AKT1 – Wikipédia, a enciclopédia livre

AKT1
Estruturas disponíveis
PDB	Pesquisa Human UniProt: PDBe RCSB
Lista de códigos id do PDB
	1H10, 1UNP, 1UNQ, 1UNR, 2UVM, 2UZR, 2UZS, 3CQU, 3CQW, 3MV5, 3MVH, 3O96, 3OCB, 3OW4, 3QKK, 3QKL, 3QKM, 4EJN, 4EKK, 4EKL, 4GV1, 5KCV
Identificadores
Nomes alternativos	AKT1
IDs externos	OMIM: 164730 HomoloGene: 3785 GeneCards: AKT1
Doenças Geneticamente Relacionadas
	cancro colorretal, síndrome de Proteus, cancro da mama, Síndrome de Cowden
Ontologia genética
Função molecular	• GTPase activating protein binding; • kinase activity; • nitric-oxide synthase regulator activity; • ATP binding; • protein kinase activity; • protein phosphatase 2A binding; • enzyme binding; • phosphatidylinositol-3,4,5-trisphosphate binding; • transferase activity; • 14-3-3 protein binding; • GO:0001948, GO:0016582 ligação a proteínas plasmáticas; • protein serine/threonine/tyrosine kinase activity; • protein kinase binding; • protein kinase C binding; • nucleotide binding; • phosphatidylinositol-3,4-bisphosphate binding; • identical protein binding; • protein serine/threonine kinase activity; • protein homodimerization activity; • calmodulin binding;
Componente celular	• citoplasma; • citosol; • membrane; • cell-cell junction; • mitocôndria; • núcleo celular; • ciliary basal body; • microtubule cytoskeleton; • membrana plasmática; • fuso mitótico; • cariolinfa; • vesícula; • postsynapse; • GO:0009327 complexo macromolecular;
Processo biológico	• germ cell development; • positive regulation of glucose import; • cellular response to nerve growth factor stimulus; • positive regulation of protein phosphorylation; • positive regulation of lipid biosynthetic process; • regulation of neuron projection development; • activation-induced cell death of T cells; • response to heat; • regulation of cell cycle checkpoint; • response to organic substance; • response to insulin-like growth factor stimulus; • positive regulation of endodeoxyribonuclease activity; • cellular response to DNA damage stimulus; • regulation of protein localization; • platelet activation; • protein phosphorylation; • cellular response to mechanical stimulus; • negative regulation of long-chain fatty acid import across plasma membrane; • negative regulation of fatty acid beta-oxidation; • cell projection organization; • cellular response to granulocyte macrophage colony-stimulating factor stimulus; • positive regulation of blood vessel endothelial cell migration; • glucose metabolic process; • glycogen metabolic process; • regulation of glycogen biosynthetic process; • glycogen cell differentiation involved in embryonic placenta development; • Proliferação celular; • negative regulation of autophagy; • cellular response to hypoxia; • negative regulation of cell size; • endocrine pancreas development; • GO:0006859 carbohydrate transport; • negative regulation of proteolysis; • insulin-like growth factor receptor signaling pathway; • GO:0051247, GO:0051200 positive regulation of protein metabolic process; • positive regulation of glycogen biosynthetic process; • glucose homeostasis; • labyrinthine layer blood vessel development; • GO:0001306 response to oxidative stress; • negative regulation of gene expression; • positive regulation of peptidyl-serine phosphorylation; • cellular response to prostaglandin E stimulus; • positive regulation of cell growth; • positive regulation of nitric-oxide synthase activity; • maternal placenta development; • regulation of myelination; • protein ubiquitination; • positive regulation of vasoconstriction; • hyaluronan metabolic process; • spinal cord development; • cellular response to insulin stimulus; • cellular response to decreased oxygen levels; • protein autophosphorylation; • inflammatory response; • positive regulation of fat cell differentiation; • positive regulation of proteasomal ubiquitin-dependent protein catabolic process; • negative regulation of neuron death; • G protein-coupled receptor signaling pathway; • diferenciação celular; • cellular response to peptide; • negative regulation of protein kinase activity; • fosforilação; • regulation of mRNA stability; • negative regulation of release of cytochrome c from mitochondria; • execution phase of apoptosis; • GO:1904579 cellular response to organic cyclic compound; • positive regulation of DNA-binding transcription factor activity; • positive regulation of glucose