Human Metabolome Database: Showing Protein RAC-alpha serine/threonine-protein kinase (HMDBP13418)

Identification Biological properties Gene properties Protein properties External links References XML Show 2 metabolites

Identification

HMDB Protein ID

HMDBP13418

Secondary Accession Numbers

None

Name

RAC-alpha serine/threonine-protein kinase

Synonyms

AKT1 kinase
Protein kinase B
Protein kinase B alpha
Proto-oncogene c-Akt
RAC-PK-alpha
Thymoma viral proto-oncogene
PKB
PKB alpha

Gene Name

AKT1

Protein Type

Unknown

Biological Properties

General Function

Not Available

Specific Function

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 (PubMed:11882383, PubMed:21620960, PubMed:21432781). AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface (PubMed:9415393). Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling (PubMed:11579209). Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport (PubMed:11994271). 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 (PubMed:22057101). Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven (PubMed:22057101). 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 (By similarity). AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis (By similarity). Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis (PubMed:10454575). Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity (By similarity). The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth (By similarity). 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 (PubMed:19778506). 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) (PubMed:11282895, PubMed:18288188). AKT mediates the antiapoptotic effects of IGF-I (PubMed:11282895). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (By similarity). May be involved in the regulation of the placental development (PubMed:12783884). 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. Phosphorylates palladin (PALLD), modulating cytoskeletal organization and cell motility. Phosphorylates prohibitin (PHB), playing an important role in cell metabolism and proliferation. Phosphorylates 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 (By similarity). Phosphorylates PCK1 at 'Ser-90', reducing the binding affinity of PCK1 to oxaloacetate and changing PCK1 into an atypical protein kinase activity using GTP as donor (By similarity). Also acts as an activator of TMEM175 potassium channel activity in response to growth factors: forms the lysoK(GF) complex together with TMEM175 and acts by promoting TMEM175 channel activation, independently of its protein kinase activity (PubMed:32228865).

Pathways

Acute myeloid leukemia
Adipocytokine signaling pathway
Adrenergic signaling in cardiomyocytes
AGE-RAGE signaling pathway in diabetic complications
Alzheimer disease
AMPK signaling pathway
Apelin signaling pathway
Apoptosis
Autophagy - animal
B cell receptor signaling pathway
Breast cancer
C-type lectin receptor signaling pathway
cAMP signaling pathway
Carbohydrate digestion and absorption
Cellular senescence
Central carbon metabolism in cancer
cGMP-PKG signaling pathway
Chagas disease
Chemical carcinogenesis - reactive oxygen species
Chemical carcinogenesis - receptor activation
Chemokine signaling pathway
Choline metabolism in cancer
Cholinergic synapse
Chronic myeloid leukemia
Colorectal cancer
Diabetic cardiomyopathy
Dopaminergic synapse
EGFR tyrosine kinase inhibitor resistance
Endocrine resistance
Endometrial cancer
Epstein-Barr virus infection
ErbB signaling pathway
Estrogen signaling pathway
Fc epsilon RI signaling pathway
Fc gamma R-mediated phagocytosis
Fluid shear stress and atherosclerosis
Focal adhesion
FoxO signaling pathway
Gastric cancer
Glioma
Glucagon signaling pathway
GnRH secretion
Growth hormone synthesis, secretion and action
Hepatitis B
Hepatitis C
Hepatocellular carcinoma
Herpes simplex virus 1 infection
HIF-1 signaling pathway
Human cytomegalovirus infection
Human immunodeficiency virus 1 infection
Human papillomavirus infection
Human T-cell leukemia virus 1 infection
Influenza A
Insulin resistance
Insulin signaling pathway
JAK-STAT signaling pathway
Kaposi sarcoma-associated herpesvirus infection
Lipid and atherosclerosis
Longevity regulating pathway
Longevity regulating pathway - multiple species
MAPK signaling pathway
Measles
Melanoma
mTOR signaling pathway
Neurotrophin signaling pathway
Neutrophil extracellular trap formation
Non-alcoholic fatty liver disease
Non-small cell lung cancer
Osteoclast differentiation
Pancreatic cancer
PD-L1 expression and PD-1 checkpoint pathway in cancer
Phospholipase D signaling pathway
PI3K-Akt signaling pathway
Platelet activation
Platinum drug resistance
Progesterone-mediated oocyte maturation
Prolactin signaling pathway
Prostate cancer
Proteoglycans in cancer
Rap1 signaling pathway
Ras signaling pathway
Regulation of lipolysis in adipocytes
Relaxin signaling pathway
Renal cell carcinoma
Salmonella infection
Signaling pathways regulating pluripotency of stem cells
Small cell lung cancer
Sphingolipid signaling pathway
Spinocerebellar ataxia
T cell receptor signaling pathway
Thyroid hormone signaling pathway
TNF signaling pathway
Toll-like receptor signaling pathway
Toxoplasmosis
Tuberculosis
VEGF signaling pathway
Yersinia infection

