Pik3c2a
entrez
18704
canonical
uniprot
Q61194
canonical
ensembl
ENSMUSG00000030660
resolver
ensp
ENSMUSP00000126092
resolver
ensp
ENSMUSP00000146181
resolver
enst
ENSMUST00000170430
resolver
enst
ENSMUST00000206219
resolver
genesymbol
Pik3c2a
resolver
genesymbol_syn
Cpk
resolver
uniprot
F8VPL2
resolver
uniprot
Q61182
resolver
uniprot_entry
F8VPL2_MOUSE
resolver
uniprot_entry
P3C2A_MOUSE
resolver
uniprot_sec
Q61182
resolver
activity_regulation
ACTIVITY REGULATION: Activated by clathrin (By similarity). Only slightly inhibited by wortmannin and LY294002. Activated by insulin. {ECO:0000250|UniProtKB:O00443, ECO:0000269|PubMed:10329640, ECO:0000269|PubMed:8663140}.
uniprot
proteins
amino_acid_sequence
MAQISNNSEFKQCSSSHPEPIRTKDVNKAEALQMEAEALAKLQKDRQMTDSPRGFELSSSTRQRTQGFNKQDYDLMVFPELDSQKRAVDIDVEKLTQAELEKILLDDNFETRKPPALPVTPVLSPSFSTQLYLRPSGQRGQWPPGLCGPSTYTLPSTYPSAYSKQATFQNGFSPRMPTFPSTESVYLRLPGQSPYFSYPLTPATPFHPQGSLPVYRPLVSPDMAKLFEKIASTSEFLKNGKARTDLEIANSKASVCNLQISPKSEDINKFDWLDLDPLSKPKVDYVEVLEHEEEKKDPVLLAEDPWDAVLLEERSPSCHLERKVNGKSLSGATVTRSQSLIIRTAQFTKAQGQVSQKDPNGTSSLPTGSSLLQEFEVQNDEVAAFCQSIMKLKTKFPYTDHCTNPGYLLSPVTVQRNMCGENASVKVSIEIEGLQLPVTFTCDVSSTVEIIIMQALCWVHDDLNQVDVGSYILKVCGQEEVLQNNHCLGSHEHIQNCRKWDTEIKLQLLTLSAMCQNLARTAEDDEAPVDLNKYLYQIEKPYKEVMTRHPVEELLDSYHYQVELALQTENQHRAVDQVIKAVRKICSALDGVETPSVTEAVKKLKRAVNLPRNKSADVTSLSGSDTRKNSTKGSLNPENPVQVSMDHLTTAIYDLLRLHANSSRCSTACPRGSRNIKEAWTATEQLQFTVYAAHGISSNWVSNYEKYYLICSLSHNGKDLFKPIQSKKVGTYKNFFYLIKWDELIIFPIQISQLPLESVLHLTLFGVLNQSSGSSPDSNKQRKGPEALGKVSLTLFDFKRFLTCGTKLLYLWTSSHTNSIPGAIPKKSYVMERIVLQVDFPSPAFDIIYTSPQIDRNIIQQDKLETLESDIKGKLLDIIHRDSSFGLSKEDKVFLWENRYYCLKHPNCLPKILASAPNWKWANLAKTYSLLHQWPPLCPLAALELLDAKFADQEVRSLAVSWMEAISDDELADLLPQFVQALKYEIYLNSSLVRFLLSRALGNIQIAHSLYWLLKDALHDTHFGSRYEHVLGALLSVGGKGLREELSKQMKLVQLLGGVAEKVRQASGSTRQVVLQKSMERVQSFFLRNKCRLPLKPSLVAKELNIKSCSFFSSNAMPLKVTMVNADPLGEEINVMFKVGEDLRQDMLALQMIKIMDKIWLKEGLDLRMVIFRCLSTGRDRGMVELVPASDTLRKIQVEYGVTGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGKFLGHAQMFGSFKRDRAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAYNLIRKQTNLFLNLLSLMIPSGLPELTSIQDLKYVRDALQPQTTDAEATIFFTRLIESSLGSIATKFNFFIHNLAQLRFSGLPSNDEPILSFSPKTYSFRQDGRIKEVSVFTYHKKYNPDKHYIYVVRILREGHLEPSFVFRTFDEFQELHNKLSIIFPLWKLPGFPNRMVLGRTHIKDVAAKRKIELNSYLQSLMNASTDVAECDLVCTFFHPLLRDEKAEGIARSAGAVPFSPTLGQIGGAVKLSVSYRNGTLFIMVMHIKDLVTEDGADPNPYVKTYLLPDTHKTSKRKTKISRKTRNPTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGITLPLKDFNLSKETVKWYQLTAATYL
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 (By similarity). {ECO:0000250|UniProtKB:O00443, ECO:0000269|PubMed:10329640, ECO:0000269|PubMed:20061534, ECO:0000269|PubMed:20974805, ECO:0000269|PubMed:8663140}.
uniprot
proteins
mass_dalton
190758
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Ser-261 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation (By similarity). Phosphorylated upon insulin stimulation; which may lead to enzyme activation. {ECO:0000250|UniProtKB:O00443, ECO:0000269|PubMed:10329640}.
uniprot
proteins
protein_family
PI3/PI4-kinase family
uniprot
proteins
pubmed
10329640
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16338929
uniprot
proteins
pubmed
17114649
uniprot
proteins
pubmed
20061534
uniprot
proteins
pubmed
20974805
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22648168
uniprot
proteins
pubmed
8662856
uniprot
proteins
pubmed
8663140
uniprot
proteins
sequence_length
1686
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00443}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:O00443}. Nucleus {ECO:0000250|UniProtKB:O00443}. Cytoplasm {ECO:0000250|UniProtKB:O00443}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O00443}. Note=Inserts preferentially into membranes containing PtdIns(4,5)P2. Associated with RNA-containing structures. {ECO:0000250|UniProtKB:O00443}.
uniprot
proteins