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Q13093

- PAFA_HUMAN

UniProt

Q13093 - PAFA_HUMAN

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Protein
Platelet-activating factor acetylhydrolase
Gene
PLA2G7, PAFAH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids.

Catalytic activityi

1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei273 – 2731Nucleophile1 Publication
Active sitei296 – 2961Charge relay system1 Publication
Active sitei351 – 3511Charge relay system1 Publication

GO - Molecular functioni

  1. 1-alkyl-2-acetylglycerophosphocholine esterase activity Source: UniProtKB-EC
  2. calcium-independent phospholipase A2 activity Source: BHF-UCL
  3. phospholipid binding Source: BHF-UCL

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. lipid catabolic process Source: UniProtKB-KW
  3. lipid oxidation Source: BHF-UCL
  4. low-density lipoprotein particle remodeling Source: BHF-UCL
  5. plasma lipoprotein particle oxidation Source: BHF-UCL
  6. positive regulation of inflammatory response Source: BHF-UCL
  7. positive regulation of monocyte chemotaxis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.4. 2681.
ReactomeiREACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
SABIO-RKQ13093.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-activating factor acetylhydrolase (EC:3.1.1.47)
Short name:
PAF acetylhydrolase
Alternative name(s):
1-alkyl-2-acetylglycerophosphocholine esterase
2-acetyl-1-alkylglycerophosphocholine esterase
Group-VIIA phospholipase A2
Short name:
gVIIA-PLA2
LDL-associated phospholipase A2
Short name:
LDL-PLA(2)
PAF 2-acylhydrolase
Gene namesi
Name:PLA2G7
Synonyms:PAFAH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9040. PLA2G7.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular region Source: Reactome
  3. low-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Platelet-activating factor acetylhydrolase deficiency (PAFAD) [MIM:614278]: An enzymatic deficiency that results in exacerbated bodily response to inflammatory agents. It can be associated with several disease states including inflammatory gastrointestinal disorders, asthma and atopy. Asthmatic individuals with PAFAD may manifest aggravated respiratory symptoms.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti279 – 2791V → F in PAFAD; loss of function; risk factor for coronary arthery disease and stroke. 4 Publications
Corresponds to variant rs16874954 [ dbSNP | Ensembl ].
VAR_004268
Natural varianti281 – 2811Q → R in PAFAD; loss of function. 1 Publication
VAR_011585
Asthma (ASTHMA) [MIM:600807]: The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with wheezing due to spasmodic contraction of the bronchi.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication
Atopic hypersensitivity (ATOPY) [MIM:147050]: A condition characterized by predisposition to develop hypersensitivity reactions. Atopic individuals can develop eczema, allergic rhinitis and allergic asthma.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081S → A: Activity is higher than wild-type.
Mutagenesisi273 – 2731S → A: Loss of activity.
Mutagenesisi286 – 2861D → A: Almost no activity.
Mutagenesisi286 – 2861D → N: Diminishes activity.
Mutagenesisi296 – 2961D → A: Loss of activity.
Mutagenesisi296 – 2961D → N: Loss of activity.
Mutagenesisi304 – 3041D → A: No change in activity.
Mutagenesisi338 – 3381D → A: Activity is higher than wild-type.
Mutagenesisi351 – 3511H → A: Loss of activity.

Keywords - Diseasei

Asthma, Disease mutation

Organism-specific databases

MIMi147050. phenotype.
600807. phenotype.
614278. phenotype.
PharmGKBiPA33368.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121
Add
BLAST
Chaini22 – 441420Platelet-activating factor acetylhydrolase
PRO_0000017833Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi423 – 4231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi433 – 4331N-linked (GlcNAc...)

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ13093.
PaxDbiQ13093.
PRIDEiQ13093.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

ArrayExpressiQ13093.
BgeeiQ13093.
CleanExiHS_PLA2G7.
GenevestigatoriQ13093.

Organism-specific databases

HPAiHPA035915.

