AKT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AKT1_HUMAN
• UniProt AC: P31749
• Protein Name: RAC-alpha serine/threonine-protein kinase
• Gene Name: AKT1
• Organism: Homo sapiens (Human).
• Sequence Length: 480
• Subcellular Localization: Cytoplasm. Nucleus. Cell membrane. Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A. Phosphorylation on Tyr-176 by TNK2 results in its localization to the cell membrane w
• Protein Description: AKT1 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. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53.; AKT1-specific substrates have been recently identified, including palladin (PALLD), which phosphorylation modulates cytoskeletal organization and cell motility; prohibitin (PHB), playing an important role in cell metabolism and proliferation; and CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation..
• Protein Sequence: MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA

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	Phosphorylation	------MSDVAIVKE ------CCCEEEEEC	40.57	101545721
8	Ubiquitination	MSDVAIVKEGWLHKR CCCEEEEECCCCCCC	44.38	21890473
8	Ubiquitination	MSDVAIVKEGWLHKR CCCEEEEECCCCCCC	44.38	21890473
8	Ubiquitination	MSDVAIVKEGWLHKR CCCEEEEECCCCCCC	44.38	21890473
14	Methylation	VKEGWLHKRGEYIKT EECCCCCCCCCCCCC	60.99	21775285
14	Acetylation	VKEGWLHKRGEYIKT EECCCCCCCCCCCCC	60.99	21775285
14	Ubiquitination	VKEGWLHKRGEYIKT EECCCCCCCCCCCCC	60.99	21775285
20	Acetylation	HKRGEYIKTWRPRYF CCCCCCCCCCCCEEE	40.93	21775285
20	Ubiquitination	HKRGEYIKTWRPRYF CCCCCCCCCCCCEEE	40.93	21775285
30	Ubiquitination	RPRYFLLKNDGTFIG CCEEEEECCCCCEEE	55.96	21890473
30	Ubiquitination	RPRYFLLKNDGTFIG CCEEEEECCCCCEEE	55.96	21890473
30	Ubiquitination	RPRYFLLKNDGTFIG CCEEEEECCCCCEEE	55.96	21890473
34	Phosphorylation	FLLKNDGTFIGYKER EEECCCCCEEEEECC	18.23	28857561
39	Ubiquitination	DGTFIGYKERPQDVD CCCEEEEECCCCCCC	41.87	-
65	Phosphorylation	AQCQLMKTERPRPNT HHHHHHCCCCCCCCE	24.22	46161783
72	Phosphorylation	TERPRPNTFIIRCLQ CCCCCCCEEEEEHHE	20.92	22817900
78	Ubiquitination	NTFIIRCLQWTTVIE CEEEEEHHEEEEEEE	3.23	-
87	Phosphorylation	WTTVIERTFHVETPE EEEEEEEEEECCCHH	12.80	45553673
92	Phosphorylation	ERTFHVETPEEREEW EEEEECCCHHHHHHH	34.61	45553679
96	Ubiquitination	HVETPEEREEWTTAI ECCCHHHHHHHHHHH	45.53	-
122	Phosphorylation	EEEMDFRSGSPSDNS HHHCCCCCCCCCCCC	43.55	29255136
124	Phosphorylation	EMDFRSGSPSDNSGA HCCCCCCCCCCCCCC	23.60	29255136
126	O-linked_Glycosylation	DFRSGSPSDNSGAEE CCCCCCCCCCCCCCC	51.63	22687243
126	Phosphorylation	DFRSGSPSDNSGAEE CCCCCCCCCCCCCCC	51.63	29255136
129	O-linked_Glycosylation	SGSPSDNSGAEEMEV CCCCCCCCCCCCEEE	44.35	22687243
129	Phosphorylation	SGSPSDNSGAEEMEV CCCCCCCCCCCCEEE	44.35	25159151
137	Phosphorylation	GAEEMEVSLAKPKHR CCCCEEEECCCCCCE	14.87	30266825
140	Ubiquitination	EMEVSLAKPKHRVTM CEEEECCCCCCEECH	60.95	-
146	Phosphorylation	AKPKHRVTMNEFEYL CCCCCEECHHHHHHH	17.78	7645411
147	Sulfoxidation	KPKHRVTMNEFEYLK CCCCEECHHHHHHHH	4.07	30846556
154	Ubiquitination	MNEFEYLKLLGKGTF HHHHHHHHHHCCCCC	40.54	-
158	Ubiquitination	EYLKLLGKGTFGKVI HHHHHHCCCCCCEEE	55.54	-
176	Phosphorylation	EKATGRYYAMKILKK ECCCCCCCHHHHHCC	10.00	20333297
189	Ubiquitination	KKEVIVAKDEVAHTL CCEEEEECHHHHHHH	43.45	-
206	Ubiquitination	NRVLQNSRHPFLTAL CCCCCCCCCHHHHHH	49.39	-
211	Phosphorylation	NSRHPFLTALKYSFQ CCCCHHHHHHHHHCC	30.26	57413601
214	Ubiquitination	HPFLTALKYSFQTHD CHHHHHHHHHCCCCC	36.06	-
219	Phosphorylation	ALKYSFQTHDRLCFV HHHHHCCCCCEEEEE	24.59	24719451
224	S-nitrosylation	FQTHDRLCFVMEYAN CCCCCEEEEEEEECC	2.23	22178444
224	S-nitrosocysteine	FQTHDRLCFVMEYAN CCCCCEEEEEEEECC	2.23	-
235	Ubiquitination	EYANGGELFFHLSRE EECCCCEEEEEEEHH	6.68	-
239	Ubiquitination	GGELFFHLSRERVFS CCEEEEEEEHHHCCC	4.33	-
246	Phosphorylation	LSRERVFSEDRARFY EEHHHCCCHHHHHHH	35.41	22817900
268	Ubiquitination	LDYLHSEKNVVYRDL HHHHHCCCCEECCCC	59.04	-
276	Sumoylation	NVVYRDLKLENLMLD CEECCCCCHHHEEEC	59.03	-
276	Ubiquitination	NVVYRDLKLENLMLD CEECCCCCHHHEEEC	59.03	21890473
276	Sumoylation	NVVYRDLKLENLMLD CEECCCCCHHHEEEC	59.03	-
284	Ubiquitination	LENLMLDKDGHIKIT HHHEEECCCCCEEEC	62.74	22410793
289	Ubiquitination	LDKDGHIKITDFGLC ECCCCCEEECCCCCC	33.60	-
291	Phosphorylation	KDGHIKITDFGLCKE CCCCEEECCCCCCCC	21.92	57413599
296	S-nitrosocysteine	KITDFGLCKEGIKDG EECCCCCCCCCCCCC	3.74	-
296	S-nitrosylation	KITDFGLCKEGIKDG EECCCCCCCCCCCCC	3.74	22178444
297	Ubiquitination	ITDFGLCKEGIKDGA ECCCCCCCCCCCCCC	65.11	-
301	Sumoylation	GLCKEGIKDGATMKT CCCCCCCCCCCCCCC	62.05	-
301	Ubiquitination	GLCKEGIKDGATMKT CCCCCCCCCCCCCCC	62.05	-
301	Sumoylation	GLCKEGIKDGATMKT CCCCCCCCCCCCCCC	62.05	-
305	Phosphorylation	EGIKDGATMKTFCGT CCCCCCCCCCCCCCC	25.40	22322096
305	O-linked_Glycosylation	EGIKDGATMKTFCGT CCCCCCCCCCCCCCC	25.40	32830957
308	Dephosphorylation	KDGATMKTFCGTPEY CCCCCCCCCCCCHHH	17.21	12637511
308	Phosphorylation	KDGATMKTFCGTPEY CCCCCCCCCCCCHHH	17.21	22039466
