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Protein Page:
PIK3C2A (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
PIK3C2A a protein of the phosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles in signaling pathways involved in cell proliferation, oncogenic transformation, cell survival, cell migration, and intracellular protein trafficking. This protein contains a lipid kinase catalytic domain as well as a C-terminal C2 domain, a characteristic of class II PI3-kinases. C2 domains act as calcium-dependent phospholipid binding motifs that mediate translocation of proteins to membranes, and may also mediate protein-protein interactions. Its PI3-kinase is not sensitive to nanomolar levels of the inhibitor wortmannin. Activated by insulin and may be involved in integrin-dependent signaling. Note: This description may include information from UniProtKB.
Protein type: Kinase, lipid; Autophagy; EC 2.7.1.154; Motility/polarity/chemotaxis; Carbohydrate Metabolism - inositol phosphate
Cellular Component: Golgi apparatus; clathrin-coated vesicle; cytoplasm; plasma membrane; nucleus; cytosol; phosphoinositide 3-kinase complex; vesicle
Molecular Function: 1-phosphatidylinositol-3-kinase activity; ATP binding; phosphoinositide 3-kinase activity; phosphatidylinositol-4-phosphate 3-kinase activity; phosphoinositide binding
Biological Process: epidermal growth factor receptor signaling pathway; clathrin cage assembly; phosphoinositide-mediated signaling; exocytosis; phospholipid metabolic process; phosphatidylinositol biosynthetic process; insulin receptor signaling pathway; vascular smooth muscle contraction; platelet-derived growth factor receptor signaling pathway; endocytosis
Reference #:  O00443 (UniProtKB)
Alt. Names/Synonyms: C2-containing phosphatidylinositol kinase; CPK; DKFZp686L193; MGC142218; P3C2A; Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha; Phosphoinositide 3-kinase-C2-alpha; phosphoinositide-3-kinase, class 2, alpha polypeptide; PI3-K-C2(ALPHA); PI3-K-C2A; PI3K-C2-alpha; PI3K-C2alpha; PIK3C2A; PtdIns-3-kinase C2 subunit alpha
Gene Symbols: PIK3C2A
Molecular weight: 190,680 Da
Basal Isoelectric point: 8.25  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Adherens Junction Dynamics  |  AMPK Signaling  |  Angiogenesis  |  Apoptosis Regulation  |  ErbB/HER Signaling  |  ESC Pluripotency and Differentiation  |  Growth And Differentiation Control by MAPKs  |  IL6 Signaling  |  Inhibition of Apoptosis  |  Microtubule Dynamics  |  Mitochondrial Control of Apoptosis  |  mTOR Signaling  |  NF-kB Signaling  |  PI3K/Akt Signaling  |  Protein Kinase C Signaling  |  SAPK/JNK Signaling Cascades  |  T Cell Receptor Signaling  |  TGF-├č Signaling  |  Translation: eIF4E and p70S6K  |  Warburg Effect
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PIK3C2A

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
protein conformation: S259‑p
protein degradation: S259‑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 K11 ISSNSGFKECPSSHP
0 3 S60-p RGFELSSsTRKKAQV
0 39 Y73-p QVYNKQDyDLMVFPE
0 1 K94-a ALDIDVEkLTQAELE
0 1 K94-u ALDIDVEkLTQAELE
0 5 S108-p EKLLLDDsFETkKTP
0 1 K112-u LDDsFETkKTPVLPV
0 2 T120-p KTPVLPVtPILsPSF
0 4 S124-p LPVtPILsPSFSAQL
0 2 R134 FSAQLYFRPTIQRGQ
0 3 K229-u DMAKLFDkIASTSEF
0 1 K238 ASTSEFLKNGKARTD
0 1 K252-u DLEITDSkVSNLQVs
1 22 S259-p kVSNLQVsPkSEDIS
0 1 K261-u SNLQVsPkSEDISkF
0 2 K267-u PkSEDISkFDWLDLD
0 1 K278-u LDLDPLSkPKVDNVE
0 1 K301-u NVSSLLAkDPWDAVL
0 1 K326 LERKVNGKsLsVATV
0 4 S327-p ERKVNGKsLsVATVT
0 2 S329-p KVNGKsLsVATVTRS
0 9 S338-p ATVTRSQsLNIRTTQ
0 1 K348 IRTTQLAKAQGHISQ
0 1 K579-u RAVDQVIkAVRKICS
0 1 S612-p RAVNLPRsktADVTS
0 2 K613-u AVNLPRsktADVTSL
0 1 T614-p VNLPRsktADVTSLF
0 1 S630-p GEDTSRSsTRGSLNP
0 1 N863 RSIIQQHNLETLEND
0 2 K872-u ETLENDIkGKLLDIL
0 1 K881-u KLLDILHkDSSLGLS
0 1 K889-u DSSLGLSkEDKAFLW
0 2 Y901-p FLWEKRYyCFKHPNC
0 1 K920 LASAPNWKWVNLAKT
0 1 K1107 VAKELNIKSCSFFSS
0 1 K1162-u IMDKIWLkEGLDLRM
0 1 S1190 MVELVPASDTLRKIQ
0 1 T1192 ELVPASDTLRKIQVE
0 1 K1217-u PLAEWLRkYNPSEEE
0 1 S1281-p GHAQMFGsFKRDRAP
0 1 K1414 PILSFSPKTYSFRQD
0 4 S1553-p SADAGSFsPTPGQIG
0 8 Y1595-p DGADPNPyVKTYLLP
  mouse

