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P47712

- PA24A_HUMAN

UniProt

P47712 - PA24A_HUMAN

Protein

Cytosolic phospholipase A2

Gene

PLA2G4A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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 activityi

    Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
    2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

    Enzyme regulationi

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

    Kineticsi

      Vmax=2.7 µmol/min/mg enzyme for the phospholipase A2 reaction1 Publication

      Vmax=4.6 µmol/min/mg enzyme for the lysophosphatase reaction1 Publication

      Sites

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Metal bindingi40 – 401Calcium 1
      Metal bindingi40 – 401Calcium 2
      Metal bindingi41 – 411Calcium 1; via carbonyl oxygen
      Metal bindingi43 – 431Calcium 1
      Metal bindingi43 – 431Calcium 2
      Metal bindingi65 – 651Calcium 1
      Metal bindingi93 – 931Calcium 2
      Metal bindingi94 – 941Calcium 2; via carbonyl oxygen
      Metal bindingi95 – 951Calcium 2
      Active sitei228 – 2281Nucleophile
      Active sitei549 – 5491Proton acceptor

      GO - Molecular functioni

      1. calcium-dependent phospholipase A2 activity Source: Reactome
      2. calcium-dependent phospholipid binding Source: UniProtKB
      3. calcium ion binding Source: UniProtKB
      4. lysophospholipase activity Source: UniProtKB-EC
      5. phospholipase A2 activity Source: UniProtKB

      GO - Biological processi

      1. arachidonic acid metabolic process Source: Reactome
      2. arachidonic acid secretion Source: Ensembl
      3. blood coagulation Source: Reactome
      4. cardiolipin acyl-chain remodeling Source: Reactome
      5. cellular response to antibiotic Source: Ensembl
      6. glycerophospholipid biosynthetic process Source: Reactome
      7. icosanoid biosynthetic process Source: Ensembl
      8. icosanoid metabolic process Source: UniProtKB
      9. phosphatidic acid biosynthetic process Source: Reactome
      10. phosphatidylcholine acyl-chain remodeling Source: Reactome
      11. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
      12. phosphatidylglycerol acyl-chain remodeling Source: Reactome
      13. phosphatidylinositol acyl-chain remodeling Source: Reactome
      14. phosphatidylserine acyl-chain remodeling Source: Reactome
      15. phospholipid catabolic process Source: InterPro
      16. phospholipid metabolic process Source: Reactome
      17. platelet activating factor biosynthetic process Source: UniProtKB
      18. platelet activation Source: Reactome
      19. regulation of cell proliferation Source: Ensembl
      20. small molecule metabolic process Source: Reactome

      Keywords - Molecular functioni

      Hydrolase

      Keywords - Biological processi

      Lipid degradation, Lipid metabolism

      Keywords - Ligandi

      Calcium, Metal-binding

      Enzyme and pathway databases

      BRENDAi3.1.1.4. 2681.
      ReactomeiREACT_120722. Acyl chain remodelling of PI.
      REACT_120829. Acyl chain remodelling of PC.
      REACT_120906. Synthesis of PA.
      REACT_120977. Hydrolysis of LPC.
      REACT_121006. Acyl chain remodeling of CL.
      REACT_121324. Acyl chain remodelling of PG.
      REACT_121369. Acyl chain remodelling of PE.
      REACT_121384. Acyl chain remodelling of PS.
      REACT_147851. Arachidonic acid metabolism.
      REACT_15466. phospho-PLA2 pathway.
      REACT_19140. ADP signalling through P2Y purinoceptor 1.
      REACT_23879. Platelet sensitization by LDL.

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Cytosolic phospholipase A2
      Short name:
      cPLA2
      Alternative name(s):
      Phospholipase A2 group IVA
      Including the following 2 domains:
      Phospholipase A2 (EC:3.1.1.4)
      Alternative name(s):
      Phosphatidylcholine 2-acylhydrolase
      Lysophospholipase (EC:3.1.1.5)
      Gene namesi
      Name:PLA2G4A
      Synonyms:CPLA2, PLA2G4
      OrganismiHomo sapiens (Human)
      Taxonomic identifieri9606 [NCBI]
      Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
      ProteomesiUP000005640: Chromosome 1

      Organism-specific databases

      HGNCiHGNC:9035. PLA2G4A.