metabolic process; • nervous system development; • response to fluid shear stress; • maintenance of protein location in mitochondrion; • GO:0044257 Oxidação de aminoácidos; • negative regulation of protein kinase activity by protein phosphorylation; • osteoblast differentiation; • response to UV-A; • response to hormone; • peptidyl-threonine phosphorylation; • lipopolysaccharide-mediated signaling pathway; • positive regulation of protein localization to nucleus; • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; • GO:0007243 intracellular signal transduction; • regulation of cell migration; • peripheral nervous system myelin maintenance; • nitric oxide biosynthetic process; • positive regulation of endothelial cell proliferation; • síntese proteica; • positive regulation of nitric oxide biosynthetic process; • cellular response to growth factor stimulus; • T cell costimulation; • regulation of nitric-oxide synthase activity; • GO:0010260 envelhecimento; • mammary gland epithelial cell differentiation; • cellular response to epidermal growth factor stimulus; • multicellular organism development; • negative regulation of JNK cascade; • glycogen biosynthetic process; • establishment of protein localization to mitochondrion; • apoptotic mitochondrial changes; • GO:0035404 peptidyl-serine phosphorylation; • GO:0061423 positive regulation of sodium ion transport; • response to growth hormone; • positive regulation of apoptotic process; • response to food; • cellular response to vascular endothelial growth factor stimulus; • striated muscle cell differentiation; • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; • positive regulation of fibroblast migration; • regulation of translation; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • GO:0072468 transdução de sinal; • negative regulation of endopeptidase activity; • GO:0097285 apoptose; • positive regulation of epidermal growth factor receptor signaling pathway; • interleukin-18-mediated signaling pathway; • GO:1901047 insulin receptor signaling pathway; • positive regulation of smooth muscle cell proliferation; • regulation of signal transduction by p53 class mediator; • negative regulation of macroautophagy; • TOR signaling; • anoikis; • positive regulation of organ growth; • I-kappaB kinase/NF-kappaB signaling; • phosphatidylinositol 3-kinase signaling; • GO:0072353 cellular response to reactive oxygen species; • NIK/NF-kappaB signaling; • GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated; • cellular response to cadmium ion; • positive regulation of I-kappaB phosphorylation; • epidermal growth factor receptor signaling pathway; • positive regulation of cell population proliferation; • positive regulation of mitochondrial membrane potential; • regulation of apoptotic process; • negative regulation of apoptotic process; • positive regulation of protein localization to plasma membrane; • carbohydrate metabolic process; • activation of protein kinase B activity; • protein kinase B signaling; • negative regulation of protein kinase B signaling; • potencial pós-sináptico excitatório; • cellular response to tumor necrosis factor; • cell migration involved in sprouting angiogenesis; • GO:1901313 positive regulation of gene expression; • cytokine-mediated signaling pathway; • negative regulation of protein ubiquitination; • negative regulation of protein binding; • positive regulation of cyclin-dependent protein serine/threonine kinase activity; • negative regulation of Notch signaling pathway; • negative regulation of protein serine/threonine kinase activity; • cellular response to oxidised low-density lipoprotein particle stimulus; • positive regulation of G1/S transition of mitotic cell cycle; • negative regulation of leukocyte cell-cell adhesion; • positive regulation of protein localization to cell surface; • negative regulation of lymphocyte migration; • protein import into nucleus;
	Sources:Amigo / QuickGO
Padrão de expressão RNA
	Mais dados de referência de expressão
Ortólogos
	207
	n/a
	ENSG00000142208
	n/a
	P31749
	n/a
NM_001014431; NM_001014432; NM_005163; NM_001382430; NM_001382431;
	NM_001382432; NM_001382433
	n/a
NP_001014431; NP_001014432; NP_005154; NP_001369359; NP_001369360;
	NP_001369361; NP_001369362
	n/a
	Wikidata
Ver/Editar Humano

AKT1, do inglês V-akt murine thymoma viral oncogene homolog 1, é uma enzima que em humanos é codificada pelo gene AKT1.

