Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
cPLA2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
cPLA2 a calcium-dependent phospholipase A2 that catalyzes the release of arachidonic acid from membrane phospholipids. Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Arachidonic acid is a precursor for the eicosanoids that are involved in hemodynamic regulation, inflammatory responses, and other cellular processes. Promotes cerebellar long-term depression and motor learning. Translocates to the Golgi and endoplasmic reticulum in a calcium-dependent fashion. Translocation and activation of at the ER facilitates the process of ER stress. Regulates the biogenesis of lipid droplets, a process dependent on JNK and ceramide kinase. Stimulated by agonists such as ATP, EGF, thrombin and bradykinin as well as by cytosolic Ca2+. The N-terminal C2 domain, by its association with lipid membranes, mediates the regulation of CPLA2 by presenting the active site to its substrate in response to elevations of cytosolic Ca2+. Inhibited when in trimolecular complex with ANXA2 and S100A10. Phosphorylation of S727 relieves this inhibitory interaction, thus activating PLA2G4A. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.1.4; Phospholipase; EC 3.1.1.5; Lipid Metabolism - ether lipid; Lipid Metabolism - glycerophospholipid; Lipid Metabolism - arachidonic acid; Lipid Metabolism - alpha-linolenic acid; Lipid Metabolism - linoleic acid
Cellular Component: Golgi apparatus; endoplasmic reticulum membrane; cytoplasmic membrane-bound vesicle; cytoplasm; mitochondrial inner membrane; cytosol
Molecular Function: phospholipase A2 activity; calcium-dependent phospholipid binding; calcium-dependent phospholipase A2 activity; calcium ion binding; lysophospholipase activity
Biological Process: icosanoid biosynthetic process; platelet activation; platelet activating factor biosynthetic process; phospholipid catabolic process; phospholipid metabolic process; glycerophospholipid biosynthetic process; icosanoid metabolic process; phosphatidic acid biosynthetic process; arachidonic acid metabolic process; arachidonic acid secretion; blood coagulation; regulation of cell proliferation
Reference #:  P47712 (UniProtKB)
Alt. Names/Synonyms: calcium-dependent phospholipid-binding protein; CPLA2; cPLA2-alpha; Cytosolic phospholipase A2; Lysophospholipase; MGC126350; PA24A; Phosphatidylcholine 2-acylhydrolase; Phospholipase A2; Phospholipase A2 group IVA; phospholipase A2, group IVA (cytosolic, calcium-dependent); PLA2G4; PLA2G4A
Gene Symbols: PLA2G4A
Molecular weight: 85,239 Da
Basal Isoelectric point: 5.22  Predict pI for various phosphorylation states
CST Pathways:  GPCR Signaling to MAPKs  |  Growth And Differentiation Control by MAPKs  |  Phospholipase Signaling  |  Regulation of P38 MAPKs
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

cPLA2

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
cell growth, altered: S505‑p
activity, induced: S228‑p, S505‑p
enzymatic activity, induced: S228‑p, S505‑p, S727‑p
intracellular localization: S505‑p, S727‑p
molecular association, regulation: S727‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S2-p ______MsFIDPYQH
0 1 T21-p HQYSHKFtVVVLRAT
0 2 K32-u LRATKVTkGAFGDML
0 1 Y96 ITLMDANYVMDETLG
0 1 T101 ANYVMDETLGTATFT
0 1 T104 VMDETLGTATFTVSS
0 2 K155-u MALCDQEkTFRQQRK
0 2 K171-a HIRESMKkLLGPKNs
0 1 S178-p kLLGPKNsEGLHSAR
4 0 S228-p ATYVAGLsGSTWYMS
0 5 T268-p HNPLLLLtPQKVKRY
0 4 K316-u NTTLSSLkEKVNTAQ
0 8 K371-u APDLFGSkFFMGTVV
0 4 S431-p ITTKHIVsNDssDsD
0 10 S434-p KHIVsNDssDsDDES
0 10 S435-p HIVsNDssDsDDESH
2 27 S437-p VsNDssDsDDESHEP
2 3 S454-p TENEDAGsDyQSDNQ
0 9 Y456-p NEDAGsDyQSDNQAS
22 13 S505-p LNTSYPLsPLSDFAT
0 1 A511 LsPLSDFATQDsFDD
0 1 T512 sPLSDFATQDsFDDD
3 4 S515-p SDFATQDsFDDDELD
0 1 D522 sFDDDELDAAVADPD
0 26 Y535-p PDEFERIyEPLDVkS
0 2 K541-u IyEPLDVkSKKIHVV
0 2 S724-p EYRRQNPsRCsVsLS
8 17 S727-p RQNPsRCsVsLSNVE
0 16 S729-p NPsRCsVsLSNVEAR
0 1 S731 sRCsVsLSNVEARRF
2831 : Phospho-cPLA2 (Ser505) Antibody
  mouse

