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P27169 (PON1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serum paraoxonase/arylesterase 1

Short name=PON 1
EC=3.1.1.2
EC=3.1.1.81
EC=3.1.8.1
Alternative name(s):
Aromatic esterase 1
Short name=A-esterase 1
K-45
Serum aryldialkylphosphatase 1
Gene names
Name:PON1
Synonyms:PON
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation. Ref.18 Ref.20

Catalytic activity

A phenyl acetate + H2O = a phenol + acetate. Ref.3 Ref.15 Ref.16 Ref.20 Ref.24

An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol. Ref.3 Ref.15 Ref.16 Ref.20 Ref.24

An N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine. Ref.3 Ref.15 Ref.16 Ref.20 Ref.24

Cofactor

Binds 2 calcium ions per subunit.

Subunit structure

Homodimer. Heterooligomer with phosphate-binding protein (HPBP). Interacts with CLU. Ref.14 Ref.20 Ref.22

Subcellular location

Secretedextracellular space.

Tissue specificity

Plasma, associated with HDL (at protein level). Expressed in liver, but not in heart, brain, placenta, lung, skeletal muscle, kidney or pancreas. Ref.13 Ref.14

Post-translational modification

Glycosylated.

The signal sequence is not cleaved.

Present in two forms, form B contains a disulfide bond, form A does not.

Polymorphism

The allelic form of the enzyme with Gln-192 (allozyme A) hydrolyzes paraoxon with a low turnover number and the one with Arg-192 (allozyme B) with a high turnover number.

Involvement in disease

Microvascular complications of diabetes 5 (MVCD5) [MIM:612633]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Homozygosity for the Leu-55 allele is strongly associated with the development of retinal disease in diabetic patients.

Miscellaneous

The preferential association of PON1 with HDL is mediated in part by its signal peptide, by binding phospholipids directly, rather than binding apo AI. The retained signal peptide may allow transfer of the protein between phospholipid surfaces.

Sequence similarities

Belongs to the paraoxonase family.

Ontologies

Keywords
   Cellular componentHDL
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaromatic compound catabolic process

Inferred from direct assay Ref.20. Source: BHF-UCL

carboxylic acid catabolic process

Inferred from direct assay Ref.17. Source: BHF-UCL

dephosphorylation

Inferred from direct assay Ref.24Ref.17. Source: GOC

organophosphate catabolic process

Inferred from direct assay Ref.17. Source: BHF-UCL

phosphatidylcholine metabolic process

Inferred from direct assay PubMed 15721011. Source: BHF-UCL

positive regulation of binding

Inferred from direct assay PubMed 15721011. Source: BHF-UCL

positive regulation of cholesterol efflux

Inferred from direct assay PubMed 15721011. Source: BHF-UCL

positive regulation of transporter activity

Inferred from direct assay PubMed 15721011. Source: BHF-UCL

response to external stimulus

Non-traceable author statement Ref.1. Source: UniProtKB

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay Ref.17. Source: BHF-UCL

high-density lipoprotein particle

Inferred from direct assay PubMed 15721011. Source: BHF-UCL

intracellular membrane-bounded organelle

Inferred from electronic annotation. Source: Ensembl

spherical high-density lipoprotein particle

Inferred from direct assay PubMed 16682745. Source: BHF-UCL

   Molecular_functionaryldialkylphosphatase activity

Inferred from direct assay Ref.24. Source: UniProtKB

arylesterase activity

Inferred from direct assay Ref.24. Source: UniProtKB

calcium ion binding

Inferred from direct assay Ref.24. Source: UniProtKB

phospholipid binding

Inferred from direct assay Ref.18. Source: BHF-UCL

protein homodimerization activity

Inferred from direct assay Ref.20. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13 Ref.14 Ref.15
Chain2 – 355354Serum paraoxonase/arylesterase 1
PRO_0000223281
Signal peptide2 – ?Not cleaved