A proteína quinase serina/treonina codificada pelo gene AKT1 está cataliticamente inactiva em fibroblastos privados de soro e em fibroblastos imortalizados. AKT1 e o ATK2 são activados por factores de crescimento derivados de plaquetas. A activação é rápida e específica, não sendo anulada por mutações no domínio de homologia a plecstrina da AKT1. Foi demonstrado que a activação ocorre através do fosfoinositol 3-quinase.

No sistema nervoso em desenvolvimento, o AKT é um mediador crítico da sobrevivência neuronal induzida por factores de crescimento. Os factores de crescimento podem suprimir a apoptose de uma maneira independente de transcrição, por activação da quinase serina/treonina AKT1, que depois fosforila e inactiva componentes da apoptose.

Múltiplos variantes de transcriptos, que sofreram splicing alternativo, foram encontrados para este gene.^[3]

Ratos que não possuem AKT1 mostram uma redução em 25% da massa corporal, indicando que este gene é fundamental para que os sinais dos factores de crescimento sejam transmitidos, mais provavelmente através do receptor IGF1. Os ratos que não possuem AKT1 são também resistentes ao cancro: apresentam atrasos consideráveis no crescimento de tumores iniciados, por exemplo pelo oncogene NEU.

Interações

AKT1 mostrou interação com Phosphoinositide-dependent kinase-1,^[4]^[5] Keratin 10,^[6] Integrin-linked kinase,^[4]^[5]^[7] TSC2,^[8]^[9] GAB2,^[10] TRIB3,^[11] NPM1,^[12] BRCA1,^[13]^[14] BRAF,^[15] C-Raf,^[16] MAPK14,^[17] MARK2,^[18] MAP2K4,^[19] MTCP1,^[20]^[21] TCL1A,^[20]^[21]^[22] Nerve Growth factor IB,^[23] MAPKAPK2,^[17] PRKCQ,^[24] Androgen receptor,^[25] Heat shock protein 90kDa alpha (cytosolic), member A1,^[26]^[27]^[28] Plexin A1,^[29] MAP3K11,^[30] TSC1,^[8]^[9] MAP3K8,^[31] Mammalian target of rapamycin,^[32]^[33]^[34] PKN2,^[35] AKTIP,^[36] YWHAZ,^[37] CHUK^[38]^[39] e CDKN1B.^[40]

