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P47712 (PA24A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. 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:
Cytosolic phospholipase A2

Short name=cPLA2
Alternative name(s):
Phospholipase A2 group IVA

Including the following 2 domains:

  1. Phospholipase A2
    EC=3.1.1.4
    Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
  2. Lysophospholipase
    EC=3.1.1.5
Gene names
Name:PLA2G4A
Synonyms:CPLA2, PLA2G4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length749 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. Ref.8 Ref.9

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate. Ref.8 Ref.9

Enzyme regulation

Stimulated by agonists such as ATP, EGF, thrombin and bradykinin as well as by cytosolic Ca2+.

Subunit structure

Interacts with KAT5. Ref.11

Subcellular location

Cytoplasm. Cytoplasmic vesicle. Note: Translocates to membrane vesicles in a calcium-dependent fashion. Ref.8 Ref.21

Tissue specificity

Expressed in various tissues such as macrophages, platelets, neutrophils, fibroblasts and lung endothelium.

Domain

The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca2+. Ref.20 Ref.21

Post-translational modification

Activated by phosphorylation at both Ser-505 and Ser-727.

Involvement in disease

PLA2G4A mutations resulting in phospholipase A2 deficiency have been found in a patient affected by recurrent episodes of multiple complicated ulcers of the small intestine, not due to cyclooxygenase inhibitors use. Disease features also include platelet dysfunction, and globally decreased eicosanoid synthesis (Ref.14).

Sequence similarities

Contains 1 C2 domain.

Contains 1 PLA2c domain.

Biophysicochemical properties

Kinetic parameters:

Vmax=2.7 µmol/min/mg enzyme for the phospholipase A2 reaction Ref.7

Vmax=4.6 µmol/min/mg enzyme for the lysophosphatase reaction

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCytoplasm
Cytoplasmic vesicle
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Traceable author statement. Source: Reactome

arachidonic acid secretion

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cardiolipin acyl-chain remodeling

Traceable author statement. Source: Reactome

cellular response to antibiotic

Inferred from electronic annotation. Source: Ensembl

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

icosanoid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

icosanoid metabolic process

Non-traceable author statement Ref.20. Source: UniProtKB

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylcholine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylethanolamine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylglycerol acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylinositol acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylserine acyl-chain remodeling

Traceable author statement. Source: Reactome

phospholipid catabolic process

Inferred from electronic annotation. Source: InterPro

phospholipid metabolic process

Traceable author statement. Source: Reactome

platelet activating factor biosynthetic process

Non-traceable author statement Ref.20. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Non-traceable author statement Ref.6. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

mitochondrial inner membrane

Traceable author statement. Source: Reactome

   Molecular_functioncalcium ion binding

Inferred from direct assay Ref.20Ref.21. Source: UniProtKB

calcium-dependent phospholipase A2 activity

Inferred from experiment. Source: Reactome

calcium-dependent phospholipid binding

Inferred from direct assay Ref.21. Source: UniProtKB

lysophospholipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phospholipase A2 activity

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 749749Cytosolic phospholipase A2
PRO_0000187262

Regions

Domain5 – 106102C2
Domain140 – 740601PLA2c
Region1 – 178178Phospholipid binding Probable

Sites

Active site2281Nucleophile Ref.7 Ref.8 Ref.9 Ref.22
Active site5491Proton acceptor Ref.7 Ref.8 Ref.9 Ref.22
Metal binding401Calcium 1
Metal binding401Calcium 2
Metal binding411Calcium 1; via carbonyl oxygen
Metal binding431Calcium 1
Metal binding431Calcium 2
Metal binding651Calcium 1
Metal binding931Calcium 2
Metal binding941Calcium 2; via carbonyl oxygen
Metal binding951Calcium 2

