PK3CA_HUMAN - dbPTM
PK3CA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PK3CA_HUMAN
UniProt AC P42336
Protein Name Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
Gene Name PIK3CA
Organism Homo sapiens (Human).
Sequence Length 1068
Subcellular Localization
Protein Description Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. Also has serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS. Plays a role in the positive regulation of phagocytosis and pinocytosis (By similarity)..
Protein Sequence MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLITIKHELFKEARKYPLHQLLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFAIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMDCFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSREAGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAMELLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRRPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQECTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDWIFHTIKQHALN
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
100UbiquitinationRLFQPFLKVIEPVGN
HHHHHHHHHHCCCCC		41.36-
111AcetylationPVGNREEKILNREIG
CCCCHHHHHHCHHCH		47.9825953088
148UbiquitinationRNILNVCKEAVDLRD
HHHHHHHHHHCCHHH		44.41-
158PhosphorylationVDLRDLNSPHSRAMY
CCHHHCCCCCCCEEE		31.1526091039
165PhosphorylationSPHSRAMYVYPPNVE
CCCCCEEEECCCCCC		8.8826552605
167PhosphorylationHSRAMYVYPPNVESS
CCCEEEECCCCCCCC		8.7626552605
173PhosphorylationVYPPNVESSPELPKH
ECCCCCCCCCCCCHH		47.0826552605
174PhosphorylationYPPNVESSPELPKHI
CCCCCCCCCCCCHHH		14.6426552605
184UbiquitinationLPKHIYNKLDKGQII
CCHHHHHCCCCCCEE		40.88-
231PhosphorylationAIRKKTRSMLLSSEQ
HHHHHHHHHHCCHHH		21.0024114839
232SulfoxidationIRKKTRSMLLSSEQL
HHHHHHHHHCCHHHH		3.8321406390
246PhosphorylationLKLCVLEYQGKYILK
HHHHHHHHCCEEHHH		20.5723917254
268PhosphorylationFLEKYPLSQYKYIRS
HHHHCCHHHHHHHHH		27.2824719451
275PhosphorylationSQYKYIRSCIMLGRM
HHHHHHHHHHHHCCC		9.8426552605
292PhosphorylationLMLMAKESLYSQLPM
HHHHHHHHHHHCCCC		31.7226552605
294PhosphorylationLMAKESLYSQLPMDC
HHHHHHHHHCCCCCC		12.0326552605
295PhosphorylationMAKESLYSQLPMDCF
HHHHHHHHCCCCCCC		30.4526552605
303PhosphorylationQLPMDCFTMPSYSRR
CCCCCCCCCCCCCCC		34.2123882029
306PhosphorylationMDCFTMPSYSRRIST
CCCCCCCCCCCCCCC		25.5626552605
307PhosphorylationDCFTMPSYSRRISTA
CCCCCCCCCCCCCCC		10.5826552605
308PhosphorylationCFTMPSYSRRISTAT
CCCCCCCCCCCCCCC		21.3023882029
312PhosphorylationPSYSRRISTATPYMN
CCCCCCCCCCCCCCC		15.3521722762
313PhosphorylationSYSRRISTATPYMNG
CCCCCCCCCCCCCCC		31.9821722762
315PhosphorylationSRRISTATPYMNGET
CCCCCCCCCCCCCCC		18.2921722762
317PhosphorylationRISTATPYMNGETST
CCCCCCCCCCCCCCC		10.0025884760
322PhosphorylationTPYMNGETSTKSLWV
CCCCCCCCCCCHHHH		42.9921722762
323PhosphorylationPYMNGETSTKSLWVI
CCCCCCCCCCHHHHH		29.5421722762
324PhosphorylationYMNGETSTKSLWVIN
CCCCCCCCCHHHHHC		31.8821722762
332PhosphorylationKSLWVINSALRIKIL
CHHHHHCHHHHHHHH		19.98-
355PhosphorylationIRDIDKIYVRTGIYH
HHHCCEEEEECCCCC		6.93-
361PhosphorylationIYVRTGIYHGGEPLC
EEEECCCCCCCEECC		8.85-
507PhosphorylationVSREAGFSYSHAGLS
CCCCCCCCCCCHHHH		25.4721945579
508PhosphorylationSREAGFSYSHAGLSN
CCCCCCCCCCHHHHH		11.3821945579
509PhosphorylationREAGFSYSHAGLSNR
CCCCCCCCCHHHHHH		12.9821945579
532UbiquitinationENDKEQLKAISTRDP
HCHHHHHHHHHCCCC		43.28-
571PhosphorylationILPKLLLSVKWNSRD
HHHHHHHHCCCCCHH		22.9424719451
576PhosphorylationLLSVKWNSRDEVAQM
HHHCCCCCHHHHHHH		39.7426434552
584PhosphorylationRDEVAQMYCLVKDWP
HHHHHHHHHHHCCCC		3.1626434552
698PhosphorylationYCRACGMYLKHLNRQ
HHHHHHHHHHHHHHH		9.62-
863AcetylationTIMQIQCKGGLKGAL
EEEEEEECCCHHHHE		39.3725953088
863UbiquitinationTIMQIQCKGGLKGAL
EEEEEEECCCHHHHE		39.37-
874PhosphorylationKGALQFNSHTLHQWL
HHHEEECHHHHHHHH		21.09-
876PhosphorylationALQFNSHTLHQWLKD
HEEECHHHHHHHHHH		26.25-
957PhosphorylationERVPFVLTQDFLIVI
CCCCEEEECCEEEEE		22.31-
973UbiquitinationKGAQECTKTREFERF
CCHHHCCCCHHHHHH		58.19-
1030UbiquitinationRKTLALDKTEQEALE
HHHHCCCHHHHHHHH		55.61-
1038PhosphorylationTEQEALEYFMKQMND
HHHHHHHHHHHHCHH		15.15-
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 PK3CA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PK3CA_HUMAN !!