 
S2 ______MSFIDPYQH
T21 HQYSHKFTVVVLRAT
K32 LRATKVTKGTFGDML
Y96-p ITLMDANyVMDEtLG
T101-p ANyVMDEtLGtATFP
T104-p VMDEtLGtATFPVSS
K155 MALCDQEKTFRQQRK
K171-a NIKENMKkLLGPKKS
S178 kLLGPKKSEGLYSTR
S228 ATYIAGLSGSTWYMS
T268-p HNPLLLLtPQKVKRY
K316 SMTLSSLKEKVNAAR
K371-u APDLFGSkFFMGTVV
S431-p ITAKHIVsNDssDsD
S434-p KHIVsNDssDsDDEA
S435-p HIVsNDssDsDDEAQ
S437-p VsNDssDsDDEAQGP
K454 TENEEAEKEyQSDNQ
Y456-p NEEAEKEyQSDNQAS
S505-p LNTSYPLsPLRDFss
S511-p LsPLRDFssQDsFDD
S512-p sPLRDFssQDsFDDE
S515-p RDFssQDsFDDELdA
D521-ca DsFDDELdAAVADPD
Y534-p PDEFERIyEPLDVKS
K540 IyEPLDVKSKKIHVV
S723-p EYRRQNPsRCsVsLs
S726-p RQNPsRCsVsLsNVE
S728-p NPsRCsVsLsNVEAR
S730-p sRCsVsLsNVEARKF
2831 : Phospho-cPLA2 (Ser505) Antibody
  rat

 
S2 ______MSFIDPYQH
T21 HQYSHKFTVVVLRAT
K32 LRATKVTKGTFGDML
Y96 ITLMDANYVMDETLG
T101 ANYVMDETLGTATFP
T104 VMDETLGTATFPVSS
K155 MALCDQEKTFRRQRK
K171 NIKENMKKLLGPKKS
S178 KLLGPKKSEGLYSTR
S228-p ATYVAGLsGSTWYMS
T268 HNPLLLLTPQKVKRY
K316 STTLSSLKEKVSAAR
K371 TPDLFGSKFFMGTVV
S431 ITAKHIVSNDssDsD
S434-p KHIVSNDssDsDDEA
S435-p HIVSNDssDsDDEAQ
S437-p VSNDssDsDDEAQGP
R454 TENEDAEREYQNDNQ
Y456 NEDAEREYQNDNQAS
S505-p LNTSYPLsPLRDFSP
S511 LsPLRDFSPQDSFDD
P512 sPLRDFSPQDSFDDD
S515 RDFSPQDSFDDDELD
D522 SFDDDELDAAVADPD
Y535 PDEFERIYEPLDVKS
K541 IYEPLDVKSKKIHVV
S724 EYRRQNPSRCsVsLS
S727-p RQNPSRCsVsLSNVE
S729-p NPSRCsVsLSNVEAR
S731 SRCsVsLSNVEARKF
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.