PK3CB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PK3CB_MOUSE
• UniProt AC: Q8BTI9
• Protein Name: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
• Gene Name: Pik3cb
• Organism: Mus musculus (Mouse).
• Sequence Length: 1064
• Subcellular Localization: Cytoplasm. Nucleus. Interaction with PIK3R2 is required for nuclear localization and export.
• 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. Involved in the activation of AKT1 upon stimulation by G-protein coupled receptors (GPCRs) ligands such as CXCL12, sphingosine 1-phosphate, and lysophosphatidic acid. May also act downstream receptor tyrosine kinases. Required in different signaling pathways for stable platelet adhesion and aggregation. Plays a role in platelet activation signaling triggered by GPCRs, alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) and ITAM (immunoreceptor tyrosine-based activation motif)-bearing receptors such as GP6. Regulates the strength of adhesion of ITGA2B/ ITGB3 activated receptors necessary for the cellular transmission of contractile forces. Required for platelet aggregation induced by F2 (thrombin) and thromboxane A2 (TXA2). Has a role in cell survival. May have a role in cell migration. Involved in the early stage of autophagosome formation. Modulates the intracellular level of PtdIns3P (Phosphatidylinositol 3-phosphate) and activates PIK3C3 kinase activity. May act as a scaffold, independently of its lipid kinase activity to positively regulate autophagy. May have a role in insulin signaling as scaffolding protein in which the lipid kinase activity is not required. May have a kinase-independent function in regulating cell proliferation and in clathrin-mediated endocytosis. Mediator of oncogenic signal in cell lines lacking PTEN. The lipid kinase activity is necessary for its role in oncogenic transformation. Required for the growth of ERBB2 and RAS driven tumors..
• Protein Sequence: MPPAMADNLDIWAVDSQIASDGAISVDFLLPTGIYIQLEVPREATISYIKQMLWKQVHNYPMFNLLMDIDSYMFACVNQTAVYEELEDETRRLCDVRPFLPVLKLVTRSCDPAEKLDSKIGVLIGKGLHEFDALKDPEVNEFRRKMRKFSEAKIQSLVGLSWIDWLKHTYPPEHEPSVLENLEDKLYGGKLVVAVHFENSQDVFSFQVSPNLNPIKINELAIQKRLTIRGKEDEASPCDYVLQVSGRVEYVFGDHPLIQFQYIRNCVMNRTLPHFILVECCKIKKMYEQEMIAIEAAINRNSSNLPLPLPPKKTRVISHIWDNNNPFQITLVKGNKLNTEETVKVHVRAGLFHGTELLCKTVVSSEISGKNDHIWNEQLEFDINICDLPRMARLCFAVYAVLDKVKTKKSTKTINPSKYQTIRKAGKVHYPVAWVNTMVFDFKGQLRSGDVILHSWSSFPDELEEMLNPMGTVQTNPYAENATALHITFPENKKQPCYYPPFDKIIEKAAELASGDSANVSSRGGKKFLAVLKEILDRDPLSQLCENEMDLIWTLRQDCRENFPQSLPKLLLSIKWNKLEDVAQLQALLQIWPKLPPREALELLDFNYPDQYVREYAVGCLRQMSDEELSQYLLQLVQVLKYEPFLDCALSRFLLERALDNRRIGQFLFWHLRSEVHTPAVSVQFGVILEAYCRGSVGHMKVLSKQVEALNKLKTLNSLIKLNAVKLSRAKGKEAMHTCLKQSAYREALSDLQSPLNPCVILSELYVEKCKYMDSKMKPLWLVYSSRAFGEDSVGVIFKNGDDLRQDMLTLQMLRLMDLLWKEAGLDLRMLPYGCLATGDRSGLIEVVSTSETIADIQLNSSNVAATAAFNKDALLNWLKEYNSGDDLDRAIEEFTLSCAGYCVASYVLGIGDRHSDNIMVKKTGQLFHIDFGHILGNFKSKFGIKRERVPFILTYDFIHVIQQGKTGNTEKFGRFRQCCEDAYLILRRHGNLFITLFALMLTAGLPELTSVKDIQYLKDSLALGKSEEEALKQFKQKFDEALRESWTTKVNWMAHTVRKDYRS

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
314	Phosphorylation	LPLPPKKTRVISHIW CCCCCCCEEEEEEEC	35.97	23984901
318	Phosphorylation	PKKTRVISHIWDNNN CCCEEEEEEECCCCC	13.18	27180971
418	Malonylation	TKTINPSKYQTIRKA CCCCCHHHHHHHHHC	42.51	26320211
419	Phosphorylation	KTINPSKYQTIRKAG CCCCHHHHHHHHHCC	18.41	22817900
421	Phosphorylation	INPSKYQTIRKAGKV CCHHHHHHHHHCCCE	21.47	29514104
498	Phosphorylation	ENKKQPCYYPPFDKI CCCCCCCCCCCHHHH	26.20	29514104
514	Phosphorylation	EKAAELASGDSANVS HHHHHHHCCCCCCCC	56.61	29514104
517	Phosphorylation	AELASGDSANVSSRG HHHHCCCCCCCCCCC	25.85	29514104
766	Phosphorylation	CVILSELYVEKCKYM CHHHHHHHHHHCCCC	11.51	22817900
956	Phosphorylation	RVPFILTYDFIHVIQ CCCEEEEEEEEHHHH	12.86	20116462
1019	Ubiquitination	VKDIQYLKDSLALGK HHHHHHHHHHHHCCC	40.10	22790023
1064	Phosphorylation	TVRKDYRS------- HHHHHHCC-------	38.04	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PK3CB_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1064	S	Phosphorylation	Phosphorylation at Ser-1064 down-regulates lipid kinase activity.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PK3CB_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FAK2_MOUSE	Ptk2b	physical	19416922
PCNA_MOUSE	Pcna	physical	19416922
NBN_MOUSE	Nbn	physical	20368419
RAD17_MOUSE	Rad17	physical	20368419

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.