Referências

↑ «Doenças geneticamente associadas a AKT1 ver/editar referências no wikidata»
↑ «Human PubMed Reference:»
↑ «Entrez Gene: AKT1 v-akt murine thymoma viral oncogene homolog 1»
↑ ^a ^b Barry, Fiona A; Gibbins Jonathan M (Abril de 2002). «Protein kinase B is regulated in platelets by the collagen receptor glycoprotein VI». United States. J. Biol. Chem. 277 (15): 12874–8. ISSN 0021-9258. PMID 11825911. doi:10.1074/jbc.M200482200
↑ ^a ^b Persad, S; Attwell S, Gray V, Mawji N, Deng J T, Leung D, Yan J, Sanghera J, Walsh M P, Dedhar S (Julho de 2001). «Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343». United States. J. Biol. Chem. 276 (29): 27462–9. ISSN 0021-9258. PMID 11313365. doi:10.1074/jbc.M102940200
↑ Paramio, J M; Segrelles C, Ruiz S, Jorcano J L (Novembro de 2001). «Inhibition of protein kinase B (PKB) and PKCzeta mediates keratin K10-induced cell cycle arrest». United States. Mol. Cell. Biol. 21 (21): 7449–59. ISSN 0270-7306. PMC 99917. PMID 11585925. doi:10.1128/MCB.21.21.7449-7459.2001
↑ Delcommenne, M; Tan C, Gray V, Rue L, Woodgett J, Dedhar S (Setembro de 1998). «Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase». UNITED STATES. Proc. Natl. Acad. Sci. U.S.A. 95 (19): 11211–6. ISSN 0027-8424. PMC 21621. PMID 9736715. doi:10.1073/pnas.95.19.11211
↑ ^a ^b Dan, Han C; Sun Mei, Yang Lin, Feldman Richard I, Sui Xue-Mei, Ou Chien Chen, Nellist Mark, Yeung Raymond S, Halley Dicky J J, Nicosia Santo V, Pledger Warren J, Cheng Jin Q (Setembro de 2002). «Phosphatidylinositol 3-kinase/Akt pathway regulates tuberous sclerosis tumor suppressor complex by phosphorylation of tuberin». United States. J. Biol. Chem. 277 (38): 35364–70. ISSN 0021-9258. PMID 12167664. doi:10.1074/jbc.M205838200
↑ ^a ^b Roux, Philippe P; Ballif Bryan A, Anjum Rana, Gygi Steven P, Blenis John (Setembro de 2004). «Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase». United States. Proc. Natl. Acad. Sci. U.S.A. 101 (37): 13489–94. ISSN 0027-8424. PMC 518784. PMID 15342917. doi:10.1073/pnas.0405659101
↑ Lynch, Danielle K; Daly Roger J (Janeiro de 2002). «PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2». England. EMBO J. 21 (1-2): 72–82. ISSN 0261-4189. PMC 125816. PMID 11782427. doi:10.1093/emboj/21.1.72
↑ Du, Keyong; Herzig Stephan, Kulkarni Rohit N, Montminy Marc (Junho de 2003). «TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver». United States. Science. 300 (5625): 1574–7. PMID 12791994. doi:10.1126/science.1079817
↑ Lee, Sang Bae; Xuan Nguyen Truong L, Choi Joung Woo, Lee Kyung-Hoon, Cho Sung-Woo, Liu Zhixue, Ye Keqiang, Bae Sun Sik, Ahn Jee-Yin (Outubro de 2008). «Nuclear Akt interacts with B23/NPM and protects it from proteolytic cleavage, enhancing cell survival». United States. Proc. Natl. Acad. Sci. U.S.A. 105 (43): 16584–9. PMC 2569968. PMID 18931307. doi:10.1073/pnas.0807668105
↑ Altiok, S; Batt D, Altiok N, Papautsky A, Downward J, Roberts T M, Avraham H (Novembro de 1999). «Heregulin induces phosphorylation of BRCA1 through phosphatidylinositol 3-Kinase/AKT in breast cancer cells». UNITED STATES. J. Biol. Chem. 274 (45): 32274–8. ISSN 0021-9258. PMID 10542266. doi:10.1074/jbc.274.45.32274
↑ Xiang, Tao; Ohashi Amiko, Huang Yuping, Pandita Tej K, Ludwig Thomas, Powell Simon N, Yang Qin (Dezembro de 2008). «Negative Regulation of AKT Activation by BRCA1». United States. Cancer Res. 68 (24): 10040–4. PMC 2605656. PMID 19074868. doi:10.1158/0008-5472.CAN-08-3009
↑ Guan, K L; Figueroa C, Brtva T R, Zhu T, Taylor J, Barber T D, Vojtek A B (Setembro de 2000). «Negative regulation of the serine/threonine kinase B-Raf by Akt». UNITED STATES. J. Biol. Chem. 275 (35): 27354–9. ISSN 0021-9258. PMID 10869359. doi:10.1074/jbc.M004371200
