HUMAN:PON1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	PON1 (synonyms: PON)
Protein Name(s)	Serum paraoxonase/arylesterase 1 PON 1 Aromatic esterase 1 A-esterase 1 K-45 Serum aryldialkylphosphatase 1
External Links
UniProt	P27169
EMBL	M63012 M63013 M63014 S56555 S56546 S56548 S64696 S64615 U55885 U55877 U55878 U55879 U55880 U55881 U55882 U55883 D84371 U53784 Z70723 AK314027 AF539592 AC004022 CH236949 CH471091 BC074719
CCDS	CCDS5638.1
PIR	A45451
RefSeq	NP_000437.3
UniGene	Hs.370995
PDB	1V04 1XHR
PDBsum	1V04 1XHR
ProteinModelPortal	P27169
SMR	P27169
BioGrid	111440
STRING	9606.ENSP00000222381
BindingDB	P27169
ChEMBL	CHEMBL3167
DrugBank	DB01327
TCDB	1.A.6.2.6
PhosphoSite	P27169
DMDM	308153572
SWISS-2DPAGE	P27169
MaxQB	P27169
PaxDb	P27169
PeptideAtlas	P27169
PRIDE	P27169
Ensembl	ENST00000222381
GeneID	5444
KEGG	hsa:5444
UCSC	uc003uns.3
CTD	5444
GeneCards	GC07M094926
H-InvDB	HIX0033662
HGNC	HGNC:9204
HPA	HPA001610
MIM	168820 612633
neXtProt	NX_P27169
Orphanet	803
PharmGKB	PA33529
eggNOG	NOG68009
GeneTree	ENSGT00390000008932
HOGENOM	HOG000252960
HOVERGEN	HBG003604
InParanoid	P27169
KO	K01045
PhylomeDB	P27169
TreeFam	TF322436
BRENDA	3.1.1.2
SABIO-RK	P27169
ChiTaRS	PON1
EvolutionaryTrace	P27169
GeneWiki	PON1
GenomeRNAi	5444
NextBio	21069
PRO	PR:P27169
Proteomes	UP000005640
Bgee	P27169
CleanEx	HS_PON1
ExpressionAtlas	P27169
Genevestigator	P27169
GO	GO:0072562 GO:0005576 GO:0005615 GO:0070062 GO:0034364 GO:0043231 GO:0034366 GO:0004063 GO:0004064 GO:0005509 GO:0005543 GO:0042803 GO:0019439 GO:0046395 GO:0016311 GO:0046434 GO:0046470 GO:0051099 GO:0010875 GO:0032411 GO:0009605 GO:0070542 GO:1902617 GO:0031667 GO:0009636
Gene3D	2.120.10.30
InterPro	IPR011042 IPR002640 IPR008363
Pfam	PF01731
PRINTS	PR01785 PR01786

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0070062	extracellular exosome	PMID:23533145^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0072562	blood microparticle	PMID:22516433^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0051099	positive regulation of binding	PMID:15721011^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0046470	phosphatidylcholine metabolic process	PMID:15721011^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0046434	organophosphate catabolic process	PMID:7638166^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0046395	carboxylic acid catabolic process	PMID:7638166^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:15772423^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
NOT\|involved_in	GO:0034445	negative regulation of plasma lipoprotein oxidation	PMID:15342686^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0034366	spherical high-density lipoprotein particle	PMID:16682745^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0034364	high-density lipoprotein particle	PMID:15721011^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0032411	positive regulation of transporter activity	PMID:15721011^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019439	aromatic compound catabolic process	PMID:15772423^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0010875	positive regulation of cholesterol efflux	PMID:15721011^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:7638166^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005543	phospholipid binding	PMID:10479665^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004064	arylesterase activity	PMID:7638166^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004063	aryldialkylphosphatase activity	PMID:7638166^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:14718574^[9]	ECO:0000303	author statement without traceable support used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:15098021^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004064	arylesterase activity	PMID:15098021^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004064	arylesterase activity	PMID:1673382^[11]	ECO:0000303	author statement without traceable support used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004063	aryldialkylphosphatase activity	PMID:15098021^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009636	response to toxic substance	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:103295 PANTHER:PTN000210195	P	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000210199 RGD:620062 UniProtKB:P27169	C	Seeded From UniProt	complete
enables	GO:0004064	arylesterase activity	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:103295 PANTHER:PTN000210195 RGD:1302965 UniProtKB:P27169 UniProtKB:Q15166	F	Seeded From UniProt	complete
enables	GO:0004063	aryldialkylphosphatase activity	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000210199 RGD:620062 UniProtKB:P27169	F	Seeded From UniProt	complete
involved_in	GO:0016311	dephosphorylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004063	P	Seeded From UniProt	complete
involved_in	GO:0016311	dephosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004063	P	Seeded From UniProt	complete
involved_in	GO:0016311	dephosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004063	P	Seeded From UniProt	complete
involved_in	GO:0016311	dephosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004063	P	Seeded From UniProt	complete
involved_in	GO:0016311	dephosphorylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004063	P	Seeded From UniProt	complete
involved_in	GO:0009636	response to toxic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P52430 ensembl:ENSMUSP00000002663	P	Seeded From UniProt	complete
involved_in	GO:0008203	cholesterol metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P52430 ensembl:ENSMUSP00000002663	P	Seeded From UniProt	complete
enables	GO:0004064	arylesterase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P52430 ensembl:ENSMUSP00000002663	F	Seeded From UniProt	complete
involved_in	GO:1902617	response to fluoride	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P55159 ensembl:ENSRNOP00000011823	P	Seeded From UniProt	complete
involved_in	GO:0070542	response to fatty acid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P55159 ensembl:ENSRNOP00000011823	P	Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P55159 ensembl:ENSRNOP00000011823	C	Seeded From UniProt	complete
involved_in	GO:0031667	response to nutrient levels	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P55159 ensembl:ENSRNOP00000011823	P	Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P55159 ensembl:ENSRNOP00000011823	P	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P55159 ensembl:ENSRNOP00000011823	C	Seeded From UniProt	complete
enables	GO:0004063	aryldialkylphosphatase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P55159 ensembl:ENSRNOP00000011823	F	Seeded From UniProt	complete
enables	GO:0004064	arylesterase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002640 InterPro:IPR008363	F	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008363	C	Seeded From UniProt	complete
enables	GO:0004064	arylesterase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.1.2	F	Seeded From UniProt	complete
enables	GO:0102007	acyl-L-homoserine-lactone lactonohydrolase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.1.81	F	Seeded From UniProt	complete
enables	GO:0004063	aryldialkylphosphatase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.8.1	F	Seeded From UniProt	complete
part_of	GO:0034364	high-density lipoprotein particle	PMID:10479665^[8]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0019372	lipoxygenase pathway	Reactome:R-HSA-2142688	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-8932633	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	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
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
part_of	GO:0034364	high-density lipoprotein particle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0345	C	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964	C	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0112	C	Seeded From UniProt	complete
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Notes

