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Protein Page:
PIK3C3 (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
PIK3C3 Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate which plays a key role in initiation and maturation of autophagosomes. Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for the abcission step in cytokinesis. Required for transport from early to late endosomes. Heterodimer. This subunit, part of a complex composed of regulatory and catalytic subunits, associates with regulatory subunit PIK3R4. Forms a complex with BECN1, PIK3R4 and either UVRAG and KIAA0226/Rubicon, or with ATG14. In this complex, presence of UVRAG and ATG14 are mutually exclusive. Part of a complex composed of PIK3R4 and PIK3CB. Interacts with RAB7A in the presence of PIK3R4. Ubiquitously expressed, with a highest expression in skeletal muscle. Belongs to the PI3/PI4-kinase family. Note: This description may include information from UniProtKB.
Protein type: Kinase, lipid; Motility/polarity/chemotaxis; Carbohydrate Metabolism - inositol phosphate; Autophagy; EC 2.7.1.137
Cellular Component: late endosome; midbody; cytosol
Molecular Function: protein binding; 1-phosphatidylinositol-3-kinase activity; ATP binding; protein kinase activity
Biological Process: response to leucine; regulation of protein secretion; phosphoinositide-mediated signaling; endosome organization and biogenesis; early endosome to late endosome transport; phospholipid metabolic process; insulin receptor signaling pathway; phosphatidylinositol biosynthetic process; cytokinesis; innate immune response; cell cycle; autophagic vacuole formation
Reference #:  Q8NEB9 (UniProtKB)
Alt. Names/Synonyms: hVps34; MGC61518; Phosphatidylinositol 3-kinase catalytic subunit type 3; Phosphatidylinositol 3-kinase p100 subunit; Phosphoinositide-3-kinase class 3; phosphoinositide-3-kinase, class 3; PI3-kinase type 3; PI3K type 3; PIK3C3; PK3C3; PtdIns-3-kinase type 3; VPS34
Gene Symbols: PIK3C3
Molecular weight: 101,549 Da
Basal Isoelectric point: 6.37  Predict pI for various phosphorylation states
CST Pathways:  Adherens Junction Dynamics  |  AMPK Signaling  |  Angiogenesis  |  Apoptosis  |  Autophagy Signaling  |  ErbB/HER Signaling  |  ESC Pluripotency and Differentiation  |  Inhibition of Apoptosis  |  Jak/Stat/IL-6 Signaling  |  MAPK/Erk in Growth and Differentiation  |  Mitochondrial Control of Apoptosis  |  mTOR Signaling  |  NF-kB Signaling  |  PI3K/Akt Signaling  |  Protein Kinase C Signaling  |  Regulation of Actin Dynamics  |  Regulation of Microtubule Dynamics  |  SAPK/JNK Signaling Cascades  |  T Cell Receptor Signaling  |  TGF-ß Signaling  |  Translation: eIF4E and p70S6K  |  Warburg Effect
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PIK3C3
Protein Structure Not Found.


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


Sites Implicated In
endocytosis, altered: T159‑p
enzymatic activity, inhibited: T159‑p, T668‑p
molecular association, regulation: T159‑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 S25-p NVQLKIGsLEGKREQ
0 1 K96-u EWLKLPVkYPDLPRN
0 1 K158-u ADGSEPTktPGRtss
1 0 T159-p DGSEPTktPGRtssT
1 0 T163-p PTktPGRtssTLSED
1 0 S164-p TktPGRtssTLSEDQ
0 1 S165-p ktPGRtssTLSEDQM
0 2 S168 GRtssTLSEDQMSRL
0 1 K209-u EMINESEkRSSNFMY
0 1 S243 YEKDGDESsPILTSF
1 8 S244-p EKDGDESsPILTSFE
0 1 S261-p KVPDPQMsMENLVEs
0 1 S268-p sMENLVEsKHHKLAR
1 0 S282-p RSLRSGPsDHDLkPN
0 1 K287-m1 GPsDHDLkPNAATRD
0 1 T305-p IIVSYPPtKQLTYEE
0 1 Y321-p DLVWKFRyyLtNQEK
0 1 Y322-p LVWKFRyyLtNQEKA
0 1 T324-p WKFRyyLtNQEKALT
0 1 K346-u WDLPQEAkQALELLG
0 1 Y379-p TNPTVRRyAVARLRQ
0 1 Y395-p DDEDLLMyLLQLVQA
0 1 S448-p DSSQIITsPLPSVss
0 1 S454-p TsPLPSVssPPPASK
1 1 S455-p sPLPSVssPPPASKT
0 1 T488-p SRACKNStLANYLYW
0 1 T513-p TQQRDPKtHEMyLNV
0 1 Y517-p DPKtHEMyLNVMRRF
0 1 S525 LNVMRRFSQALLKGD
0 1 K530 RFSQALLKGDKSVRV
0 1 K533 QALLKGDKSVRVMRS
0 1 K630-u FKTEDGGkYPVIFKH
1 0 T668-p ENLDLKLtPYKVLAT
0 1 K778 KPLPPPMKLNKEMVE
0 1 K800 EQYQEFRKQCyTAFL
0 1 Y803-p QEFRKQCyTAFLHLR
0 2 Y884-p QIHKFAQyWRK____
  mouse