↑ Zimmermann, S; Moelling K (Novembro de 1999). «Phosphorylation and regulation of Raf by Akt (protein kinase B)». UNITED STATES. Science. 286 (5445): 1741–4. ISSN 0036-8075. PMID 10576742. doi:10.1126/science.286.5445.1741
↑ ^a ^b Rane, M J; Coxon P Y, Powell D W, Webster R, Klein J B, Pierce W, Ping P, McLeish K R (Fevereiro de 2001). «p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils». United States. J. Biol. Chem. 276 (5): 3517–23. ISSN 0021-9258. PMID 11042204. doi:10.1074/jbc.M005953200
↑ Dickey, Chad A; Koren John, Zhang Yong-Jie, Xu Ya-Fei, Jinwal Umesh K, Birnbaum Morris J, Monks Bobby, Sun Mei, Cheng Jin Q, Patterson Cam, Bailey Rachel M, Dunmore Judith, Soresh Sareh, Leon Carlos, Morgan Dave, Petrucelli Leonard (Março de 2008). «Akt and CHIP coregulate tau degradation through coordinated interactions». United States. Proc. Natl. Acad. Sci. U.S.A. 105 (9): 3622–7. PMC 2265134. PMID 18292230. doi:10.1073/pnas.0709180105
↑ Park, Hee-Sae; Kim Mi-Sung, Huh Sung-Ho, Park Jihyun, Chung Jongkyeong, Kang Sang Sun, Choi Eui-Ju (Janeiro de 2002). «Akt (protein kinase B) negatively regulates SEK1 by means of protein phosphorylation». United States. J. Biol. Chem. 277 (4): 2573–8. ISSN 0021-9258. PMID 11707464. doi:10.1074/jbc.M110299200
↑ ^a ^b Laine, Jarmo; Künstle Gerald, Obata Toshiyuki, Noguchi Masayuki (Fevereiro de 2002). «Differential regulation of Akt kinase isoforms by the members of the TCL1 oncogene family». United States. J. Biol. Chem. 277 (5): 3743–51. ISSN 0021-9258. PMID 11707444. doi:10.1074/jbc.M107069200
↑ ^a ^b Laine, J; Künstle G, Obata T, Sha M, Noguchi M (Agosto de 2000). «The protooncogene TCL1 is an Akt kinase coactivator». UNITED STATES. Mol. Cell. 6 (2): 395–407. ISSN 1097-2765. PMID 10983986. doi:10.1016/S1097-2765(00)00039-3
↑ French, Samuel W; Shen Rhine R, Koh Patricia J, Malone Cindy S, Mallick Parag, Teitell Michael A (Maio de 2002). «A modeled hydrophobic domain on the TCL1 oncoprotein mediates association with AKT at the cytoplasmic membrane». United States. Biochemistry. 41 (20): 6376–82. ISSN 0006-2960. PMID 12009899. doi:10.1021/bi016068o
↑ Pekarsky, Y; Hallas C, Palamarchuk A, Koval A, Bullrich F, Hirata Y, Bichi R, Letofsky J, Croce C M (Março de 2001). «Akt phosphorylates and regulates the orphan nuclear receptor Nur77». United States. Proc. Natl. Acad. Sci. U.S.A. 98 (7): 3690–4. ISSN 0027-8424. PMC 31113. PMID 11274386. doi:10.1073/pnas.051003198
↑ Bauer, B; Krumböck N, Fresser F, Hochholdinger F, Spitaler M, Simm A, Uberall F, Schraven B, Baier G (Agosto de 2001). «Complex formation and cooperation of protein kinase C theta and Akt1/protein kinase B alpha in the NF-kappa B transactivation cascade in Jurkat T cells». United States. J. Biol. Chem. 276 (34): 31627–34. ISSN 0021-9258. PMID 11410591. doi:10.1074/jbc.M103098200
↑ Lin, H K; Yeh S, Kang H Y, Chang C (Junho de 2001). «Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor». United States. Proc. Natl. Acad. Sci. U.S.A. 98 (13): 7200–5. ISSN 0027-8424. PMC 34646. PMID 11404460. doi:10.1073/pnas.121173298
↑ Haendeler, Judith; Hoffmann Jörg, Rahman Sandy, Zeiher Andreas M, Dimmeler Stefanie (Fevereiro de 2003). «Regulation of telomerase activity and anti-apoptotic function by protein-protein interaction and phosphorylation». Netherlands. FEBS Lett. 536 (1-3): 180–6. ISSN 0014-5793. PMID 12586360. doi:10.1016/S0014-5793(03)00058-9
