MGI:Akt1

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Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0000060	protein import into nucleus, translocation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0000166	nucleotide binding	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0547	F	From MGI
	GO:0001649	osteoblast differentiation	MGI:MGI:3837587 PMID:19208758^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:88177 MGI:MGI:96440	P	From MGI
	GO:0001893	maternal placenta development	MGI:MGI:2673047 PMID:12783884^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675202	P	From MGI
	GO:0001934	positive regulation of protein phosphorylation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0004672	protein kinase activity	MGI:MGI:3028410 PMID:14730361^[3]	IDA: Inferred from Direct Assay		F	From MGI
	GO:0004672	protein kinase activity	MGI:MGI:3047434 PMID:15192701^[4]	IDA: Inferred from Direct Assay		F	From MGI
	GO:0004672	protein kinase activity	MGI:MGI:3510060 PMID:15010863^[5]	IDA: Inferred from Direct Assay		F	From MGI
	GO:0004672	protein kinase activity	MGI:MGI:3616720 PMID:16510873^[6]	IDA: Inferred from Direct Assay		F	From MGI
	GO:0004672	protein kinase activity	MGI:MGI:3690209 PMID:16357133^[7]	IDA: Inferred from Direct Assay		F	From MGI
	GO:0004672	protein kinase activity	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	F	From MGI
	GO:0004674	protein serine/threonine kinase activity	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	F	From MGI
	GO:0004674	protein serine/threonine kinase activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	F	From MGI
	GO:0004674	protein serine/threonine kinase activity	MGI:MGI:5306704 PMID:22057101^[8]	IDA: Inferred from Direct Assay		F	From MGI
	GO:0005080	protein kinase C binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3579938 PMID:15722337^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q60760	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3581096 PMID:15753085^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q5SNZ0	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3687885 PMID:12791994^[11]	IPI: Inferred from Physical Interaction	UniProtKB:Q8K4K2	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3690209 PMID:16357133^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q53EL6	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3690676 PMID:16051150^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q91YI4	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3836212 PMID:19139280^[13]	IPI: Inferred from Physical Interaction	UniProtKB:B9EHT4	F	From MGI
	GO:0005515	protein binding	MGI:MGI:4440773 PMID:20333297^[14]	IPI: Inferred from Physical Interaction	UniProtKB:O54967	F	From MGI
	GO:0005515	protein binding	MGI:MGI:4849347 PMID:21030605^[15]	IPI: Inferred from Physical Interaction	UniProtKB:P70227	F	From MGI
	GO:0005515	protein binding	MGI:MGI:5306546 PMID:21339740^[16]	IPI: Inferred from Physical Interaction	UniProtKB:Q8TCU6	F	From MGI
	GO:0005515	protein binding	MGI:MGI:5306704 PMID:22057101^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q91V17	F	From MGI
	GO:0005524	ATP binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	F	From MGI
	GO:0005524	ATP binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	F	From MGI
	GO:0005543	phospholipid binding	MGI:MGI:2152098	IEA: Inferred from Electronic Annotation	InterPro:IPR001849	F	From MGI
	GO:0005547	phosphatidylinositol-3,4,5-trisphosphate binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	F	From MGI
	GO:0005622	intracellular	MGI:MGI:3050929 PMID:15249583^[17]	IGI: Inferred from Genetic Interaction	MGI:MGI:102548 MGI:MGI:1270849 MGI:MGI:1927343 MGI:MGI:99454	C	From MGI
	GO:0005624	membrane fraction	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	C	From MGI
	GO:0005625	soluble fraction	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	C	From MGI
	GO:0005634	nucleus	MGI:MGI:4440773 PMID:20333297^[14]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005634	nucleus	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:B7Z5R1	C	From MGI
	GO:0005737	cytoplasm	MGI:MGI:2387238 PMID:12124386^[18]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005737	cytoplasm	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	C	From MGI
	GO:0005737	cytoplasm	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	C	From MGI
	GO:0005819	spindle	MGI:MGI:3056244 PMID:15509711^[19]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005829	cytosol	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	C	From MGI
	GO:0005829	cytosol	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	C	From MGI
	GO:0005886	plasma membrane	MGI:MGI:3027417 PMID:14749367^[20]	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	C	From MGI