Reactions

Not Available

GO Classification

Biological Process
regulation of neuron projection development
peptidyl-serine phosphorylation
signal transduction
cellular response to prostaglandin E stimulus
gene expression
positive regulation of apoptotic process
positive regulation of vasoconstriction
translation
negative regulation of release of cytochrome c from mitochondria
maternal placenta development
positive regulation of glycogen biosynthetic process
negative regulation of protein ubiquitination
positive regulation of proteasomal ubiquitin-dependent protein catabolic process
positive regulation of cell proliferation
negative regulation of apoptotic process
response to hormone stimulus
peripheral nervous system myelin maintenance
cell migration involved in sprouting angiogenesis
positive regulation of glucose metabolic process
negative regulation of cell size
response to oxidative stress
inflammatory response
protein catabolic process
NIK/NF-kappaB signaling
cellular response to tumor necrosis factor
response to growth hormone stimulus
response to DNA damage stimulus
insulin-like growth factor receptor signaling pathway
insulin receptor signaling pathway
positive regulation of endothelial cell migration
positive regulation of protein phosphorylation
response to food
cellular response to vascular endothelial growth factor stimulus
protein kinase B signaling cascade
regulation of translation
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
negative regulation of intrinsic apoptotic signaling pathway
cytoskeleton organization
negative regulation of endopeptidase activity
labyrinthine layer blood vessel development
glycogen metabolic process
positive regulation of G1/S transition of mitotic cell cycle
response to organic substance
I-kappaB kinase/NF-kappaB cascade
positive regulation of protein localization to plasma membrane
positive regulation of nitric oxide biosynthetic process
positive regulation of blood vessel endothelial cell migration
cellular response to nerve growth factor stimulus
cellular response to insulin stimulus
positive regulation of glucose import
osteoblast differentiation
cellular response to organic cyclic compound
glucose metabolic process
regulation of protein localization
spinal cord development
positive regulation of cellular protein metabolic process
apoptotic mitochondrial changes
positive regulation of sequence-specific DNA binding transcription factor activity
regulation of cell migration
glucose homeostasis
positive regulation of transcription, DNA-dependent
positive regulation of nitric-oxide synthase activity
germ cell development
cellular response to epidermal growth factor stimulus
positive regulation of transcription from RNA polymerase II promoter
establishment of protein localization to mitochondrion
maintenance of protein location in mitochondrion
activation-induced cell death of T cells
cellular response to decreased oxygen levels
cellular response to peptide
positive regulation of cell growth
cellular response to cadmium ion
execution phase of apoptosis
glycogen cell differentiation involved in embryonic placenta development
hyaluronan metabolic process
cellular response to reactive oxygen species
negative regulation of calcium import into the mitochondrion
regulation of apoptotic process
negative regulation of fatty acid beta-oxidation
negative regulation of leukocyte cell-cell adhesion
negative regulation of long-chain fatty acid import across plasma membrane
negative regulation of lymphocyte migration
negative regulation of proteolysis
protein phosphorylation
phosphatidylinositol 3-kinase signaling
positive regulation of cyclin-dependent protein serine/threonine kinase activity
positive regulation of endodeoxyribonuclease activity
positive regulation of fibroblast migration
positive regulation of I-kappaB phosphorylation
positive regulation of lipid biosynthetic process
positive regulation of mitochondrial membrane potential
positive regulation of organ growth
positive regulation of protein localization to nucleus
regulation of aerobic respiration
cellular response to granulocyte macrophage colony-stimulating factor stimulus
regulation of myelination
response to insulin-like growth factor stimulus
negative regulation of JNK cascade
response to ischemia
response to UV-A
sphingosine-1-phosphate receptor signaling pathway
striated muscle cell differentiation
aging
cell projection organization
negative regulation of protein binding
carbohydrate transport
positive regulation of fat cell differentiation
cellular response to mechanical stimulus
regulation of glycogen biosynthetic process
cellular response to oxidised low-density lipoprotein particle stimulus
lipopolysaccharide-mediated signaling pathway
peptidyl-threonine phosphorylation
cellular response to growth factor stimulus
positive regulation of gene expression
response to fluid shear stress
cellular response to hypoxia
positive regulation of endothelial cell proliferation
protein import into nucleus
positive regulation of smooth muscle cell proliferation
negative regulation of gene expression
positive regulation of peptidyl-serine phosphorylation
negative regulation of superoxide anion generation
glycogen biosynthetic process
phosphorylation
epidermal growth factor receptor signaling pathway
interleukin-18-mediated signaling pathway
intracellular signal transduction
negative regulation of protein kinase activity
negative regulation of autophagy
positive regulation of protein localization to cell surface
positive regulation of sodium ion transport
protein ubiquitination
Cellular Component
cytosol
spindle
microtubule cytoskeleton
protein-containing complex
cytoplasm
mitochondrion
plasma membrane
nucleus
cell-cell junction
nucleoplasm
vesicle
ciliary basal body
Molecular Function
protein kinase binding
kinase activity
phosphatidylinositol-3,4,5-trisphosphate binding
ATP binding
protein homodimerization activity
14-3-3 protein binding
GTPase activating protein binding
nitric-oxide synthase regulator activity
phosphatidylinositol-3,4-bisphosphate binding
potassium channel activator activity
protein serine/threonine/tyrosine kinase activity
protein kinase C binding
protein serine kinase activity
protein kinase activity
protein serine/threonine kinase activity
protein threonine kinase activity
enzyme binding
identical protein binding
calmodulin binding
protein phosphatase 2A binding