      Subcellular locationi

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

      GO - Cellular componenti

      1. cytoplasm Source: HPA
      2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
      3. cytosol Source: UniProtKB
      4. endoplasmic reticulum membrane Source: Reactome
      5. Golgi apparatus Source: Ensembl
      6. mitochondrial inner membrane Source: Reactome

      Keywords - Cellular componenti

      Cytoplasm, Cytoplasmic vesicle

      Pathology & Biotechi

      Involvement in diseasei

      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 (PubMed:18451993).1 Publication

      Mutagenesis

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Mutagenesisi139 – 1391C → A: No effect on phospholipase activity; when associated with A-141 and A-151. 1 Publication
      Mutagenesisi141 – 1411C → A: No effect on phospholipase activity; when associated with A-139 and A-151. 1 Publication
      Mutagenesisi151 – 1511C → A: No effect on phospholipase activity; when associated with A-139 and A-141. 1 Publication
      Mutagenesisi195 – 1951S → A: 5-fold reduced phospholipase and lysophosphatase activities. 100-fold reduced phospholipase and lysophosphatase activities; when associated with A-577. 1 Publication
      Mutagenesisi200 – 2001R → A or H: Abolishes phospholipase activity. 1 Publication
      Mutagenesisi200 – 2001R → K: Reduces phospholipase activity 200-fold. 1 Publication
      Mutagenesisi215 – 2151S → A: No effect on phospholipase or lysophosphatase activity. 1 Publication
      Mutagenesisi220 – 2201C → A: No effect on phospholipase activity. 1 Publication
      Mutagenesisi228 – 2281S → A, C or T: Abolishes both phospholipase and lysophosphatase activities. 3 Publications
      Mutagenesisi324 – 3241C → A: No effect on phospholipase activity; when associated with A-331. 1 Publication
      Mutagenesisi331 – 3311C → A: No effect on phospholipase activity; when associated with A-324. 1 Publication
      Mutagenesisi505 – 5051S → A: Decreases agonist-stimulated release of arachidonic acid. 1 Publication
      Mutagenesisi549 – 5491D → A: Abolishes phospholipiase activity. 1 Publication
      Mutagenesisi549 – 5491D → E: Reduces phospholipiase activity 2000-fold. 1 Publication
      Mutagenesisi549 – 5491D → N: Reduces phospholipiase activity 300-fold. 1 Publication
      Mutagenesisi577 – 5771S → A: 7-fold reduced phospholipase and lysophosphatase activities. 100-fold reduced phospholipase and lysophosphatase activities; when associated with A-195. 1 Publication
      Mutagenesisi620 – 6201C → A: No effect on phospholipase activity; when associated with A-634. 1 Publication
      Mutagenesisi634 – 6341C → A: No effect on phospholipase activity; when associated with A-620. 1 Publication
      Mutagenesisi726 – 7261C → A: No effect on phospholipase activity. 1 Publication

      Keywords - Diseasei

      Disease mutation

      Organism-specific databases

      PharmGKBiPA271.

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 749749Cytosolic phospholipase A2PRO_0000187262Add
      BLAST

      Amino acid modifications

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Modified residuei268 – 2681Phosphothreonine2 Publications
      Modified residuei437 – 4371Phosphoserine3 Publications
      Modified residuei505 – 5051Phosphoserine; by MAPK2 Publications
      Modified residuei727 – 7271Phosphoserine2 Publications
      Modified residuei729 – 7291Phosphoserine3 Publications

      Post-translational modificationi

      Activated by phosphorylation at both Ser-505 and Ser-727.6 Publications

      Keywords - PTMi

      Phosphoprotein

      Proteomic databases

      MaxQBiP47712.
      PaxDbiP47712.
      PRIDEiP47712.

      PTM databases

      PhosphoSiteiP47712.

      Miscellaneous databases

      PMAP-CutDBP47712.

      Expressioni

      Tissue specificityi

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

      Gene expression databases

      ArrayExpressiP47712.
      BgeeiP47712.
      CleanExiHS_PLA2G4A.
      GenevestigatoriP47712.