	GO:0005886	plasma membrane	MGI:MGI:3574751 PMID:15775979^[21]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005886	plasma membrane	MGI:MGI:4440773 PMID:20333297^[14]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005886	plasma membrane	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	C	From MGI
	GO:0005975	carbohydrate metabolic process	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0119	P	From MGI
	GO:0005977	glycogen metabolic process	MGI:MGI:2673047 PMID:12783884^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675202	P	From MGI
	GO:0005978	glycogen biosynthetic process	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0005979	regulation of glycogen biosynthetic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0006006	glucose metabolic process	MGI:MGI:4413494 PMID:19897600^[22]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0006412	translation	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0006417	regulation of translation	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0810	P	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:2384368 PMID:12145204^[23]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:3027417 PMID:14749367^[20]	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:3028410 PMID:14730361^[3]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:3047434 PMID:15192701^[4]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:3589701 PMID:15937334^[24]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:4440773 PMID:20333297^[14]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0006469	negative regulation of protein kinase activity	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0006469	negative regulation of protein kinase activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0006810	transport	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0813	P	From MGI
	GO:0006915	apoptotic process	MGI:MGI:2387238 PMID:12124386^[18]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006924	activation-induced cell death of T cells	MGI:MGI:3027417 PMID:14749367^[20]	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0006954	inflammatory response	MGI:MGI:3028410 PMID:14730361^[3]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0007010	cytoskeleton organization	MGI:MGI:5306704 PMID:22057101^[8]	TAS: Traceable Author Statement		P	From MGI
	GO:0007165	signal transduction	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0007275	multicellular organismal development	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0217	P	From MGI
	GO:0007281	germ cell development	MGI:MGI:2384228 PMID:12140361^[25]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0007399	nervous system development	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0524	P	From MGI
	GO:0007568	aging	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0008286	insulin receptor signaling pathway	MGI:MGI:3687709 PMID:9415393^[26]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0008286	insulin receptor signaling pathway	MGI:MGI:3688072 PMID:11282895^[27]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0008286	insulin receptor signaling pathway	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0008286	insulin receptor signaling pathway	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0008637	apoptotic mitochondrial changes	MGI:MGI:2669068 PMID:12869584^[28]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0008643	carbohydrate transport	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0762	P	From MGI
	GO:0009725	response to hormone stimulus	MGI:MGI:3690209 PMID:16357133^[7]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0010748	negative regulation of plasma membrane long-chain fatty acid transport	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0010765	positive regulation of sodium ion transport	MGI:MGI:2154458	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0010765	positive regulation of sodium ion transport	MGI:MGI:3761956 PMID:17715136^[29]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0010765	positive regulation of sodium ion transport	MGI:MGI:3761956 PMID:17715136^[29]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0010907	positive regulation of glucose metabolic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0010975	regulation of neuron projection development	MGI:MGI:4411937 PMID:19778506^[30]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0015630	microtubule cytoskeleton	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:B7Z5R1	C	From MGI
	GO:0015758	glucose transport	MGI:MGI:3687709 PMID:9415393^[26]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0016020	membrane	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0472	C	From MGI
	GO:0016301	kinase activity	MGI:MGI:3027417 PMID:14749367^[20]	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	F	From MGI
	GO:0016310	phosphorylation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0016567	protein ubiquitination	MGI:MGI:2384368 PMID:12145204^[23]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0016740	transferase activity	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0808	F	From MGI
