PK3CA_MOUSE - dbPTM
PK3CA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PK3CA_MOUSE
UniProt AC P42337
Protein Name Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
Gene Name Pik3ca
Organism Mus musculus (Mouse).
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. [PubMed: 19604150]
Protein Sequence MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLVTIKHELFREARKYPLHQLLQDETSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFVIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPIDSFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSREAGFSYSHTGLSNRLARDNELRENDKEQLRALCTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAMELLDCNYPDPMVRSFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRQPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQEYTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFTKQMNDAHHGGWTTKMDWIFHTIKQHALN
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
68PhosphorylationLLQDETSYIFVSVTQ
HHCCCCCEEEEEECC		13.0525177544
158PhosphorylationVDLRDLNSPHSRAMY
CCHHHCCCCCCCEEE		31.1529514104
165PhosphorylationSPHSRAMYVYPPNVE
CCCCCEEEECCCCCC		8.8829514104
236PhosphorylationTRSMLLSSEQLKLCV
HHHHHCCHHHHHHHH		29.3629514104
246PhosphorylationLKLCVLEYQGKYILK
HHHHHHHHCCEEHHH		20.5722345495
250PhosphorylationVLEYQGKYILKVCGC
HHHHCCEEHHHHCCC		20.5022345495
275PhosphorylationSQYKYIRSCIMLGRM
HHHHHHHHHHHHCCC		9.8428059163
294PhosphorylationLMAKESLYSQLPIDS
HHHHHHHHHCCCCCC		12.0329514104
308PhosphorylationSFTMPSYSRRISTAT
CCCCCCCCCCCCCCC		21.3029514104
312PhosphorylationPSYSRRISTATPYMN
CCCCCCCCCCCCCCC		15.3524759943
313PhosphorylationSYSRRISTATPYMNG
CCCCCCCCCCCCCCC		31.9824759943
315PhosphorylationSRRISTATPYMNGET
CCCCCCCCCCCCCCC		18.2924759943
317PhosphorylationRISTATPYMNGETST
CCCCCCCCCCCCCCC		10.0022817900
322PhosphorylationTPYMNGETSTKSLWV
CCCCCCCCCCCHHHH		42.9924759943
507PhosphorylationVSREAGFSYSHTGLS
CCCCCCCCCCCCCHH		25.4729514104
508PhosphorylationSREAGFSYSHTGLSN
CCCCCCCCCCCCHHH		11.3822817900
509PhosphorylationREAGFSYSHTGLSNR
CCCCCCCCCCCHHHH		17.2429514104
511PhosphorylationAGFSYSHTGLSNRLA
CCCCCCCCCHHHHHH		33.6029514104
514PhosphorylationSYSHTGLSNRLARDN
CCCCCCHHHHHHHCC		22.6529514104
557PhosphorylationFLWSHRHYCVTIPEI
HHHHCCCEEEEHHHH		6.6425195567
720UbiquitinationINLTDILKQEKKDET
HHHHHHHHHHCCCCH		57.6622790023
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PK3CA_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P85A_MOUSEPik3r1physical
24651434
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PK3CA_MOUSE

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Related Literatures of Post-Translational Modification

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