Sites

Active site1151Proton acceptor Probable
Metal binding531Calcium 1; catalytic
Metal binding541Calcium 2
Metal binding1171Calcium 2; via carbonyl oxygen
Metal binding1681Calcium 1; catalytic
Metal binding1691Calcium 2
Metal binding2241Calcium 1; catalytic
Metal binding2691Calcium 1; catalytic
Metal binding2701Calcium 1; catalytic

Amino acid modifications

Glycosylation2271N-linked (GlcNAc...) Ref.21
Glycosylation2531N-linked (GlcNAc...) Ref.19 Ref.21 Ref.23
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Ref.21 Ref.23
Disulfide bond42 ↔ 353In form B Ref.14 Ref.24

Natural variations

Natural variant551L → M. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Corresponds to variant rs854560 [ dbSNP | Ensembl ].
VAR_006043
Natural variant1021I → V Polymorphism associated with decreased activity that seems to be associated with an increased risk for prostate cancer. Ref.27
VAR_015882
Natural variant1601R → G.
Corresponds to variant rs13306698 [ dbSNP | Ensembl ].
VAR_055342
Natural variant1921Q → R Polymorphism important for activity. Ref.1 Ref.2 Ref.3 Ref.4 Ref.8 Ref.25 Ref.28
Corresponds to variant rs662 [ dbSNP | Ensembl ].
VAR_006044

Experimental info

Mutagenesis20 – 212HQ → AA: The signal peptide is cleaved; not associated with HDL. Ref.18
Mutagenesis1151H → Q: Reduces activity 10000-fold. Ref.18 Ref.24
Mutagenesis1341H → Q: Substantially reduced activity. Ref.18 Ref.24
Mutagenesis2841C → A or S: No loss of activity. Ref.17 Ref.18

Secondary structure

.................................................................. 355
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27169 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: 9B5895509166167E

FASTA35539,731
        10         20         30         40         50         60 
MAKLIALTLL GMGLALFRNH QSSYQTRLNA LREVQPVELP NCNLVKGIET GSEDLEILPN 

        70         80         90        100        110        120 
GLAFISSGLK YPGIKSFNPN SPGKILLMDL NEEDPTVLEL GITGSKFDVS SFNPHGISTF 

       130        140        150        160        170        180 
TDEDNAMYLL VVNHPDAKST VELFKFQEEE KSLLHLKTIR HKLLPNLNDI VAVGPEHFYG 

       190        200        210        220        230        240 
TNDHYFLDPY LQSWEMYLGL AWSYVVYYSP SEVRVVAEGF DFANGINISP DGKYVYIAEL 

       250        260        270        280        290        300 
LAHKIHVYEK HANWTLTPLK SLDFNTLVDN ISVDPETGDL WVGCHPNGMK IFFYDSENPP 