	GO:0016772	transferase activity, transferring phosphorus-containing groups	MGI:MGI:2152098	IEA: Inferred from Electronic Annotation	InterPro:IPR011009	F	From MGI
	GO:0018105	peptidyl-serine phosphorylation	MGI:MGI:3769319 PMID:16513828^[31]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0018105	peptidyl-serine phosphorylation	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0018105	peptidyl-serine phosphorylation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0019899	enzyme binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	F	From MGI
	GO:0019901	protein kinase binding	MGI:MGI:5306704 PMID:22057101^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q9WV60	F	From MGI
	GO:0030027	lamellipodium	MGI:MGI:2675770 PMID:12944902^[32]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0030030	cell projection organization	MGI:MGI:3610880 PMID:16286931^[33]	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0030163	protein catabolic process	MGI:MGI:2384368 PMID:12145204^[23]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0030235	nitric-oxide synthase regulator activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	F	From MGI
	GO:0030307	positive regulation of cell growth	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0030307	positive regulation of cell growth	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0030334	regulation of cell migration	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0030334	regulation of cell migration	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0031659	positive regulation of cyclin-dependent protein kinase activity involved in G1/S	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0031999	negative regulation of fatty acid beta-oxidation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0032094	response to food	MGI:MGI:3769319 PMID:16513828^[31]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0032270	positive regulation of cellular protein metabolic process	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0032287	peripheral nervous system myelin maintenance	MGI:MGI:4454957 PMID:20448149^[34]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	MGI:MGI:3589701 PMID:15937334^[24]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0032869	cellular response to insulin stimulus	MGI:MGI:2154458	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0032869	cellular response to insulin stimulus	MGI:MGI:3761956 PMID:17715136^[29]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0032869	cellular response to insulin stimulus	MGI:MGI:3761956 PMID:17715136^[29]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0032869	cellular response to insulin stimulus	MGI:MGI:3836212 PMID:19139280^[13]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0032869	cellular response to insulin stimulus	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0032869	cellular response to insulin stimulus	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0032880	regulation of protein localization	MGI:MGI:2154458	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0032880	regulation of protein localization	MGI:MGI:3761956 PMID:17715136^[29]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0033138	positive regulation of peptidyl-serine phosphorylation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0034405	response to fluid shear stress	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0035556	intracellular signal transduction	MGI:MGI:3027417 PMID:14749367^[20]	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0042593	glucose homeostasis	MGI:MGI:4413494 PMID:19897600^[22]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0042640	anagen	MGI:MGI:3531621 PMID:15713628^[35]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675202	P	From MGI
	GO:0042802	identical protein binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	F	From MGI
	GO:0043065	positive regulation of apoptotic process	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:3688072 PMID:11282895^[27]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0043154	negative regulation of cysteine-type endopeptidase activity involved in apoptotic process	MGI:MGI:5294538 PMID:18977203^[36]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0043325	phosphatidylinositol-3,4-bisphosphate binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	F	From MGI
	GO:0043491	protein kinase B signaling cascade	MGI:MGI:3050929 PMID:15249583^[17]	IGI: Inferred from Genetic Interaction	MGI:MGI:102548 MGI:MGI:1270849 MGI:MGI:1927343 MGI:MGI:99454	P	From MGI