↑ Kawauchi, Kiyotaka; Ihjima Kimiko, Yamada Osamu (Maio de 2005). «IL-2 increases human telomerase reverse transcriptase activity transcriptionally and posttranslationally through phosphatidylinositol 3'-kinase/Akt, heat shock protein 90, and mammalian target of rapamycin in transformed NK cells». United States. J. Immunol. 174 (9): 5261–9. ISSN 0022-1767. PMID 15843522
↑ Sato, S; Fujita N, Tsuruo T (Setembro de 2000). «Modulation of Akt kinase activity by binding to Hsp90». UNITED STATES. Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10832–7. ISSN 0027-8424. PMC 27109. PMID 10995457. doi:10.1073/pnas.170276797
↑ Turner, Laura J; Nicholls Sarah, Hall Alan (Agosto de 2004). «The activity of the plexin-A1 receptor is regulated by Rac». United States. J. Biol. Chem. 279 (32): 33199–205. ISSN 0021-9258. PMID 15187088. doi:10.1074/jbc.M402943200
↑ Barthwal, Manoj K; Sathyanarayana Pradeep, Kundu Chanakya N, Rana Basabi, Pradeep Anamika, Sharma Chandan, Woodgett James R, Rana Ajay (Fevereiro de 2003). «Negative regulation of mixed lineage kinase 3 by protein kinase B/AKT leads to cell survival». United States. J. Biol. Chem. 278 (6): 3897–902. ISSN 0021-9258. PMID 12458207. doi:10.1074/jbc.M211598200
↑ Kane, Lawrence P; Mollenauer Marianne N, Xu Zheng, Turck Christoph W, Weiss Arthur (Agosto de 2002). «Akt-dependent phosphorylation specifically regulates Cot induction of NF-kappa B-dependent transcription». United States. Mol. Cell. Biol. 22 (16): 5962–74. ISSN 0270-7306. PMC 133991. PMID 12138205. doi:10.1128/MCB.22.16.5962-5974.2002
↑ Sarbassov, D D; Guertin David A, Ali Siraj M, Sabatini David M (Fevereiro de 2005). «Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex». United States. Science. 307 (5712): 1098–101. PMID 15718470. doi:10.1126/science.1106148
↑ Sekulić, A; Hudson C C, Homme J L, Yin P, Otterness D M, Karnitz L M, Abraham R T (Julho de 2000). «A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells». UNITED STATES. Cancer Res. 60 (13): 3504–13. ISSN 0008-5472. PMID 10910062
↑ Cheng, Susan W Y; Fryer Lee G D, Carling David, Shepherd Peter R (Abril de 2004). «Thr2446 is a novel mammalian target of rapamycin (mTOR) phosphorylation site regulated by nutrient status». United States. J. Biol. Chem. 279 (16): 15719–22. ISSN 0021-9258. PMID 14970221. doi:10.1074/jbc.C300534200
↑ Koh, H; Lee K H, Kim D, Kim S, Kim J W, Chung J (Novembro de 2000). «Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage». UNITED STATES. J. Biol. Chem. 275 (44): 34451–8. ISSN 0021-9258. PMID 10926925. doi:10.1074/jbc.M001753200
↑ Remy, Ingrid; Michnick Stephen W (Fevereiro de 2004). «Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt». United States. Mol. Cell. Biol. 24 (4): 1493–504. ISSN 0270-7306. PMC 344167. PMID 14749367. doi:10.1128/MCB.24.4.1493-1504.2004
↑ Powell, David W; Rane Madhavi J, Chen Qingdan, Singh Saurabh, McLeish Kenneth R (Junho de 2002). «Identification of 14-3-3zeta as a protein kinase B/Akt substrate». United States. J. Biol. Chem. 277 (24): 21639–42. ISSN 0021-9258. PMID 11956222. doi:10.1074/jbc.M203167200
↑ Ozes, O N; Mayo L D, Gustin J A, Pfeffer S R, Pfeffer L M, Donner D B (Setembro de 1999). «NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase». ENGLAND. Nature. 401 (6748): 82–5. ISSN 0028-0836. PMID 10485710. doi:10.1038/43466
↑ Romashkova, J A; Makarov S S (Setembro de 1999). «NF-kappaB is a target of AKT in anti-apoptotic PDGF signalling». ENGLAND. Nature. 401 (6748): 86–90. ISSN 0028-0836. PMID 10485711. doi:10.1038/43474
↑ Fujita, Naoya; Sato Saori, Katayama Kazuhiro, Tsuruo Takashi (Agosto de 2002). «Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization». United States. J. Biol. Chem. 277 (32): 28706–13. ISSN 0021-9258. PMID 12042314. doi:10.1074/jbc.M203668200

