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P47712

- PA24A_HUMAN

UniProt

P47712 - PA24A_HUMAN

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Protein
Cytosolic phospholipase A2
Gene
PLA2G4A, CPLA2, PLA2G4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publications
2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.2 Publications

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 reaction

    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 – 2281Nucleophile4 Publications
    Active sitei549 – 5491Proton acceptor4 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. calcium-dependent phospholipase A2 activity Source: Reactome
    3. calcium-dependent phospholipid 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
    Complete GO annotation...

    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.2 Publications

    GO - Cellular componenti

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

    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 (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 A2
    PRO_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.

    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 KAT5.1 Publication

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    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.

    Miscellaneous databases

    EvolutionaryTraceiP47712.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 106102C2
    Add
    BLAST
    Domaini140 – 740601PLA2c
    Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 178178Phospholipid binding Inferred
    Add
    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.
    Contains 1 PLA2c domain.

    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

    « Hide 'large scale' publications
    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: September 3, 2014
    This is version 156 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

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