       310        320        330        340        350 
ASEVLRIQNI LTEEPKVTQV YAENGTVLQG STVASVYKGK LLIGTVFHKA LYCEL 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence."
Hassett C., Richter R.J., Humbert R., Chapline C., Crabb J.W., Omiecinski C.J., Furlong C.E.
Biochemistry 30:10141-10149(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-55 AND ARG-192.
Tissue: Liver.
[2]"Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B allozymes."
Adkins S., Gan K.N., Mody M., La Du B.N.
Am. J. Hum. Genet. 52:598-608(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-55 AND ARG-192.
[3]"Studies on human serum paraoxonase/arylesterase."
La Du B.N., Adkins S., Kuo C.L., Lipsig D.
Chem. Biol. Interact. 87:25-34(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, VARIANTS MET-55 AND ARG-192.
Tissue: Liver.
[4]"Human and rabbit paraoxonases: purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification."
Furlong C.E., Costa L.G., Hassett C., Richter R.J., Sundstrom J.A., Adler D.A., Disteche C.M., Omiecinski C.J., Chapline C., Crabb J.W.
Chem. Biol. Interact. 87:35-48(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-55 AND ARG-192, CHARACTERIZATION.
Tissue: Liver.
[5]"Structural organization of the human PON1 gene."
Clendenning J.B., Humbert R., Green E.D., Wood C., Traver D., Furlong C.E.
Genomics 35:586-589(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-55.
Tissue: Lymphoblast.
[6]"Differential expression of a cDNA clone in human liver versus hepatic cancer -- highly homologous to aryl-dialkyl-phosphatase."
Wang K.K., Wan D.F., Qiu X.K., Lu P.X., Gu J.R.
Cell Res. 7:79-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[7]"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. expand/collapse author list , 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], VARIANT MET-55.
Tissue: Liver.
[8]SeattleSNPs variation discovery resource
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-192.
[9]"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. expand/collapse author list , 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].
[10]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]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. expand/collapse author list , 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].
[12]"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].
Tissue: Brain.
[13]"Identification of a distinct human high-density lipoprotein subspecies defined by a lipoprotein-associated protein, K-45. Identity of K-45 with paraoxonase."
Blatter M.-C., James R.W., Messmer S., Barja F., Pometta D.
Eur. J. Biochem. 211:871-879(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21, TISSUE SPECIFICITY.
[14]"Apolipoprotein J is associated with paraoxonase in human plasma."
Kelso G.J., Stuart W.D., Richter R.J., Furlong C.E., Jordan-Starck T.C., Harmony J.A.K.
Biochemistry 33:832-839(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21; 234-244; 291-305 AND 350-355, INTERACTION WITH CLU, TISSUE SPECIFICITY, DISULFIDE BOND.
Tissue: Plasma.
[15]"Purification of rabbit and human serum paraoxonase."
Furlong C.E., Richter R.J., Chapline C., Crabb J.W.
Biochemistry 30:10133-10140(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11, CATALYTIC ACTIVITY.
[16]"Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities."
Gan K.N., Smolen A., Eckerson H.W., La Du B.N.
Drug Metab. Dispos. 19:100-106(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[17]"Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase."
Sorenson R.C., Primo-Parmo S.L., Kuo C.-L., Adkins S., Lockridge O., La Du B.N.
Proc. Natl. Acad. Sci. U.S.A. 92:7187-7191(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-284.
[18]"Human serum paraoxonase/arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids: apolipoprotein A-I stabilizes activity."
Sorenson R.C., Bisgaier C.L., Aviram M., Hsu C., Billecke S., La Du B.N.
Arterioscler. Thromb. Vasc. Biol. 19:2214-2225(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 20-HIS-GLN-21, FUNCTION OF THE UNCLEAVED SIGNAL PEPTIDE.
[19]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253.
Tissue: Plasma.
[20]"Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities."
Draganov D.I., Teiber J.F., Speelman A., Osawa Y., Sunahara R., La Du B.N.
J. Lipid Res. 46:1239-1247(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[21]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227; ASN-253 AND ASN-324.
Tissue: Plasma.
[22]"Serendipitous discovery and X-ray structure of a human phosphate binding apolipoprotein."
Morales R., Berna A., Carpentier P., Contreras-Martel C., Renault F., Nicodeme M., Chesne-Seck M.-L., Bernier F., Dupuy J., Schaeffer C., Diemer H., van Dorsselaer A., Fontecilla-Camps J.C., Masson P., Rochu D., Chabriere E.
Structure 14:601-609(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HPBP.
[23]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253 AND ASN-324.
Tissue: Liver.
[24]"Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes."
Harel M., Aharoni A., Gaidukov L., Brumshtein B., Khersonsky O., Meged R., Dvir H., Ravelli R.B.G., McCarthy A., Toker L., Silman I., Sussman J.L., Tawfik D.S.
Nat. Struct. Mol. Biol. 11:412-419(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, MUTAGENESIS OF HIS-115 AND HIS-134, CATALYTIC ACTIVITY, DISULFIDE BOND.
[25]"The molecular basis of the human serum paraoxonase activity polymorphism."
Humbert R., Adler D.A., Disteche C.M., Hassett C., Omiecinski C.J., Furlong C.E.
Nat. Genet. 3:73-76(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-192.
[26]"A variant of paraoxonase (PON1) gene is associated with diabetic retinopathy in IDDM."
Kao Y.-L., Donaghue K., Chan A., Knight J., Silink M.
J. Clin. Endocrinol. Metab. 83:2589-2592(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH DIABETIC RETINOPATHY SUSCEPTIBILITY.
[27]"New paraoxonase 1 polymorphism I102V and the risk of prostate cancer in Finnish men."
Marchesani M., Hakkarainen A., Tuomainen T.P., Kaikkonen J., Pukkala E., Uimari P., Seppala E., Matikainen M., Kallioniemi O.-P., Schleutker J., Lehtimaki T., Salonen J.T.
J. Natl. Cancer Inst. 95:812-818(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-102.
[28]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-192.
+Additional computationally mapped references.

