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HUMAN:PA2GA

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) PLA2G2A (synonyms: PLA2B, PLA2L, RASF-A)
Protein Name(s) Phospholipase A2, membrane associated

GIIC sPLA2 Group IIA phospholipase A2 Non-pancreatic secretory phospholipase A2 NPS-PLA2 Phosphatidylcholine 2-acylhydrolase 2A

External Links
UniProt P14555
EMBL M22430
M22431
AY656695
CR456865
AY462114
AL358253
AK291302
CH471134
BC005919
CCDS CCDS201.1
PIR A32862
RefSeq NP_000291.1
NP_001155199.1
NP_001155200.1
NP_001155201.1
UniGene Hs.466804
PDB 1AYP
1BBC
1DB4
1DB5
1DCY
1J1A
1KQU
1KVO
1N28
1N29
1POD
1POE
2GNY
3U8B
3U8D
3U8H
3U8I
PDBsum 1AYP
1BBC
1DB4
1DB5
1DCY
1J1A
1KQU
1KVO
1N28
1N29
1POD
1POE
2GNY
3U8B
3U8D
3U8H
3U8I
ProteinModelPortal P14555
SMR P14555
BioGrid 111337
IntAct P14555
MINT MINT-1206447
STRING 9606.ENSP00000364252
BindingDB P14555
ChEMBL CHEMBL3474
DrugBank DB00586
DB01381
DB00328
DB04786
GuidetoPHARMACOLOGY 1417
PhosphoSite P14555
DMDM 129483
PaxDb P14555
PeptideAtlas P14555
PRIDE P14555
DNASU 5320
Ensembl ENST00000375111
ENST00000400520
GeneID 5320
KEGG hsa:5320
UCSC uc001bcu.3
CTD 5320
GeneCards GC01M020301
HGNC HGNC:9031
HPA HPA015236
MIM 172411
neXtProt NX_P14555
PharmGKB PA270
eggNOG NOG271943
GeneTree ENSGT00760000119160
HOGENOM HOG000231749
HOVERGEN HBG008137
InParanoid P14555
KO K01047
OMA RGCGTKF
OrthoDB EOG7N63PF
PhylomeDB P14555
TreeFam TF319283
Reactome REACT_120722
REACT_120829
REACT_120906
REACT_121324
REACT_121369
REACT_121384
ChiTaRS PLA2G2A
EvolutionaryTrace P14555
GeneWiki PLA2G2A
GenomeRNAi 5320
NextBio 20582
PRO PR:P14555
Proteomes UP000005640
Bgee P14555
CleanEx HS_PLA2G2A
ExpressionAtlas P14555
Genevestigator P14555
GO GO:0005783
GO:0005789
GO:0005576
GO:0005615
GO:0070062
GO:0005739
GO:0030141
GO:0005509
GO:0047498
GO:0004623
GO:0005543
GO:0050830
GO:0046474
GO:0016042
GO:0034374
GO:0050680
GO:0006654
GO:0046473
GO:0036151
GO:0036152
GO:0036148
GO:0036149
GO:0036150
GO:0006644
GO:0050729
GO:0010744
GO:0044281
GO:0035019
Gene3D 1.20.90.10
InterPro IPR001211
IPR013090
IPR016090
PANTHER PTHR11716
Pfam PF00068
PRINTS PR00389
SMART SM00085
SUPFAM SSF48619
PROSITE PS00119
PS00118

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0070374

positive regulation of ERK1 and ERK2 cascade

PMID:22837859[1]

ECO:0000314

P

Figure 6 shows that Group V phospholipase A2 activity has an effect on human pulmonary endothelial cells' intracellular signaling.

complete
CACAO 5637

GO:0010518

positive regulation of phospholipase activity

PMID:22837859[1]

ECO:0000314

P

Figure 6 shows that Group V phospholipase A2 activity has an effect on human pulmonary endothelial cells' intracellular signaling.

complete

involved_in

GO:0070374

positive regulation of ERK1 and ERK2 cascade

PMID:22837859[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:23533145[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:23580065[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001827)

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

GO_REF:0000054

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0046473

phosphatidic acid metabolic process

PMID:9032461[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006644

phospholipid metabolic process

PMID:17069818[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:17069818[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005543

phospholipid binding

PMID:9032461[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004623

phospholipase A2 activity

PMID:17069818[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0047498

calcium-dependent phospholipase A2 activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000919171
RGD:3340
RGD:61949
RGD:62051
RGD:620857
UniProtKB:P04054

F

Seeded From UniProt

complete

involved_in

GO:0006644

phospholipid metabolic process

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:101899
MGI:MGI:1349661
PANTHER:PTN000919171
RGD:61949
RGD:620857
UniProtKB:P14555