308	O-linked_Glycosylation	KDGATMKTFCGTPEY CCCCCCCCCCCCHHH	17.21	11278835
310	Glutathionylation	GATMKTFCGTPEYLA CCCCCCCCCCHHHHC	7.79	22555962
310	S-nitrosylation	GATMKTFCGTPEYLA CCCCCCCCCCHHHHC	7.79	22178444
310	S-nitrosocysteine	GATMKTFCGTPEYLA CCCCCCCCCCHHHHC	7.79	-
312	Phosphorylation	TMKTFCGTPEYLAPE CCCCCCCCHHHHCHH	17.71	22322096
312	O-linked_Glycosylation	TMKTFCGTPEYLAPE CCCCCCCCHHHHCHH	17.71	32830957
315	Ubiquitination	TFCGTPEYLAPEVLE CCCCCHHHHCHHHHC	14.90	-
315	Phosphorylation	TFCGTPEYLAPEVLE CCCCCHHHHCHHHHC	14.90	22322096
326	Phosphorylation	EVLEDNDYGRAVDWW HHHCCCCCCCCHHHH	18.11	142487
338	Ubiquitination	DWWGLGVVMYEMMCG HHHHHHHHHHHHHHC	2.99	-
377	Ubiquitination	RTLGPEAKSLLSGLL CHHCHHHHHHHHHHC	39.72	21890473
378	Phosphorylation	TLGPEAKSLLSGLLK HHCHHHHHHHHHHCC	41.41	63776055
381	Phosphorylation	PEAKSLLSGLLKKDP HHHHHHHHHHCCCCH	32.46	20873877
396	Phosphorylation	KQRLGGGSEDAKEIM HHCCCCCCHHHHHHH	35.26	68699577
400	Ubiquitination	GGGSEDAKEIMQHRF CCCCHHHHHHHHHHH	61.16	-
417	Phosphorylation	GIVWQHVYEKKLSPP HHHHHHHHHCCCCCC	21.65	45553667
420	Acetylation	WQHVYEKKLSPPFKP HHHHHHCCCCCCCCC	42.11	19817937
422	Phosphorylation	HVYEKKLSPPFKPQV HHHHCCCCCCCCCCC	39.13	28348404
426	Ubiquitination	KKLSPPFKPQVTSET CCCCCCCCCCCCCCC	40.07	-
426	Acetylation	KKLSPPFKPQVTSET CCCCCCCCCCCCCCC	40.07	19817949
430	Phosphorylation	PPFKPQVTSETDTRY CCCCCCCCCCCCCCC	18.65	30624053
431	Phosphorylation	PFKPQVTSETDTRYF CCCCCCCCCCCCCCC	39.37	26657352
435	Phosphorylation	QVTSETDTRYFDEEF CCCCCCCCCCCCHHC	34.39	-
437	Phosphorylation	TSETDTRYFDEEFTA CCCCCCCCCCHHCEE	19.92	22817900
443	Phosphorylation	RYFDEEFTAQMITIT CCCCHHCEEEEEEEC	21.18	69006271
448	Phosphorylation	EFTAQMITITPPDQD HCEEEEEEECCCCCC	17.29	26657352
450	Phosphorylation	TAQMITITPPDQDDS EEEEEEECCCCCCCC	21.81	21464307
457	Phosphorylation	TPPDQDDSMECVDSE CCCCCCCCCCCCCCC	25.44	68996393
473	Phosphorylation	RPHFPQFSYSASGTA CCCCCCCCCCCCCCC	16.96	15855334
473	O-linked_Glycosylation	RPHFPQFSYSASGTA CCCCCCCCCCCCCCC	16.96	11313365
473	Dephosphorylation	RPHFPQFSYSASGTA CCCCCCCCCCCCCCC	16.96	12637511
474	Phosphorylation	PHFPQFSYSASGTA- CCCCCCCCCCCCCC-	15.00	22322096
475	Phosphorylation	HFPQFSYSASGTA-- CCCCCCCCCCCCC--	18.11	22322096
477	Phosphorylation	PQFSYSASGTA---- CCCCCCCCCCC----	30.64	22322096
479	Phosphorylation	FSYSASGTA------ CCCCCCCCC------	27.05	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
72	T	Phosphorylation	Kinase	AKT1	P31749	PSP
129	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
176	Y	Phosphorylation	Kinase	TNK2	Q07912	Uniprot
246	S	Phosphorylation	Kinase	AKT1	P31749	PSP
308	T	Phosphorylation	Kinase	AXL	P30530	PSP
308	T	Phosphorylation	Kinase	TYRO3	Q06418	PSP
308	T	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
308	T	Phosphorylation	Kinase	PIK3CA	P42336	PSP
308	T	Phosphorylation	Kinase	PDK1	O15530	PSP
308	T	Phosphorylation	Kinase	PDK1	Q15118	GPS
308	T	Phosphorylation	Kinase	MERTK	Q12866	GPS
308	T	Phosphorylation	Kinase	PRKD1	Q15139	PSP
308	T	Phosphorylation	Kinase	PRKCB	P05771	GPS
308	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
308	T	Phosphorylation	Kinase	CAMKK2	Q96RR4	PSP
308	T	Phosphorylation	Kinase	IKBKE	Q14164	GPS
312	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
315	Y	Phosphorylation	Kinase	RET	P07949	PSP
315	Y	Phosphorylation	Kinase	PTK6	Q13882	GPS
326	Y	Phosphorylation	Kinase	PTK6	Q13882	GPS
450	T	Phosphorylation	Kinase	MTOR	P42345	PSP
473	S	Phosphorylation	Kinase	IKBKE	Q14164	GPS
473	S	Phosphorylation	Kinase	AXL	P30530	PSP
473	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
473	S	Phosphorylation	Kinase	PIKFYVE	Q9Y2I7	PSP
473	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
473	S	Phosphorylation	Kinase	PDPK1	O15530	PhosphoELM
473	S	Phosphorylation	Kinase	PDK1	Q15118	GPS
473	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
473	S	Phosphorylation	Kinase	PIK3R1	P27986	PSP
473	S	Phosphorylation	Kinase	MTOR	Q9JLN9	PSP
473	S	Phosphorylation	Kinase	MTOR	P42345	Uniprot
473	S	Phosphorylation	Kinase	MERTK	Q12866	GPS
473	S	Phosphorylation	Kinase	ILK	Q13418	PSP
473	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
473	S	Phosphorylation	Kinase	LRRK2	Q5S007	PSP
473	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
473	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
477	S	Phosphorylation	Kinase	CDK2	P24941	PSP
479	T	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:19074868
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM13	O60858	PMID:21333377
-	K	Ubiquitination	E3 ubiquitin ligase	MUL1	Q969V5	PMID:22410793
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:23195959
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	TTC3	P53804	PMID:20059950
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF6	Q9Y4K3	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:18292230
-	K	Ubiquitination	E3 ubiquitin ligase	ZNRF1	Q8ND25	PMID:14561866

