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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
g O-GlcNAc
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: Lipid Metabolism - linoleic acid; Lipid Metabolism - ether lipid; Lipid Metabolism - arachidonic acid; Lipid Metabolism - alpha-linolenic acid; Phospholipase; Lipid Metabolism - glycerophospholipid; EC 3.1.1.5; EC 3.1.1.4
Cellular Component: Golgi apparatus; endoplasmic reticulum membrane; perinuclear region of cytoplasm; mitochondrial inner membrane; nucleus; cytosol
Molecular Function: phospholipase A2 activity; calcium-dependent phospholipid binding; calcium-dependent phospholipase A2 activity; hydrolase activity; calcium ion binding; lysophospholipase activity
Biological Process: platelet activating factor biosynthetic process; luteolysis; positive regulation of apoptosis; response to glucocorticoid stimulus; positive regulation of vesicle fusion; response to lipopolysaccharide; decidualization; response to vitamin D; phospholipid metabolic process; positive regulation of cell proliferation; response to methylmercury; arachidonic acid metabolic process; positive regulation of prostaglandin biosynthetic process; aging; icosanoid biosynthetic process; platelet activation; phospholipid catabolic process; glycerophospholipid biosynthetic process; icosanoid metabolic process; response to organic nitrogen; ovulation from ovarian follicle; positive regulation of bone mineralization; arachidonic acid secretion; response to hydrogen peroxide; response to heat; positive regulation of fever; phosphatidic acid biosynthetic process; response to calcium ion; blood coagulation; surfactant homeostasis
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:  GPCRs Signaling to MAPK/Erk  |  MAPK/Erk in Growth and Differentiation  |  Phospholipase Signaling  |  Signaling Pathways Activating p38 MAPK
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  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
cell growth, altered: S505‑p
activation: 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 T21-p HQYSHKFtVVVLRAT
0 1 T31-p VLRATKVtkGAFGDM
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 K176-a MKkLLGPkNsEGLHs
0 1 S178-p kLLGPkNsEGLHsAR
0 1 S183-p kNsEGLHsARDVPVV
4 0 S228-p ATYVAGLsGSTWYMS
0 3 T268-p HNPLLLLtPQKVkRY
0 1 K273-u LLtPQKVkRYVESLW
0 4 K316-u NTTLSSLkEKVNTAQ
0 1 Y359-p YEIGMAKyGTFMAPD
0 8 K371-u APDLFGSkFFMGTVV
0 4 S431-p ITTKHIVsNDssDsD
0 7 S434-p KHIVsNDssDsDDES
0 8 S435-p HIVsNDssDsDDESH
2 21 S437-p VsNDssDsDDESHEP
0 1 T447-p ESHEPKGtENEDAGs
2 2 S454-p tENEDAGsDyQsDNQ
0 9 Y456-p NEDAGsDyQsDNQAs
0 1 S458-p DAGsDyQsDNQAsWI
0 1 S463-p yQsDNQAsWIHRMIM
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 1 K691 QYPNQAFKRLHDLMH
0 2 S724 EYRRQNPSRCsVsLS
8 15 S727-p RQNPSRCsVsLSNVE
0 13 S729-p NPSRCsVsLSNVEAR
0 1 S731 SRCsVsLSNVEARRF
0 1 K741-u EARRFFNkEFLSKPK
2831 : Phospho-cPLA2 (Ser505) Antibody
  mouse

 
T21 HQYSHKFTVVVLRAT
T31 VLRATKVTKGTFGDM
K32 LRATKVTKGTFGDML
Y96-p ITLMDANyVMDEtLG
T101-p ANyVMDEtLGtATFP
T104-p VMDEtLGtATFPVSS
K155 MALCDQEKTFRQQRK
K171-a NIKENMKkLLGPKKS
K176 MKkLLGPKKSEGLYS
S178 kLLGPKKSEGLYSTR
S183 KKSEGLYSTRDVPVV
S228 ATYIAGLSGSTWYMS
T268-p HNPLLLLtPQKVKRY
K273 LLtPQKVKRYVESLW
K316 SMTLSSLKEKVNAAR
Y359 YEIGMAKYGTFMAPD
K371-u APDLFGSkFFMGTVV
S431-p ITAKHIVsNDssDsD
S434-p KHIVsNDssDsDDEA
S435-p HIVsNDssDsDDEAQ
S437-p VsNDssDsDDEAQGP
T447 EAQGPKGTENEEAEK
K454 TENEEAEKEyQSDNQ
Y456-p NEEAEKEyQSDNQAS
S458 EAEKEyQSDNQASWV
S463 yQSDNQASWVHRMLM
S505-p LNTSYPLsPLRDFss
S511-p LsPLRDFssQDsFDD
S512-p sPLRDFssQDsFDDE
S515-p RDFssQDsFDDELdA
D521-ca DsFDDELdAAVADPD
Y534-p PDEFERIyEPLDVKS
K540 IyEPLDVKSKKIHVV
K690-a QYPNQAFkRLHDLMY
S723-p EYRRQNPsRCsVsLs
S726-p RQNPsRCsVsLsNVE
S728-p NPsRCsVsLsNVEAR
S730-p sRCsVsLsNVEARKF
K740 EARKFFNKEFLSKPT
2831 : Phospho-cPLA2 (Ser505) Antibody
  rat

 
T21 HQYSHKFTVVVLRAT
T31 VLRATKVTKGTFGDM
K32 LRATKVTKGTFGDML
Y96 ITLMDANYVMDETLG
T101 ANYVMDETLGTATFP
T104 VMDETLGTATFPVSS
K155 MALCDQEKTFRRQRK
K171 NIKENMKKLLGPKKS
K176 MKKLLGPKKSEGLYS
S178 KLLGPKKSEGLYSTR
S183 KKSEGLYSTRDVPVV
S228-p ATYVAGLsGSTWYMS
T268 HNPLLLLTPQKVKRY
K273 LLTPQKVKRYVESLW
K316 STTLSSLKEKVSAAR
Y359 YEIGMAKYGTFMTPD
K371 TPDLFGSKFFMGTVV
S431 ITAKHIVSNDssDsD
S434-p KHIVSNDssDsDDEA
S435-p HIVSNDssDsDDEAQ
S437-p VSNDssDsDDEAQGP
T447 EAQGPKGTENEDAER
R454 TENEDAEREYQNDNQ
Y456 NEDAEREYQNDNQAS
N458 DAEREYQNDNQASWV
S463 YQNDNQASWVHRMLM
S505-p LNTSYPLsPLRDFSP
S511 LsPLRDFSPQDSFDD
P512 sPLRDFSPQDSFDDD
S515 RDFSPQDSFDDDELD
D522 SFDDDELDAAVADPD
Y535 PDEFERIYEPLDVKS
K541 IYEPLDVKSKKIHVV
K691 QYPNQAFKRLHDLMY
S724 EYRRQNPSRCsVsLS
S727-p RQNPSRCsVsLSNVE
S729-p NPSRCsVsLSNVEAR
S731 SRCsVsLSNVEARKF
K741 EARKFFNKEFLSKPT
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