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P27169

- PON1_HUMAN

UniProt

P27169 - PON1_HUMAN

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Protein
Serum paraoxonase/arylesterase 1
Gene
PON1, PON
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

A phenyl acetate + H2O = a phenol + acetate.5 Publications
An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.5 Publications
An N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine.5 Publications

Cofactori

Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Calcium 1; catalytic
Metal bindingi54 – 541Calcium 2
Active sitei115 – 1151Proton acceptor Inferred
Metal bindingi117 – 1171Calcium 2; via carbonyl oxygen
Metal bindingi168 – 1681Calcium 1; catalytic
Metal bindingi169 – 1691Calcium 2
Metal bindingi224 – 2241Calcium 1; catalytic
Metal bindingi269 – 2691Calcium 1; catalytic
Metal bindingi270 – 2701Calcium 1; catalytic

GO - Molecular functioni

  1. aryldialkylphosphatase activity Source: UniProtKB
  2. arylesterase activity Source: UniProtKB
  3. calcium ion binding Source: UniProtKB
  4. phospholipid binding Source: BHF-UCL
  5. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. aromatic compound catabolic process Source: BHF-UCL
  2. carboxylic acid catabolic process Source: BHF-UCL
  3. dephosphorylation Source: GOC
  4. organophosphate catabolic process Source: BHF-UCL
  5. phosphatidylcholine metabolic process Source: BHF-UCL
  6. positive regulation of binding Source: BHF-UCL
  7. positive regulation of cholesterol efflux Source: BHF-UCL
  8. positive regulation of transporter activity Source: BHF-UCL
  9. response to external stimulus Source: UniProtKB
  10. response to toxic substance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.2. 2681.
SABIO-RKP27169.

Protein family/group databases

TCDBi1.A.6.2.6. the epithelial na(+) channel (enac) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Serum paraoxonase/arylesterase 1 (EC:3.1.1.2, EC:3.1.1.81, EC:3.1.8.1)
Short name:
PON 1
Alternative name(s):
Aromatic esterase 1
Short name:
A-esterase 1
K-45
Serum aryldialkylphosphatase 1
Gene namesi
Name:PON1
Synonyms:PON
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:9204. PON1.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProt
  5. high-density lipoprotein particle Source: BHF-UCL
  6. intracellular membrane-bounded organelle Source: Ensembl
  7. spherical high-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

HDL, Secreted

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 212HQ → AA: The signal peptide is cleaved; not associated with HDL. 1 Publication
Mutagenesisi115 – 1151H → Q: Reduces activity 10000-fold. 2 Publications
Mutagenesisi134 – 1341H → Q: Substantially reduced activity. 2 Publications
Mutagenesisi284 – 2841C → A or S: No loss of activity. 2 Publications

Organism-specific databases

MIMi168820. gene+phenotype.
612633. phenotype.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA33529.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 355354Serum paraoxonase/arylesterase 1
PRO_0000223281Add
BLAST
Signal peptidei2 – ?Not cleaved

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 353In form B2 Publications
Glycosylationi227 – 2271N-linked (GlcNAc...)1 Publication
Glycosylationi253 – 2531N-linked (GlcNAc...)3 Publications
Glycosylationi270 – 2701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi324 – 3241N-linked (GlcNAc...)2 Publications

Post-translational modificationi

Glycosylated.
The signal sequence is not cleaved.
Present in two forms, form B contains a disulfide bond, form A does not.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP27169.
PaxDbiP27169.
PeptideAtlasiP27169.
PRIDEiP27169.

2D gel databases

SWISS-2DPAGEP27169.

PTM databases

PhosphoSiteiP27169.

Expressioni

Tissue specificityi

Plasma, associated with HDL (at protein level). Expressed in liver, but not in heart, brain, placenta, lung, skeletal muscle, kidney or pancreas.2 Publications

Gene expression databases

ArrayExpressiP27169.
BgeeiP27169.
CleanExiHS_PON1.
GenevestigatoriP27169.

Organism-specific databases

HPAiHPA001610.

Interactioni

Subunit structurei

Homodimer. Heterooligomer with phosphate-binding protein (HPBP). Interacts with CLU.3 Publications

Protein-protein interaction databases

BioGridi111440. 2 interactions.
STRINGi9606.ENSP00000222381.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 279
Turni28 – 314
Beta strandi54 – 574
Beta strandi61 – 677
Beta strandi84 – 896
Beta strandi92 – 943
Beta strandi97 – 993
Beta strandi101 – 1033
Beta strandi105 – 1073
Helixi109 – 1113
Beta strandi114 – 1218
Beta strandi127 – 1337
Beta strandi140 – 1478
Turni148 – 1514
Beta strandi152 – 1598
Beta strandi165 – 17410
Beta strandi177 – 1837
Helixi189 – 1979
Beta strandi203 – 2086
Beta strandi213 – 22816
Beta strandi232 – 2398
Turni240 – 2434
Beta strandi244 – 2507
Beta strandi256 – 2638
Beta strandi265 – 2739
Turni275 – 2773
Beta strandi280 – 2867
Helixi288 – 2925
Beta strandi302 – 3087
Beta strandi312 – 3143
Beta strandi316 – 3238
Beta strandi325 – 3284
Beta strandi330 – 3378
Beta strandi340 – 3489
Beta strandi350 – 3534

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V04X-ray2.20A1-353[»]
1XHRmodel-A40-355[»]
ProteinModelPortaliP27169.
SMRiP27169. Positions 20-355.

Miscellaneous databases

EvolutionaryTraceiP27169.