P

Seeded From UniProt

complete

enables

GO:0005543

phospholipid binding

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000919171
UniProtKB:P14555

F

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000919171
UniProtKB:P04054

F

Seeded From UniProt

complete

enables

GO:0004623

phospholipase A2 activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:101842
MGI:MGI:101899
MGI:MGI:1349661
PANTHER:PTN000919171
RGD:61935
RGD:61949
UniProtKB:P00592
UniProtKB:P04054
UniProtKB:P14555

F

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14423
ensembl:ENSRNOP00000022827

C

Seeded From UniProt

complete

enables

GO:0047498

calcium-dependent phospholipase A2 activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14423
ensembl:ENSRNOP00000022827

F

Seeded From UniProt

complete

part_of

GO:0030141

secretory granule

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14423
ensembl:ENSRNOP00000022827

C

Seeded From UniProt

complete

involved_in

GO:0006644

phospholipid metabolic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14423
ensembl:ENSRNOP00000022827

P

Seeded From UniProt

complete

enables

GO:0004623

phospholipase A2 activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001211
InterPro:IPR016090
InterPro:IPR036444

F

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001211

F

Seeded From UniProt

complete

involved_in

GO:0006644

phospholipid metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016090
InterPro:IPR036444

P

Seeded From UniProt

complete

involved_in

GO:0016042

lipid catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001211

P

Seeded From UniProt

complete

involved_in

GO:0050482

arachidonic acid secretion

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016090
InterPro:IPR036444

P

Seeded From UniProt

complete

enables

GO:0102568

phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine)

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.4

F

Seeded From UniProt

complete

enables

GO:0102567

phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine)

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.4

F

Seeded From UniProt

complete

enables

GO:0004623

phospholipase A2 activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.4

F

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

PMID:9272153[7]
Reactome:R-HSA-8862771
Reactome:R-HSA-1602446
Reactome:R-HSA-1602417
Reactome:R-HSA-1602398
Reactome:R-HSA-1602377
Reactome:R-HSA-1602374
Reactome:R-HSA-1602368

ECO:0000304

author statement supported by traceable reference used in manual assertion








C

Seeded From UniProt

complete

involved_in

GO:0050830

defense response to Gram-positive bacterium

PMID:18827909[8]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0050729

positive regulation of inflammatory response

PMID:18827909[8]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034374

low-density lipoprotein particle remodeling

PMID:18827909[8]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0010744

positive regulation of macrophage derived foam cell differentiation

PMID:18827909[8]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0047498

calcium-dependent phospholipase A2 activity

PMID:9272153[7]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0036152

phosphatidylethanolamine acyl-chain remodeling

Reactome:R-HSA-1482839

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0036151

phosphatidylcholine acyl-chain remodeling

Reactome:R-HSA-1482788

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0036150

phosphatidylserine acyl-chain remodeling

Reactome:R-HSA-1482801

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0036149

phosphatidylinositol acyl-chain remodeling

Reactome:R-HSA-1482922

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0036148

phosphatidylglycerol acyl-chain remodeling

Reactome:R-HSA-1482925

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019730

antimicrobial humoral response

Reactome:R-HSA-6803157

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006654

phosphatidic acid biosynthetic process

Reactome:R-HSA-1483166

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005789

endoplasmic reticulum membrane

Reactome:R-HSA-1482907
Reactome:R-HSA-1482887
Reactome:R-HSA-1482868
Reactome:R-HSA-1482816
Reactome:R-HSA-1482776
Reactome:R-HSA-1482679

ECO:0000304

author statement supported by traceable reference used in manual assertion






C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964
UniProtKB-SubCell:SL-0243

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0016042

lipid catabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0442

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0006629

lipid metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0443

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Muñoz, NM et al. () Group V phospholipase A(2) increases pulmonary endothelial permeability through direct hydrolysis of the cell membrane. Pulm Circ 2 182-92 PubMed GONUTS page
  2. Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
  3. Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page
  4. 4.0 4.1 Snitko, Y et al. (1997) High specificity of human secretory class II phospholipase A2 for phosphatidic acid. Biochem. J. 321 ( Pt 3) 737-41 PubMed GONUTS page
  5. 5.0 5.1 5.2 Luchtefeld, M et al. (2007) Angiotensin II type 1-receptor antagonism prevents type IIA secretory phospholipase A2-dependent lipid peroxidation. Atherosclerosis 194 62-70 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 6.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  7. 7.0 7.1 Nimmrich, I et al. (1997) Loss of the PLA2G2A gene in a sporadic colorectal tumor of a patient with a PLA2G2A germline mutation and absence of PLA2G2A germline alterations in patients with FAP. Hum. Genet. 100 345-9 PubMed GONUTS page
  8. 8.0 8.1 8.2 8.3 Divchev, D & Schieffer, B (2008) The secretory phospholipase A2 group IIA: a missing link between inflammation, activated renin-angiotensin system, and atherogenesis? Vasc Health Risk Manag 4 597-604 PubMed GONUTS page