Cellular Location

Not Available

Gene Properties

Chromosome Location

Not Available

Locus

Not Available

SNPs

Not Available

Gene Sequence

Not Available

Protein Properties

Number of Residues

488

Molecular Weight

55706.955

Theoretical pI

6.322

Pfam Domain Function

PH (PF00169 )
Pkinase (PF00069 )
Pkinase_C (PF00433 )

Signals

Not Available

Transmembrane Regions

Not Available

Protein Sequence

Not Available

External Links

GenBank ID Protein

Not Available

UniProtKB/Swiss-Prot ID

P31750

UniProtKB/Swiss-Prot Entry Name

AKT1_MOUSE

PDB IDs

Not Available

GenBank Gene ID

Not Available

GeneCard ID

Not Available

GenAtlas ID

Not Available

HGNC ID

Not Available

References

General References

Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
Carninci P, Kasukawa T, Katayama S, Gough J, Frith MC, Maeda N, Oyama R, Ravasi T, Lenhard B, Wells C, Kodzius R, Shimokawa K, Bajic VB, Brenner SE, Batalov S, Forrest AR, Zavolan M, Davis MJ, Wilming LG, Aidinis V, Allen JE, Ambesi-Impiombato A, Apweiler R, Aturaliya RN, Bailey TL, Bansal M, Baxter L, Beisel KW, Bersano T, Bono H, Chalk AM, Chiu KP, Choudhary V, Christoffels A, Clutterbuck DR, Crowe ML, Dalla E, Dalrymple BP, de Bono B, Della Gatta G, di Bernardo D, Down T, Engstrom P, Fagiolini M, Faulkner G, Fletcher CF, Fukushima T, Furuno M, Futaki S, Gariboldi M, Georgii-Hemming P, Gingeras TR, Gojobori T, Green RE, Gustincich S, Harbers M, Hayashi Y, Hensch TK, Hirokawa N, Hill D, Huminiecki L, Iacono M, Ikeo K, Iwama A, Ishikawa T, Jakt M, Kanapin A, Katoh M, Kawasawa Y, Kelso J, Kitamura H, Kitano H, Kollias G, Krishnan SP, Kruger A, Kummerfeld SK, Kurochkin IV, Lareau LF, Lazarevic D, Lipovich L, Liu J, Liuni S, McWilliam S, Madan Babu M, Madera M, Marchionni L, Matsuda H, Matsuzawa S, Miki H, Mignone F, Miyake S, Morris K, Mottagui-Tabar S, Mulder N, Nakano N, Nakauchi H, Ng P, Nilsson R, Nishiguchi S, Nishikawa S, Nori F, Ohara O, Okazaki Y, Orlando V, Pang KC, Pavan WJ, Pavesi G, Pesole G, Petrovsky N, Piazza S, Reed J, Reid JF, Ring BZ, Ringwald M, Rost B, Ruan Y, Salzberg SL, Sandelin A, Schneider C, Schonbach C, Sekiguchi K, Semple CA, Seno S, Sessa L, Sheng Y, Shibata Y, Shimada H, Shimada K, Silva D, Sinclair B, Sperling S, Stupka E, Sugiura K, Sultana R, Takenaka Y, Taki K, Tammoja K, Tan SL, Tang S, Taylor MS, Tegner J, Teichmann SA, Ueda HR, van Nimwegen E, Verardo R, Wei CL, Yagi K, Yamanishi H, Zabarovsky E, Zhu S, Zimmer A, Hide W, Bult C, Grimmond SM, Teasdale RD, Liu ET, Brusic V, Quackenbush J, Wahlestedt C, Mattick JS, Hume DA, Kai C, Sasaki D, Tomaru Y, Fukuda S, Kanamori-Katayama M, Suzuki M, Aoki J, Arakawa T, Iida J, Imamura K, Itoh M, Kato T, Kawaji H, Kawagashira N, Kawashima T, Kojima M, Kondo S, Konno H, Nakano K, Ninomiya N, Nishio T, Okada M, Plessy C, Shibata K, Shiraki T, Suzuki S, Tagami M, Waki K, Watahiki A, Okamura-Oho Y, Suzuki H, Kawai J, Hayashizaki Y: The transcriptional landscape of the mammalian genome. Science. 2005 Sep 2;309(5740):1559-63. [PubMed:16141072 ]
