P3C2A_MOUSE - dbPTM
P3C2A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P3C2A_MOUSE
UniProt AC Q61194
Protein Name Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
Gene Name Pik3c2a
Organism Mus musculus (Mouse).
Sequence Length 1686
Subcellular Localization Cell membrane . Golgi apparatus . Cytoplasmic vesicle, clathrin-coated vesicle . Nucleus . Cytoplasm . Inserts preferentially into membranes containing PtdIns(4,5)P2. Associated with RNA-containing structures.
Protein Description 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 MAQISNNSEFKQCSSSHPEPIRTKDVNKAEALQMEAEALAKLQKDRQMTDSPRGFELSSSTRQRTQGFNKQDYDLMVFPELDSQKRAVDIDVEKLTQAELEKILLDDNFETRKPPALPVTPVLSPSFSTQLYLRPSGQRGQWPPGLCGPSTYTLPSTYPSAYSKQATFQNGFSPRMPTFPSTESVYLRLPGQSPYFSYPLTPATPFHPQGSLPVYRPLVSPDMAKLFEKIASTSEFLKNGKARTDLEIANSKASVCNLQISPKSEDINKFDWLDLDPLSKPKVDYVEVLEHEEEKKDPVLLAEDPWDAVLLEERSPSCHLERKVNGKSLSGATVTRSQSLIIRTAQFTKAQGQVSQKDPNGTSSLPTGSSLLQEFEVQNDEVAAFCQSIMKLKTKFPYTDHCTNPGYLLSPVTVQRNMCGENASVKVSIEIEGLQLPVTFTCDVSSTVEIIIMQALCWVHDDLNQVDVGSYILKVCGQEEVLQNNHCLGSHEHIQNCRKWDTEIKLQLLTLSAMCQNLARTAEDDEAPVDLNKYLYQIEKPYKEVMTRHPVEELLDSYHYQVELALQTENQHRAVDQVIKAVRKICSALDGVETPSVTEAVKKLKRAVNLPRNKSADVTSLSGSDTRKNSTKGSLNPENPVQVSMDHLTTAIYDLLRLHANSSRCSTACPRGSRNIKEAWTATEQLQFTVYAAHGISSNWVSNYEKYYLICSLSHNGKDLFKPIQSKKVGTYKNFFYLIKWDELIIFPIQISQLPLESVLHLTLFGVLNQSSGSSPDSNKQRKGPEALGKVSLTLFDFKRFLTCGTKLLYLWTSSHTNSIPGAIPKKSYVMERIVLQVDFPSPAFDIIYTSPQIDRNIIQQDKLETLESDIKGKLLDIIHRDSSFGLSKEDKVFLWENRYYCLKHPNCLPKILASAPNWKWANLAKTYSLLHQWPPLCPLAALELLDAKFADQEVRSLAVSWMEAISDDELADLLPQFVQALKYEIYLNSSLVRFLLSRALGNIQIAHSLYWLLKDALHDTHFGSRYEHVLGALLSVGGKGLREELSKQMKLVQLLGGVAEKVRQASGSTRQVVLQKSMERVQSFFLRNKCRLPLKPSLVAKELNIKSCSFFSSNAMPLKVTMVNADPLGEEINVMFKVGEDLRQDMLALQMIKIMDKIWLKEGLDLRMVIFRCLSTGRDRGMVELVPASDTLRKIQVEYGVTGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGKFLGHAQMFGSFKRDRAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAYNLIRKQTNLFLNLLSLMIPSGLPELTSIQDLKYVRDALQPQTTDAEATIFFTRLIESSLGSIATKFNFFIHNLAQLRFSGLPSNDEPILSFSPKTYSFRQDGRIKEVSVFTYHKKYNPDKHYIYVVRILREGHLEPSFVFRTFDEFQELHNKLSIIFPLWKLPGFPNRMVLGRTHIKDVAAKRKIELNSYLQSLMNASTDVAECDLVCTFFHPLLRDEKAEGIARSAGAVPFSPTLGQIGGAVKLSVSYRNGTLFIMVMHIKDLVTEDGADPNPYVKTYLLPDTHKTSKRKTKISRKTRNPTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGITLPLKDFNLSKETVKWYQLTAATYL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAQISNNSE
------CCCCCCCHH		27.07-
11UbiquitinationISNNSEFKQCSSSHP
CCCCHHHCCCCCCCC		46.47-
49PhosphorylationLQKDRQMTDSPRGFE
HHHHHHCCCCCCCCC		25.6129514104
51PhosphorylationKDRQMTDSPRGFELS
HHHHCCCCCCCCCCC		13.8229514104
58PhosphorylationSPRGFELSSSTRQRT
CCCCCCCCHHHHHHC		18.2929176673
59PhosphorylationPRGFELSSSTRQRTQ
CCCCCCCHHHHHHCC		48.6429176673
60PhosphorylationRGFELSSSTRQRTQG
CCCCCCHHHHHHCCC		25.0027149854
61PhosphorylationGFELSSSTRQRTQGF
CCCCCHHHHHHCCCC		32.5429176673
73PhosphorylationQGFNKQDYDLMVFPE
CCCCHHCCEEEEECC		14.4225367039
120PhosphorylationKPPALPVTPVLSPSF
CCCCCCCCCCCCCCC		13.0226060331
124PhosphorylationLPVTPVLSPSFSTQL
CCCCCCCCCCCCEEE		20.8026824392
126PhosphorylationVTPVLSPSFSTQLYL
CCCCCCCCCCEEEEE		28.5826060331
134MethylationFSTQLYLRPSGQRGQ
CCEEEEECCCCCCCC		15.1318963901
134DimethylationFSTQLYLRPSGQRGQ
CCEEEEECCCCCCCC		15.13-
216DimethylationQGSLPVYRPLVSPDM
CCCCCCCCCCCCHHH		20.50-
216MethylationQGSLPVYRPLVSPDM
CCCCCCCCCCCCHHH		20.5018962551
