Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha  

UniProtKB / Swiss-Prot ID :  P3C2A_HUMAN

Gene Name (Synonyms) : 
PIK3C2A  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane. Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle. Nucleus. Cytoplasm. Note=According to PubMed:10766823 and PubMed:11239472, it is found in the cell membrane, the Golgi apparatus and in clathrin-coated vesicles. According to P 

Protein Function :  Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin- mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin- independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function. 

Protein Sequence MAQISSNSGFKECPSSHPEPTRAKDVDKEEALQMEAEALAKLQKDRQVTDNQRGFELSSSTRKKAQVYNK...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHCCCCCCCCEEECCHHHHHHHCCCC...
Protein Variant
LocationDescription
1415T -> A (in dbSNP:rs11604561). VAR_023333
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAQISS
---CCCCCC
27.07UniProtKB
Link-
60PhosphoserineELSSSTRKK
EECCHHHHH
28.93HPRD
Link-
60PhosphoserineELSSSTRKK
EECCHHHHH
28.93PhosphoELM
Link-
60PhosphoserineELSSSTRKK
EECCHHHHH
28.93Phosphositeplus
Link-
60PhosphoserineELSSSTRKK
EECCHHHHH
28.93SysPTM
Link-
60Phosphoserine.ELSSSTRKK
EECCHHHHH
28.93UniProtKB
Link-
73PhosphotyrosineNKQDYDLMV
CCCCCEEEE
14.42HPRD
Link-
73PhosphotyrosineNKQDYDLMV
CCCCCEEEE
14.42Phosphositeplus
Link-
94Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IDVEKLTQA
CCHHHHHHH
57.60Phosphositeplus
Link-
94N6-acetyllysineIDVEKLTQA
CCHHHHHHH
57.60Phosphositeplus
Link-
108PhosphoserineLLDDSFETK
HHCCCCCCC
25.34HPRD
Link-
108PhosphoserineLLDDSFETK
HHCCCCCCC
25.34PhosphoELM
Link-
108PhosphoserineLLDDSFETK
HHCCCCCCC
25.34Phosphositeplus
Link-
108PhosphoserineLLDDSFETK
HHCCCCCCC
25.34SysPTM
Link-
108Phosphoserine.LLDDSFETK
HHCCCCCCC
25.34UniProtKB
Link-
112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SFETKKTPV
CCCCCCCCC
47.67Phosphositeplus
Link-
229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KLFDKIAST
HHHHHHHHH
32.60Phosphositeplus
Link-
252Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ITDSKVSNL
EECCCCCCC
53.12Phosphositeplus
Link-
254Phosphoserine.DSKVSNLQV
CCCCCCCEE
35.24UniProtKB
Link-
259PhosphoserineNLQVSPKSE
CCEECCCCC
17.41HPRD
Link-
259PhosphoserineNLQVSPKSE
CCEECCCCC
17.41Phosphositeplus
Link-
259PhosphoserineNLQVSPKSE
CCEECCCCC
17.41SysPTM
Link-
259Phosphoserine (CDK1)NLQVSPKSE
CCEECCCCC
17.41PhosphoELM
Link-
259Phosphoserine.NLQVSPKSE
CCEECCCCC
17.41UniProtKB
Link-
261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QVSPKSEDI
EECCCCCCC
60.00Phosphositeplus
Link-
267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EDISKFDWL
CCCCCCCCC
47.91Phosphositeplus
Link-
278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DPLSKPKVD
CCCCCCCCC
57.45Phosphositeplus
Link-
301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SLLAKDPWD
EEEECCCCC
65.38Phosphositeplus
Link-
327PhosphoserineVNGKSLSVA
CCCCCCCCC
27.55Phosphositeplus
Link-
338PhosphoserineTRSQSLNIR
EECCCCCCC
25.32HPRD
Link-
338PhosphoserineTRSQSLNIR
EECCCCCCC
25.32PhosphoELM
Link-
338PhosphoserineTRSQSLNIR
EECCCCCCC
25.32Phosphositeplus
Link-
338PhosphoserineTRSQSLNIR
EECCCCCCC
25.32SysPTM
Link-
338Phosphoserine.TRSQSLNIR
EECCCCCCC
25.32UniProtKB
Link-
579Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DQVIKAVRK
HHHHHHHHH
41.81Phosphositeplus
Link-
613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LPRSKTADV
CCCCHHHHH
49.35Phosphositeplus
Link-
872Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ENDIKGKLL
HHHHHHHHH
53.51Phosphositeplus
Link-
881Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DILHKDSSL
HHHHCCCCC
56.72Phosphositeplus
Link-
889Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LGLSKEDKA
CCHHHHHHH
74.99Phosphositeplus
Link-
1162Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KIWLKEGLD
HHHHHCCCC
34.44Phosphositeplus
Link-
1217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EWLRKYNPS
HHHHHHCCC
47.40Phosphositeplus
Link-
1551PhosphoserineADAGSFSPT
CCCCCCCCC
25.03HPRD
Link-
1553PhosphoserineAGSFSPTPG
CCCCCCCCC
29.57HPRD
Link-
1553PhosphoserineAGSFSPTPG
CCCCCCCCC
29.57Phosphositeplus
Link-
1553PhosphoserineAGSFSPTPG
CCCCCCCCC
29.57SysPTM
Link-
1553Phosphoserine.AGSFSPTPG
CCCCCCCCC
29.57UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Mitotic and stress-induced phosphorylation of HsPI3K-C2alpha targetsthe protein for degradation.";
Didichenko S.A., Fragoso C.M., Thelen M.;
J. Biol. Chem. 278:26055-26064(2003).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-259, MUTAGENESIS OF SER-254; SER-259;SER-262 AND SER-266, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-259 ANDSER-1553, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-108; SER-259 ANDSER-338, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-254; SER-259;SER-338 AND SER-1553, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures