PIK3C2A
entrez
5286
canonical
uniprot
O00443
canonical
ensembl
ENSG00000011405
resolver
ensp
ENSP00000509400
resolver
ensp
ENSP00000561529
resolver
ensp
ENSP00000561530
resolver
ensp
ENSP00000598108
resolver
genesymbol
PIK3C2A
resolver
hgnc
HGNC:8971
resolver
uniprot
B0LPH2
resolver
uniprot
B4DG55
resolver
uniprot
B4E2G4
resolver
uniprot
Q14CQ9
resolver
uniprot_entry
B4DG55_HUMAN
resolver
uniprot_entry
P3C2A_HUMAN
resolver
uniprot_sec
B0LPH2
resolver
uniprot_sec
B4E2G4
resolver
uniprot_sec
Q14CQ9
resolver
activity_regulation
ACTIVITY REGULATION: Activated by insulin (By similarity). Only slightly inhibited by wortmannin and LY294002. Activated by clathrin. {ECO:0000250|UniProtKB:Q61194, ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:9337861}.
uniprot
proteins
amino_acid_sequence
MAQISSNSGFKECPSSHPEPTRAKDVDKEEALQMEAEALAKLQKDRQVTDNQRGFELSSSTRKKAQVYNKQDYDLMVFPESDSQKRALDIDVEKLTQAELEKLLLDDSFETKKTPVLPVTPILSPSFSAQLYFRPTIQRGQWPPGLPGPSTYALPSIYPSTYSKQAAFQNGFNPRMPTFPSTEPIYLSLPGQSPYFSYPLTPATPFHPQGSLPIYRPVVSTDMAKLFDKIASTSEFLKNGKARTDLEITDSKVSNLQVSPKSEDISKFDWLDLDPLSKPKVDNVEVLDHEEEKNVSSLLAKDPWDAVLLEERSTANCHLERKVNGKSLSVATVTRSQSLNIRTTQLAKAQGHISQKDPNGTSSLPTGSSLLQEVEVQNEEMAAFCRSITKLKTKFPYTNHRTNPGYLLSPVTAQRNICGENASVKVSIDIEGFQLPVTFTCDVSSTVEIIIMQALCWVHDDLNQVDVGSYVLKVCGQEEVLQNNHCLGSHEHIQNCRKWDTEIRLQLLTFSAMCQNLARTAEDDETPVDLNKHLYQIEKPCKEAMTRHPVEELLDSYHNQVELALQIENQHRAVDQVIKAVRKICSALDGVETLAITESVKKLKRAVNLPRSKTADVTSLFGGEDTSRSSTRGSLNPENPVQVSINQLTAAIYDLLRLHANSGRSPTDCAQSSKSVKEAWTTTEQLQFTIFAAHGISSNWVSNYEKYYLICSLSHNGKDLFKPIQSKKVGTYKNFFYLIKWDELIIFPIQISQLPLESVLHLTLFGILNQSSGSSPDSNKQRKGPEALGKVSLPLFDFKRFLTCGTKLLYLWTSSHTNSVPGTVTKKGYVMERIVLQVDFPSPAFDIIYTTPQVDRSIIQQHNLETLENDIKGKLLDILHKDSSLGLSKEDKAFLWEKRYYCFKHPNCLPKILASAPNWKWVNLAKTYSLLHQWPALYPLIALELLDSKFADQEVRSLAVTWIEAISDDELTDLLPQFVQALKYEIYLNSSLVQFLLSRALGNIQIAHNLYWLLKDALHDVQFSTRYEHVLGALLSVGGKRLREELLKQTKLVQLLGGVAEKVRQASGSARQVVLQRSMERVQSFFQKNKCRLPLKPSLVAKELNIKSCSFFSSNAVPLKVTMVNADPMGEEINVMFKVGEDLRQDMLALQMIKIMDKIWLKEGLDLRMVIFKCLSTGRDRGMVELVPASDTLRKIQVEYGVTGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGKFLGHAQMFGSFKRDRAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAYNLIRKQTNLFLNLLSLMIPSGLPELTSIQDLKYVRDALQPQTTDAEATIFFTRLIESSLGSIATKFNFFIHNLAQLRFSGLPSNDEPILSFSPKTYSFRQDGRIKEVSVFTYHKKYNPDKHYIYVVRILREGQIEPSFVFRTFDEFQELHNKLSIIFPLWKLPGFPNRMVLGRTHIKDVAAKRKIELNSYLQSLMNASTDVAECDLVCTFFHPLLRDEKAEGIARSADAGSFSPTPGQIGGAVKLSISYRNGTLFIMVMHIKDLVTEDGADPNPYVKTYLLPDNHKTSKRKTKISRKTRNPTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGVTLPLKDFNLSKETVKWYQLTAATYL
uniprot
proteins
disease_involvement
DISEASE: Oculoskeletodental syndrome (OCSKD) [MIM:618440]: An autosomal recessive syndrome characterized by congenital cataracts, short stature, dysmorphic features with coarse facies, dental anomalies, multiple skeletal abnormalities, and neurological manifestations. Other recurrent features include hearing loss, secondary glaucoma, and nephrocalcinosis. {ECO:0000269|PubMed:31034465}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.1.137
uniprot
proteins
ec_number
2.7.1.153
uniprot
proteins
ec_number
2.7.1.154
uniprot
proteins
function
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. Involved in the regulation of ciliogenesis and trafficking of ciliary components (PubMed:31034465). {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:12719431, ECO:0000269|PubMed:16215232, ECO:0000269|PubMed:21081650, ECO:0000269|PubMed:31034465, ECO:0000269|PubMed:9337861}.