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
14	K	Acetylation	Deacetylated at Lys-14 and Lys-20 by SIRT1.	19713527
14	K	Acetylation	Acetylated on Lys-14 and Lys-20 by the histone acetyltransferases EP300 and KAT2B.	19713527
20	K	Acetylation	Acetylated on Lys-14 and Lys-20 by the histone acetyltransferases EP300 and KAT2B.	21775285
20	K	Acetylation	Deacetylated at Lys-14 and Lys-20 by SIRT1.	21775285
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.	19713527
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.	19713527
48	K	ubiquitylation	Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination.	19713527
284	K	ubiquitylation	Phosphorylated, undergoes 'Lys-48'-linked polyubiquitination preferentially at Lys-284 catalyzed by MUL1, leading to its proteasomal degradation.	22410793
284	K	Phosphorylation	Phosphorylated, undergoes 'Lys-48'-linked polyubiquitination preferentially at Lys-284 catalyzed by MUL1, leading to its proteasomal degradation.	22410793
305	T	Phosphorylation	O-GlcNAcylation at Thr-305 and Thr-312 inhibits activating phosphorylation at Thr-308 via disrupting the interaction between AKT1 and PDPK1.	22629392
308	T	Phosphorylation	This phosphorylated form localizes to the cell membrane, where it is targeted by PDPK1 and PDPK2 for further phosphorylations on Thr-308 and Ser-473 leading to its activation.	8978681
308	T	Phosphorylation	Ser-473 phosphorylation by mTORC2 favors Thr-308 phosphorylation by PDPK1.	8978681
308	T	Phosphorylation	Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity.	8978681
308	T	Phosphorylation	Phosphorylated at Thr-308 and Ser-473 by IKBKE and TBK1.	8978681
308	T	Phosphorylation	O-GlcNAcylation at Thr-305 and Thr-312 inhibits activating phosphorylation at Thr-308 via disrupting the interaction between AKT1 and PDPK1.	8978681
308	T	Phosphorylation	Dephosphorylated at Thr-308 and Ser-473 by PP2A phosphatase.	8978681
312	T	Phosphorylation	O-GlcNAcylation at Thr-305 and Thr-312 inhibits activating phosphorylation at Thr-308 via disrupting the interaction between AKT1 and PDPK1.	22629392
473	S	Phosphorylation	Ser-473 phosphorylation is enhanced by signaling through activated FLT3 (By similarity).	9736715
473	S	Phosphorylation	Ser-473 phosphorylation is enhanced in focal cortical dysplasias with Taylor-type balloon cells.	9736715
473	S	Phosphorylation	This phosphorylated form localizes to the cell membrane, where it is targeted by PDPK1 and PDPK2 for further phosphorylations on Thr-308 and Ser-473 leading to its activation.	9736715
473	S	Phosphorylation	Ser-473 phosphorylation is enhanced by interaction with AGAP2 isoform 2 (PIKE-A).	9736715
473	S	Phosphorylation	Ser-473 phosphorylation by mTORC2 favors Thr-308 phosphorylation by PDPK1.	9736715
473	S	Phosphorylation	Ser-473 is dephosphorylated by PHLPP.	9736715
473	S	Phosphorylation	Ser-473 is dephosphorylated by CPPED1, leading to termination of signaling.	9736715
473	S	Phosphorylation	Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity.	9736715
473	S	Phosphorylation	Phosphorylated at Thr-308 and Ser-473 by IKBKE and TBK1.	9736715
473	S	Phosphorylation	O-GlcNAcylation at Ser-473 also probably interferes with phosphorylation at this site.	9736715
473	S	Phosphorylation	Dephosphorylated at Thr-308 and Ser-473 by PP2A phosphatase.	9736715