229UbiquitinationDMAKLFEKIASTSEF
HHHHHHHHHHCCHHH		35.92-
238UbiquitinationASTSEFLKNGKARTD
HCCHHHHHCCCCCCC		69.81-
261 (in isoform 2)Phosphorylation-17.2019144319
261PhosphorylationSVCNLQISPKSEDIN
CEECEEECCCCCCCC		17.2025521595
327UbiquitinationLERKVNGKSLSGATV
EEEEECCEECCCCEE		42.91-
328PhosphorylationERKVNGKSLSGATVT
EEEECCEECCCCEEC		29.2126643407
330PhosphorylationKVNGKSLSGATVTRS
EECCEECCCCEECCC		33.2130352176
333PhosphorylationGKSLSGATVTRSQSL
CEECCCCEECCCCEE		26.4026643407
335PhosphorylationSLSGATVTRSQSLII
ECCCCEECCCCEEEE		21.9026643407
337PhosphorylationSGATVTRSQSLIIRT
CCCEECCCCEEEEEE		18.1126643407
339PhosphorylationATVTRSQSLIIRTAQ
CEECCCCEEEEEEEE		23.8422942356
344PhosphorylationSQSLIIRTAQFTKAQ
CCEEEEEEEEEEECC		17.8823984901
348PhosphorylationIIRTAQFTKAQGQVS
EEEEEEEEECCCCCC		17.2523984901
349UbiquitinationIRTAQFTKAQGQVSQ
EEEEEEEECCCCCCC		39.75-
364PhosphorylationKDPNGTSSLPTGSSL
CCCCCCCCCCCCCHH		37.9023649490
542PhosphorylationLYQIEKPYKEVMTRH
HHHCCCCHHHHHHHC		30.7429514104
614UbiquitinationAVNLPRNKSADVTSL
HHCCCCCCCCCCCCC		48.58-
615PhosphorylationVNLPRNKSADVTSLS
HCCCCCCCCCCCCCC		33.0030352176
620PhosphorylationNKSADVTSLSGSDTR
CCCCCCCCCCCCCCC		22.0130352176
622PhosphorylationSADVTSLSGSDTRKN
CCCCCCCCCCCCCCC		35.7025521595
630PhosphorylationGSDTRKNSTKGSLNP
CCCCCCCCCCCCCCC		34.2329514104
863UbiquitinationRNIIQQDKLETLESD
CCHHHHHHHHHHHHH		43.83-
872UbiquitinationETLESDIKGKLLDII
HHHHHHHCCHHHHHH		55.79-
920UbiquitinationLASAPNWKWANLAKT
HHCCCCCHHHHHHHH		42.97-
1069PhosphorylationKVRQASGSTRQVVLQ
HHHHCCCCCHHHHHH		20.23-
1070PhosphorylationVRQASGSTRQVVLQK
HHHCCCCCHHHHHHH		28.75-
1098O-linked_GlycosylationCRLPLKPSLVAKELN
CCCCCCHHHHHHHCC		33.6130059200
1107UbiquitinationVAKELNIKSCSFFSS
HHHHCCCCCCCCCCC		44.32-
1190PhosphorylationMVELVPASDTLRKIQ
CEEEEECHHHHHEEE		25.6729895711
1192PhosphorylationELVPASDTLRKIQVE
EEEECHHHHHEEEEE		26.4329895711
1281PhosphorylationGHAQMFGSFKRDRAP
CCHHHHCCCCCCCCC		19.1426824392
1292PhosphorylationDRAPFVLTSDMAYVI
CCCCEEEECCEEEEC		19.8528494245
1297PhosphorylationVLTSDMAYVINGGEK
EEECCEEEECCCCCC		8.6728494245
1306PhosphorylationINGGEKPTIRFQLFV
CCCCCCCEEEHHHHH		35.5328494245
1346PhosphorylationPSGLPELTSIQDLKY
CCCCCCCCCHHHHHH		23.3221183079
1347PhosphorylationSGLPELTSIQDLKYV
CCCCCCCCHHHHHHH		30.7721183079
1353PhosphorylationTSIQDLKYVRDALQP
CCHHHHHHHHHHHCC		14.1721183079
1384PhosphorylationSSLGSIATKFNFFIH
HHHHHHHHHHHHHHH		34.2029899451
1399PhosphorylationNLAQLRFSGLPSNDE
CHHHHHHCCCCCCCC		32.7428973931
1414UbiquitinationPILSFSPKTYSFRQD
CCEEECCCEEEECCC		59.92-
1416PhosphorylationLSFSPKTYSFRQDGR
EEECCCEEEECCCCC		16.3729514104
1553PhosphorylationSAGAVPFSPTLGQIG
CCCCCCCCCCHHHCC		15.7626745281
1555PhosphorylationGAVPFSPTLGQIGGA
CCCCCCCCHHHCCCE		42.1826745281
1595PhosphorylationDGADPNPYVKTYLLP
CCCCCCCCCCEEECC		22.6325195567
1599PhosphorylationPNPYVKTYLLPDTHK
CCCCCCEEECCCCCC		10.6725195567
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of P3C2A_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
261SPhosphorylation

10329640
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of P3C2A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of P3C2A_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P3C2A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASSSPECTROMETRY.

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