIPi DIP-46924N.
IntActi Q9Y2Q3. 7 interactions.
MINTi MINT-3084797.
STRINGi 9606.ENSP00000367415.

Chemistry

BindingDBi Q9Y2Q3.
ChEMBLi CHEMBL4491.
DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei Q9Y2Q3.

Polymorphism databases

DMDMi 12643338.

Proteomic databases

MaxQBi Q9Y2Q3.
PaxDbi Q9Y2Q3.
PRIDEi Q9Y2Q3.

Protocols and materials databases

DNASUi 373156.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358406 ; ENSP00000351181 ; ENSG00000197448 . [Q9Y2Q3-1 ]
ENST00000409500 ; ENSP00000386944 ; ENSG00000197448 . [Q9Y2Q3-3 ]
ENST00000443571 ; ENSP00000415813 ; ENSG00000197448 . [Q9Y2Q3-4 ]
ENST00000479303 ; ENSP00000431049 ; ENSG00000197448 . [Q9Y2Q3-2 ]
GeneIDi 373156.
KEGGi hsa:373156.
UCSCi uc003wci.3. human. [Q9Y2Q3-1 ]
uc003wcj.3. human. [Q9Y2Q3-2 ]
uc011ksy.2. human. [Q9Y2Q3-4 ]
uc011ksz.2. human. [Q9Y2Q3-3 ]

Organism-specific databases

CTDi 373156.
GeneCardsi GC07P142942.
HGNCi HGNC:16906. GSTK1.
HPAi HPA006311.
HPA022904.
MIMi 602321. gene.
neXtProti NX_Q9Y2Q3.
PharmGKBi PA134948237.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG70325.
HOGENOMi HOG000219769.
HOVERGENi HBG051852.
KOi K13299.
OMAi ELWRRIW.
PhylomeDBi Q9Y2Q3.
TreeFami TF105323.

Miscellaneous databases

ChiTaRSi GSTK1. human.
EvolutionaryTracei Q9Y2Q3.
GeneWikii GSTK1.
GenomeRNAii 373156.
NextBioi 100114.
PROi Q9Y2Q3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y2Q3.
Bgeei Q9Y2Q3.
CleanExi HS_GSTK1.
Genevestigatori Q9Y2Q3.

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. "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.
    , 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.
    , 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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. 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. 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.

Entry informationi

Entry nameiGSTK1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2Q3
Secondary accession number(s): B4DIH1
, B4DSY2, Q6P4H0, Q7Z520, Q9P1S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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