Interactioni

Protein-protein interaction databases

BioGridi113667. 1 interaction.
IntActiQ13093. 3 interactions.
STRINGi9606.ENSP00000274793.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi54 – 563
Beta strandi61 – 7515
Beta strandi78 – 8811
Beta strandi95 – 984
Helixi101 – 11111
Helixi115 – 12511
Beta strandi129 – 1346
Beta strandi144 – 1507
Turni157 – 1604
Helixi161 – 1699
Beta strandi173 – 1775
Beta strandi184 – 1896
Helixi193 – 1986
Beta strandi202 – 2054
Helixi211 – 2133
Helixi214 – 24027
Helixi255 – 2584
Beta strandi262 – 27211
Helixi274 – 28512
Beta strandi291 – 2966
Helixi304 – 3085
Beta strandi314 – 3196
Turni320 – 3223
Helixi325 – 3328
Beta strandi337 – 3393
Beta strandi341 – 3466
Helixi351 – 3544
Helixi356 – 3594
Helixi363 – 3686
Helixi377 – 39620
Helixi402 – 4054
Helixi406 – 4094
Beta strandi416 – 4194

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D59X-ray1.50A/B47-429[»]
3D5EX-ray2.10A/B47-429[»]
3F96X-ray2.10A/B47-429[»]
3F97X-ray1.70A/B47-429[»]
3F98X-ray1.70A/B/C47-429[»]
3F9CX-ray2.30A/B47-429[»]
ProteinModelPortaliQ13093.
SMRiQ13093. Positions 54-427.

Miscellaneous databases

EvolutionaryTraceiQ13093.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4188.
HOGENOMiHOG000008053.
HOVERGENiHBG001322.
InParanoidiQ13093.
KOiK01062.
OMAiWLMGNIL.
OrthoDBiEOG7MSMQ5.
PhylomeDBiQ13093.
TreeFamiTF313831.

Family and domain databases

Gene3Di3.40.50.1820. 3 hits.
InterProiIPR029058. AB_hydrolase.
IPR005065. PAF_acetylhydro.
IPR016715. PAF_acetylhydro_eukaryote.
[Graphical view]
PANTHERiPTHR10272. PTHR10272. 1 hit.
PfamiPF03403. PAF-AH_p_II. 1 hit.
[Graphical view]
PIRSFiPIRSF018169. PAF_acetylhydrolase. 1 hit.
SUPFAMiSSF53474. SSF53474. 3 hits.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q13093-1 [UniParc]FASTAAdd to Basket

« Hide

MVPPKLHVLF CLCGCLAVVY PFDWQYINPV AHMKSSAWVN KIQVLMAAAS    50
FGQTKIPRGN GPYSVGCTDL MFDHTNKGTF LRLYYPSQDN DRLDTLWIPN 100
KEYFWGLSKF LGTHWLMGNI LRLLFGSMTT PANWNSPLRP GEKYPLVVFS 150
HGLGAFRTLY SAIGIDLASH GFIVAAVEHR DRSASATYYF KDQSAAEIGD 200
KSWLYLRTLK QEEETHIRNE QVRQRAKECS QALSLILDID HGKPVKNALD 250
LKFDMEQLKD SIDREKIAVI GHSFGGATVI QTLSEDQRFR CGIALDAWMF 300
PLGDEVYSRI PQPLFFINSE YFQYPANIIK MKKCYSPDKE RKMITIRGSV 350
HQNFADFTFA TGKIIGHMLK LKGDIDSNVA IDLSNKASLA FLQKHLGLHK 400
DFDQWDCLIE GDDENLIPGT NINTTNQHIM LQNSSGIEKY N 441
Length:441
Mass (Da):50,077
Last modified:November 1, 1997 - v1
Checksum:i3BA9EEA9E8094A57
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451L → P.1 Publication
Corresponds to variant rs45521937 [ dbSNP | Ensembl ].
VAR_047970
Natural varianti92 – 921R → H Common polymorphism. 2 Publications
Corresponds to variant rs1805017 [ dbSNP | Ensembl ].
VAR_011583
Natural varianti191 – 1911K → N.1 Publication
Corresponds to variant rs45454695 [ dbSNP | Ensembl ].
VAR_047971
Natural varianti198 – 1981I → T Common polymorphism; associated with asthma and atopy. 2 Publications
Corresponds to variant rs1805018 [ dbSNP | Ensembl ].
VAR_011584
Natural varianti279 – 2791V → F in PAFAD; loss of function; risk factor for coronary arthery disease and stroke. 4 Publications
Corresponds to variant rs16874954 [ dbSNP | Ensembl ].
VAR_004268
Natural varianti281 – 2811Q → R in PAFAD; loss of function. 1 Publication
VAR_011585
Natural varianti379 – 3791V → A Common polymorphism. 4 Publications
Corresponds to variant rs1051931 [ dbSNP | Ensembl ].
VAR_011586