	GO:0043536	positive regulation of blood vessel endothelial cell migration	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0045429	positive regulation of nitric oxide biosynthetic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0045600	positive regulation of fat cell differentiation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0045725	positive regulation of glycogen biosynthetic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0045768	positive regulation of anti-apoptosis	MGI:MGI:5294538 PMID:18977203^[36]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0045792	negative regulation of cell size	MGI:MGI:3610880 PMID:16286931^[33]	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0045884	regulation of survival gene product expression	MGI:MGI:3028410 PMID:14730361^[3]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0045907	positive regulation of vasoconstriction	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0045944	positive regulation of transcription from RNA polymerase II promoter	MGI:MGI:3806392 PMID:18762576^[37]	IGI: Inferred from Genetic Interaction	MGI:MGI:96434	P	From MGI
	GO:0046326	positive regulation of glucose import	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0046329	negative regulation of JNK cascade	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0046889	positive regulation of lipid biosynthetic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0048009	insulin-like growth factor receptor signaling pathway	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0051000	positive regulation of nitric-oxide synthase activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0051091	positive regulation of sequence-specific DNA binding transcription factor activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0051146	striated muscle cell differentiation	MGI:MGI:3806392 PMID:18762576^[37]	IGI: Inferred from Genetic Interaction	MGI:MGI:96440	P	From MGI
	GO:0060709	glycogen cell development involved in embryonic placenta development	MGI:MGI:2673047 PMID:12783884^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675202	P	From MGI
	GO:0060716	labyrinthine layer blood vessel development	MGI:MGI:2673047 PMID:12783884^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675202	P	From MGI
	GO:0070141	response to UV-A	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0071363	cellular response to growth factor stimulus	MGI:MGI:4366664 PMID:19744960^[38]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0071364	cellular response to epidermal growth factor stimulus	MGI:MGI:5292318 PMID:21712384^[39]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0071456	cellular response to hypoxia	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P47196	P	From MGI
	GO:0090004	positive regulation of establishment of protein localization in plasma membrane	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P31749	P	From MGI
	GO:0090201	negative regulation of release of cytochrome c from mitochondria	MGI:MGI:5294538 PMID:18977203^[36]	IDA: Inferred from Direct Assay		P	From MGI
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Mukherjee A & Rotwein P (2009) Akt promotes BMP2-mediated osteoblast differentiation and bone development. J Cell Sci 122: 716-26 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Yang ZZ et al. (2003) Protein kinase B alpha/Akt1 regulates placental development and fetal growth. J Biol Chem 278: 32124-31 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Song J et al. (2004) The costimulation-regulated duration of PKB activation controls T cell longevity. Nat Immunol 5: 150-8 PubMed GONUTS page
↑ ^4.0 ^4.1 Baki L et al. (2004) PS1 activates PI3K thus inhibiting GSK-3 activity and tau overphosphorylation: effects of FAD mutations. EMBO J 23: 2586-96 PubMed GONUTS page
↑ Tuhácková Z et al. (2004) IL2-dependent phosphorylation of 40S ribosomal protein S6 is controlled by PI-3K/mTOR signalling in CTLL2 cells. Int J Mol Med 13: 601-5 PubMed GONUTS page
↑ Wu X et al. (2006) Cdc42 controls progenitor cell differentiation and beta-catenin turnover in skin. Genes Dev 20: 571-85 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Palamarchuk A et al. (2005) Akt phosphorylates and regulates Pdcd4 tumor suppressor protein. Cancer Res 65: 11282-6 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Wakatsuki S et al. (2011) ZNRF1 promotes Wallerian degeneration by degrading AKT to induce GSK3B-dependent CRMP2 phosphorylation. Nat Cell Biol 13: 1415-23 PubMed GONUTS page
↑ Urschel S et al. (2005) Phosphorylation of grb10 regulates its interaction with 14-3-3. J Biol Chem 280: 16987-93 PubMed GONUTS page
↑ Anai M et al. (2005) A novel protein kinase B (PKB)/AKT-binding protein enhances PKB kinase activity and regulates DNA synthesis. J Biol Chem 280: 18525-35 PubMed GONUTS page
↑ Du K et al. (2003) TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver. Science 300: 1574-7 PubMed GONUTS page
↑ Beaulieu JM et al. (2005) An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell 122: 261-73 PubMed GONUTS page
