Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phospholipase A2

Gene

PLA2G1B

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

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

Ca2+By similarityNote: Binds 1 Ca2+ 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

  • bile acid binding Source: BHF-UCL
  • calcium-dependent phospholipase A2 activity Source: BHF-UCL
  • calcium ion binding Source: BHF-UCL
  • phospholipase A2 activity Source: BHF-UCL
  • receptor binding Source: UniProtKB

GO - Biological processi

  • actin filament organization Source: ProtInc
  • activation of MAPK activity Source: BHF-UCL
  • activation of phospholipase A2 activity Source: BHF-UCL
  • antibacterial humoral response Source: UniProtKB
  • arachidonic acid secretion Source: BHF-UCL
  • cellular response to insulin stimulus Source: BHF-UCL
  • defense response to Gram-positive bacterium Source: UniProtKB
  • fatty acid biosynthetic process Source: BHF-UCL
  • glucose transport Source: BHF-UCL
  • glycerophospholipid biosynthetic process Source: Reactome
  • innate immune response in mucosa Source: UniProtKB
  • interleukin-8 production Source: BHF-UCL
  • intracellular signal transduction Source: BHF-UCL
  • leukotriene biosynthetic process Source: BHF-UCL
  • multicellular organismal lipid catabolic process Source: BHF-UCL
  • neutrophil chemotaxis Source: BHF-UCL
  • neutrophil mediated immunity Source: BHF-UCL
  • phosphatidic acid biosynthetic process Source: Reactome
  • phosphatidylcholine acyl-chain remodeling Source: Reactome
  • phosphatidylcholine metabolic process Source: BHF-UCL
  • phosphatidylethanolamine acyl-chain remodeling Source: Reactome
  • phosphatidylglycerol acyl-chain remodeling Source: Reactome
  • phosphatidylinositol acyl-chain remodeling Source: Reactome
  • phosphatidylserine acyl-chain remodeling Source: Reactome
  • phospholipid metabolic process Source: Reactome
  • positive regulation of calcium ion transport into cytosol Source: BHF-UCL
  • positive regulation of DNA replication Source: BHF-UCL
  • positive regulation of fibroblast proliferation Source: BHF-UCL
  • positive regulation of immune response Source: BHF-UCL
  • positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  • positive regulation of protein secretion Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • signal transduction Source: ProtInc
  • 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

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 Componenti: 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

  • cell surface Source: BHF-UCL
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • secretory granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33361.

Chemistry

DrugBankiDB02659. Cholic Acid.
DB04552. Niflumic Acid.
DB00795. Sulfasalazine.

Polymorphism and mutation databases

BioMutaiPLA2G1B.
DMDMi129404.

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

BgeeiP04054.
CleanExiHS_PLA2G1B.
ExpressionAtlasiP04054. baseline and differential.
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 – 233Combined sources
Helixi25 – 306Combined sources
Helixi31 – 333Combined sources
Helixi40 – 445Combined sources
Beta strandi45 – 473Combined sources
Turni48 – 503Combined sources
Beta strandi51 – 544Combined sources
Helixi62 – 7716Combined sources
Helixi81 – 833Combined sources
Turni84 – 874Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi103 – 1064Combined sources
Helixi112 – 13019Combined sources
Helixi135 – 1373Combined sources
Helixi142 – 1454Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP04054.
KOiK01047.
OMAiDELDKCC.
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

        10         20         30         40         50
MKLLVLAVLL TVAAADSGIS PRAVWQFRKM IKCVIPGSDP FLEYNNYGCY
60 70 80 90 100
CGLGGSGTPV DELDKCCQTH DNCYDQAKKL DSCKFLLDNP YTHTYSYSCS
110 120 130 140
GSAITCSSKN KECEAFICNC DRNAAICFSK APYNKAHKNL DTKKYCQS
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBiP04054.
ChEMBLiCHEMBL4426.
DrugBankiDB02659. Cholic Acid.
DB04552. Niflumic Acid.
DB00795. Sulfasalazine.

PTM databases

PhosphoSiteiP04054.

Polymorphism and mutation databases

BioMutaiPLA2G1B.
DMDMi129404.

Proteomic databases

PaxDbiP04054.
PRIDEiP04054.

Protocols and materials databases

DNASUi5319.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5319.
GeneCardsiGC12M120759.
HGNCiHGNC:9030. PLA2G1B.
HPAiHPA047822.
HPA060803.
MIMi172410. gene.
neXtProtiNX_P04054.
PharmGKBiPA33361.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG290764.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP04054.
KOiK01047.
OMAiDELDKCC.
OrthoDBiEOG7N63PF.
PhylomeDBiP04054.
TreeFamiTF319283.

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.

Miscellaneous databases

ChiTaRSiPLA2G1B. human.
EvolutionaryTraceiP04054.
GeneWikiiPLA2G1B.
GenomeRNAii5319.
NextBioi20578.
PROiP04054.
SOURCEiSearch...

Gene expression databases

BgeeiP04054.
CleanExiHS_PLA2G1B.
ExpressionAtlasiP04054. baseline and differential.
GenevestigatoriP04054.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 161 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.