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of AKT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANDR_HUMAN	AR	physical	11404460
PAK1_HUMAN	PAK1	physical	14749719
AKTIP_HUMAN	AKTIP	physical	14749367
TRIB3_HUMAN	TRIB3	physical	12791994
IRAK1_HUMAN	IRAK1	physical	11976320
IMDH2_HUMAN	IMPDH2	physical	10930578
BRAF_HUMAN	BRAF	physical	10869359
HSPB1_HUMAN	HSPB1	physical	11042204
MAPK2_HUMAN	MAPKAPK2	physical	11042204
MK14_HUMAN	MAPK14	physical	11042204
K1C10_HUMAN	KRT10	physical	11585925
RAF1_HUMAN	RAF1	physical	10576742
BAD_HUMAN	BAD	physical	11500364
MTOR_HUMAN	MTOR	physical	10910062
MTOR_HUMAN	MTOR	physical	14970221
GSK3B_HUMAN	GSK3B	physical	16009706
HS90A_HUMAN	HSP90AA1	physical	15843522
TERT_HUMAN	TERT	physical	15843522
TSC1_HUMAN	TSC1	physical	12167664
TSC2_HUMAN	TSC2	physical	12167664
CHSP1_HUMAN	CARHSP1	physical	15910284
CDN1B_HUMAN	CDKN1B	physical	12042314
NR4A1_HUMAN	NR4A1	physical	11274386
MP2K4_HUMAN	MAP2K4	physical	11707464
MTCP1_HUMAN	MTCP1	physical	10983986
TCL1A_HUMAN	TCL1A	physical	10983986
TCL1B_HUMAN	TCL1B	physical	10983986
HS90A_HUMAN	HSP90AA1	physical	10995457
HS90B_HUMAN	HSP90AB1	physical	10995457
GAB2_HUMAN	GAB2	physical	11782427
IKKA_HUMAN	CHUK	physical	10485710
JIP1_HUMAN	MAPK8IP1	physical	12194869
PKN2_HUMAN	PKN2	physical	10926925
M3K8_HUMAN	MAP3K8	physical	12138205
1433Z_HUMAN	YWHAZ	physical	11956222
IKKA_HUMAN	CHUK	physical	10485711
ARFP2_HUMAN	ARFIP2	physical	9312003
ILK_HUMAN	ILK	physical	11313365
PDPK1_HUMAN	PDPK1	physical	11313365
BRCA1_HUMAN	BRCA1	physical	19074868
NPM_HUMAN	NPM1	physical	18931307
CHIP_HUMAN	STUB1	physical	18292230
MARK2_HUMAN	MARK2	physical	18292230
MERL_HUMAN	NF2	physical	17891137
PIAS1_HUMAN	PIAS1	physical	17533377
PIAS2_HUMAN	PIAS2	physical	17533377
MAD1_HUMAN	MXD1	physical	19526459
NCOR2_HUMAN	NCOR2	physical	16613989
SNF5_HUMAN	SMARCB1	physical	16568092
ACTS_HUMAN	ACTA1	physical	16568092
SMRC1_HUMAN	SMARCC1	physical	16568092
SMRC2_HUMAN	SMARCC2	physical	16568092
EZH2_HUMAN	EZH2	physical	16224021
FOXO1_HUMAN	FOXO1	physical	16076959
XIAP_HUMAN	XIAP	physical	14645242
HSP74_HUMAN	HSPA4	physical	12750378
NOTC1_HUMAN	NOTCH1	physical	18440314
HS90A_HUMAN	HSP90AA1	physical	12176997
CDC37_HUMAN	CDC37	physical	12176997
IKKB_HUMAN	IKBKB	physical	15856005
EP300_HUMAN	EP300	physical	18182168
MDM2_HUMAN	MDM2	physical	11923280
MDM2_HUMAN	MDM2	physical	11715018
SETB1_HUMAN	SETDB1	physical	17577629
FANCA_HUMAN	FANCA	physical	11855836
CBP_HUMAN	CREBBP	physical	19995607
GSK3A_HUMAN	GSK3A	physical	19995607
GSK3B_HUMAN	GSK3B	physical	19995607
DNMT1_HUMAN	DNMT1	physical	21151116
SKP2_HUMAN	SKP2	physical	19270694
MDM2_HUMAN	MDM2	physical	21930127
PA2G4_HUMAN	PA2G4	physical	21930127
ERBB3_HUMAN	ERBB3	physical	21930127
TRI13_HUMAN	TRIM13	physical	21333377
TTC3_HUMAN	TTC3	physical	20059950
ESR1_HUMAN	ESR1	physical	11139588
NCOA4_HUMAN	NCOA4	physical	18624398
APOH_HUMAN	APOH	physical	18624398
ASXL1_HUMAN	ASXL1	physical	18624398
PMGE_HUMAN	BPGM	physical	18624398
COMD1_HUMAN	COMMD1	physical	18624398
DNJB1_HUMAN	DNAJB1	physical	18624398
PEPL_HUMAN	PPL	physical	18624398
P4K2B_HUMAN	PI4K2B	physical	18624398
ZHX1_HUMAN	ZHX1	physical	21900206
EF1G_HUMAN	EEF1G	physical	21900206
DCTN1_HUMAN	DCTN1	physical	21900206
PP2AA_HUMAN	PPP2CA	physical	18191226
ARRB2_HUMAN	ARRB2	physical	18191226
MAD1_HUMAN	MXD1	physical	18451027
WNK4_HUMAN	WNK4	physical	20525693
SKP2_HUMAN	SKP2	physical	19270695
UBP4_HUMAN	USP4	physical	22706160
GSK3A_HUMAN	GSK3A	physical	11509608
MUL1_HUMAN	MUL1	physical	22410793
TOPB1_HUMAN	TOPBP1	physical	17006541
RNF11_HUMAN	RNF11	physical	16123141
RN115_HUMAN	RNF115	physical	16123141
GSK3B_HUMAN	GSK3B	physical	16123141
GSK3B_HUMAN	GSK3B	physical	15470047
SH3R1_HUMAN	SH3RF1	physical	17535800
GSK3A_HUMAN	GSK3A	physical	17505062
IBTK_HUMAN	IBTK	physical	18596081
BAD_HUMAN	BAD	physical	11994280
TERA_HUMAN	VCP	physical	16551632
TERA_HUMAN	VCP	physical	16027165
NSF_HUMAN	NSF	physical	16027165
HSP7C_HUMAN	HSPA8	physical	16027165
KCC2A_HUMAN	CAMK2A	physical	16027165
ENOG_HUMAN	ENO2	physical	16027165
KCRB_HUMAN	CKB	physical	16027165
GBB1_HUMAN	GNB1	physical	16027165
CLH1_HUMAN	CLTC	physical	16027165
HXK1_HUMAN	HK1	physical	16027165
AT1A1_HUMAN	ATP1A1	physical	16027165
TBB5_HUMAN	TUBB	physical	16027165
1433G_HUMAN	YWHAG	physical	16027165
1433Z_HUMAN	YWHAZ	physical	16027165
1433E_HUMAN	YWHAE	physical	16027165
ENOA_HUMAN	ENO1	physical	16027165
G3P_HUMAN	GAPDH	physical	16027165
GRP78_HUMAN	HSPA5	physical	16027165
PEBP1_HUMAN	PEBP1	physical	16027165
UCHL1_HUMAN	UCHL1	physical	16027165
MDHC_HUMAN	MDH1	physical	16027165
LDHA_HUMAN	LDHA	physical	16027165
HBB_HUMAN	HBB	physical	16027165
PPIA_HUMAN	PPIA	physical	16027165
ALDOA_HUMAN	ALDOA	physical	16027165
IF4A1_HUMAN	EIF4A1	physical	16027165
PSB4_HUMAN	PSMB4	physical	16027165
HS90A_HUMAN	HSP90AA1	physical	16027165
GUAD_HUMAN	GDA	physical	16027165
VPP2_HUMAN	ATP6V0A2	physical	16027165
SKI_HUMAN	SKI	physical	19875456
STK4_HUMAN	STK4	physical	19940129
VIME_HUMAN	VIM	physical	20856200
DDX5_HUMAN	DDX5	physical	20856200
GRP75_HUMAN	HSPA9	physical	20856200
TPM4_HUMAN	TPM4	physical	20856200
TPM2_HUMAN	TPM2	physical	20856200
ACTB_HUMAN	ACTB	physical	20856200
TBB5_HUMAN	TUBB	physical	20856200
TRHDE_HUMAN	TRHDE	physical	20856200
MDM2_HUMAN	MDM2	physical	20856200
GSK3B_HUMAN	GSK3B	physical	20856200
GSK3A_HUMAN	GSK3A	physical	14645548
GSK3B_HUMAN	GSK3B	physical	14645548
BAD_HUMAN	BAD	physical	15998799
JIP1_HUMAN	MAPK8IP1	physical	15998799
MP2K4_HUMAN	MAP2K4	physical	15998799
PINK1_HUMAN	PINK1	physical	21177249
F261_HUMAN	PFKFB1	physical	15896703
NOS3_HUMAN	NOS3	physical	11425855
A4_HUMAN	APP	physical	21832049
PHB2_HUMAN	PHB2	physical	15173318
KAT2B_HUMAN	KAT2B	physical	21775285
SIR1_HUMAN	SIRT1	physical	21775285
FOXO3_HUMAN	FOXO3	physical	21775285
BRCA1_HUMAN	BRCA1	physical	21242970
CTNB1_HUMAN	CTNNB1	physical	15492215
PRKDC_HUMAN	PRKDC	physical	15262962
GSK3A_HUMAN	GSK3A	physical	15678105
PRKDC_HUMAN	PRKDC	physical	15678105
CREB1_HUMAN	CREB1	physical	9829964
MDM2_HUMAN	MDM2	physical	15527798
TISB_HUMAN	ZFP36L1	physical	17030608
RPTOR_HUMAN	RPTOR	physical	21339740
RICTR_HUMAN	RICTOR	physical	21339740
PREX1_HUMAN	PREX1	physical	21339740
ANDR_HUMAN	AR	physical	18332867
MDM2_HUMAN	MDM2	physical	18332867
SRTD4_HUMAN	SERTAD4	physical	20368287
RL23_MOUSE	Rpl23	physical	20368287
SRTD4_MOUSE	Sertad4	physical	20368287
RON_HUMAN	MST1R	physical	14505491
BCL10_HUMAN	BCL10	physical	16280327
AKT1_HUMAN	AKT1	physical	16280327
STK3_HUMAN	STK3	physical	20086174
CLK2_HUMAN	CLK2	physical	20682768
GSK3B_HUMAN	GSK3B	physical	20682768
CSK_HUMAN	CSK	physical	19262695
IGSF8_HUMAN	IGSF8	physical	23463506
CD81_HUMAN	CD81	physical	23463506
RARA_HUMAN	RARA	physical	16417524
STK4_HUMAN	STK4	physical	17932490
GRDN_HUMAN	CCDC88A	physical	16139227
M3K5_HUMAN	MAP3K5	physical	11154276
STK3_HUMAN	STK3	physical	20231902