Pekarsky Y, Koval A, Hallas C, Bichi R, Tresini M, Malstrom S, Russo G, Tsichlis P, Croce CM: Tcl1 enhances Akt kinase activity and mediates its nuclear translocation. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3028-33. [PubMed:10716693 ]
Maira SM, Galetic I, Brazil DP, Kaech S, Ingley E, Thelen M, Hemmings BA: Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane. Science. 2001 Oct 12;294(5541):374-80. [PubMed:11598301 ]
Kane S, Sano H, Liu SC, Asara JM, Lane WS, Garner CC, Lienhard GE: A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain. J Biol Chem. 2002 Jun 21;277(25):22115-8. Epub 2002 May 6. [PubMed:11994271 ]
Urschel S, Bassermann F, Bai RY, Munch S, Peschel C, Duyster J: Phosphorylation of grb10 regulates its interaction with 14-3-3. J Biol Chem. 2005 Apr 29;280(17):16987-93. Epub 2005 Feb 18. [PubMed:15722337 ]
Ravichandran LV, Chen H, Li Y, Quon MJ: Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor. Mol Endocrinol. 2001 Oct;15(10):1768-80. [PubMed:11579209 ]
Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [PubMed:21183079 ]
Church DM, Goodstadt L, Hillier LW, Zody MC, Goldstein S, She X, Bult CJ, Agarwala R, Cherry JL, DiCuccio M, Hlavina W, Kapustin Y, Meric P, Maglott D, Birtle Z, Marques AC, Graves T, Zhou S, Teague B, Potamousis K, Churas C, Place M, Herschleb J, Runnheim R, Forrest D, Amos-Landgraf J, Schwartz DC, Cheng Z, Lindblad-Toh K, Eichler EE, Ponting CP: Lineage-specific biology revealed by a finished genome assembly of the mouse. PLoS Biol. 2009 May 5;7(5):e1000112. doi: 10.1371/journal.pbio.1000112. Epub 2009 May 26. [PubMed:19468303 ]
Villen J, Beausoleil SA, Gerber SA, Gygi SP: Large-scale phosphorylation analysis of mouse liver. Proc Natl Acad Sci U S A. 2007 Jan 30;104(5):1488-93. doi: 10.1073/pnas.0609836104. Epub 2007 Jan 22. [PubMed:17242355 ]
Bellacosa A, Franke TF, Gonzalez-Portal ME, Datta K, Taguchi T, Gardner J, Cheng JQ, Testa JR, Tsichlis PN: Structure, expression and chromosomal mapping of c-akt: relationship to v-akt and its implications. Oncogene. 1993 Mar;8(3):745-54. [PubMed:8437858 ]
Yang ZZ, Tschopp O, Hemmings-Mieszczak M, Feng J, Brodbeck D, Perentes E, Hemmings BA: Protein kinase B alpha/Akt1 regulates placental development and fetal growth. J Biol Chem. 2003 Aug 22;278(34):32124-31. doi: 10.1074/jbc.M302847200. Epub 2003 Jun 3. [PubMed:12783884 ]
Cong LN, Chen H, Li Y, Zhou L, McGibbon MA, Taylor SI, Quon MJ: Physiological role of Akt in insulin-stimulated translocation of GLUT4 in transfected rat adipose cells. Mol Endocrinol. 1997 Dec;11(13):1881-90. doi: 10.1210/mend.11.13.0027. [PubMed:9415393 ]
Kitamura T, Kitamura Y, Kuroda S, Hino Y, Ando M, Kotani K, Konishi H, Matsuzaki H, Kikkawa U, Ogawa W, Kasuga M: Insulin-induced phosphorylation and activation of cyclic nucleotide phosphodiesterase 3B by the serine-threonine kinase Akt. Mol Cell Biol. 1999 Sep;19(9):6286-96. doi: 10.1128/MCB.19.9.6286. [PubMed:10454575 ]