 
K11-u ISNNSEFkQCSSSHP
S60 RGFELSSSTRQRTQG
Y73 QGFNKQDYDLMVFPE
K94 AVDIDVEKLTQAELE
K94 AVDIDVEKLTQAELE
N108 EKILLDDNFETRKPP
R112 LDDNFETRKPPALPV
T120 KPPALPVTPVLSPSF
S124 LPVTPVLSPSFSTQL
R134-m2 FSTQLYLrPSGQRGQ
K229-u DMAKLFEkIASTSEF
K238-u ASTSEFLkNGKARTD
K252 DLEIANSKASVCNLQ
S261-p SVCNLQIsPKSEDIN
K263 CNLQIsPKSEDINKF
K269 PKSEDINKFDWLDLD
K280 LDLDPLSKPKVDYVE
E303 KDPVLLAEDPWDAVL
K327-u LERKVNGkSLsGATV
S328 ERKVNGkSLsGATVT
S330-p KVNGkSLsGATVTRS
S339-p ATVTRSQsLIIRTAQ
K349-u IRTAQFTkAQGQVSQ
K580 RAVDQVIKAVRKICS
N613 RAVNLPRNkSADVTS
K614-u AVNLPRNkSADVTSL
S615 VNLPRNkSADVTSLS
S630 GSDTRKNSTKGSLNP
K863-u RNIIQQDkLETLESD
K872-u ETLESDIkGKLLDII
R881 KLLDIIHRDSSFGLS
K889 DSSFGLSKEDKVFLW
Y901 FLWENRYYCLKHPNC
K920-u LASAPNWkWANLAKT
K1107-u VAKELNIkSCSFFSS
K1162 IMDKIWLKEGLDLRM
S1190 MVELVPASDTLRKIQ
T1192 ELVPASDTLRKIQVE
K1217 PLAEWLRKYNPSEEE
S1281 GHAQMFGSFKRDRAP
K1414-u PILSFSPkTYSFRQD
S1553-p SAGAVPFsPTLGQIG
Y1595 DGADPNPYVKTYLLP
  rat

 
K11 ISNNSEFKQCSSSHP
S60 RGFELSNSTRQRTQG
Y73 QGFNKQDYDLMVFPE
K94 ALDIDVEKLTQAELE
K94 ALDIDVEKLTQAELE
N108 EKILLDDNFETRKTP
R112 LDDNFETRKTPASPV
T120 KTPASPVTPVLSPSF
S124 SPVTPVLSPSFSAQL
R134 FSAQLYLRPAVQRSQ
K229 DMAKLFDKIASTSEF
K238 ASTSEFLKNGKARTD
K252 DLEIANSKASVCNLQ
S261-p SVCNLQIsPKSEDIN
K263 CNLQIsPKSEDINKF
K269 PKSEDINKFDWLDLD
K280 LDLDPLSKPKIDCVE
E303 KNPVLLAEDPWDAVL
K328 LERKVNGKSLsGATV
S329 ERKVNGKSLsGATVT
S331-p KVNGKSLsGATVTRS
S340-p ATVTRSQsLIVRTTQ
K350 VRTTQVTKAQSQVSQ
K581 RAIDQVIKAVRKICS
N614 RAVNLPRNKSADVTS
K615 AVNLPRNKSADVTSL
S616 VNLPRNKSADVTSLS
S631 GGDTSKNSTRGSLNL
K864 RNIIQQYKLEALENE
K873 EALENEIKGKLLDIV
R882 KLLDIVHRDSSFGLS
K890 DSSFGLSKEDKAFLW
Y902 FLWEKRYYCLKHPNC
K921 LASAPNWKWANLAKT
K1108 VAKELNIKSCSFFSS
K1163 IMDKIWLKEGLDLRM
S1191-p MVELVPAsDtLRKIQ
T1193-p ELVPAsDtLRKIQVE
K1218 PLAEWLRKYNPSEEE
S1282 GHAQMFGSFKRDRAP
K1415 PILSFSPKTYSFRQD
S1554 STGTSPFSPTLGQIG
Y1596 DGADPNPYVKTYLLP
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