References

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

↑ 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
↑ Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Rosenblat, M et al. (2005) Paraoxonase 1 (PON1) enhances HDL-mediated macrophage cholesterol efflux via the ABCA1 transporter in association with increased HDL binding to the cells: a possible role for lysophosphatidylcholine. Atherosclerosis 179 69-77 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 Sorenson, RC et al. (1995) Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase. Proc. Natl. Acad. Sci. U.S.A. 92 7187-91 PubMed GONUTS page
↑ ^5.0 ^5.1 Draganov, DI et al. (2005) Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J. Lipid Res. 46 1239-47 PubMed GONUTS page
↑ Teiber, JF et al. (2004) Purified human serum PON1 does not protect LDL against oxidation in the in vitro assays initiated with copper or AAPH. J. Lipid Res. 45 2260-8 PubMed GONUTS page
↑ Christoffersen, C et al. (2006) Isolation and characterization of human apolipoprotein M-containing lipoproteins. J. Lipid Res. 47 1833-43 PubMed GONUTS page
↑ ^8.0 ^8.1 Sorenson, RC et al. (1999) Human serum Paraoxonase/Arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids : apolipoprotein A-I stabilizes activity. Arterioscler. Thromb. Vasc. Biol. 19 2214-25 PubMed GONUTS page
↑ Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Harel, M et al. (2004) Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes. Nat. Struct. Mol. Biol. 11 412-9 PubMed GONUTS page
↑ Gan, KN et al. () Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities. Drug Metab. Dispos. 19 100-6 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 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:23533145-1] 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:22516433-2] Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page

[PMID:15721011-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Rosenblat, M et al. (2005) Paraoxonase 1 (PON1) enhances HDL-mediated macrophage cholesterol efflux via the ABCA1 transporter in association with increased HDL binding to the cells: a possible role for lysophosphatidylcholine. Atherosclerosis 179 69-77 PubMed GONUTS page

[PMID:7638166-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 Sorenson, RC et al. (1995) Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase. Proc. Natl. Acad. Sci. U.S.A. 92 7187-91 PubMed GONUTS page

[PMID:15772423-5] 5.0 ^5.1 Draganov, DI et al. (2005) Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J. Lipid Res. 46 1239-47 PubMed GONUTS page

[PMID:15342686-6] Teiber, JF et al. (2004) Purified human serum PON1 does not protect LDL against oxidation in the in vitro assays initiated with copper or AAPH. J. Lipid Res. 45 2260-8 PubMed GONUTS page

[PMID:16682745-7] Christoffersen, C et al. (2006) Isolation and characterization of human apolipoprotein M-containing lipoproteins. J. Lipid Res. 47 1833-43 PubMed GONUTS page

[PMID:10479665-8] 8.0 ^8.1 Sorenson, RC et al. (1999) Human serum Paraoxonase/Arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids : apolipoprotein A-I stabilizes activity. Arterioscler. Thromb. Vasc. Biol. 19 2214-25 PubMed GONUTS page

[PMID:14718574-9] Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page

[PMID:15098021-10] 10.0 ^10.1 ^10.2 Harel, M et al. (2004) Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes. Nat. Struct. Mol. Biol. 11 412-9 PubMed GONUTS page

[PMID:1673382-11] Gan, KN et al. () Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities. Drug Metab. Dispos. 19 100-6 PubMed GONUTS page

[PMID:21873635-12] 12.0 ^12.1 ^12.2 ^12.3 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:PON1

Contents

Annotations

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