Mizuki M, Fenski R, Halfter H, Matsumura I, Schmidt R, Muller C, Gruning W, Kratz-Albers K, Serve S, Steur C, Buchner T, Kienast J, Kanakura Y, Berdel WE, Serve H: Flt3 mutations from patients with acute myeloid leukemia induce transformation of 32D cells mediated by the Ras and STAT5 pathways. Blood. 2000 Dec 1;96(12):3907-14. [PubMed:11090077 ]
Yamashita K, Kajstura J, Discher DJ, Wasserlauf BJ, Bishopric NH, Anversa P, Webster KA: Reperfusion-activated Akt kinase prevents apoptosis in transgenic mouse hearts overexpressing insulin-like growth factor-1. Circ Res. 2001 Mar 30;88(6):609-14. doi: 10.1161/01.res.88.6.609. [PubMed:11282895 ]
Xu J, Liu D, Songyang Z: The role of Asp-462 in regulating Akt activity. J Biol Chem. 2002 Sep 20;277(38):35561-6. doi: 10.1074/jbc.M203805200. Epub 2002 Jul 17. [PubMed:12124386 ]
Anai M, Shojima N, Katagiri H, Ogihara T, Sakoda H, Onishi Y, Ono H, Fujishiro M, Fukushima Y, Horike N, Viana A, Kikuchi M, Noguchi N, Takahashi S, Takata K, Oka Y, Uchijima Y, Kurihara H, Asano T: A novel protein kinase B (PKB)/AKT-binding protein enhances PKB kinase activity and regulates DNA synthesis. J Biol Chem. 2005 May 6;280(18):18525-35. doi: 10.1074/jbc.M500586200. Epub 2005 Mar 7. [PubMed:15753085 ]
Fritzius T, Burkard G, Haas E, Heinrich J, Schweneker M, Bosse M, Zimmermann S, Frey AD, Caelers A, Bachmann AS, Moelling K: A WD-FYVE protein binds to the kinases Akt and PKCzeta/lambda. Biochem J. 2006 Oct 1;399(1):9-20. doi: 10.1042/BJ20060511. [PubMed:16792529 ]
Nawa M, Kanekura K, Hashimoto Y, Aiso S, Matsuoka M: A novel Akt/PKB-interacting protein promotes cell adhesion and inhibits familial amyotrophic lateral sclerosis-linked mutant SOD1-induced neuronal death via inhibition of PP2A-mediated dephosphorylation of Akt/PKB. Cell Signal. 2008 Mar;20(3):493-505. doi: 10.1016/j.cellsig.2007.11.004. Epub 2007 Nov 17. [PubMed:18160256 ]
Fritzius T, Moelling K: Akt- and Foxo1-interacting WD-repeat-FYVE protein promotes adipogenesis. EMBO J. 2008 May 7;27(9):1399-410. doi: 10.1038/emboj.2008.67. Epub 2008 Apr 3. [PubMed:18388859 ]
Kang ES, Han D, Park J, Kwak TK, Oh MA, Lee SA, Choi S, Park ZY, Kim Y, Lee JW: O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic beta cells. Exp Cell Res. 2008 Jul 1;314(11-12):2238-48. doi: 10.1016/j.yexcr.2008.04.014. Epub 2008 May 9. [PubMed:18570920 ]
Yang X, Ongusaha PP, Miles PD, Havstad JC, Zhang F, So WV, Kudlow JE, Michell RH, Olefsky JM, Field SJ, Evans RM: Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature. 2008 Feb 21;451(7181):964-9. doi: 10.1038/nature06668. [PubMed:18288188 ]
Kim JY, Duan X, Liu CY, Jang MH, Guo JU, Pow-anpongkul N, Kang E, Song H, Ming GL: DISC1 regulates new neuron development in the adult brain via modulation of AKT-mTOR signaling through KIAA1212. Neuron. 2009 Sep 24;63(6):761-73. doi: 10.1016/j.neuron.2009.08.008. [PubMed:19778506 ]
