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P14555

- PA2GA_HUMAN

UniProt

P14555 - PA2GA_HUMAN

Protein

Phospholipase A2, membrane associated

Gene

PLA2G2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Thought to participate in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

    Catalytic activityi

    Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

    Cofactori

    Binds 1 calcium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi47 – 471Calcium; via carbonyl oxygen
    Metal bindingi49 – 491Calcium; via carbonyl oxygen
    Metal bindingi51 – 511Calcium; via carbonyl oxygen
    Active sitei67 – 671By similarity
    Metal bindingi68 – 681Calcium
    Active sitei111 – 1111By similarity

    GO - Molecular functioni

    1. calcium-dependent phospholipase A2 activity Source: UniProtKB
    2. calcium ion binding Source: InterPro
    3. phospholipase A2 activity Source: BHF-UCL
    4. phospholipid binding Source: BHF-UCL

    GO - Biological processi

    1. defense response to Gram-positive bacterium Source: BHF-UCL
    2. glycerophospholipid biosynthetic process Source: Reactome
    3. lipid catabolic process Source: UniProtKB-KW
    4. low-density lipoprotein particle remodeling Source: BHF-UCL
    5. phosphatidic acid biosynthetic process Source: Reactome
    6. phosphatidic acid metabolic process Source: BHF-UCL
    7. phosphatidylcholine acyl-chain remodeling Source: Reactome
    8. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
    9. phosphatidylglycerol acyl-chain remodeling Source: Reactome
    10. phosphatidylinositol acyl-chain remodeling Source: Reactome
    11. phosphatidylserine acyl-chain remodeling Source: Reactome
    12. phospholipid metabolic process Source: BHF-UCL
    13. positive regulation of inflammatory response Source: BHF-UCL
    14. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
    15. 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

    ReactomeiREACT_120722. Acyl chain remodelling of PI.
    REACT_120829. Acyl chain remodelling of PC.
    REACT_120906. Synthesis of PA.
    REACT_121324. Acyl chain remodelling of PG.
    REACT_121369. Acyl chain remodelling of PE.
    REACT_121384. Acyl chain remodelling of PS.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phospholipase A2, membrane associated (EC:3.1.1.4)
    Alternative name(s):
    GIIC sPLA2
    Group IIA phospholipase A2
    Non-pancreatic secretory phospholipase A2
    Short name:
    NPS-PLA2
    Phosphatidylcholine 2-acylhydrolase 2A
    Gene namesi
    Name:PLA2G2A
    Synonyms:PLA2B, PLA2L, RASF-A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9031. PLA2G2A.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: LIFEdb
    2. endoplasmic reticulum membrane Source: Reactome
    3. extracellular region Source: Reactome
    4. extracellular space Source: BHF-UCL
    5. secretory granule Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA270.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20204 PublicationsAdd
    BLAST
    Chaini21 – 144124Phospholipase A2, membrane associatedPRO_0000022750Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 137
    Disulfide bondi48 ↔ 64
    Disulfide bondi63 ↔ 117
    Disulfide bondi69 ↔ 144
    Disulfide bondi70 ↔ 110
    Disulfide bondi79 ↔ 103
    Disulfide bondi97 ↔ 108

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP14555.
    PeptideAtlasiP14555.
    PRIDEiP14555.

    PTM databases

    PhosphoSiteiP14555.

    Expressioni

    Gene expression databases

    BgeeiP14555.
    CleanExiHS_PLA2G2A.
    GenevestigatoriP14555.

    Organism-specific databases

    HPAiHPA015236.

    Interactioni

    Protein-protein interaction databases

    BioGridi111337. 20 interactions.
    IntActiP14555. 3 interactions.
    MINTiMINT-1206447.
    STRINGi9606.ENSP00000364252.