Amino acid modifications

Modified residue2681Phosphothreonine Ref.16 Ref.17
Modified residue4371Phosphoserine Ref.16 Ref.17 Ref.19
Modified residue5051Phosphoserine; by MAPK Ref.6 Ref.10
Modified residue7271Phosphoserine Ref.10 Ref.16
Modified residue7291Phosphoserine Ref.13 Ref.16 Ref.17

Natural variations

Natural variant1031G → R.
Corresponds to variant rs28395828 [ dbSNP | Ensembl ].
VAR_029276
Natural variant1111S → P Probable disease-associated mutation found in a compound heterozygote affected by phospholipase A2 deficiency also carrying H-485. Ref.14
Corresponds to variant rs121434634 [ dbSNP | Ensembl ].
VAR_070778
Natural variant2241V → I. Ref.3
Corresponds to variant rs12720588 [ dbSNP | Ensembl ].
VAR_018760
Natural variant4421H → Q in a breast cancer sample; somatic mutation. Ref.23
VAR_035826
Natural variant4851R → H Probable disease-associated mutation found in a compound heterozygote affected by phospholipase A2 deficiency also carrying P-111. Ref.14
Corresponds to variant rs121434635 [ dbSNP | Ensembl ].
VAR_070779
Natural variant6371I → V.
Corresponds to variant rs28395831 [ dbSNP | Ensembl ].
VAR_062128
Natural variant6511R → K. Ref.1 Ref.2 Ref.3 Ref.5 Ref.14
Corresponds to variant rs2307198 [ dbSNP | Ensembl ].
VAR_018424

Experimental info

Mutagenesis1391C → A: No effect on phospholipase activity; when associated with A-141 and A-151. Ref.7
Mutagenesis1411C → A: No effect on phospholipase activity; when associated with A-139 and A-151. Ref.7
Mutagenesis1511C → A: No effect on phospholipase activity; when associated with A-139 and A-141. Ref.7
Mutagenesis1951S → A: 5-fold reduced phospholipase and lysophosphatase activities. 100-fold reduced phospholipase and lysophosphatase activities; when associated with A-577. Ref.7
Mutagenesis2001R → A or H: Abolishes phospholipase activity. Ref.9
Mutagenesis2001R → K: Reduces phospholipase activity 200-fold. Ref.9
Mutagenesis2151S → A: No effect on phospholipase or lysophosphatase activity. Ref.7
Mutagenesis2201C → A: No effect on phospholipase activity. Ref.7
Mutagenesis2281S → A, C or T: Abolishes both phospholipase and lysophosphatase activities. Ref.7 Ref.8 Ref.9
Mutagenesis3241C → A: No effect on phospholipase activity; when associated with A-331. Ref.7
Mutagenesis3311C → A: No effect on phospholipase activity; when associated with A-324. Ref.7
Mutagenesis5051S → A: Decreases agonist-stimulated release of arachidonic acid. Ref.6
Mutagenesis5491D → A: Abolishes phospholipiase activity. Ref.9
Mutagenesis5491D → E: Reduces phospholipiase activity 2000-fold. Ref.9
Mutagenesis5491D → N: Reduces phospholipiase activity 300-fold. Ref.9
Mutagenesis5771S → A: 7-fold reduced phospholipase and lysophosphatase activities. 100-fold reduced phospholipase and lysophosphatase activities; when associated with A-195. Ref.7
Mutagenesis6201C → A: No effect on phospholipase activity; when associated with A-634. Ref.7
Mutagenesis6341C → A: No effect on phospholipase activity; when associated with A-620. Ref.7
Mutagenesis7261C → A: No effect on phospholipase activity. Ref.7

Secondary structure

.................................................................................................................. 749
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P47712 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: EE71CA0EBE617856

FASTA74985,239
        10         20         30         40         50         60 
MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI STTPDSRKRT 

        70         80         90        100        110        120 
RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE TLGTATFTVS SMKVGEKKEV 

       130        140        150        160        170        180 
PFIFNQVTEM VLEMSLEVCS CPDLRFSMAL CDQEKTFRQQ RKEHIRESMK KLLGPKNSEG 