      Organism-specific databases

      HPAiCAB010050.
      HPA050062.

      Interactioni

      Subunit structurei

      Interacts with KAT5.4 Publications

      Protein-protein interaction databases

      BioGridi111338. 6 interactions.
      IntActiP47712. 1 interaction.
      MINTiMINT-118843.
      STRINGi9606.ENSP00000356436.

      Structurei

      Secondary structure

      1
      749
      Legend: HelixTurnBeta strand
      Show more details
      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Beta strandi18 – 2912
      Helixi34 – 396
      Beta strandi44 – 496
      Beta strandi51 – 544
      Beta strandi57 – 604
      Beta strandi70 – 7910
      Beta strandi86 – 938
      Beta strandi96 – 983
      Beta strandi100 – 1089
      Helixi109 – 1113
      Beta strandi117 – 1248
      Turni125 – 1273
      Beta strandi128 – 13710
      Beta strandi143 – 1464
      Helixi152 – 17726
      Helixi179 – 1813
      Beta strandi190 – 1945
      Helixi198 – 21417
      Helixi218 – 2203
      Beta strandi221 – 2266
      Helixi228 – 23912
      Turni241 – 2455
      Helixi248 – 26013
      Helixi263 – 2664
      Helixi269 – 28416
      Helixi291 – 30414
      Helixi305 – 3073
      Helixi313 – 3186
      Turni319 – 3213
      Beta strandi326 – 3338
      Helixi341 – 3433
      Beta strandi344 – 3496
      Beta strandi354 – 3563
      Turni357 – 3604
      Beta strandi361 – 3633
      Helixi365 – 3673
      Beta strandi370 – 3734
      Beta strandi376 – 3794
      Helixi386 – 3938
      Helixi396 – 3994
      Helixi401 – 4044
      Helixi417 – 4237
      Helixi426 – 4294
      Helixi463 – 47614
      Beta strandi488 – 4903
      Turni492 – 4954
      Beta strandi543 – 5486
      Helixi550 – 5523
      Helixi558 – 5614
      Helixi564 – 5663
      Beta strandi570 – 5756
      Helixi588 – 59912
      Helixi611 – 6155
      Beta strandi619 – 6235
      Beta strandi636 – 6416
      Helixi646 – 6483
      Beta strandi650 – 6523
      Helixi660 – 6667
      Beta strandi670 – 6723
      Helixi687 – 70216
      Helixi705 – 71814

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      EntryMethodResolution (Å)ChainPositionsPDBsum
      1BCINMR-A1-138[»]
      1CJYX-ray2.50A/B1-749[»]
      1RLWX-ray2.40A17-141[»]
      ProteinModelPortaliP47712.
      SMRiP47712. Positions 13-721.
      ModBaseiSearch...
      MobiDBiSearch...

      Miscellaneous databases

      EvolutionaryTraceiP47712.

      Family & Domainsi

      Domains and Repeats

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Domaini5 – 106102C2PROSITE-ProRule annotationAdd
      BLAST
      Domaini140 – 740601PLA2cPROSITE-ProRule annotationAdd
      BLAST

      Region

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Regioni1 – 178178Phospholipid bindingCuratedAdd
      BLAST

      Domaini

      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+.2 Publications

      Sequence similaritiesi

      Contains 1 C2 domain.PROSITE-ProRule annotation
      Contains 1 PLA2c domain.PROSITE-ProRule annotation

      Phylogenomic databases

      eggNOGiNOG257248.
      HOGENOMiHOG000115420.
      HOVERGENiHBG053479.
      InParanoidiP47712.
      KOiK16342.
      OMAiETLIHNR.
      OrthoDBiEOG73V6JM.
      PhylomeDBiP47712.
      TreeFamiTF325228.

      Family and domain databases

      Gene3Di2.60.40.150. 1 hit.
      InterProiIPR016035. Acyl_Trfase/lysoPLipase.
      IPR000008. C2_dom.
      IPR002642. LysoPLipase_cat_dom.
      [Graphical view]
      PfamiPF00168. C2. 1 hit.
      PF01735. PLA2_B. 1 hit.
      [Graphical view]
      SMARTiSM00239. C2. 1 hit.
      SM00022. PLAc. 1 hit.
      [Graphical view]
      SUPFAMiSSF49562. SSF49562. 1 hit.
      SSF52151. SSF52151. 1 hit.
      PROSITEiPS50004. C2. 1 hit.
      PS51210. PLA2C. 1 hit.
      [Graphical view]

      Sequencei

      Sequence statusi: Complete.