DAB2P_HUMAN	DAB2IP	physical	19903888
CYLD_HUMAN	CYLD	physical	23300340
GSK3B_HUMAN	GSK3B	physical	19713527
B2CL1_HUMAN	BCL2L1	physical	16282323
PEPL_HUMAN	PPL	physical	12244133
RGCC_HUMAN	RGCC	physical	19162005
TBCD4_HUMAN	TBC1D4	physical	11994271
AKT1_HUMAN	AKT1	physical	19203586
BAD_HUMAN	BAD	physical	19667065
JADE1_HUMAN	JADE1	physical	23824745
GSK3B_HUMAN	GSK3B	physical	23824745
TRAF6_HUMAN	TRAF6	physical	21816939
XIAP_HUMAN	XIAP	physical	23640046
DAB2P_HUMAN	DAB2IP	physical	24912918
SIR6_HUMAN	SIRT6	physical	25074979
GSK3B_HUMAN	GSK3B	physical	15688030
ITPR1_HUMAN	ITPR1	physical	18250332
ITPR3_HUMAN	ITPR3	physical	18250332
KPCZ_HUMAN	PRKCZ	physical	18353613
GSK3B_HUMAN	GSK3B	physical	18505846
GRB10_HUMAN	GRB10	physical	15722337
BAD_HUMAN	BAD	physical	15722337
GRDN_HUMAN	CCDC88A	physical	15753085
THOC4_HUMAN	ALYREF	physical	18562279
VINEX_HUMAN	SORBS3	physical	15784622
AKT1_HUMAN	AKT1	physical	15784622
BAD_HUMAN	BAD	physical	15784622
KPCZ_HUMAN	PRKCZ	physical	18650932
YBOX1_HUMAN	YBX1	physical	15806160
GATA2_HUMAN	GATA2	physical	15837948
TRMB_HUMAN	METTL1	physical	15861136
FOXO1_HUMAN	FOXO1	physical	18786403
HSPB1_HUMAN	HSPB1	physical	17510053
MAPK2_HUMAN	MAPKAPK2	physical	17510053
H2B2E_HUMAN	HIST2H2BE	physical	17510053
GSK3B_HUMAN	GSK3B	physical	8524413
TAU_HUMAN	MAPT	physical	19014373
RAF1_HUMAN	RAF1	physical	19058874
GATA1_HUMAN	GATA1	physical	16107690
ARRB2_HUMAN	ARRB2	physical	19122674
CLIP3_HUMAN	CLIP3	physical	19139280
PKHO1_HUMAN	PLEKHO1	physical	17942896
FOXO1_MOUSE	Foxo1	physical	10377430
NOS3_HUMAN	NOS3	physical	10376603
FOXO1_HUMAN	FOXO1	physical	10358075
BAD_HUMAN	BAD	physical	10358075
FOXO1_HUMAN	FOXO1	physical	10358014
GSK3B_HUMAN	GSK3B	physical	17428466
TCL1A_HUMAN	TCL1A	physical	25416956
EP300_HUMAN	EP300	physical	15224190
KAT6A_HUMAN	KAT6A	physical	23431171
F110C_HUMAN	FAM110C	physical	19698782
ACAP1_HUMAN	ACAP1	physical	16256741
CDN1C_HUMAN	CDKN1C	physical	23421998
SNAI1_HUMAN	SNAI1	physical	22158034
FOXO4_HUMAN	FOXO4	physical	16272144
RHG07_HUMAN	DLC1	physical	16338927
JIP1_HUMAN	MAPK8IP1	physical	16343492
YBOX1_HUMAN	YBX1	physical	16354698
BAD_HUMAN	BAD	physical	23085457
1433S_HUMAN	SFN	physical	20005908
PP2AA_HUMAN	PPP2CA	physical	20005908
PLCG1_HUMAN	PLCG1	physical	16525023
PP1A_HUMAN	PPP1CA	physical	20186153
PP1B_HUMAN	PPP1CB	physical	20186153
CDN1B_HUMAN	CDKN1B	physical	16780593
CDN1B_MOUSE	Cdkn1b	physical	16780593
CDN1A_HUMAN	CDKN1A	physical	16982699
TBK1_HUMAN	TBK1	physical	21106850
PDE3A_HUMAN	PDE3A	physical	17124499
CTNB1_HUMAN	CTNNB1	physical	17287208
AKTS1_HUMAN	AKT1S1	physical	17386266
NHRF1_HUMAN	SLC9A3R1	physical	25492869
ACK1_HUMAN	TNK2	physical	25257795
CSK_HUMAN	CSK	physical	26344197
PK3CB_HUMAN	PIK3CB	physical	26344197
RPE_HUMAN	RPE	physical	26344197
PP1A_HUMAN	PPP1CA	physical	16186112
AGR3_HUMAN	AGR3	physical	25640309
CASC3_HUMAN	CASC3	physical	25640309
ESIP1_HUMAN	EPSTI1	physical	25640309
I13R2_HUMAN	IL13RA2	physical	25640309
IL24_HUMAN	IL24	physical	25640309
MRC2_HUMAN	MRC2	physical	25640309
MTA3_HUMAN	MTA3	physical	25640309
OSGI1_HUMAN	OSGIN1	physical	25640309
RSLAB_HUMAN	RASL10B	physical	25640309
S10AE_HUMAN	S100A14	physical	25640309
SPB5_HUMAN	SERPINB5	physical	25640309
ST14_HUMAN	ST14	physical	25640309
TFF1_HUMAN	TFF1	physical	25640309
THRSP_HUMAN	THRSP	physical	25640309
NSD3_HUMAN	WHSC1L1	physical	25640309
THIC_HUMAN	ACAT2	physical	25640309
GET4_HUMAN	GET4	physical	25640309
