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P04054

- PA21B_HUMAN

UniProt

P04054 - PA21B_HUMAN

Protein

Phospholipase A2

Gene

PLA2G1B

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

    PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides, this releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi50 – 501Calcium; via carbonyl oxygenBy similarity
    Metal bindingi52 – 521Calcium; via carbonyl oxygenBy similarity
    Metal bindingi54 – 541Calcium; via carbonyl oxygenBy similarity
    Active sitei70 – 701By similarity
    Metal bindingi71 – 711CalciumBy similarity
    Active sitei121 – 1211By similarity

    GO - Molecular functioni

    1. bile acid binding Source: BHF-UCL
    2. calcium-dependent phospholipase A2 activity Source: BHF-UCL
    3. calcium ion binding Source: BHF-UCL
    4. phospholipase A2 activity Source: BHF-UCL
    5. receptor binding Source: UniProtKB

    GO - Biological processi

    1. actin filament organization Source: ProtInc
    2. activation of MAPK activity Source: BHF-UCL
    3. activation of phospholipase A2 activity Source: BHF-UCL
    4. antibacterial humoral response Source: UniProt
    5. arachidonic acid secretion Source: BHF-UCL
    6. cellular response to insulin stimulus Source: BHF-UCL
    7. defense response to Gram-positive bacterium Source: UniProt
    8. fatty acid biosynthetic process Source: BHF-UCL
    9. glucose transport Source: BHF-UCL
    10. glycerophospholipid biosynthetic process Source: Reactome
    11. innate immune response in mucosa Source: UniProt
    12. interleukin-8 production Source: BHF-UCL
    13. intracellular signal transduction Source: BHF-UCL
    14. leukotriene biosynthetic process Source: BHF-UCL
    15. multicellular organismal lipid catabolic process Source: BHF-UCL
    16. neutrophil chemotaxis Source: BHF-UCL
    17. neutrophil mediated immunity Source: BHF-UCL
    18. phosphatidic acid biosynthetic process Source: Reactome
    19. phosphatidylcholine acyl-chain remodeling Source: Reactome
    20. phosphatidylcholine metabolic process Source: BHF-UCL
    21. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
    22. phosphatidylglycerol acyl-chain remodeling Source: Reactome
    23. phosphatidylinositol acyl-chain remodeling Source: Reactome
    24. phosphatidylserine acyl-chain remodeling Source: Reactome
    25. phospholipid metabolic process Source: Reactome
    26. positive regulation of calcium ion transport into cytosol Source: BHF-UCL
    27. positive regulation of DNA replication Source: BHF-UCL
    28. positive regulation of fibroblast proliferation Source: BHF-UCL
    29. positive regulation of immune response Source: BHF-UCL
    30. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
    31. positive regulation of protein secretion Source: BHF-UCL
    32. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    33. signal transduction Source: ProtInc
    34. 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 (EC:3.1.1.4)
    Alternative name(s):
    Group IB phospholipase A2
    Phosphatidylcholine 2-acylhydrolase 1B
    Gene namesi
    Name:PLA2G1B
    Synonyms:PLA2, PLA2A, PPLA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9030. PLA2G1B.

    Subcellular locationi

    Secreted 1 Publication
    Note: secreted from pancreatic acinar cells in its inactive form.

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. extracellular region Source: Reactome
    3. extracellular space Source: BHF-UCL
    4. secretory granule Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33361.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 15151 PublicationAdd
    BLAST
    Propeptidei16 – 227Activation peptide1 PublicationPRO_0000022739
    Chaini23 – 148126Phospholipase A21 PublicationPRO_0000022740Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 ↔ 991 Publication
    Disulfide bondi49 ↔ 1461 Publication
    Disulfide bondi51 ↔ 671 Publication
    Disulfide bondi66 ↔ 1271 Publication
    Disulfide bondi73 ↔ 1201 Publication
    Disulfide bondi83 ↔ 1131 Publication
    Disulfide bondi106 ↔ 1181 Publication

    Post-translational modificationi

    Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically.

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiP04054.
    PRIDEiP04054.

    PTM databases

    PhosphoSiteiP04054.

    Expressioni

    Gene expression databases

    ArrayExpressiP04054.
    BgeeiP04054.
    CleanExiHS_PLA2G1B.
    GenevestigatoriP04054.

    Organism-specific databases

    HPAiHPA047822.
    HPA060803.

    Interactioni

    Subunit structurei

    Monomer or homodimer By similarity. The inactive pro-form is a homotrimer.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi111336. 2 interactions.
    IntActiP04054. 1 interaction.
    STRINGi9606.ENSP00000312286.

    Structurei

    Secondary structure

    1
    148
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 233
    Helixi25 – 306
    Helixi31 – 333
    Helixi40 – 445
    Beta strandi45 – 473
    Turni48 – 503
    Beta strandi51 – 544
    Helixi62 – 7716
    Helixi81 – 833
    Turni84 – 874
    Beta strandi97 – 1004
    Beta strandi103 – 1064
    Helixi112 – 13019
    Helixi135 – 1373
    Helixi142 – 1454

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YSKmodel-A23-146[»]
    3ELOX-ray1.55A16-148[»]
    ProteinModelPortaliP04054.
    SMRiP04054. Positions 16-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04054.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phospholipase A2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG290764.
    HOGENOMiHOG000231749.
    HOVERGENiHBG008137.
    InParanoidiP04054.
    KOiK01047.
    OMAiDICEVAY.
    OrthoDBiEOG7N63PF.
    PhylomeDBiP04054.
    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.

    P04054-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLLVLAVLL TVAAADSGIS PRAVWQFRKM IKCVIPGSDP FLEYNNYGCY    50
    CGLGGSGTPV DELDKCCQTH DNCYDQAKKL DSCKFLLDNP YTHTYSYSCS 100
    GSAITCSSKN KECEAFICNC DRNAAICFSK APYNKAHKNL DTKKYCQS 148
    Length:148
    Mass (Da):16,360
    Last modified:February 1, 1991 - v3
    Checksum:iC8E38B2B64AEE8CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441Missing AA sequence (PubMed:6349696)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161D → A.
    Corresponds to variant rs5632 [ dbSNP | Ensembl ].
    VAR_011911
    Natural varianti89 – 891N → K.
    Corresponds to variant rs5636 [ dbSNP | Ensembl ].
    VAR_011913
    Natural varianti89 – 891N → T.
    Corresponds to variant rs5635 [ dbSNP | Ensembl ].
    VAR_011912

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21056, M22970 Genomic DNA. Translation: AAA60107.1.
    M21054 mRNA. Translation: AAA36450.1.
    AK311830 mRNA. Translation: BAG34772.1.
    AY438977 Genomic DNA. Translation: AAR05441.1.
    AC003982 Genomic DNA. Translation: AAB95635.1.
    CH471054 Genomic DNA. Translation: EAW98184.1.
    BC106725 mRNA. Translation: AAI06726.1.
    BC106726 mRNA. Translation: AAI06727.1.
    CCDSiCCDS9195.1.
    PIRiC25793. PSHU.
    RefSeqiNP_000919.1. NM_000928.2.
    UniGeneiHs.992.

    Genome annotation databases

    EnsembliENST00000308366; ENSP00000312286; ENSG00000170890.
    GeneIDi5319.
    KEGGihsa:5319.
    UCSCiuc001tyd.3. human.

    Polymorphism databases

    DMDMi129404.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21056 , M22970 Genomic DNA. Translation: AAA60107.1 .
    M21054 mRNA. Translation: AAA36450.1 .
    AK311830 mRNA. Translation: BAG34772.1 .
    AY438977 Genomic DNA. Translation: AAR05441.1 .
    AC003982 Genomic DNA. Translation: AAB95635.1 .
    CH471054 Genomic DNA. Translation: EAW98184.1 .
    BC106725 mRNA. Translation: AAI06726.1 .
    BC106726 mRNA. Translation: AAI06727.1 .
    CCDSi CCDS9195.1.
    PIRi C25793. PSHU.
    RefSeqi NP_000919.1. NM_000928.2.
    UniGenei Hs.992.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YSK model - A 23-146 [» ]
    3ELO X-ray 1.55 A 16-148 [» ]
    ProteinModelPortali P04054.
    SMRi P04054. Positions 16-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111336. 2 interactions.
    IntActi P04054. 1 interaction.
    STRINGi 9606.ENSP00000312286.

    Chemistry

    BindingDBi P04054.
    ChEMBLi CHEMBL4426.

    PTM databases

    PhosphoSitei P04054.

    Polymorphism databases

    DMDMi 129404.

    Proteomic databases

    PaxDbi P04054.
    PRIDEi P04054.

    Protocols and materials databases

    DNASUi 5319.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308366 ; ENSP00000312286 ; ENSG00000170890 .
    GeneIDi 5319.
    KEGGi hsa:5319.
    UCSCi uc001tyd.3. human.

    Organism-specific databases

    CTDi 5319.
    GeneCardsi GC12M120759.
    HGNCi HGNC:9030. PLA2G1B.
    HPAi HPA047822.
    HPA060803.
    MIMi 172410. gene.
    neXtProti NX_P04054.
    PharmGKBi PA33361.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290764.
    HOGENOMi HOG000231749.
    HOVERGENi HBG008137.
    InParanoidi P04054.
    KOi K01047.
    OMAi DICEVAY.
    OrthoDBi EOG7N63PF.
    PhylomeDBi P04054.
    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 PLA2G1B. human.
    EvolutionaryTracei P04054.
    GeneWikii PLA2G1B.
    GenomeRNAii 5319.
    NextBioi 20578.
    PROi P04054.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04054.
    Bgeei P04054.
    CleanExi HS_PLA2G1B.
    Genevestigatori P04054.

    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. "Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung."
      Seilhamer J.J., Randall T.L., Yamanaka M., Johnson L.K.
      DNA 5:519-527(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Lung.
    2. "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: Urinary bladder.
    3. NIEHS SNPs program
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region."
      Grataroli R., Dijkman R., Dutilh C.E., van der Ouderaa F., de Haas G.H., Figarella C.
      Eur. J. Biochem. 122:111-117(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-22.
      Tissue: Pancreas.
    8. "The complete primary structure of phospholipase A2 from human pancreas."
      Verheij H.M., Westerman J., Sternby B., de Haas G.H.
      Biochim. Biophys. Acta 747:93-99(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-148.
      Tissue: Pancreas.
    9. "Structural insight into the activation mechanism of human pancreatic prophospholipase A2."
      Xu W., Yi L., Feng Y., Chen L., Liu J.
      J. Biol. Chem. 284:16659-16666(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 16-148, DISULFIDE BONDS, SUBUNIT, AUTOPROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, FUNCTION.

    Entry informationi

    Entry nameiPA21B_HUMAN
    AccessioniPrimary (citable) accession number: P04054
    Secondary accession number(s): B2R4H5, Q3KPI1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1986
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 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 12
      Human chromosome 12: 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