Rodgers JT, Haas W, Gygi SP, Puigserver P: Cdc2-like kinase 2 is an insulin-regulated suppressor of hepatic gluconeogenesis. Cell Metab. 2010 Jan;11(1):23-34. doi: 10.1016/j.cmet.2009.11.006. [PubMed:20074525 ]
Oh WJ, Wu CC, Kim SJ, Facchinetti V, Julien LA, Finlan M, Roux PP, Su B, Jacinto E: mTORC2 can associate with ribosomes to promote cotranslational phosphorylation and stability of nascent Akt polypeptide. EMBO J. 2010 Dec 1;29(23):3939-51. doi: 10.1038/emboj.2010.271. Epub 2010 Nov 2. [PubMed:21045808 ]
Walz HA, Shi X, Chouinard M, Bue CA, Navaroli DM, Hayakawa A, Zhou QL, Nadler J, Leonard DM, Corvera S: Isoform-specific regulation of Akt signaling by the endosomal protein WDFY2. J Biol Chem. 2010 May 7;285(19):14101-8. doi: 10.1074/jbc.M110.110536. Epub 2010 Feb 26. [PubMed:20189988 ]
Mahajan K, Coppola D, Challa S, Fang B, Chen YA, Zhu W, Lopez AS, Koomen J, Engelman RW, Rivera C, Muraoka-Cook RS, Cheng JQ, Schonbrunn E, Sebti SM, Earp HS, Mahajan NP: Ack1 mediated AKT/PKB tyrosine 176 phosphorylation regulates its activation. PLoS One. 2010 Mar 19;5(3):e9646. doi: 10.1371/journal.pone.0009646. [PubMed:20333297 ]
Arora D, Stopp S, Bohmer SA, Schons J, Godfrey R, Masson K, Razumovskaya E, Ronnstrand L, Tanzer S, Bauer R, Bohmer FD, Muller JP: Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling. J Biol Chem. 2011 Apr 1;286(13):10918-29. doi: 10.1074/jbc.M110.205021. Epub 2011 Jan 24. [PubMed:21262971 ]
Wakatsuki S, Saitoh F, Araki T: ZNRF1 promotes Wallerian degeneration by degrading AKT to induce GSK3B-dependent CRMP2 phosphorylation. Nat Cell Biol. 2011 Nov 6;13(12):1415-23. doi: 10.1038/ncb2373. [PubMed:22057101 ]
Nicholson KM, Anderson NG: The protein kinase B/Akt signalling pathway in human malignancy. Cell Signal. 2002 May;14(5):381-95. doi: 10.1016/s0898-6568(01)00271-6. [PubMed:11882383 ]
Hers I, Vincent EE, Tavare JM: Akt signalling in health and disease. Cell Signal. 2011 Oct;23(10):1515-27. doi: 10.1016/j.cellsig.2011.05.004. Epub 2011 May 17. [PubMed:21620960 ]
Heron-Milhavet L, Khouya N, Fernandez A, Lamb NJ: Akt1 and Akt2: differentiating the aktion. Histol Histopathol. 2011 May;26(5):651-62. doi: 10.14670/HH-26.651. [PubMed:21432781 ]
Nawa M, Matsuoka M: KCTD20, a relative of BTBD10, is a positive regulator of Akt. BMC Biochem. 2013 Oct 24;14:27. doi: 10.1186/1471-2091-14-27. [PubMed:24156551 ]
Yao Y, Suraokar M, Darnay BG, Hollier BG, Shaiken TE, Asano T, Chen CH, Chang BH, Lu Y, Mills GB, Sarbassov D, Mani SA, Abbruzzese JL, Reddy SA: BSTA promotes mTORC2-mediated phosphorylation of Akt1 to suppress expression of FoxC2 and stimulate adipocyte differentiation. Sci Signal. 2013 Jan 8;6(257):ra2. doi: 10.1126/scisignal.2003295. [PubMed:23300339 ]
Oh S, Paknejad N, Hite RK: Gating and selectivity mechanisms for the lysosomal K(+) channel TMEM175. Elife. 2020 Mar 31;9. pii: 53430. doi: 10.7554/eLife.53430. [PubMed:32228865 ]