↑ ^13.0 ^13.1 Ding J & Du K (2009) ClipR-59 interacts with Akt and regulates Akt cellular compartmentalization. Mol Cell Biol 29: 1459-71 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 Mahajan K et al. (2010) Ack1 mediated AKT/PKB tyrosine 176 phosphorylation regulates its activation. PLoS One 5: e9646 PubMed GONUTS page
↑ Giorgi C et al. (2010) PML regulates apoptosis at endoplasmic reticulum by modulating calcium release. Science 330: 1247-51 PubMed GONUTS page
↑ Kim EK et al. (2011) Selective activation of Akt1 by mammalian target of rapamycin complex 2 regulates cancer cell migration, invasion, and metastasis. Oncogene 30: 2954-63 PubMed GONUTS page
↑ ^17.0 ^17.1 Harrington LS et al. (2004) The TSC1-2 tumor suppressor controls insulin-PI3K signaling via regulation of IRS proteins. J Cell Biol 166: 213-23 PubMed GONUTS page
↑ ^18.0 ^18.1 Xu J et al. (2002) The role of Asp-462 in regulating Akt activity. J Biol Chem 277: 35561-6 PubMed GONUTS page
↑ Liu J et al. (2004) Serine-threonine kinases and transcription factors active in signal transduction are detected at high levels of phosphorylation during mitosis in preimplantation embryos and trophoblast stem cells. Reproduction 128: 643-54 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 ^20.4 Remy I & Michnick SW (2004) Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt. Mol Cell Biol 24: 1493-504 PubMed GONUTS page
↑ Tunggal JA et al. (2005) E-cadherin is essential for in vivo epidermal barrier function by regulating tight junctions. EMBO J 24: 1146-56 PubMed GONUTS page
↑ ^22.0 ^22.1 Gleason CE et al. (2010) Role of insulin-like growth factor-binding protein 5 (IGFBP5) in organismal and pancreatic beta-cell growth. Mol Endocrinol 24: 178-92 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 Lin HK et al. (2002) Phosphorylation-dependent ubiquitylation and degradation of androgen receptor by Akt require Mdm2 E3 ligase. EMBO J 21: 4037-48 PubMed GONUTS page
↑ ^24.0 ^24.1 Auger R et al. (2005) A role for mitogen-activated protein kinase(Erk1/2) activation and non-selective pore formation in P2X7 receptor-mediated thymocyte death. J Biol Chem 280: 28142-51 PubMed GONUTS page
↑ De Miguel MP et al. (2002) Dissection of the c-Kit signaling pathway in mouse primordial germ cells by retroviral-mediated gene transfer. Proc Natl Acad Sci U S A 99: 10458-63 PubMed GONUTS page
↑ ^26.0 ^26.1 Cong LN et al. (1997) Physiological role of Akt in insulin-stimulated translocation of GLUT4 in transfected rat adipose cells. Mol Endocrinol 11: 1881-90 PubMed GONUTS page
↑ ^27.0 ^27.1 Yamashita K et al. (2001) Reperfusion-activated Akt kinase prevents apoptosis in transgenic mouse hearts overexpressing insulin-like growth factor-1. Circ Res 88: 609-14 PubMed GONUTS page
↑ Fox CJ et al. (2003) The serine/threonine kinase Pim-2 is a transcriptionally regulated apoptotic inhibitor. Genes Dev 17: 1841-54 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 ^29.4 Lee IH et al. (2007) Akt mediates the effect of insulin on epithelial sodium channels by inhibiting Nedd4-2. J Biol Chem 282: 29866-73 PubMed GONUTS page
↑ Kim JY et al. (2009) DISC1 regulates new neuron development in the adult brain via modulation of AKT-mTOR signaling through KIAA1212. Neuron 63: 761-73 PubMed GONUTS page
↑ ^31.0 ^31.1 Luque RM & Kineman RD (2006) Impact of obesity on the growth hormone axis: evidence for a direct inhibitory effect of hyperinsulinemia on pituitary function. Endocrinology 147: 2754-63 PubMed GONUTS page
↑ Figueroa C & Vojtek AB (2003) Akt negatively regulates translation of the ternary complex factor Elk-1. Oncogene 22: 5554-61 PubMed GONUTS page
↑ ^33.0 ^33.1 Tavazoie SF et al. (2005) Regulation of neuronal morphology and function by the tumor suppressors Tsc1 and Tsc2. Nat Neurosci 8: 1727-34 PubMed GONUTS page
↑ Cotter L et al. (2010) Dlg1-PTEN interaction regulates myelin thickness to prevent damaging peripheral nerve overmyelination. Science 328: 1415-8 PubMed GONUTS page
↑ Di-Poï N et al. (2005) Epithelium-mesenchyme interactions control the activity of peroxisome proliferator-activated receptor beta/delta during hair follicle development. Mol Cell Biol 25: 1696-712 PubMed GONUTS page
↑ ^36.0 ^36.1 ^36.2 Sun X et al. (2008) Akt activation prevents Apop-1-induced death of cells. Biochem Biophys Res Commun 377: 1097-101 PubMed GONUTS page
↑ ^37.0 ^37.1 Ren H et al. (2008) IGFBP-5 regulates muscle cell differentiation by binding to IGF-II and switching on the IGF-II auto-regulation loop. J Cell Biol 182: 979-91 PubMed GONUTS page
↑ Giovannone B et al. (2009) GIGYF2 gene disruption in mice results in neurodegeneration and altered insulin-like growth factor signaling. Hum Mol Genet 18: 4629-39 PubMed GONUTS page
↑ Rahman P et al. (2011) Silencer of death domains (SODD) inhibits skeletal muscle and kidney enriched inositol 5-phosphatase (SKIP) and regulates phosphoinositide 3-kinase (PI3K)/Akt signaling to the actin cytoskeleton. J Biol Chem 286: 29758-70 PubMed GONUTS page

