AKT3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AKT3_MOUSE
• UniProt AC: Q9WUA6
• Protein Name: RAC-gamma serine/threonine-protein kinase
• Gene Name: Akt3
• Organism: Mus musculus (Mouse).
• Sequence Length: 479
• Subcellular Localization: Nucleus. Cytoplasm. Membrane; Peripheral membrane protein. Membrane-associated after cell stimulation leading to its translocation.
• Protein Description: AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis..
• Protein Sequence: MSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDDDGMDGMDNERRPHFPQFSYSASGRE

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
2	Acetylation	------MSDVTIVKE ------CCCCEEEEC	40.56	-
34	Phosphorylation	FLLKTDGSFIGYKEK EEEECCCCCCCCCCC	19.25	174877
120	Phosphorylation	EEERMNCSPTSQIDN HHHHHCCCCCHHCCC	26.63	22817900
122	Phosphorylation	ERMNCSPTSQIDNIG HHHCCCCCHHCCCCC	19.57	30635358
123	Phosphorylation	RMNCSPTSQIDNIGE HHCCCCCHHCCCCCC	28.64	30635358
136	Phosphorylation	GEEEMDASTTHHKRK CCCCCCCCCCCCCCC	29.58	20415495
137	Phosphorylation	EEEMDASTTHHKRKT CCCCCCCCCCCCCCC	31.69	20415495
138	Phosphorylation	EEMDASTTHHKRKTM CCCCCCCCCCCCCCC	21.35	20415495
158	Phosphorylation	LKLLGKGTFGKVILV HHHHCCCCCCEEEEE	32.47	25338131
173	Phosphorylation	REKASGKYYAMKILK EECCCCCCEEEEECC	10.44	22817900
174	Phosphorylation	EKASGKYYAMKILKK ECCCCCCEEEEECCC	12.05	22817900
248	Phosphorylation	RVFSEDRTRFYGAEI HCCCCCCHHHHHHHH	37.14	28576409
273	Ubiquitination	KIVYRDLKLENLMLD CEEEEEECHHHCEEC	59.03	-
298	Phosphorylation	GLCKEGITDAATMKT CCCCCCCCCHHHHHH	30.37	22322096
302	Phosphorylation	EGITDAATMKTFCGT CCCCCHHHHHHHCCC	22.41	22322096
302	O-linked_Glycosylation	EGITDAATMKTFCGT CCCCCHHHHHHHCCC	22.41	-
305	Phosphorylation	TDAATMKTFCGTPEY CCHHHHHHHCCCHHH	17.21	22322096
309	O-linked_Glycosylation	TMKTFCGTPEYLAPE HHHHHCCCHHHHCHH	17.71	-
309	Phosphorylation	TMKTFCGTPEYLAPE HHHHHCCCHHHHCHH	17.71	22322096
312	Phosphorylation	TFCGTPEYLAPEVLE HHCCCHHHHCHHHHC	14.90	11445557
323	Phosphorylation	EVLEDNDYGRAVDWW HHHCCCCCCCCHHHH	18.11	141681
445	Phosphorylation	EFTAQTITITPPEKY CEEEEEEEECCCHHC	23.37	24925903
447	Phosphorylation	TAQTITITPPEKYDD EEEEEEECCCHHCCC	24.92	30352176
447 (in isoform 2)	Phosphorylation	-	24.92	25521595
472	Phosphorylation	RPHFPQFSYSASGRE CCCCCCCCCCCCCCC	16.96	22322096
473	Phosphorylation	PHFPQFSYSASGRE- CCCCCCCCCCCCCC-	15.00	22322096
474	Phosphorylation	HFPQFSYSASGRE-- CCCCCCCCCCCCC--	18.11	22322096
476	Phosphorylation	PQFSYSASGRE---- CCCCCCCCCCC----	32.23	22322096

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
305	T	Phosphorylation	Kinase	PDPK1	Q9Z2A0	Uniprot
472	S	Phosphorylation	Kinase	PRKCZ	Q02956	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Ttc3	O88196	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
48	K	Phosphorylation	When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome (By similarity).	-
48	K	ubiquitylation	When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome (By similarity).	-
302	T	Phosphorylation	O-GlcNAcylation at Thr-302 and Thr-309 inhibits activating phosphorylation at Thr-305 via disrupting the interaction between AKT and PDK1.	-
305	T	Phosphorylation	O-GlcNAcylation at Thr-302 and Thr-309 inhibits activating phosphorylation at Thr-305 via disrupting the interaction between AKT and PDK1.	-
305	T	Phosphorylation	Phosphorylation on Thr-305 and Ser-472 is required for full activity.	-
309	T	Phosphorylation	O-GlcNAcylation at Thr-302 and Thr-309 inhibits activating phosphorylation at Thr-305 via disrupting the interaction between AKT and PDK1.	-
472	S	Phosphorylation	Phosphorylation on Thr-305 and Ser-472 is required for full 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 AKT3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BTBDA_MOUSE	Btbd10	physical	18160256

Drug and Disease Associations

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