       190        200        210        220        230        240 
LHSARDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH 

       250        260        270        280        290        300 
PDFPEKGPEE INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG 

       310        320        330        340        350        360 
ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG 

       370        380        390        400        410        420 
TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS QSRGSTMEEE 

       430        440        450        460        470        480 
LENITTKHIV SNDSSDSDDE SHEPKGTENE DAGSDYQSDN QASWIHRMIM ALVSDSALFN 

       490        500        510        520        530        540 
TREGRAGKVH NFMLGLNLNT SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV 

       550        560        570        580        590        600 
KSKKIHVVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN 

       610        620        630        640        650        660 
KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EKDCPTIIHF VLANINFRKY RAPGVPRETE 

       670        680        690        700        710        720 
EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMHFN TLNNIDVIKE AMVESIEYRR 

       730        740 
QNPSRCSVSL SNVEARRFFN KEFLSKPKA 

« Hide

References

« Hide 'large scale' references
[1]"A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP."
Clark J.D., Lin L.-L., Kriz R.W., Ramesha C.S., Sultzman L.A., Lin A.Y., Milona N., Knopf J.L.
Cell 65:1043-1051(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT LYS-651.
[2]"Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2."
Sharp J., White D., Chiou G., Goodson T., Gamboa G., McClure D., Burgett S., Hoskins J., Skatrud P., Sportsman J., Becker G., Kang L., Roberts E., Kramer R.
J. Biol. Chem. 266:14850-14853(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-651.
[3]NIEHS SNPs program
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-224 AND LYS-651.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 LYS-651.
[6]"cPLA2 is phosphorylated and activated by MAP kinase."
Lin L.-L., Wartmann M., Lin A.Y., Knopf J.L., Seth A., Davis R.J.
Cell 72:269-278(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-505, PHOSPHORYLATION AT SER-505.
[7]"Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2."
Sharp J.D., Pickard R.T., Chiou X.G., Manetta J.V., Kovacevic S., Miller J.R., Varshavsky A.D., Roberts E.F., Strifler B.A., Brems D.N., Kramer R.M.
J. Biol. Chem. 269:23250-23254(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE, MUTAGENESIS OF CYS-139; CYS-141; CYS-151; SER-195; SER-215; CYS-220; SER-228; CYS-324; CYS-331; SER-577; CYS-620; CYS-634 AND CYS-726, BIOPHYSICOCHEMICAL PROPERTIES.
[8]"Functional identification of the active-site nucleophile of the human 85-kDa cytosolic phospholipase A2."
Huang Z., Payette P., Abdullah K., Cromlish W.A., Kennedy B.P.
Biochemistry 35:3712-3721(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVE SITE, MUTAGENESIS OF SER-228.
[9]"Identification of essential residues for the catalytic function of 85-kDa cytosolic phospholipase A2. Probing the role of histidine, aspartic acid, cysteine, and arginine."
Pickard R.T., Chiou X.G., Strifler B.A., DeFelippis M.R., Hyslop P.A., Tebbe A.L., Yee Y.K., Reynolds L.J., Dennis E.A., Kramer R.M., Sharp J.D.
J. Biol. Chem. 271:19225-19231(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-200; SER-228 AND ASP-549.
[10]"Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells."
Boersch-Haubold A.G., Bartoli F., Asselin J., Dudler T., Kramer R.M., Apitz-Castro R., Watson S.P., Gelb M.H.
J. Biol. Chem. 273:4449-4458(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-505 AND SER-727.
[11]"PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production."
Sheridan A.M., Force T., Yoon H.J., O'Leary E., Choukroun G., Taheri M.R., Bonventre J.V.
Mol. Cell. Biol. 21:4470-4481(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KAT5.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Inherited human cPLA(2alpha) deficiency is associated with impaired eicosanoid biosynthesis, small intestinal ulceration, and platelet dysfunction."
Adler D.H., Cogan J.D., Phillips J.A., Schnetz-Boutaud N., Milne G.L., Iverson T., Stein J.A., Brenner D.A., Morrow J.D., Boutaud O., Oates J.A.
J. Clin. Invest. 118:2121-2131(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PHOSPHOLIPASE A2 DEFICIENCY, VARIANTS PRO-111; HIS-485 AND LYS-651.
[15]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; SER-437; SER-727 AND SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; SER-437 AND SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2."
Perisic O., Fong S., Lynch D.E., Bycroft M., Williams R.L.
J. Biol. Chem. 273:1596-1604(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 16-141 IN COMPLEX WITH CALCIUM IONS, DOMAIN.
[21]"Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2."
Xu G.-Y., McDonagh T., Yu H.-A., Nalefski E.A., Clark J.D., Cumming D.A.
J. Mol. Biol. 280:485-500(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-138 IN COMPLEX WITH CALCIUM IONS, DOMAIN, SUBCELLULAR LOCATION.
[22]"Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism."
Dessen A., Tang J., Schmidt H., Stahl M., Clark J.D., Seehra J., Somers W.S.
Cell 97:349-360(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, ACTIVE SITE.
[23]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-442.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M72393 mRNA. Translation: AAB00789.1.
M68874 mRNA. Translation: AAA60105.1.
AY552098 Genomic DNA. Translation: AAS45712.1.
AL022147 Genomic DNA. Translation: CAB42689.2.
AL049797, AL022147 Genomic DNA. Translation: CAI22252.1.
BC114340 mRNA. Translation: AAI14341.1.
CCDSCCDS1372.1.
PIRA39329.
RefSeqNP_077734.1. NM_024420.2.
UniGeneHs.497200.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCINMR-A1-138[»]
1CJYX-ray2.50A/B1-749[»]
1RLWX-ray2.40A17-141[»]
ProteinModelPortalP47712.
SMRP47712. Positions 13-721.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111338. 6 interactions.
IntActP47712. 1 interaction.
MINTMINT-118843.
STRING9606.ENSP00000356436.