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U20157 mRNA. Translation: AAC50126.1.
U24577 mRNA. Translation: AAB04170.1.
EF568110 Genomic DNA. Translation: ABQ01234.1.
AL591242 Genomic DNA. Translation: CAH73907.1.
CH471081 Genomic DNA. Translation: EAX04301.1.
BC038452 mRNA. Translation: AAH38452.1.
CCDSiCCDS4917.1.
PIRiS60247.
RefSeqiNP_001161829.1. NM_001168357.1.
NP_005075.3. NM_005084.3.
XP_005249465.1. XM_005249408.2.
UniGeneiHs.584823.

Genome annotation databases

EnsembliENST00000274793; ENSP00000274793; ENSG00000146070.
ENST00000537365; ENSP00000445666; ENSG00000146070.
GeneIDi7941.
KEGGihsa:7941.
UCSCiuc010jzf.3. human.

Polymorphism databases

DMDMi2497687.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U20157 mRNA. Translation: AAC50126.1 .
U24577 mRNA. Translation: AAB04170.1 .
EF568110 Genomic DNA. Translation: ABQ01234.1 .
AL591242 Genomic DNA. Translation: CAH73907.1 .
CH471081 Genomic DNA. Translation: EAX04301.1 .
BC038452 mRNA. Translation: AAH38452.1 .
CCDSi CCDS4917.1.
PIRi S60247.
RefSeqi NP_001161829.1. NM_001168357.1.
NP_005075.3. NM_005084.3.
XP_005249465.1. XM_005249408.2.
UniGenei Hs.584823.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3D59 X-ray 1.50 A/B 47-429 [» ]
3D5E X-ray 2.10 A/B 47-429 [» ]
3F96 X-ray 2.10 A/B 47-429 [» ]
3F97 X-ray 1.70 A/B 47-429 [» ]
3F98 X-ray 1.70 A/B/C 47-429 [» ]
3F9C X-ray 2.30 A/B 47-429 [» ]
ProteinModelPortali Q13093.
SMRi Q13093. Positions 54-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113667. 1 interaction.
IntActi Q13093. 3 interactions.
STRINGi 9606.ENSP00000274793.

Chemistry

BindingDBi Q13093.
ChEMBLi CHEMBL3514.
GuidetoPHARMACOLOGYi 1432.

Polymorphism databases

DMDMi 2497687.

Proteomic databases

MaxQBi Q13093.
PaxDbi Q13093.
PRIDEi Q13093.

Protocols and materials databases

DNASUi 7941.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274793 ; ENSP00000274793 ; ENSG00000146070 .
ENST00000537365 ; ENSP00000445666 ; ENSG00000146070 .
GeneIDi 7941.
KEGGi hsa:7941.
UCSCi uc010jzf.3. human.

Organism-specific databases

CTDi 7941.
GeneCardsi GC06M046719.
HGNCi HGNC:9040. PLA2G7.
HPAi HPA035915.
MIMi 147050. phenotype.
600807. phenotype.
601690. gene.
614278. phenotype.
neXtProti NX_Q13093.
PharmGKBi PA33368.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4188.
HOGENOMi HOG000008053.
HOVERGENi HBG001322.
InParanoidi Q13093.
KOi K01062.
OMAi WLMGNIL.
OrthoDBi EOG7MSMQ5.
PhylomeDBi Q13093.
TreeFami TF313831.

Enzyme and pathway databases

BRENDAi 3.1.1.4. 2681.
Reactomei REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
SABIO-RK Q13093.

Miscellaneous databases

EvolutionaryTracei Q13093.
GeneWikii Lipoprotein-associated_phospholipase_A2.
GenomeRNAii 7941.
NextBioi 30458.
PROi Q13093.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13093.
Bgeei Q13093.
CleanExi HS_PLA2G7.
Genevestigatori Q13093.