Leitura adicional

Hemmings BA (1997). «Akt signaling: linking membrane events to life and death decisions.». Science. 275 (5300): 628-30. PMID 9019819
Vanhaesebroeck B, Alessi DR (2000). «The PI3K-PDK1 connection: more than just a road to PKB.». Biochem. J. 346 Pt 3: 561-76. PMID 10698680
Chan TO, Rittenhouse SE, Tsichlis PN (2000). «AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation.». Annu. Rev. Biochem. 68: 965-1014. PMID 10872470. doi:10.1146/annurev.biochem.68.1.965
Pekarsky Y, Hallas C, Croce CM (2001). «Molecular basis of mature T-cell leukemia.». JAMA. 286 (18): 2308-14. PMID 11710897
Dickson LM, Rhodes CJ (2004). «Pancreatic beta-cell growth and survival in the onset of type 2 diabetes: a role for protein kinase B in the Akt?». Am. J. Physiol. Endocrinol. Metab. 287 (2): E192-8. PMID 15271644. doi:10.1152/ajpendo.00031.2004
Manning BD (2004). «Balancing Akt with S6K: implications for both metabolic diseases and tumorigenesis.». J. Cell Biol. 167 (3): 399-403. PMID 15533996. doi:10.1083/jcb.200408161
Shinohara M, Chung YJ, Saji M, Ringel MD (2007). «AKT in thyroid tumorigenesis and progression.». Endocrinology. 148 (3): 942-7. PMID 16946008. doi:10.1210/en.2006-0937

[1] «Doenças geneticamente associadas a AKT1 ver/editar referências no wikidata»

[2] «Human PubMed Reference:»

[3] «Entrez Gene: AKT1 v-akt murine thymoma viral oncogene homolog 1»

[pmid11825911-4] Barry, Fiona A; Gibbins Jonathan M (Abril de 2002). «Protein kinase B is regulated in platelets by the collagen receptor glycoprotein VI». United States. J. Biol. Chem. 277 (15): 12874–8. ISSN 0021-9258. PMID 11825911. doi:10.1074/jbc.M200482200

[pmid11313365-5] Persad, S; Attwell S, Gray V, Mawji N, Deng J T, Leung D, Yan J, Sanghera J, Walsh M P, Dedhar S (Julho de 2001). «Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343». United States. J. Biol. Chem. 276 (29): 27462–9. ISSN 0021-9258. PMID 11313365. doi:10.1074/jbc.M102940200

[pmid11585925-6] Paramio, J M; Segrelles C, Ruiz S, Jorcano J L (Novembro de 2001). «Inhibition of protein kinase B (PKB) and PKCzeta mediates keratin K10-induced cell cycle arrest». United States. Mol. Cell. Biol. 21 (21): 7449–59. ISSN 0270-7306. PMC 99917. PMID 11585925. doi:10.1128/MCB.21.21.7449-7459.2001