[PMID:19208758-0] Mukherjee A & Rotwein P (2009) Akt promotes BMP2-mediated osteoblast differentiation and bone development. J Cell Sci 122: 716-26 PubMed GONUTS page

[PMID:12783884-1] 2.0 ^2.1 ^2.2 ^2.3 Yang ZZ et al. (2003) Protein kinase B alpha/Akt1 regulates placental development and fetal growth. J Biol Chem 278: 32124-31 PubMed GONUTS page

[PMID:14730361-2] 3.0 ^3.1 ^3.2 ^3.3 Song J et al. (2004) The costimulation-regulated duration of PKB activation controls T cell longevity. Nat Immunol 5: 150-8 PubMed GONUTS page

[PMID:15192701-3] 4.0 ^4.1 Baki L et al. (2004) PS1 activates PI3K thus inhibiting GSK-3 activity and tau overphosphorylation: effects of FAD mutations. EMBO J 23: 2586-96 PubMed GONUTS page

[PMID:15010863-4] Tuhácková Z et al. (2004) IL2-dependent phosphorylation of 40S ribosomal protein S6 is controlled by PI-3K/mTOR signalling in CTLL2 cells. Int J Mol Med 13: 601-5 PubMed GONUTS page

[PMID:16510873-5] Wu X et al. (2006) Cdc42 controls progenitor cell differentiation and beta-catenin turnover in skin. Genes Dev 20: 571-85 PubMed GONUTS page

[PMID:16357133-6] 7.0 ^7.1 ^7.2 Palamarchuk A et al. (2005) Akt phosphorylates and regulates Pdcd4 tumor suppressor protein. Cancer Res 65: 11282-6 PubMed GONUTS page

[PMID:22057101-7] 8.0 ^8.1 ^8.2 ^8.3 Wakatsuki S et al. (2011) ZNRF1 promotes Wallerian degeneration by degrading AKT to induce GSK3B-dependent CRMP2 phosphorylation. Nat Cell Biol 13: 1415-23 PubMed GONUTS page

[PMID:15722337-8] Urschel S et al. (2005) Phosphorylation of grb10 regulates its interaction with 14-3-3. J Biol Chem 280: 16987-93 PubMed GONUTS page

[PMID:15753085-9] Anai M et al. (2005) A novel protein kinase B (PKB)/AKT-binding protein enhances PKB kinase activity and regulates DNA synthesis. J Biol Chem 280: 18525-35 PubMed GONUTS page

[PMID:12791994-10] Du K et al. (2003) TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver. Science 300: 1574-7 PubMed GONUTS page

[PMID:16051150-11] Beaulieu JM et al. (2005) An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell 122: 261-73 PubMed GONUTS page

[PMID:19139280-12] 13.0 ^13.1 Ding J & Du K (2009) ClipR-59 interacts with Akt and regulates Akt cellular compartmentalization. Mol Cell Biol 29: 1459-71 PubMed GONUTS page

[PMID:20333297-13] 14.0 ^14.1 ^14.2 ^14.3 Mahajan K et al. (2010) Ack1 mediated AKT/PKB tyrosine 176 phosphorylation regulates its activation. PLoS One 5: e9646 PubMed GONUTS page

[PMID:21030605-14] Giorgi C et al. (2010) PML regulates apoptosis at endoplasmic reticulum by modulating calcium release. Science 330: 1247-51 PubMed GONUTS page

[PMID:21339740-15] Kim EK et al. (2011) Selective activation of Akt1 by mammalian target of rapamycin complex 2 regulates cancer cell migration, invasion, and metastasis. Oncogene 30: 2954-63 PubMed GONUTS page

[PMID:15249583-16] 17.0 ^17.1 Harrington LS et al. (2004) The TSC1-2 tumor suppressor controls insulin-PI3K signaling via regulation of IRS proteins. J Cell Biol 166: 213-23 PubMed GONUTS page

[PMID:12124386-17] 18.0 ^18.1 Xu J et al. (2002) The role of Asp-462 in regulating Akt activity. J Biol Chem 277: 35561-6 PubMed GONUTS page

[PMID:15509711-18] Liu J et al. (2004) Serine-threonine kinases and transcription factors active in signal transduction are detected at high levels of phosphorylation during mitosis in preimplantation embryos and trophoblast stem cells. Reproduction 128: 643-54 PubMed GONUTS page

[PMID:14749367-19] 20.0 ^20.1 ^20.2 ^20.3 ^20.4 Remy I & Michnick SW (2004) Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt. Mol Cell Biol 24: 1493-504 PubMed GONUTS page

[PMID:15775979-20] Tunggal JA et al. (2005) E-cadherin is essential for in vivo epidermal barrier function by regulating tight junctions. EMBO J 24: 1146-56 PubMed GONUTS page

[PMID:19897600-21] 22.0 ^22.1 Gleason CE et al. (2010) Role of insulin-like growth factor-binding protein 5 (IGFBP5) in organismal and pancreatic beta-cell growth. Mol Endocrinol 24: 178-92 PubMed GONUTS page

[PMID:12145204-22] 23.0 ^23.1 ^23.2 Lin HK et al. (2002) Phosphorylation-dependent ubiquitylation and degradation of androgen receptor by Akt require Mdm2 E3 ligase. EMBO J 21: 4037-48 PubMed GONUTS page