Chemistry

BindingDBP47712.
ChEMBLCHEMBL3816.
DrugBankDB00180. Flunisolide.
DB00591. Fluocinolone Acetonide.
DB01047. Fluocinonide.
DB00324. Fluorometholone.
DB00846. Flurandrenolide.
DB00588. Fluticasone Propionate.
DB00253. Medrysone.
DB01103. Quinacrine.

PTM databases

PhosphoSiteP47712.

Polymorphism databases

DMDM317373312.

Proteomic databases

MaxQBP47712.
PaxDbP47712.
PRIDEP47712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367466; ENSP00000356436; ENSG00000116711.
GeneID5321.
KEGGhsa:5321.
UCSCuc001gsc.3. human.

Organism-specific databases

CTD5321.
GeneCardsGC01P186798.
HGNCHGNC:9035. PLA2G4A.
HPACAB010050.
HPA050062.
MIM600522. gene.
neXtProtNX_P47712.
PharmGKBPA271.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG257248.
HOGENOMHOG000115420.
HOVERGENHBG053479.
InParanoidP47712.
KOK16342.
OMAETLIHNR.
OrthoDBEOG73V6JM.
PhylomeDBP47712.
TreeFamTF325228.

Enzyme and pathway databases

BRENDA3.1.1.4. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP47712.
BgeeP47712.
CleanExHS_PLA2G4A.
GenevestigatorP47712.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR016035. Acyl_Trfase/lysoPLipase.
IPR000008. C2_dom.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF52151. SSF52151. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS51210. PLA2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP47712.
GeneWikiPLA2G4A.
GenomeRNAi5321.
NextBio20586.
PMAP-CutDBP47712.
PROP47712.
SOURCESearch...

Entry information

Entry namePA24A_HUMAN
AccessionPrimary (citable) accession number: P47712
Secondary accession number(s): B1AKG4, Q29R80
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 155 of the entry and version 2 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 1

Human chromosome 1: entries, gene names and cross-references to MIM