Q9Y2Q3 (GSTK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GSTK1
ORF Names:	HDCMD47P

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing
Molecular function	Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial matrix Inferred from electronic annotation. Source: Compara peroxisome Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	glutathione peroxidase activity Inferred from direct assay Ref.2. Source: UniProtKB glutathione transferase activity Inferred from direct assay Ref.2. Source: UniProtKB protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 226

225

Glutathione S-transferase kappa 1

PRO_0000185891

Regions

Region

16 – 18

3

Glutathione binding

Region

200 – 201

2

Glutathione binding

Sites

Binding site

53

1

Glutathione

Binding site

183

1

Glutathione; via amide nitrogen and carbonyl oxygen

Amino acid modifications

Modified residue

71

1

N6-acetyllysine Ref.11

Modified residue

169

1

N6-acetyllysine Ref.11

Natural variations

Alternative sequence

52 – 94

43

Missing in isoform 4.

VSP_040978

Alternative sequence

128

1

R → RVSVGLWESSGRTLDDFLTF PRHVFRVMILPPPGGSTVLP VTPLSPHRLPAVFSSSQ in isoform 2.

VSP_040025

Alternative sequence

129 – 140

12

Missing in isoform 3.

VSP_040979

Experimental info

Sequence conflict

51

1

S → R in BAG61794. Ref.6

Sequence conflict

171

1

T → A in BAG61794. Ref.6

Sequence conflict

179

1

G → R in AAF65506. Ref.4

Sequence conflict

206

1

L → V in AAP97160. Ref.5

Sequence conflict

220

1

P → S in AAF65506. Ref.4

Secondary structure

1

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226

Helix Strand Turn

Details...

Beta strand

6 – 12

7

Helix

17 – 29

13

Turn

30 – 32

3

Beta strand

33 – 41

9

Helix

44 – 47

4

Beta strand

57 – 59

3

Helix

61 – 77

17

Helix

88 – 94

7

Helix

97 – 109

13

Helix

111 – 113

3

Helix

114 – 126

13

Helix

135 – 144

10

Helix

149 – 156

8

Turn

157 – 160

4

Helix

162 – 177

16

Beta strand

181 – 183

3

Beta strand

185 – 190

6

Beta strand

193 – 201

9

Helix

203 – 210

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D3FDAFD1533B58A4	FASTA	226	25,497
	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
	Isoform 2 [UniParc]. Checksum: 6F88B28A6081324D	FASTA	282	31,566
	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 LWMRVWSRVS VGLWESSGRT LDDFLTFPRH VFRVMILPPP GGSTVLPVTP LSPHRLPAVF 190 200 210 220 230 240 SSSQNEDITE PQSILAAAEK AGMSAEQAQG LLEKIATPKV KNQLKETTEA ACRYGAFGLP 250 260 270 280 ITVAHVDGQT HMLFGSDRME LLAHLLGEKW MGPIPPAVNA RL
	Isoform 3 [UniParc]. Checksum: FA98AC407CF8FB7B	FASTA	214	24,185
	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 LWMRVWSRAA EKAGMSAEQA QGLLEKIATP KVKNQLKETT EAACRYGAFG LPITVAHVDG 190 200 210 QTHMLFGSDR MELLAHLLGE KWMGPIPPAV NARL
	Isoform 4 [UniParc]. Checksum: 2AA664FBDBB510C9	FASTA	183	20,538
	10 20 30 40 50 60 MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGSLSAMRFL 70 80 90 100 110 120 TAVNLEHPEM LEKASRELWM RVWSRNEDIT EPQSILAAAE KAGMSAEQAQ GLLEKIATPK 130 140 150 160 170 180 VKNQLKETTE AACRYGAFGL PITVAHVDGQ THMLFGSDRM ELLAHLLGEK WMGPIPPAVN ARL

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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. , 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, MASS SPECTROMETRY.
[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.

IPI

IPI00219673.
IPI00440703.
IPI00909432.
IPI00917714.

RefSeq

NP_001137151.1. NM_001143679.1.
NP_001137152.1. NM_001143680.1.
NP_001137153.1. NM_001143681.1.
NP_057001.1. NM_015917.2.

UniGene

Hs.390667.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9Y2Q3.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46924N.

IntAct

Q9Y2Q3. 6 interactions.

STRING

9606.ENSP00000367415.

PTM databases

PhosphoSite

Q9Y2Q3.

Polymorphism databases

DMDM

12643338.

Proteomic databases

PaxDb

Q9Y2Q3.

PRIDE

Q9Y2Q3.

Protocols and materials databases

DNASU

373156.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358406; ENSP00000351181; ENSG00000197448.
ENST00000409500; ENSP00000386944; ENSG00000197448.
ENST00000443571; ENSP00000415813; ENSG00000197448.
ENST00000479303; ENSP00000431049; ENSG00000197448.

GeneID

373156.

KEGG

hsa:373156.

UCSC

uc003wci.3. human.
uc003wcj.3. human.
uc011ksy.2. human.
uc011ksz.2. human.

Organism-specific databases

CTD

373156.

GeneCards

GC07P142942.

HGNC

HGNC:16906. GSTK1.

HPA

HPA006311.
HPA022904.

MIM

602321. gene.

neXtProt

NX_Q9Y2Q3.

PharmGKB

PA134948237.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG70325.

HOGENOM

HOG000219769.

HOVERGEN

HBG051852.

KO

K13299.

OMA

MRVWSRD.

PhylomeDB

Q9Y2Q3.

Gene expression databases

ArrayExpress

Q9Y2Q3.

Bgee

Q9Y2Q3.

CleanEx

HS_GSTK1.

Genevestigator

Q9Y2Q3.

GermOnline

ENSG00000197448. Homo sapiens.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR001853. DSBA-like_thioredoxin_dom.
IPR014440. HCCAis_GSTk.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF01323. DSBA. 1 hit.
[Graphical view]

PIRSF

PIRSF006386. HCCAis_GSTk. 1 hit.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q9Y2Q3.

ChEMBL

CHEMBL4491.

ChiTaRS

GSTK1. human.

DrugBank

DB00143. Glutathione.

EvolutionaryTrace

Q9Y2Q3.

GenomeRNAi

373156.

NextBio

100114.

SOURCE

Search...

Entry information

Entry name

GSTK1_HUMAN

Accession

Primary (citable) accession number: Q9Y2Q3
Secondary accession number(s): B4DIH1 , B4DSY2, Q6P4H0, Q7Z520, Q9P1S4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.