RAC-beta serine/threonine-protein kinase Recombinant Protein | AKT2 recombinant protein

Recombinant Human RAC-beta serine/threonine-protein kinase

Cat. Num. AAA951263

• Gene Names: AKT2; PKBB; PRKBB; HIHGHH; PKBBETA; RAC-BETA
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: RAC-beta serine/threonine-protein kinase; Recombinant Human RAC-beta serine/threonine-protein kinase; Protein kinase Akt-2; Protein kinase B beta; PKB beta; RAC-PK-beta; AKT2 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 2-481aa; Full Length
• Sequence: NEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIRE
• Sequence Length: 438

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for AKT2 recombinant protein

AKT2 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 th, 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 mbers 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 PI3P-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 tpo 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 (PI3K) 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. One of the few specific substrates of AKT2 identified recently is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 ses also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. Phosphorylates CLK2 on 'Thr-343'.

Product Categories/Family for AKT2 recombinant protein

Apoptosis

References

Molecular cloning of a second form of rac protein kinase.Jones P.F., Jakubowicz T., Hemmings B.A.Cell Regul. 2:1001-1009(1991) AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas.Cheng J.Q., Godwin A.K., Bellacosa A., Taguchi T., Franke T.F., Hamilton T.C., Tsichlis P.N., Testa J.R.Proc. Natl. Acad. Sci. U.S.A. 89:9267-9271(1992) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The DNA sequence and biology of human chromosome 19.Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.Nature 428:529-535(2004) NIEHS SNPs programActivation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro comparison with protein kinase B alpha.Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., Alessi D.R.Biochem. J. 331:299-308(1998) The protooncogene TCL1 is an Akt kinase coactivator.Laine J., Kuenstle G., Obata T., Sha M., Noguchi M.Mol. Cell 6:395-407(2000) Activation of a GST-tagged AKT2/PKBbeta.Baer K., Lisinski I., Gompert M., Stuhlmann D., Schmolz K., Klein H.W., Al-Hasani H.Biochim. Biophys. Acta 1725:340-347(2005) Kinetic mechanism of AKT/PKB enzyme family.Zhang X., Zhang S., Yamane H., Wahl R., Ali A., Lofgren J.A., Kendall R.L.J. Biol. Chem. 281:13949-13956(2006) Akt2 is implicated in skeletal muscle differentiation and specifically binds Prohibitin2/REA.Heron-Milhavet L., Mamaeva D., Rochat A., Lamb N.J., Fernandez A.J. Cell. Physiol. 214:158-165(2008) 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) The E3 ligase TTC3 facilitates ubiquitination and degradation of phosphorylated Akt.Suizu F., Hiramuki Y., Okumura F., Matsuda M., Okumura A.J., Hirata N., Narita M., Kohno T., Yokota J., Bohgaki M., Obuse C., Hatakeyama S., Obata T., Noguchi M.Dev. Cell 17:800-810(2009) ClipR-59 interacts with Akt and regulates Akt cellular compartmentalization.Ding J., Du K.Mol. Cell. Biol. 29:1459-1471(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) The E3 ligase TRAF6 regulates Akt ubiquitination and activation.Yang W.-L., Wang J., Chan C.-H., Lee S.-W., Campos A.D., Lamothe B., Hur L., Grabiner B.C., Lin X., Darnay B.G., Lin H.-K.Science 325:1134-1138(2009) Akt2 and Akt3 play a pivotal role in malignant gliomas.Mure H., Matsuzaki K., Kitazato K.T., Mizobuchi Y., Kuwayama K., Kageji T., Nagahiro S.Neuro-oncol. 12:221-232(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Akt signalling in health and disease.Hers I., Vincent E.E., Tavare J.M.Cell. Signal. 23:1515-1527(2011) Akt1 and Akt2 differentiating the aktion.Heron-Milhavet L., Khouya N., Fernandez A., Lamb N.J.Histol. Histopathol. 