HUMAN:PRDX6

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	PRDX6 (synonyms: AOP2, KIAA0106)
Protein Name(s)	Peroxiredoxin-6 1-Cys peroxiredoxin 1-Cys PRX 24 kDa protein Acidic calcium-independent phospholipase A2 aiPLA2 Antioxidant protein 2 Liver 2D page spot 40 Non-selenium glutathione peroxidase NSGPx Red blood cells page spot 12
External Links
UniProt	P30041
EMBL	D14662 DQ230990 AL139142 AK289352 CH471067 BC035857 BC053550 AJ844621
CCDS	CCDS1307.1
RefSeq	NP_004896.1
UniGene	Hs.120 Hs.731505
PDB	1PRX
PDBsum	1PRX
ProteinModelPortal	P30041
SMR	P30041
BioGrid	114956
IntAct	P30041
MINT	MINT-4999165
STRING	9606.ENSP00000342026
PeroxiBase	4426
PhosphoSite	P30041
DMDM	1718024
DOSAC-COBS-2DPAGE	P30041
OGP	P30041
REPRODUCTION-2DPAGE	IPI00220301 P30041
SWISS-2DPAGE	P30041
MaxQB	P30041
PaxDb	P30041
PeptideAtlas	P30041
PRIDE	P30041
DNASU	9588
Ensembl	ENST00000340385
GeneID	9588
KEGG	hsa:9588
UCSC	uc001giy.1
CTD	9588
GeneCards	GC01P173446
H-InvDB	HIX0028696
HGNC	HGNC:16753
HPA	CAB008663 HPA006983
MIM	602316
neXtProt	NX_P30041
PharmGKB	PA134992760
eggNOG	COG0450
HOGENOM	HOG000022346
HOVERGEN	HBG105234
InParanoid	P30041
KO	K11188
OMA	HPNANDT
OrthoDB	EOG7CNZGP
PhylomeDB	P30041
TreeFam	TF105183
BRENDA	1.11.1.15
Reactome	REACT_172715
ChiTaRS	PRDX6
EvolutionaryTrace	P30041
GeneWiki	PRDX6
GenomeRNAi	9588
NextBio	35979
PRO	PR:P30041
Proteomes	UP000005640
Bgee	P30041
CleanEx	HS_PRDX6
ExpressionAtlas	P30041
Genevestigator	P30041
GO	GO:0005737 GO:0016023 GO:0005829 GO:0005615 GO:0070062 GO:0005764 GO:0016020 GO:0016209 GO:0004602 GO:0051920 GO:0004623 GO:0042744 GO:0009395 GO:0006979
Gene3D	3.40.30.10
InterPro	IPR000866 IPR024706 IPR019479 IPR012336
Pfam	PF10417 PF00578
PIRSF	PIRSF000239
SUPFAM	SSF52833
PROSITE	PS51352