CCNI_HUMAN	CCNI	physical	25640309
CLAP2_HUMAN	CLASP2	physical	25640309
ENOG_HUMAN	ENO2	physical	25640309
FAS_HUMAN	FASN	physical	25640309
GFAP_HUMAN	GFAP	physical	25640309
NMDE1_HUMAN	GRIN2A	physical	25640309
ODPB_HUMAN	PDHB	physical	25640309
PICK1_HUMAN	PICK1	physical	25640309
MYPR_HUMAN	PLP1	physical	25640309
KPCB_HUMAN	PRKCB	physical	25640309
PRS8_HUMAN	PSMC5	physical	25640309
PTGDS_HUMAN	PTGDS	physical	25640309
PTN3_HUMAN	PTPN3	physical	25640309
SYUB_HUMAN	SNCB	physical	25640309
SRR_HUMAN	SRR	physical	25640309
ST4A1_HUMAN	SULT4A1	physical	25640309
UCHL1_HUMAN	UCHL1	physical	25640309
ZN691_HUMAN	ZNF691	physical	25640309
TCOF_HUMAN	TCOF1	physical	26496610
MDM2_HUMAN	MDM2	physical	25241761
XIAP_HUMAN	XIAP	physical	25241761
PIAS2_HUMAN	PIAS2	physical	25241761
SMAD3_HUMAN	SMAD3	physical	25241761
MAPK2_HUMAN	MAPKAPK2	physical	25241761
PPM1A_HUMAN	PPM1A	physical	25241761
MTOR_HUMAN	MTOR	physical	25241761
IKKB_HUMAN	IKBKB	physical	25241761
CDN1A_HUMAN	CDKN1A	physical	25241761
IKKA_HUMAN	CHUK	physical	25241761
SRC_HUMAN	SRC	physical	25241761
KS6B1_HUMAN	RPS6KB1	physical	25241761
NOS3_HUMAN	NOS3	physical	25241761
FOXO3_HUMAN	FOXO3	physical	25241761
FOXO1_HUMAN	FOXO1	physical	25241761
4EBP1_HUMAN	EIF4EBP1	physical	25241761
CDN1B_HUMAN	CDKN1B	physical	25241761
BRAF_HUMAN	BRAF	physical	25241761
BAD_HUMAN	BAD	physical	25241761
PYGO2_HUMAN	PYGO2	physical	26170450
TRAF4_HUMAN	TRAF4	physical	24993240
KLHL3_HUMAN	KLHL3	physical	26435498
MERL_HUMAN	NF2	physical	21750658
LT4R2_HUMAN	LTB4R2	physical	22044535
GSK3A_HUMAN	GSK3A	physical	16998585
HSPB1_HUMAN	HSPB1	physical	12740362
NGB_HUMAN	NGB	physical	23904011
GSK3A_HUMAN	GSK3A	physical	22504172
AHSA1_HUMAN	AHSA1	physical	22504172
HS90A_HUMAN	HSP90AA1	physical	22504172
CDC37_HUMAN	CDC37	physical	22504172
GSK3A_HUMAN	GSK3A	physical	14701753
GSK3B_HUMAN	GSK3B	physical	14701753
GABR2_HUMAN	GABBR2	physical	15905570
H2B1B_HUMAN	HIST1H2BB	physical	15905570
CHK1_HUMAN	CHEK1	genetic	28319113
PRKDC_HUMAN	PRKDC	genetic	28319113
P85A_HUMAN	PIK3R1	physical	19117013
PK3CA_HUMAN	PIK3CA	physical	19117013
GBB1_HUMAN	GNB1	physical	19117013
IKBA_HUMAN	NFKBIA	physical	11278366
IKKA_HUMAN	CHUK	physical	11278366
AGAP2_HUMAN	AGAP2	physical	22450747
ACK1_HUMAN	TNK2	physical	25945695
FGFR1_HUMAN	FGFR1	physical	25945695
GSK3B_HUMAN	GSK3B	physical	22337773
AKT2_HUMAN	AKT2	physical	28514442
SRPK2_HUMAN	SRPK2	physical	19592491
FAK1_HUMAN	PTK2	physical	25792870
MTOR_HUMAN	MTOR	physical	25792870
GSK3A_HUMAN	GSK3A	physical	11546794
FANCI_HUMAN	FANCI	physical	27097374
GSK3B_HUMAN	GSK3B	physical	27563096
VHL_HUMAN	VHL	physical	27563096
EGLN1_HUMAN	EGLN1	physical	27563096
PP2AA_HUMAN	PPP2CA	physical	27563096
PDPK1_HUMAN	PDPK1	physical	27563096
FACD2_HUMAN	FANCD2	physical	27097374
UBP1_HUMAN	USP1	physical	27097374
CDN1B_HUMAN	CDKN1B	physical	28919423
KC1D_RAT	Csnk1d	physical	17594292
CE57L_HUMAN	CEP57L1	physical	27229929
CEP76_HUMAN	CEP76	physical	27229929
CTDS2_HUMAN	CTDSP2	physical	27229929
NOL4_HUMAN	NOL4	physical	27229929
NOTC1_HUMAN	NOTCH1	physical	27229929
TCL1A_HUMAN	TCL1A	physical	27229929
TRM2_HUMAN	TRMT2B	physical	27229929
IRS1_HUMAN	IRS1	physical	17640984
UBE2S_HUMAN	UBE2S	physical	27593939
BCL3_HUMAN	BCL3	physical	28689659
CCNF_HUMAN	CCNF	physical	28954236
KMT2D_HUMAN	KMT2D	physical	28336670
CDN1A_HUMAN	CDKN1A	physical	11463845
ITB3_HUMAN	ITGB3	physical	10896934
RAC1_HUMAN	RAC1	physical	10617634