      P47712-1 [UniParc]FASTAAdd to Basket

      « Hide

      MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI    50
      STTPDSRKRT RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE 100
      TLGTATFTVS SMKVGEKKEV PFIFNQVTEM VLEMSLEVCS CPDLRFSMAL 150
      CDQEKTFRQQ RKEHIRESMK KLLGPKNSEG LHSARDVPVV AILGSGGGFR 200
      AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH PDFPEKGPEE 250
      INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG 300
      ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS 350
      PYEIGMAKYG TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL 400
      FNRVLGVSGS QSRGSTMEEE LENITTKHIV SNDSSDSDDE SHEPKGTENE 450
      DAGSDYQSDN QASWIHRMIM ALVSDSALFN TREGRAGKVH NFMLGLNLNT 500
      SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV KSKKIHVVDS 550
      GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN 600
      KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EKDCPTIIHF VLANINFRKY 650
      RAPGVPRETE EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMHFN 700
      TLNNIDVIKE AMVESIEYRR QNPSRCSVSL SNVEARRFFN KEFLSKPKA 749
      Length:749
      Mass (Da):85,239
      Last modified:January 11, 2011 - v2
      Checksum:iEE71CA0EBE617856
      GO

      Natural variant

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Natural varianti103 – 1031G → R.
      Corresponds to variant rs28395828 [ dbSNP | Ensembl ].
      VAR_029276
      Natural varianti111 – 1111S → P Probable disease-associated mutation found in a compound heterozygote affected by phospholipase A2 deficiency also carrying H-485. 1 Publication
      Corresponds to variant rs121434634 [ dbSNP | Ensembl ].
      VAR_070778
      Natural varianti224 – 2241V → I.1 Publication
      Corresponds to variant rs12720588 [ dbSNP | Ensembl ].
      VAR_018760
      Natural varianti442 – 4421H → Q in a breast cancer sample; somatic mutation. 1 Publication
      VAR_035826
      Natural varianti485 – 4851R → H Probable disease-associated mutation found in a compound heterozygote affected by phospholipase A2 deficiency also carrying P-111. 1 Publication
      Corresponds to variant rs121434635 [ dbSNP | Ensembl ].
      VAR_070779
      Natural varianti637 – 6371I → V.
      Corresponds to variant rs28395831 [ dbSNP | Ensembl ].
      VAR_062128
      Natural varianti651 – 6511R → K.5 Publications
      Corresponds to variant rs2307198 [ dbSNP | Ensembl ].
      VAR_018424

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      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.
      CCDSiCCDS1372.1.
      PIRiA39329.
      RefSeqiNP_077734.1. NM_024420.2.
      UniGeneiHs.497200.

      Genome annotation databases

      EnsembliENST00000367466; ENSP00000356436; ENSG00000116711.
      GeneIDi5321.
      KEGGihsa:5321.
      UCSCiuc001gsc.3. human.

      Polymorphism databases

      DMDMi317373312.

      Keywords - Coding sequence diversityi

      Polymorphism

      Cross-referencesi

      Web resourcesi

      NIEHS-SNPs
      Atlas of Genetics and Cytogenetics in Oncology and Haematology

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      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 .
      CCDSi CCDS1372.1.
      PIRi A39329.
      RefSeqi NP_077734.1. NM_024420.2.
      UniGenei Hs.497200.

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      Entry Method Resolution (Å) Chain Positions PDBsum
      1BCI NMR - A 1-138 [» ]
      1CJY X-ray 2.50 A/B 1-749 [» ]
      1RLW X-ray 2.40 A 17-141 [» ]
      ProteinModelPortali P47712.
      SMRi P47712. Positions 13-721.
      ModBasei Search...
      MobiDBi Search...

      Protein-protein interaction databases

      BioGridi 111338. 6 interactions.
      IntActi P47712. 1 interaction.
      MINTi MINT-118843.
      STRINGi 9606.ENSP00000356436.