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:16186110^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0048026	positive regulation of mRNA splicing, via spliceosome	PMID:16186110^[1]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q8IWL8	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16186110^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16186110^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0045296	cadherin binding	PMID:25468996^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:25468996^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:9587003^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0098869	cellular oxidant detoxification	PMID:10893423^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004602	glutathione peroxidase activity	PMID:10893423^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:19725078^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:23580065^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
involved_in	GO:0046475	glycerophospholipid catabolic process	PMID:10893423^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	PMID:10893423^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:9497358^[11]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:19188445^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0047499	calcium-independent phospholipase A2 activity	PMID:10893423^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(CHEBI:40265)	Seeded From UniProt	complete
involved_in	GO:0042744	hydrogen peroxide catabolic process	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0031479 FB:FBgn0033518 FB:FBgn0033520 PANTHER:PTN002460592 RGD:71005	P		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002460592 SGD:S000000160 UniProtKB:Q5A5A0	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0031479 FB:FBgn0033518 FB:FBgn0033520 MGI:MGI:894320 PANTHER:PTN000073790 UniProtKB:Q8IAM2	C		Seeded From UniProt	complete
enables	GO:0004601	peroxidase activity	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0031479 FB:FBgn0033518 FB:FBgn0033520 MGI:MGI:894320 PANTHER:PTN002460592 RGD:71005 SGD:S000000160 UniProtKB:A2SZW8 UniProtKB:P30041 UniProtKB:Q5A5A0	F		Seeded From UniProt	complete
involved_in	GO:0042744	hydrogen peroxide catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35244 ensembl:ENSRNOP00000030323	P		Seeded From UniProt	complete
enables	GO:0004602	glutathione peroxidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35244 ensembl:ENSRNOP00000030323	F		Seeded From UniProt	complete
enables	GO:0016209	antioxidant activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000866	F		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000866	F		Seeded From UniProt	complete
involved_in	GO:0045454	cell redox homeostasis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013766	P		Seeded From UniProt	complete
enables	GO:0051920	peroxiredoxin activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR019479	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000866 InterPro:IPR019479	P		Seeded From UniProt	complete
enables	GO:0102567	phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine)	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.1.4	F		Seeded From UniProt	complete
enables	GO:0004623	phospholipase A2 activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.1.4	F		Seeded From UniProt	complete
enables	GO:0051920	peroxiredoxin activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.11.1.15	F		Seeded From UniProt	complete
enables	GO:0102568	phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine)	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.1.4	F		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035578	azurophil granule lumen	Reactome:R-HSA-6798751	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	Reactome:R-HSA-3299685	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-3343700	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6798751	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004601	peroxidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0575	F		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F		Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	P		Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
involved_in	GO:0016042	lipid catabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0442	P		Seeded From UniProt	complete
enables	GO:0016209	antioxidant activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0049	F		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0458 UniProtKB-SubCell:SL-0158	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Gao, L et al. (2005) Saitohin, which is nested in the tau locus and confers allele-specific susceptibility to several neurodegenerative diseases, interacts with peroxiredoxin 6. J. Biol. Chem. 280 39268-72 PubMed GONUTS page
↑ ^2.0 ^2.1 Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page
↑ Choi, HJ et al. (1998) Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Nat. Struct. Biol. 5 400-6 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 Chen, JW et al. (2000) 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. J. Biol. Chem. 275 28421-7 PubMed GONUTS page
↑ Davison, EJ et al. (2009) Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 9 4284-97 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page
↑ Kang, SW et al. (1998) Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J. Biol. Chem. 273 6303-11 PubMed GONUTS page
↑ Vascotto, C et al. (2009) APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process. Mol. Cell. Biol. 29 1834-54 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:16186110-1] 1.0 ^1.1 ^1.2 ^1.3 Gao, L et al. (2005) Saitohin, which is nested in the tau locus and confers allele-specific susceptibility to several neurodegenerative diseases, interacts with peroxiredoxin 6. J. Biol. Chem. 280 39268-72 PubMed GONUTS page

[PMID:25468996-2] 2.0 ^2.1 Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page

[PMID:9587003-3] Choi, HJ et al. (1998) Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Nat. Struct. Biol. 5 400-6 PubMed GONUTS page

[PMID:10893423-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 Chen, JW et al. (2000) 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. J. Biol. Chem. 275 28421-7 PubMed GONUTS page

[PMID:19725078-5] Davison, EJ et al. (2009) Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 9 4284-97 PubMed GONUTS page

[PMID:23533145-6] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19946888-7] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:19056867-8] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-9] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:23580065-10] Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page

[PMID:9497358-11] Kang, SW et al. (1998) Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J. Biol. Chem. 273 6303-11 PubMed GONUTS page

[PMID:19188445-12] Vascotto, C et al. (2009) APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process. Mol. Cell. Biol. 29 1834-54 PubMed GONUTS page

[PMID:21873635-13] 13.0 ^13.1 ^13.2 ^13.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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HUMAN:PRDX6

Contents

Annotations

Notes

References

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