uniprot
proteins
mass_dalton
190680
uniprot
proteins
mutagenesis
MUTAGEN 103..107; /note="LLLDD->AAAAA: Reduces clathrin binding."; /evidence="ECO:0000269|PubMed:11239472"; MUTAGEN 254; /note="S->A: No effect on phosphorylation in vitro."; /evidence="ECO:0000269|PubMed:12719431"; MUTAGEN 259; /note="S->A,D,E: Abolishes phosphorylation, no change in activity."; /evidence="ECO:0000269|PubMed:12719431"; MUTAGEN 259; /note="S->A: Protects from proteolysis."; /evidence="ECO:0000269|PubMed:12719431"; MUTAGEN 262; /note="S->A: No effect on phosphorylation in vitro."; /evidence="ECO:0000269|PubMed:12719431"; MUTAGEN 266; /note="S->A: No effect on phosphorylation in vitro."; /evidence="ECO:0000269|PubMed:12719431"; MUTAGEN 1250; /note="D->A: Abolishes lipid kinase activity. Affects clathrin distribution when combined with a truncation encompassing the region of clathrin interaction."; /evidence="ECO:0000269|PubMed:16215232"; MUTAGEN 1488; /note="R->A: Reduces affinity for PtdIns(4,5)P2-containing membranes 7-fold."; /evidence="ECO:0000269|PubMed:17038310"; MUTAGEN 1490; /note="V->A: Reduces affinity for PtdIns(4,5)P2-containing membranes 7-fold."; /evidence="ECO:0000269|PubMed:17038310"; MUTAGEN 1491; /note="L->A: Reduces affinity for PtdIns(4,5)P2-containing membranes 5-fold."; /evidence="ECO:0000269|PubMed:17038310"; MUTAGEN 1493; /note="R->A: Reduces affinity for PtdIns(4,5)P2-containing membranes 23-fold."; /evidence="ECO:0000269|PubMed:17038310"; MUTAGEN 1503; /note="R->A: Abolishes interaction with PtdIns(4,5)P2-containing membranes."; /evidence="ECO:0000269|PubMed:17038310
uniprot
proteins
post_translational_modification
PTM: Phosphorylated upon insulin stimulation; which may lead to enzyme activation (By similarity). Phosphorylated on Ser-259 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation. Ser-259 phosphorylation may be mediated by CDK1 or JNK, depending on the physiological state of the cell. {ECO:0000250|UniProtKB:Q61194, ECO:0000269|PubMed:11606566, ECO:0000269|PubMed:12719431}.
uniprot
proteins
protein_family
PI3/PI4-kinase family
uniprot
proteins
pubmed
10766823
uniprot
proteins
pubmed
10805725
uniprot
proteins
pubmed
11239472
uniprot
proteins
pubmed
11606566
uniprot
proteins
pubmed
12719431
uniprot
proteins
pubmed
14563213
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16215232
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17038310
uniprot
proteins
pubmed
17371240
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21081650
uniprot
proteins
pubmed
21127054
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
31034465
uniprot
proteins
pubmed
9337861
uniprot
proteins
sequence_length
1686
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:17038310}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:11239472}. Nucleus {ECO:0000269|PubMed:11606566}. Cytoplasm {ECO:0000269|PubMed:11606566, ECO:0000269|PubMed:14563213}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:11239472}. Note=Inserts preferentially into membranes containing PtdIns(4,5)P2 (PubMed:17038310). Associated with RNA-containing structures (PubMed:11606566). {ECO:0000269|PubMed:11606566, ECO:0000269|PubMed:17038310}.
uniprot
proteins