    Structurei

    Secondary structure

    1
    144
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 3312
    Helixi37 – 404
    Turni41 – 433
    Turni45 – 473
    Beta strandi48 – 503
    Helixi59 – 7618
    Beta strandi81 – 833
    Beta strandi88 – 914
    Beta strandi94 – 974
    Helixi102 – 12019
    Helixi122 – 1243
    Helixi127 – 1293
    Helixi134 – 1363

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AYPX-ray2.57A/B/C/D/E/F21-144[»]
    1BBCX-ray2.20A21-144[»]
    1DB4X-ray2.20A21-144[»]
    1DB5X-ray2.80A21-144[»]
    1DCYX-ray2.70A21-144[»]
    1J1AX-ray2.20A/B21-144[»]
    1KQUX-ray2.10A21-144[»]
    1KVOX-ray2.00A/B/C/D/E/F21-144[»]
    1N28X-ray1.50A/B21-144[»]
    1N29X-ray2.60A21-144[»]
    1PODX-ray2.10A21-144[»]
    1POEX-ray2.10A/B21-144[»]
    2GNYmodel-A21-144[»]
    3U8BX-ray2.30A21-144[»]
    3U8DX-ray1.80A/B21-144[»]
    3U8HX-ray2.30A/B21-144[»]
    3U8IX-ray1.10A/B21-144[»]
    ProteinModelPortaliP14555.
    SMRiP14555. Positions 21-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14555.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phospholipase A2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG271943.
    HOGENOMiHOG000231749.
    HOVERGENiHBG008137.
    InParanoidiP14555.
    KOiK01047.
    OMAiFNNDELN.
    OrthoDBiEOG7N63PF.
    PhylomeDBiP14555.
    TreeFamiTF319283.

    Family and domain databases

    Gene3Di1.20.90.10. 1 hit.
    InterProiIPR001211. PLipase_A2.
    IPR013090. PLipase_A2_AS.
    IPR016090. PLipase_A2_dom.
    [Graphical view]
    PANTHERiPTHR11716. PTHR11716. 1 hit.
    PfamiPF00068. Phospholip_A2_1. 1 hit.
    [Graphical view]
    PRINTSiPR00389. PHPHLIPASEA2.
    SMARTiSM00085. PA2c. 1 hit.
    [Graphical view]
    SUPFAMiSSF48619. SSF48619. 1 hit.
    PROSITEiPS00119. PA2_ASP. 1 hit.
    PS00118. PA2_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14555-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTLLLLAVI MIFGLLQAHG NLVNFHRMIK LTTGKEAALS YGFYGCHCGV    50
    GGRGSPKDAT DRCCVTHDCC YKRLEKRGCG TKFLSYKFSN SGSRITCAKQ 100
    DSCRSQLCEC DKAAATCFAR NKTTYNKKYQ YYSNKHCRGS TPRC 144
    Length:144
    Mass (Da):16,083
    Last modified:April 1, 1990 - v2
    Checksum:i923C5FA0C6979CDA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121I → Y in AAT73043. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191H → Y.1 Publication
    Corresponds to variant rs11573162 [ dbSNP | Ensembl ].
    VAR_018953

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22430 mRNA. Translation: AAA36550.1.
    M22431 Genomic DNA. Translation: AAA36549.1.
    AY656695 mRNA. Translation: AAT73043.1.
    CR456865 mRNA. Translation: CAG33146.1.
    AY462114 Genomic DNA. Translation: AAR16084.1.
    AL358253 Genomic DNA. Translation: CAH74017.1.
    AK291302 mRNA. Translation: BAF83991.1.
    CH471134 Genomic DNA. Translation: EAW94907.1.
    BC005919 mRNA. Translation: AAH05919.1.
    CCDSiCCDS201.1.
    PIRiA32862. PSHUYF.
    RefSeqiNP_000291.1. NM_000300.3.
    NP_001155199.1. NM_001161727.1.
    NP_001155200.1. NM_001161728.1.
    NP_001155201.1. NM_001161729.1.
    UniGeneiHs.466804.

    Genome annotation databases

    EnsembliENST00000375111; ENSP00000364252; ENSG00000188257.
    ENST00000400520; ENSP00000383364; ENSG00000188257.
    GeneIDi5320.
    KEGGihsa:5320.
    UCSCiuc001bcu.3. human.

    Polymorphism databases

    DMDMi129483.

    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
    M22430 mRNA. Translation: AAA36550.1 .
    M22431 Genomic DNA. Translation: AAA36549.1 .
    AY656695 mRNA. Translation: AAT73043.1 .
    CR456865 mRNA. Translation: CAG33146.1 .
    AY462114 Genomic DNA. Translation: AAR16084.1 .
    AL358253 Genomic DNA. Translation: CAH74017.1 .
    AK291302 mRNA. Translation: BAF83991.1 .
    CH471134 Genomic DNA. Translation: EAW94907.1 .
    BC005919 mRNA. Translation: AAH05919.1 .
    CCDSi CCDS201.1.
    PIRi A32862. PSHUYF.
    RefSeqi NP_000291.1. NM_000300.3.
    NP_001155199.1. NM_001161727.1.
    NP_001155200.1. NM_001161728.1.
    NP_001155201.1. NM_001161729.1.
    UniGenei Hs.466804.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AYP X-ray 2.57 A/B/C/D/E/F 21-144 [» ]
    1BBC X-ray 2.20 A 21-144 [» ]
    1DB4 X-ray 2.20 A 21-144 [» ]
    1DB5 X-ray 2.80 A 21-144 [» ]
    1DCY X-ray 2.70 A 21-144 [» ]
    1J1A X-ray 2.20 A/B 21-144 [» ]
    1KQU X-ray 2.10 A 21-144 [» ]
    1KVO X-ray 2.00 A/B/C/D/E/F 21-144 [» ]
    1N28 X-ray 1.50 A/B 21-144 [» ]
    1N29 X-ray 2.60 A 21-144 [» ]
    1POD X-ray 2.10 A 21-144 [» ]
    1POE X-ray 2.10 A/B 21-144 [» ]
    2GNY model - A 21-144 [» ]
    3U8B X-ray 2.30 A 21-144 [» ]
    3U8D X-ray 1.80 A/B 21-144 [» ]
    3U8H X-ray 2.30 A/B 21-144 [» ]
    3U8I X-ray 1.10 A/B 21-144 [» ]
    ProteinModelPortali P14555.
    SMRi P14555. Positions 21-144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111337. 20 interactions.
    IntActi P14555. 3 interactions.
    MINTi MINT-1206447.
    STRINGi 9606.ENSP00000364252.

    Chemistry

    BindingDBi P14555.
    ChEMBLi CHEMBL3474.
    GuidetoPHARMACOLOGYi 1417.

    PTM databases

    PhosphoSitei P14555.

    Polymorphism databases

    DMDMi 129483.

    Proteomic databases

    PaxDbi P14555.
    PeptideAtlasi P14555.
    PRIDEi P14555.

    Protocols and materials databases

    DNASUi 5320.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375111 ; ENSP00000364252 ; ENSG00000188257 .
    ENST00000400520 ; ENSP00000383364 ; ENSG00000188257 .
    GeneIDi 5320.
    KEGGi hsa:5320.
    UCSCi uc001bcu.3. human.

    Organism-specific databases

    CTDi 5320.
    GeneCardsi GC01M020301.
    HGNCi HGNC:9031. PLA2G2A.
    HPAi HPA015236.
    MIMi 172411. gene.
    neXtProti NX_P14555.
    PharmGKBi PA270.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271943.
    HOGENOMi HOG000231749.
    HOVERGENi HBG008137.
    InParanoidi P14555.
    KOi K01047.
    OMAi FNNDELN.
    OrthoDBi EOG7N63PF.
    PhylomeDBi P14555.
    TreeFami TF319283.

    Enzyme and pathway databases

    Reactomei REACT_120722. Acyl chain remodelling of PI.
    REACT_120829. Acyl chain remodelling of PC.
    REACT_120906. Synthesis of PA.
    REACT_121324. Acyl chain remodelling of PG.
    REACT_121369. Acyl chain remodelling of PE.
    REACT_121384. Acyl chain remodelling of PS.

    Miscellaneous databases

    ChiTaRSi PLA2G2A. human.
    EvolutionaryTracei P14555.
    GeneWikii PLA2G2A.
    GenomeRNAii 5320.
    NextBioi 20582.
    PROi P14555.
    SOURCEi Search...