[PMID:15937334-23] 24.0 ^24.1 Auger R et al. (2005) A role for mitogen-activated protein kinase(Erk1/2) activation and non-selective pore formation in P2X7 receptor-mediated thymocyte death. J Biol Chem 280: 28142-51 PubMed GONUTS page

[PMID:12140361-24] De Miguel MP et al. (2002) Dissection of the c-Kit signaling pathway in mouse primordial germ cells by retroviral-mediated gene transfer. Proc Natl Acad Sci U S A 99: 10458-63 PubMed GONUTS page

[PMID:9415393-25] 26.0 ^26.1 Cong LN et al. (1997) Physiological role of Akt in insulin-stimulated translocation of GLUT4 in transfected rat adipose cells. Mol Endocrinol 11: 1881-90 PubMed GONUTS page

[PMID:11282895-26] 27.0 ^27.1 Yamashita K et al. (2001) Reperfusion-activated Akt kinase prevents apoptosis in transgenic mouse hearts overexpressing insulin-like growth factor-1. Circ Res 88: 609-14 PubMed GONUTS page

[PMID:12869584-27] Fox CJ et al. (2003) The serine/threonine kinase Pim-2 is a transcriptionally regulated apoptotic inhibitor. Genes Dev 17: 1841-54 PubMed GONUTS page

[PMID:17715136-28] 29.0 ^29.1 ^29.2 ^29.3 ^29.4 Lee IH et al. (2007) Akt mediates the effect of insulin on epithelial sodium channels by inhibiting Nedd4-2. J Biol Chem 282: 29866-73 PubMed GONUTS page

[PMID:19778506-29] Kim JY et al. (2009) DISC1 regulates new neuron development in the adult brain via modulation of AKT-mTOR signaling through KIAA1212. Neuron 63: 761-73 PubMed GONUTS page

[PMID:16513828-30] 31.0 ^31.1 Luque RM & Kineman RD (2006) Impact of obesity on the growth hormone axis: evidence for a direct inhibitory effect of hyperinsulinemia on pituitary function. Endocrinology 147: 2754-63 PubMed GONUTS page

[PMID:12944902-31] Figueroa C & Vojtek AB (2003) Akt negatively regulates translation of the ternary complex factor Elk-1. Oncogene 22: 5554-61 PubMed GONUTS page

[PMID:16286931-32] 33.0 ^33.1 Tavazoie SF et al. (2005) Regulation of neuronal morphology and function by the tumor suppressors Tsc1 and Tsc2. Nat Neurosci 8: 1727-34 PubMed GONUTS page

[PMID:20448149-33] Cotter L et al. (2010) Dlg1-PTEN interaction regulates myelin thickness to prevent damaging peripheral nerve overmyelination. Science 328: 1415-8 PubMed GONUTS page

[PMID:15713628-34] Di-Poï N et al. (2005) Epithelium-mesenchyme interactions control the activity of peroxisome proliferator-activated receptor beta/delta during hair follicle development. Mol Cell Biol 25: 1696-712 PubMed GONUTS page

[PMID:18977203-35] 36.0 ^36.1 ^36.2 Sun X et al. (2008) Akt activation prevents Apop-1-induced death of cells. Biochem Biophys Res Commun 377: 1097-101 PubMed GONUTS page

[PMID:18762576-36] 37.0 ^37.1 Ren H et al. (2008) IGFBP-5 regulates muscle cell differentiation by binding to IGF-II and switching on the IGF-II auto-regulation loop. J Cell Biol 182: 979-91 PubMed GONUTS page

[PMID:19744960-37] Giovannone B et al. (2009) GIGYF2 gene disruption in mice results in neurodegeneration and altered insulin-like growth factor signaling. Hum Mol Genet 18: 4629-39 PubMed GONUTS page

[PMID:21712384-38] Rahman P et al. (2011) Silencer of death domains (SODD) inhibits skeletal muscle and kidney enriched inositol 5-phosphatase (SKIP) and regulates phosphoinositide 3-kinase (PI3K)/Akt signaling to the actin cytoskeleton. J Biol Chem 286: 29758-70 PubMed GONUTS page

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Species (Taxon ID)	Mus musculus (house mouse) (taxon:10090)
Gene Name(s)	Akt1 ( synonyms: Akt, PKB, PKB/Akt, PKBalpha )
Protein Name(s)	thymoma viral proto-oncogene 1,
External Links
MGI	MGI:87986

MGI:Akt1

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