Glutathione S-transferase kappa 1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q9Y2Q3 (GSTK1_HUMAN)

Last modified October 13, 2009. Version 84. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Glutathione S-transferase kappa 1
    EC=2.5.1.18
Alternative name(s):
    Glutathione S-transferase subunit 13
    GST 13-13
    GST class-kappa
    GSTK1-1
      Short name=hGSTK1

Gene names

Name:	GSTK1
ORF Names:	HDCMD47P

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.

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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.
Subcellular location	Peroxisome. Ref.2
Tissue specificity	Ubiquitous. Ref.2
Sequence similarities	Belongs to the GST superfamily. Kappa family.

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Ontologies

Keywords
Cellular component	Peroxisome
Molecular function	Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Cellular component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione transferase activity Inferred from electronic annotation. Source: EC identical protein binding Inferred from physical interaction. Source: IntAct protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-1053767,EBI-1053767
ATXN10	Q9UBB4	1	EBI-1053767,EBI-702390
CYCS	P99999	1	EBI-1053767,EBI-446479
DCTN1	Q14203	1	EBI-1053767,EBI-724352
DDOST	P39656	1	EBI-1053767,EBI-358866
EFTUD2	Q15029	1	EBI-1053767,EBI-357897
EPPK1	P58107	1	EBI-1053767,EBI-297954
FANCI	Q9NVI1	1	EBI-1053767,EBI-1013291
HEATR2	Q86Y56	1	EBI-1053767,EBI-719966
HNRNPM	P52272	1	EBI-1053767,EBI-486809
HRNR	Q86YZ3	1	EBI-1053767,EBI-1047017
HTR1B	P28222	1	EBI-1053767,EBI-1056863
IPO4	Q8TEX9	1	EBI-1053767,EBI-395967
KIAA1279	Q96EK5	1	EBI-1053767,EBI-744150
KIAA1967	Q8N163	1	EBI-1053767,EBI-355410
LRPPRC	P42704	1	EBI-1053767,EBI-1050853
MATR3	P43243	1	EBI-1053767,EBI-352602
MCM7	P33993	1	EBI-1053767,EBI-355924
PDCD6IP	Q8WUM4	1	EBI-1053767,EBI-310624
RPN1	P04843	1	EBI-1053767,EBI-355963
RPN2	P04844	1	EBI-1053767,EBI-719731
SEC63	Q9UGP8	1	EBI-1053767,EBI-1045560
SLC3A2	P08195	1	EBI-1053767,EBI-702356
TSC22D1	Q15714	1	EBI-1053767,EBI-712609
XPO5	Q9HAV4	1	EBI-1053767,EBI-517949
ZW10	O43264	1	EBI-1053767,EBI-1001217

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 226

225

Glutathione S-transferase kappa 1

PRO_0000185891

Amino acid modifications

Modified residue

N6-acetyllysine Ref.9

Modified residue

169

N6-acetyllysine Ref.9

Experimental info

Sequence conflict

179

G → R in AAF65506. Ref.4

Sequence conflict

206

L → V in AAP97160. Ref.5

Sequence conflict

220

P → S in AAF65506. Ref.4

Secondary structure

226

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9Y2Q3-1 [UniParc].

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

« Hide

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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: 14709161] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 14742434] [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: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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]. 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].
[6]	"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. Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix and Pancreas.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71 AND LYS-169, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.
BC001231 mRNA. Translation: AAH01231.1.
BC050715 mRNA. Translation: AAH50715.1.

IPI

IPI00219673.

RefSeq

NP_001137151.1.
NP_001137153.1.
NP_057001.1.

UniGene

Hs.390667

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YZX	X-ray	1.93	A/B	1-226	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y2Q3. 96 interactions.

STRING

Q9Y2Q3.

PTM databases

PhosphoSite

Q9Y2Q3.

Proteomic databases

PRIDE

Q9Y2Q3.

Genome annotation databases

Ensembl

ENST00000358406; ENSP00000351181; ENSG00000197448; Homo sapiens. [Genome view]
ENST00000378173; ENSP00000367415; ENSG00000197448; Homo sapiens. [Genome view]
ENST00000409500; ENSP00000386944; ENSG00000197448; Homo sapiens. [Genome view]
ENST00000436038; ENSP00000408341; ENSG00000197448; Homo sapiens. [Genome view]
ENST00000442394; ENSP00000406802; ENSG00000197448; Homo sapiens. [Genome view]
ENST00000443571; ENSP00000415813; ENSG00000197448; Homo sapiens. [Genome view]

GeneID

373156.

KEGG

hsa:373156.

UCSC

uc003wci.1. human.

Organism-specific databases

CTD

373156.

GeneCards

GC07P142670.

H-InvDB

HIX0007166.

HGNC

HGNC:16906. GSTK1.

HPA

HPA006311.
HPA022904.

MIM

602321. gene.

PharmGKB

PA134948237.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9Y2Q3.

Enzyme and pathway databases

BRENDA

2.5.1.18. 247.

Gene expression databases

ArrayExpress

Q9Y2Q3.

Bgee

Q9Y2Q3.

CleanEx

HS_GSTK1.

Genevestigator

Q9Y2Q3.

GermOnline

ENSG00000197448. Homo sapiens.

Family and domain databases

InterPro

IPR014440. HCCAis_GSTk.
IPR001853. OxRdtase_DSBA.
[Graphical view]

Pfam

PF01323. DSBA. 1 hit.
[Graphical view]

PIRSF

PIRSF006386. HCCAis_GSTk. 1 hit.

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

100114.

SOURCE

Search...

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Entry information

Entry name

GSTK1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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Relevant documents

Human chromosome 7

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents