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P14555

- PA2GA_HUMAN

UniProt

P14555 - PA2GA_HUMAN

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Protein
Phospholipase A2, membrane associated
Gene
PLA2G2A, PLA2B, PLA2L, RASF-A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

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 – 671 By similarity
Metal bindingi68 – 681Calcium
Active sitei111 – 1111 By similarity

GO - Molecular functioni

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

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
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, 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
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA270.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20204 Publications
Add
BLAST
Chaini21 – 144124Phospholipase A2, membrane associated
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP14555.

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.

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

Natural variant

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

Sequence conflict

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

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 169 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

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