    Gene expression databases

    Bgeei P14555.
    CleanExi HS_PLA2G2A.
    Genevestigatori P14555.

    Family and domain databases

    Gene3Di 1.20.90.10. 1 hit.
    InterProi IPR001211. PLipase_A2.
    IPR013090. PLipase_A2_AS.
    IPR016090. PLipase_A2_dom.
    [Graphical view ]
    PANTHERi PTHR11716. PTHR11716. 1 hit.
    Pfami PF00068. Phospholip_A2_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00389. PHPHLIPASEA2.
    SMARTi SM00085. PA2c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48619. SSF48619. 1 hit.
    PROSITEi PS00119. PA2_ASP. 1 hit.
    PS00118. PA2_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid."
      Seilhamer J.J., Pruzanski W., Vadas P., Plant S., Miller J.A., Kloss J., Johnson L.K.
      J. Biol. Chem. 264:5335-5338(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Rheumatoid arthritic synovial fluid.
    2. "Structure and properties of a human non-pancreatic phospholipase A2."
      Kramer R.M., Hession C., Johansen B., Hayes G., McGray P., Chow E.P., Tizard R., Pepinsky R.B.
      J. Biol. Chem. 264:5768-5775(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Structure and properties of a secretable phospholipase A2 from human platelets."
      Kramer R.M., Johansen B., Hession C., Pepinsky R.B.
      Adv. Exp. Med. Biol. 275:35-53(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Cloning and sequence determination of human platelet phospholipase A2 from liver tissues."
      Liang N.S., Fang Z.W., Li Y., Yang F., Lu Y., Xie Y.A.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. NIEHS SNPs program
      Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-19.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Tongue.
    8. "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].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Prostate.
    11. "The primary structure of a membrane-associated phospholipase A2 from human spleen."
      Kanda A., Ono T., Yoshida N., Tojo H., Okamoto M.
      Biochem. Biophys. Res. Commun. 163:42-48(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-144.
      Tissue: Spleen.
    12. "Amino acid composition and NH2-terminal amino acid sequence of human phospholipase A2 purified from rheumatoid synovial fluid."
      Hara S., Kudo I., Matsuta K., Miyamoto T., Inoue K.
      J. Biochem. 104:326-328(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-54.
      Tissue: Synovial fluid.
    13. "Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme."
      Lai C.Y., Wada K.
      Biochem. Biophys. Res. Commun. 157:488-493(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-33.
      Tissue: Synovial fluid.
    14. "Purification and characterization of a phospholipase A2 from human ileal mucosa."
      Minami T., Tojo H., Shinomura Y., Matsuzawa Y., Okamoto M.
      Biochim. Biophys. Acta 1170:125-130(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-75.
      Tissue: Ileal mucosa.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    16. "Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate."
      Scott D.L., White S.P., Browning J.L., Rosa J.J., Gelb M.H., Sigler P.B.
      Science 254:1007-1010(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    17. "Structure-based design of the first potent and selective inhibitor of human non-pancreatic secretory phospholipase A2."
      Schevitz R.W., Bach N.J., Carlson D.G., Chirgadze N.Y., Clawson D.K., Dillard R.D., Draheim S.E., Hartley L.W., Jones N.D., Mihelich E.D., Olkowski J.L., Snyder D.W., Dand S.C., Wery J.-P.
      Nat. Struct. Biol. 2:458-465(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    18. "Crystal structure of human secretory phospholipase A2-IIA complex with the potent indolizine inhibitor 120-1032."
      Kitadokoro K., Hagishita S., Sato T., Ohtan M., Miki K.
      J. Biochem. 123:619-623(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiPA2GA_HUMAN
    AccessioniPrimary (citable) accession number: P14555
    Secondary accession number(s): A8K5I7
    , Q6DN24, Q6IBD9, Q9UCD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 170 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

    Miscellaneous

    Group II phospholipase A2 is found in many cells and also extracellularly. The membrane-bound and secreted forms are identical and are encoded by a single gene.

    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