Family & Domainsi

Sequence similaritiesi

Belongs to the paraoxonase family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG68009.
HOGENOMiHOG000252960.
HOVERGENiHBG003604.
InParanoidiP27169.
KOiK01045.
OMAiMVEFSIT.
PhylomeDBiP27169.
TreeFamiTF322436.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008363. Paraoxonase1.
[Graphical view]
PfamiPF01731. Arylesterase. 1 hit.
[Graphical view]
PRINTSiPR01785. PARAOXONASE.
PR01786. PARAOXONASE1.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27169-1 [UniParc]FASTAAdd to Basket

« Hide

MAKLIALTLL GMGLALFRNH QSSYQTRLNA LREVQPVELP NCNLVKGIET    50
GSEDLEILPN GLAFISSGLK YPGIKSFNPN SPGKILLMDL NEEDPTVLEL 100
GITGSKFDVS SFNPHGISTF TDEDNAMYLL VVNHPDAKST VELFKFQEEE 150
KSLLHLKTIR HKLLPNLNDI VAVGPEHFYG TNDHYFLDPY LQSWEMYLGL 200
AWSYVVYYSP SEVRVVAEGF DFANGINISP DGKYVYIAEL LAHKIHVYEK 250
HANWTLTPLK SLDFNTLVDN ISVDPETGDL WVGCHPNGMK IFFYDSENPP 300
ASEVLRIQNI LTEEPKVTQV YAENGTVLQG STVASVYKGK LLIGTVFHKA 350
LYCEL 355
Length:355
Mass (Da):39,731
Last modified:October 5, 2010 - v3
Checksum:i9B5895509166167E
GO

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551L → M.6 Publications
Corresponds to variant rs854560 [ dbSNP | Ensembl ].
VAR_006043
Natural varianti102 – 1021I → V Polymorphism associated with decreased activity that seems to be associated with an increased risk for prostate cancer. 1 Publication
VAR_015882
Natural varianti160 – 1601R → G.
Corresponds to variant rs13306698 [ dbSNP | Ensembl ].
VAR_055342
Natural varianti192 – 1921Q → R Polymorphism important for activity. 7 Publications
Corresponds to variant rs662 [ dbSNP | Ensembl ].
VAR_006044

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, 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.
CCDSiCCDS5638.1.
PIRiA45451.
RefSeqiNP_000437.3. NM_000446.5.
UniGeneiHs.370995.

Genome annotation databases

EnsembliENST00000222381; ENSP00000222381; ENSG00000005421.
GeneIDi5444.
KEGGihsa:5444.
UCSCiuc003uns.3. human.

Polymorphism databases

DMDMi308153572.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, 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 .
CCDSi CCDS5638.1.
PIRi A45451.
RefSeqi NP_000437.3. NM_000446.5.
UniGenei Hs.370995.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1V04 X-ray 2.20 A 1-353 [» ]
1XHR model - A 40-355 [» ]
ProteinModelPortali P27169.
SMRi P27169. Positions 20-355.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111440. 2 interactions.
STRINGi 9606.ENSP00000222381.

Chemistry

BindingDBi P27169.
ChEMBLi CHEMBL3167.
DrugBanki DB01076. Atorvastatin.
DB01327. Cefazolin.

Protein family/group databases

TCDBi 1.A.6.2.6. the epithelial na(+) channel (enac) family.

PTM databases

PhosphoSitei P27169.

Polymorphism databases

DMDMi 308153572.

2D gel databases

SWISS-2DPAGE P27169.

Proteomic databases

MaxQBi P27169.
PaxDbi P27169.
PeptideAtlasi P27169.
PRIDEi P27169.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222381 ; ENSP00000222381 ; ENSG00000005421 .
GeneIDi 5444.
KEGGi hsa:5444.
UCSCi uc003uns.3. human.

Organism-specific databases

CTDi 5444.
GeneCardsi GC07M094926.
H-InvDB HIX0033662.
HGNCi HGNC:9204. PON1.
HPAi HPA001610.
MIMi 168820. gene+phenotype.
612633. phenotype.
neXtProti NX_P27169.
Orphaneti 803. Amyotrophic lateral sclerosis.
PharmGKBi PA33529.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG68009.
HOGENOMi HOG000252960.
HOVERGENi HBG003604.
InParanoidi P27169.
KOi K01045.
OMAi MVEFSIT.
PhylomeDBi P27169.
TreeFami TF322436.

Enzyme and pathway databases

BRENDAi 3.1.1.2. 2681.
SABIO-RK P27169.

Miscellaneous databases

ChiTaRSi PON1. human.
EvolutionaryTracei P27169.
GeneWikii PON1.
GenomeRNAii 5444.
NextBioi 21069.
PROi P27169.
SOURCEi Search...

Gene expression databases

ArrayExpressi P27169.
Bgeei P27169.
CleanExi HS_PON1.
Genevestigatori P27169.

Family and domain databases

Gene3Di 2.120.10.30. 1 hit.
InterProi IPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008363. Paraoxonase1.
[Graphical view ]
Pfami PF01731. Arylesterase. 1 hit.
[Graphical view ]
PRINTSi PR01785. PARAOXONASE.
PR01786. PARAOXONASE1.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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.
    , 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. 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. 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. 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. Cited for: VARIANT VAL-102.
  28. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-192.

Entry informationi

Entry nameiPON1_HUMAN
AccessioniPrimary (citable) accession number: P27169
Secondary accession number(s): B2RA40
, Q16052, Q6B0J6, Q9UCB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 5, 2010
Last modified: September 3, 2014
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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