      Chemistry

      BindingDBi P47712.
      ChEMBLi CHEMBL3816.
      DrugBanki DB00180. Flunisolide.
      DB00591. Fluocinolone Acetonide.
      DB01047. Fluocinonide.
      DB00324. Fluorometholone.
      DB00846. Flurandrenolide.
      DB00588. Fluticasone Propionate.
      DB00253. Medrysone.
      DB01103. Quinacrine.

      PTM databases

      PhosphoSitei P47712.

      Polymorphism databases

      DMDMi 317373312.

      Proteomic databases

      MaxQBi P47712.
      PaxDbi P47712.
      PRIDEi P47712.

      Protocols and materials databases

      Structural Biology Knowledgebase Search...

      Genome annotation databases

      Ensembli ENST00000367466 ; ENSP00000356436 ; ENSG00000116711 .
      GeneIDi 5321.
      KEGGi hsa:5321.
      UCSCi uc001gsc.3. human.

      Organism-specific databases

      CTDi 5321.
      GeneCardsi GC01P186798.
      HGNCi HGNC:9035. PLA2G4A.
      HPAi CAB010050.
      HPA050062.
      MIMi 600522. gene.
      neXtProti NX_P47712.
      PharmGKBi PA271.
      GenAtlasi Search...

      Phylogenomic databases

      eggNOGi NOG257248.
      HOGENOMi HOG000115420.
      HOVERGENi HBG053479.
      InParanoidi P47712.
      KOi K16342.
      OMAi ETLIHNR.
      OrthoDBi EOG73V6JM.
      PhylomeDBi P47712.
      TreeFami TF325228.

      Enzyme and pathway databases

      BRENDAi 3.1.1.4. 2681.
      Reactomei REACT_120722. Acyl chain remodelling of PI.
      REACT_120829. Acyl chain remodelling of PC.
      REACT_120906. Synthesis of PA.
      REACT_120977. Hydrolysis of LPC.
      REACT_121006. Acyl chain remodeling of CL.
      REACT_121324. Acyl chain remodelling of PG.
      REACT_121369. Acyl chain remodelling of PE.
      REACT_121384. Acyl chain remodelling of PS.
      REACT_147851. Arachidonic acid metabolism.
      REACT_15466. phospho-PLA2 pathway.
      REACT_19140. ADP signalling through P2Y purinoceptor 1.
      REACT_23879. Platelet sensitization by LDL.

      Miscellaneous databases

      EvolutionaryTracei P47712.
      GeneWikii PLA2G4A.
      GenomeRNAii 5321.
      NextBioi 20586.
      PMAP-CutDB P47712.
      PROi P47712.
      SOURCEi Search...

      Gene expression databases

      ArrayExpressi P47712.
      Bgeei P47712.
      CleanExi HS_PLA2G4A.
      Genevestigatori P47712.

      Family and domain databases

      Gene3Di 2.60.40.150. 1 hit.
      InterProi IPR016035. Acyl_Trfase/lysoPLipase.
      IPR000008. C2_dom.
      IPR002642. LysoPLipase_cat_dom.
      [Graphical view ]
      Pfami PF00168. C2. 1 hit.
      PF01735. PLA2_B. 1 hit.
      [Graphical view ]
      SMARTi SM00239. C2. 1 hit.
      SM00022. PLAc. 1 hit.
      [Graphical view ]
      SUPFAMi SSF49562. SSF49562. 1 hit.
      SSF52151. SSF52151. 1 hit.
      PROSITEi PS50004. C2. 1 hit.
      PS51210. PLA2C. 1 hit.
      [Graphical view ]
      ProtoNeti Search...

      Publicationsi

      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.
        , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
        Tissue: Platelet.
      16. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-442.

      Entry informationi

      Entry nameiPA24A_HUMAN
      AccessioniPrimary (citable) accession number: P47712
      Secondary accession number(s): B1AKG4, Q29R80
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: February 1, 1996
      Last sequence update: January 11, 2011
      Last modified: October 1, 2014
      This is version 157 of the entry and version 2 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 1
        Human chromosome 1: 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