 
S25 NVQLKIGSLEGKREQ
K96 EWLKLPVKYPDLPRN
R158 ADGSEPTRtPGRTSS
T159-p DGSEPTRtPGRTSST
T163 PTRtPGRTSSTLsED
S164 TRtPGRTSSTLsEDQ
S165 RtPGRTSSTLsEDQM
S168-p GRTSSTLsEDQMSRL
K209 EMINESEKRSSNFMY
S243-p YEKDGDEssPILTSF
S244-p EKDGDEssPILTSFE
S261 KVPDPQMSMENLVES
S268 SMENLVESKHHKLAR
S282 RSLRSGPSDHDLKPN
K287 GPSDHDLKPNATTRD
T305 IIVSYPPTKQLTYEE
Y321 DLVWKFRYYLTNQEK
Y322 LVWKFRYYLTNQEKA
T324 WKFRYYLTNQEKALT
K346 WDLPQEAKQALELLG
Y379 TNPTVRRYAVARLRQ
Y395 DDEDLLMYLLQLVQA
N448 DSSQIITNPLPPVAS
A454 TNPLPPVASPPPASK
S455 NPLPPVASPPPASKA
T488 SRACKNSTLANYLYW
T513 TQQRDPKTHEMYLNV
Y517 DPKTHEMYLNVMRRF
S525-p LNVMRRFsQALLkGD
K530-a RFsQALLkGDkSVRV
K533-a QALLkGDkSVRVMRS
K630 FKTEDGGKYPVIFKH
T668 ENLDLKLTPYKVLAT
K778-a KPLPPPMkLNKEMVE
K800-a EQYQEFRkQCYTAFL
Y803 QEFRkQCYTAFLHLR
Y884 QIHKFAQYWRK____
  rat

 
S25 NVQLKIGSLEGKREQ
K96 EWLKLPVKYPDLPRN
R158 ADGSEPTRTPGRTSS
T159 DGSEPTRTPGRTSST
T163 PTRTPGRTSSTLSED
S164 TRTPGRTSSTLSEDQ
S165 RTPGRTSSTLSEDQM
S168 GRTSSTLSEDQMSRL
K209 EMINESEKRSSNFMY
S243 YEKDGDESsPILTSF
S244-p EKDGDESsPILTSFE
S261 KVPDPQMSMENLVES
S268 SMENLVESKHHKLAR
S282 RSLRSGPSDHDLKPN
K287 GPSDHDLKPNATTRD
T305 IIVSYPPTKQLTYEE
Y321 DLVWKFRYYLTNQEK
Y322 LVWKFRYYLTNQEKA
T324 WKFRYYLTNQEKALT
K346 WDLPQEAKQALELLG
Y379 TNPTVRRYAVARLRQ
Y395 DDEDLLMYLLQLVQA
N448 DSSQIITNPLPPVAS
A454 TNPLPPVASPPPASK
S455 NPLPPVASPPPASKS
T488 SRACKNSTLANYLYW
T513 TQQRDPKTHEMYLNV
Y517 DPKTHEMYLNVMRRF
S525 LNVMRRFSQALLKGD
K530 RFSQALLKGDKSVRV
K533 QALLKGDKSVRVMRS
K630 FKTEDGGKYPVIFKH
T668 ENLDLKLTPYKVLAT
K778 KPLPPPMKLNKEMVE
K800 EQYQEFRKQCYTAFL
Y803 QEFRKQCYTAFLHLR
Y884 QIHKFAQYWRK____
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