Drug and Disease Associations

• Kegg Disease
• H00539: PTEN hamartoma tumor syndrome (PHTS), including: Cowden syndrome; Bannayan-Riley-Ruvalcaba syndrome;
• OMIM Disease
• 114480: Breast cancer (BC)
• 114500: Colorectal cancer (CRC)
• : Note=Genetic variations in AKT1 may play a role in susceptibility to ovarian cancer.
• 176920:
• 615109: Cowden syndrome 6 (CWS6)
• Kegg Drug
• D10381: Afuresertib (USAN)
• D10382: Afuresertib hydrochloride (USAN)
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"The deacetylase SIRT1 promotes membrane localization and activationof Akt and PDK1 during tumorigenesis and cardiac hypertrophy.";
Sundaresan N.R., Pillai V.B., Wolfgeher D., Samant S., Vasudevan P.,Parekh V., Raghuraman H., Cunningham J.M., Gupta M., Gupta M.P.;
Sci. Signal. 4:RA46-RA46(2011).
Cited for: INTERACTION WITH SIRT1, ACETYLATION AT LYS-14 AND LYS-20,DEACETYLATION AT LYS-14 AND LYS-20, AND MUTAGENESIS OF LYS-14; GLU-17AND LYS-20.
PubMed: 21775285

O-linked Glycosylation

"Extensive crosstalk between O-GlcNAcylation and phosphorylationregulates Akt signaling.";
Wang S., Huang X., Sun D., Xin X., Pan Q., Peng S., Liang Z., Luo C.,Yang Y., Jiang H., Huang M., Chai W., Ding J., Geng M.;
PLoS ONE 7:E37427-E37427(2012).
Cited for: GLYCOSYLATION AT SER-126; SER-129; THR-305 AND THR-312.
PubMed: 22629392

Phosphorylation

"Ack1 mediated AKT/PKB tyrosine 176 phosphorylation regulates itsactivation.";
Mahajan K., Coppola D., Challa S., Fang B., Chen Y.A., Zhu W.,Lopez A.S., Koomen J., Engelman R.W., Rivera C., Muraoka-Cook R.S.,Cheng J.Q., Schoenbrunn E., Sebti S.M., Earp H.S., Mahajan N.P.;
PLoS ONE 5:E9646-E9646(2010).
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-176; THR-308AND SER-473, MUTAGENESIS OF TYR-176, INTERACTION WITH TNK2, AND TISSUESPECIFICITY.
PubMed: 20333297

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-126 ANDSER-129, AND MASS SPECTROMETRY.
PubMed: 18669648

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-126 ANDSER-129, AND MASS SPECTROMETRY.
PubMed: 17081983

"Activation of Akt independent of PTEN and CTMP tumor-suppressor genemutations in epilepsy-associated Taylor-type focal corticaldysplasias.";
Schick V., Majores M., Engels G., Spitoni S., Koch A., Elger C.E.,Simon M., Knobbe C., Bluemcke I., Becker A.J.;
Acta Neuropathol. 112:715-725(2006).
Cited for: PHOSPHORYLATION AT SER-473.
PubMed: 17013611

"Phosphorylation and regulation of Akt/PKB by the rictor-mTORcomplex.";
Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.;
Science 307:1098-1101(2005).
Cited for: PHOSPHORYLATION AT THR-308, AND PHOSPHORYLATION AT SER-473 BY MTOR.
PubMed: 15718470

"LGI1, a putative tumor metastasis suppressor gene, controls in vitroinvasiveness and expression of matrix metalloproteinases in gliomacells through the ERK1/2 pathway.";
Kunapuli P., Kasyapa C.S., Hawthorn L., Cowell J.K.;
J. Biol. Chem. 279:23151-23157(2004).
Cited for: PHOSPHORYLATION AT SER-473.
PubMed: 15047712

"PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Aktactivity and mediates cellular invasion.";
Ahn J.-Y., Rong R., Kroll T.G., Van Meir E.G., Snyder S.H., Ye K.;
J. Biol. Chem. 279:16441-16451(2004).
Cited for: INTERACTION WITH AGAP2, AND PHOSPHORYLATION AT SER-473.
PubMed: 14761976

"Mechanism of activation of protein kinase B by insulin and IGF-1.";
Alessi D.R., Andjelkovic M., Caudwell F.B., Cron P., Morrice N.,Cohen P., Hemmings B.A.;
EMBO J. 15:6541-6551(1996).
Cited for: MUTAGENESIS OF THR-308 AND SER-473, AND PHOSPHORYLATION AT THR-308 ANDSER-473.
PubMed: 8978681

"Phosphoinositide-3-OH kinase-dependent regulation of glycogensynthase kinase 3 and protein kinase B/AKT by the integrin-linkedkinase.";
Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S.;
Proc. Natl. Acad. Sci. U.S.A. 95:11211-11216(1998).
Cited for: ENZYME REGULATION, AND PHOSPHORYLATION AT SER-473.
PubMed: 9736715

"Design of selective, ATP-competitive inhibitors of Akt.";
Freeman-Cook K.D., Autry C., Borzillo G., Gordon D.,Barbacci-Tobin E., Bernardo V., Briere D., Clark T., Corbett M.,Jakubczak J., Kakar S., Knauth E., Lippa B., Luzzio M.J., Mansour M.,Martinelli G., Marx M., Nelson K., Pandit J., Rajamohan F.,Robinson S., Subramanyam C., Wei L., Wythes M., Morris J.;
J. Med. Chem. 53:4615-4622(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 144-480, PHOSPHORYLATION ATTHR-308, AND ENZYME REGULATION.
PubMed: 20481595

"Synthesis and structure based optimization of novel Akt inhibitors.";
Lippa B., Pan G., Corbett M., Li C., Kauffman G.S., Pandit J.,Robinson S., Wei L., Kozina E., Marr E.S., Borzillo G., Knauth E.,Barbacci-Tobin E.G., Vincent P., Troutman M., Baker D., Rajamohan F.,Kakar S., Clark T., Morris J.;
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Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 144-480, PHOSPHORYLATION ATTHR-308, AND ENZYME REGULATION.
PubMed: 18456494

"Activation of protein kinase B beta and gamma isoforms by insulin invivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro:comparison with protein kinase B alpha.";
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Biochem. J. 331:299-308(1998).
Cited for: FUNCTION, ENZYME REGULATION, AND PHOSPHORYLATION AT THR-308 BY PDPK1.
PubMed: 9512493

"Direct identification of tyrosine 474 as a regulatory phosphorylationsite for the Akt protein kinase.";
Conus N.M., Hannan K.M., Cristiano B.E., Hemmings B.A., Pearson R.B.;
J. Biol. Chem. 277:38021-38028(2002).
Cited for: PHOSPHORYLATION AT TYR-474, AND MUTAGENESIS OF TYR-474.
PubMed: 12149249