26:651-662(2011) Ankrd2/ARPP is a novel Akt2 specific substrate and regulates myogenic differentiation upon cellular exposure to H(2) O(2) .Cenni V., Bavelloni A., Beretti F., Tagliavini F., Manzoli L., Lattanzi G., Maraldi N.M., Cocco L., Marmiroli S.Mol. Biol. Cell 22:2946-2956(2011) Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation.Yang J., Cron P., Thompson V., Good V.M., Hess D., Hemmings B.A., Barford D.Mol. Cell 9:1227-1240(2002) Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP.Yang J., Cron P., Good V.M., Thompson V., Hemmings B.A., Barford D.Nat. Struct. Biol. 9:940-944(2002) Crystal structure of an inactive Akt2 kinase domain.Huang X., Begley M., Morgenstern K.A., Gu Y., Rose P., Zhao H., Zhu X.Structure 11:21-30(2003) Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt) . Interaction with inositol phosphates.Auguin D., Barthe P., Auge-Senegas M.T., Stern M.H., Noguchi M., Roumestand C.J. Biomol. NMR 28:137-155(2004) A structural comparison of inhibitor binding to PKB, PKA and PKA-PKB chimera.Davies T.G., Verdonk M.L., Graham B., Saalau-Bethell S., Hamlett C.C., McHardy T., Collins I., Garrett M.D., Workman P., Woodhead S.J., Jhoti H., Barford D.J. Mol. Biol. 367:882-894(2007) Identification of 4-(2-(4-amino-1,2,5-oxadiazol-3-yl) -1-ethyl-7-{oxy}-1H-imidazopyridin-4-yl) -2-methyl-3-butyn-2-ol (GSK690693) , a novel inhibitor of AKT kinase.Heerding D.A., Rhodes N., Leber J.D., Clark T.J., Keenan R.M., Lafrance L.V., Li M., Safonov I.G., Takata D.T., Venslavsky J.W., Yamashita D.S., Choudhry A.E., Copeland R.A., Lai Z., Schaber M.D., Tummino P.J., Strum S.L., Wood E.R., Duckett D.R., Eberwein D., Knick V.B., Lansing T.J., McConnell R.T., Zhang S., Minthorn E.A., Concha N.O., Warren G.L., Kumar R.J. Med. Chem. 51:5663-5679(2008) Aminofurazans as potent inhibitors of AKT kinase.Rouse M.B., Seefeld M.A., Leber J.D., McNulty K.C., Sun L., Miller W.H., Zhang S., Minthorn E.A., Concha N.O., Choudhry A.E., Schaber M.D., Heerding D.A.Bioorg. Med. Chem. Lett. 19:1508-1511(2009) A family with severe insulin resistance and diabetes due to a mutation in AKT2.George S., Rochford J.J., Wolfrum C., Gray S.L., Schinner S., Wilson J.C., Soos M.A., Murgatroyd P.R., Williams R.M., Acerini C.L., Dunger D.B., Barford D., Umpleby A.M., Wareham N.J., Davies H.A., Schafer A.J., Stoffel M., O'Rahilly S., Barroso I.Science 304:1325-1328(2004) Patterns of somatic mutation in human cancer genomes.Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.Nature 446:153-158(2007) Postreceptor insulin resistance contributes to human dyslipidemia and hepatic steatosis.Semple R.K., Sleigh A., Murgatroyd P.R., Adams C.A., Bluck L., Jackson S., Vottero A., Kanabar D., Charlton-Menys V., Durrington P., Soos M.A., Carpenter T.A., Lomas D.J., Cochran E.K., Gorden P., O'Rahilly S., Savage D.B.J. Clin. Invest. 119:315-322(2009) An activating mutation of AKT2 and human hypoglycemia.Hussain K., Challis B., Rocha N., Payne F., Minic M., Thompson A., Daly A., Scott C., Harris J., Smillie B.J., Savage D.B., Ramaswami U., De Lonlay P., O'Rahilly S., Barroso I., Semple R.K.Science 334:474-474(2011) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 4502023
• NCBI GeneID: 208
• NCBI Accession #: NP_001617.1
• NCBI GenBank Nucleotide #: NM_001626.5
• UniProt Accession #: P31751; Q05BV0; Q0VAN0; Q0VAN1; Q68GC0; B2RBD8
• Molecular Weight: 71.6 kDa
• NCBI Official Full Name: RAC-beta serine/threonine-protein kinase isoform 1
• NCBI Official Synonym Full Names: v-akt murine thymoma viral oncogene homolog 2
• NCBI Official Symbol: AKT2
• NCBI Official Synonym Symbols: PKBB; PRKBB; HIHGHH; PKBBETA; RAC-BETA
• NCBI Protein Information: RAC-beta serine/threonine-protein kinase
• UniProt Protein Name: RAC-beta serine/threonine-protein kinase
• Protein Family: RAC-beta serine/threonine-protein kinase
• UniProt Gene Name: AKT2
• UniProt Synonym Gene Names: PKB beta
• UniProt Entry Name: AKT2_HUMAN

NCBI Description

This gene is a putative oncogene encoding a protein belonging to a subfamily of serine/threonine kinases containing SH2-like (Src homology 2-like) domains. The gene was shown to be amplified and overexpressed in 2 of 8 ovarian carcinoma cell lines and 2 of 15 primary ovarian tumors. Overexpression contributes to the malignant phenotype of a subset of human ductal pancreatic cancers. The encoded protein is a general protein kinase capable of phophorylating several known proteins. [provided by RefSeq, Jul 2008]

Uniprot Description

AKT2 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 PI3P-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 (PI3K) 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.