Web resources

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63012 mRNA. Translation: AAB59538.1.
M63013 mRNA. Translation: AAA60142.1.
M63014 mRNA. Translation: AAA60143.1.
S56555, S56546, S56548 Genomic DNA. Translation: AAB25717.1.
S64696 mRNA. Translation: AAB27899.1.
S64615 mRNA. Translation: AAB27714.2.
U55885 expand/collapse EMBL AC list , U55877, U55878, U55879, U55880, U55881, U55882, U55883 Genomic DNA. Translation: AAB41835.1.
D84371 mRNA. Translation: BAA12327.1.
U53784 mRNA. Translation: AAA97957.1.
Z70723 mRNA. Translation: CAA94728.1.
AK314027 mRNA. Translation: BAG36737.1.
AF539592 Genomic DNA. Translation: AAM97935.1.
AC004022 Genomic DNA. Translation: AAC35293.1.
CH236949 Genomic DNA. Translation: EAL24133.1.
CH471091 Genomic DNA. Translation: EAW76771.1.
BC074719 mRNA. Translation: AAH74719.1.
PIRA45451.
RefSeqNP_000437.3. NM_000446.5.
UniGeneHs.370995.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V04X-ray2.20A1-353[»]
1XHRmodel-A40-355[»]
ProteinModelPortalP27169.
SMRP27169. Positions 20-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111440. 2 interactions.
STRING9606.ENSP00000222381.

Chemistry

BindingDBP27169.
ChEMBLCHEMBL3167.
DrugBankDB01076. Atorvastatin.
DB01327. Cefazolin.

Protein family/group databases

TCDB1.A.6.2.6. the epithelial na(+) channel (enac) family.

PTM databases

PhosphoSiteP27169.

Polymorphism databases

DMDM308153572.

2D gel databases

SWISS-2DPAGEP27169.

Proteomic databases

PaxDbP27169.
PeptideAtlasP27169.
PRIDEP27169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222381; ENSP00000222381; ENSG00000005421.
GeneID5444.
KEGGhsa:5444.
UCSCuc003uns.3. human.

Organism-specific databases

CTD5444.
GeneCardsGC07M094926.
H-InvDBHIX0033662.
HGNCHGNC:9204. PON1.
HPAHPA001610.
MIM168820. gene+phenotype.
612633. phenotype.
neXtProtNX_P27169.
Orphanet803. Amyotrophic lateral sclerosis.
PharmGKBPA33529.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68009.
HOGENOMHOG000252960.
HOVERGENHBG003604.
InParanoidP27169.
KOK01045.
PhylomeDBP27169.
TreeFamTF322436.

Enzyme and pathway databases

BRENDA3.1.1.2. 2681.
SABIO-RKP27169.

Gene expression databases

ArrayExpressP27169.
BgeeP27169.
CleanExHS_PON1.
GenevestigatorP27169.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008363. Paraoxonase1.
[Graphical view]
PfamPF01731. Arylesterase. 1 hit.
[Graphical view]
PRINTSPR01785. PARAOXONASE.
PR01786. PARAOXONASE1.
ProtoNetSearch...

Other

ChiTaRSPON1. human.
EvolutionaryTraceP27169.
GeneWikiPON1.
GenomeRNAi5444.
NextBio21069.
PROP27169.
SOURCESearch...

Entry information

Entry namePON1_HUMAN
AccessionPrimary (citable) accession number: P27169
Secondary accession number(s): B2RA40 expand/collapse secondary AC list , Q16052, Q6B0J6, Q9UCB1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

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