Family and domain databases

Gene3Di 3.40.50.1820. 3 hits.
InterProi IPR029058. AB_hydrolase.
IPR005065. PAF_acetylhydro.
IPR016715. PAF_acetylhydro_eukaryote.
[Graphical view ]
PANTHERi PTHR10272. PTHR10272. 1 hit.
Pfami PF03403. PAF-AH_p_II. 1 hit.
[Graphical view ]
PIRSFi PIRSF018169. PAF_acetylhydrolase. 1 hit.
SUPFAMi SSF53474. SSF53474. 3 hits.
PROSITEi PS00120. LIPASE_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-57.
    Tissue: Myeloid.
  2. "Purification, properties, sequencing, and cloning of a lipoprotein-associated, serine-dependent phospholipase involved in the oxidative modification of low-density lipoproteins."
    Tew D.G., Southan C., Rice S.Q.J., Lawrence M.P., Li H., Boyd H.F., Moores K., Gloger I.S., Macphee C.H.
    Arterioscler. Thromb. Vasc. Biol. 16:591-599(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Lymphoma.
  3. SeattleSNPs variation discovery resource
    Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-45; HIS-92; ASN-191; THR-198 AND ALA-379.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-379.
  6. "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], VARIANT ALA-379.
    Tissue: Blood.
  7. "Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad."
    Tjoelker L.W., Eberhardt C., Unger J., le Trong H., Zimmerman G.A., McIntyre T.M., Stafforini D.M., Prescott S.M., Gray P.W.
    J. Biol. Chem. 270:25481-25487(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  8. "Crystal structure of human plasma platelet-activating factor acetylhydrolase: structural implication to lipoprotein binding and catalysis."
    Samanta U., Bahnson B.J.
    J. Biol. Chem. 283:31617-31624(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 47-429 ALONE AND IN COMPLEX WITH PARAOXON, ACTIVE SITE.
  9. "Crystal structures of human group-VIIA phospholipase A2 inhibited by organophosphorus nerve agents exhibit non-aged complexes."
    Samanta U., Kirby S.D., Srinivasan P., Cerasoli D.M., Bahnson B.J.
    Biochem. Pharmacol. 78:420-429(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 47-429 IN COMPLEX WITH ORGANOPHOSPHORUS NERVE AGENTS.
  10. "Platelet-activating factor acetylhydrolase deficiency. A missense mutation near the active site of an anti-inflammatory phospholipase."
    Stafforini D.M., Satoh K., Atkinson D.L., Tjoelker L.W., Eberhardt C., Yoshida H., Imaizumi T., Takamatsu S., Zimmerman G.A., McIntyre T.M., Gray P.W., Prescott S.M.
    J. Clin. Invest. 97:2784-2791(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PAFAD PHE-279.
  11. "Loss of activity of plasma platelet-activating factor acetylhydrolase due to a novel Gln281-->Arg mutation."
    Yamada Y., Yokota M.
    Biochem. Biophys. Res. Commun. 236:772-775(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PAFAD ARG-281.
  12. "A mutation in plasma platelet-activating factor acetylhydrolase (Val279-->Phe) is a genetic risk factor for stroke."
    Hiramoto M., Yoshida H., Imaizumi T., Yoshimizu N., Satoh K.
    Stroke 28:2417-2420(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PAFAD PHE-279.
  13. "Identification of the G994--> T missense in exon 9 of the plasma platelet-activating factor acetylhydrolase gene as an independent risk factor for coronary artery disease in Japanese men."
    Yamada Y., Ichihara S., Fujimura T., Yokota M.
    Metabolism 47:177-181(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PAFAD PHE-279.
  14. "A mutation in plasma platelet-activating factor acetylhydrolase (Val279Phe) is a genetic risk factor for cerebral hemorrhage but not for hypertension."
    Yoshida H., Imaizumi T., Fujimoto K., Itaya H., Hiramoto M., Yoshimizu N., Fukushi K., Satoh K.
    Thromb. Haemost. 80:372-375(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PAFAD PHE-279.
  15. "The Ile198Thr and Ala379Val variants of plasmatic PAF-acetylhydrolase impair catalytical activities and are associated with atopy and asthma."
    Kruse S., Mao X.-Q., Heinzmann A., Blattmann S., Roberts M.H., Braun S., Gao P.-S., Forster J., Kuehr J., Hopkin J.M., Shirakawa T., Deichmann K.A.
    Am. J. Hum. Genet. 66:1522-1530(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HIS-92; THR-198 AND ALA-379, INVOLVEMENT IN ASTHMA AND ATOPY.

Entry informationi

Entry nameiPAFA_HUMAN
AccessioniPrimary (citable) accession number: Q13093
Secondary accession number(s): A5HTT5
, Q15692, Q5VTT1, Q8IVA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 142 of the entry and version 1 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 6
    Human chromosome 6: 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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