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 PK3CA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRP3_HUMANRASGRP3physical
15213298
RASH_HUMANHRASphysical
14724584
RHES_HUMANRASD2physical
14724584
ADAP1_HUMANADAP1physical
12893243
DGKZ_HUMANDGKZphysical
12890670
ARHG1_HUMANARHGEF1physical
12754211
RASH_HUMANHRASphysical
8665852
SGK1_HUMANSGK1physical
10357815
CASL_HUMANNEDD9physical
18624398
SQSTM_HUMANSQSTM1physical
18624398
AMBP_HUMANAMBPphysical
18624398
ATIF1_HUMANATPIF1physical
18624398
SYVM_HUMANVARS2physical
18624398
DDX5_HUMANDDX5physical
18624398
DNJB6_HUMANDNAJB6physical
18624398
FRIL_HUMANFTLphysical
18624398
ITIH1_HUMANITIH1physical
18624398
RS20_HUMANRPS20physical
18624398
UFD1_HUMANUFD1Lphysical
18624398
CBL_HUMANCBLphysical
9119889
CBL_HUMANCBLphysical
11157475
STAT1_HUMANSTAT1physical
11438544
APC7_MOUSEAnapc7physical
20368287
SMAD2_HUMANSMAD2physical
16806069
SMAD3_HUMANSMAD3physical
16806069
AKT1_HUMANAKT1physical
21816939
BEX1_HUMANBEX1physical
25640309
BEX2_HUMANBEX2physical
25640309
I13R2_HUMANIL13RA2physical
25640309
IL24_HUMANIL24physical
25640309
HOP2_HUMANPSMC3IPphysical
25640309
THRSP_HUMANTHRSPphysical
25640309
TNF13_HUMANTNFSF13physical
25640309
UMPS_HUMANUMPSphysical
25640309
P85B_HUMANPIK3R2physical
26496610
P55G_HUMANPIK3R3physical
26496610
TSN14_HUMANTSPAN14physical
26496610
DPY30_HUMANDPY30physical
26496610
AKT1_HUMANAKT1physical
21041639
PDK1_HUMANPDK1physical
21041639
CYH3_HUMANCYTH3physical
21041639
CYH2_HUMANCYTH2physical
21041639
RIR2_HUMANRRM2genetic
28319113
AKT1_HUMANAKT1physical
25793261
RAC1_HUMANRAC1physical
25819133
DERL1_HUMANDERL1physical
28178653
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Glu-542Note=PIK3CA mutations are involved in various type of cancer. Most of the cancer-associated mutations are missense mutations and map to one of the three hotspots
Glu-545 and His-1047. Mutated isoforms participate in cellular transformation and tumorigenesis induced by oncogenic receptor tyrosine kinases (RTKs) and HRAS/KRAS. Interaction with HRAS/KRAS is required for Ras-driven tumor formation. Mutations increasing the lipid kinase activity are required for oncogenic signaling. The protein kinase activity may not be required for tumorigenesis.
114500
114480Breast cancer (BC)
167000Ovarian cancer (OC)
114550Hepatocellular carcinoma (HCC)
182000Keratosis, seborrheic (KERSEB)
602501Megalencephaly-capillary malformation-polymicrogyria syndrome (MCAP)
612918Congenital lipomatous overgrowth, vascular malformations, and epidermal nevi (CLOVE)
615108Cowden syndrome 5 (CWS5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00201Caffeine
Regulatory Network of PK3CA_HUMAN

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Related Literatures of Post-Translational Modification

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