[pmid9736715-7] Delcommenne, M; Tan C, Gray V, Rue L, Woodgett J, Dedhar S (Setembro de 1998). «Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase». UNITED STATES. Proc. Natl. Acad. Sci. U.S.A. 95 (19): 11211–6. ISSN 0027-8424. PMC 21621. PMID 9736715. doi:10.1073/pnas.95.19.11211

[pmid12167664-8] Dan, Han C; Sun Mei, Yang Lin, Feldman Richard I, Sui Xue-Mei, Ou Chien Chen, Nellist Mark, Yeung Raymond S, Halley Dicky J J, Nicosia Santo V, Pledger Warren J, Cheng Jin Q (Setembro de 2002). «Phosphatidylinositol 3-kinase/Akt pathway regulates tuberous sclerosis tumor suppressor complex by phosphorylation of tuberin». United States. J. Biol. Chem. 277 (38): 35364–70. ISSN 0021-9258. PMID 12167664. doi:10.1074/jbc.M205838200

[pmid15342917-9] Roux, Philippe P; Ballif Bryan A, Anjum Rana, Gygi Steven P, Blenis John (Setembro de 2004). «Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase». United States. Proc. Natl. Acad. Sci. U.S.A. 101 (37): 13489–94. ISSN 0027-8424. PMC 518784. PMID 15342917. doi:10.1073/pnas.0405659101

[pmid11782427-10] Lynch, Danielle K; Daly Roger J (Janeiro de 2002). «PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2». England. EMBO J. 21 (1-2): 72–82. ISSN 0261-4189. PMC 125816. PMID 11782427. doi:10.1093/emboj/21.1.72

[pmid12791994-11] Du, Keyong; Herzig Stephan, Kulkarni Rohit N, Montminy Marc (Junho de 2003). «TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver». United States. Science. 300 (5625): 1574–7. PMID 12791994. doi:10.1126/science.1079817

[pmid18931307-12] Lee, Sang Bae; Xuan Nguyen Truong L, Choi Joung Woo, Lee Kyung-Hoon, Cho Sung-Woo, Liu Zhixue, Ye Keqiang, Bae Sun Sik, Ahn Jee-Yin (Outubro de 2008). «Nuclear Akt interacts with B23/NPM and protects it from proteolytic cleavage, enhancing cell survival». United States. Proc. Natl. Acad. Sci. U.S.A. 105 (43): 16584–9. PMC 2569968. PMID 18931307. doi:10.1073/pnas.0807668105

[pmid10542266-13] Altiok, S; Batt D, Altiok N, Papautsky A, Downward J, Roberts T M, Avraham H (Novembro de 1999). «Heregulin induces phosphorylation of BRCA1 through phosphatidylinositol 3-Kinase/AKT in breast cancer cells». UNITED STATES. J. Biol. Chem. 274 (45): 32274–8. ISSN 0021-9258. PMID 10542266. doi:10.1074/jbc.274.45.32274

[pmid19074868-14] Xiang, Tao; Ohashi Amiko, Huang Yuping, Pandita Tej K, Ludwig Thomas, Powell Simon N, Yang Qin (Dezembro de 2008). «Negative Regulation of AKT Activation by BRCA1». United States. Cancer Res. 68 (24): 10040–4. PMC 2605656. PMID 19074868. doi:10.1158/0008-5472.CAN-08-3009

[pmid10869359-15] Guan, K L; Figueroa C, Brtva T R, Zhu T, Taylor J, Barber T D, Vojtek A B (Setembro de 2000). «Negative regulation of the serine/threonine kinase B-Raf by Akt». UNITED STATES. J. Biol. Chem. 275 (35): 27354–9. ISSN 0021-9258. PMID 10869359. doi:10.1074/jbc.M004371200

[pmid10576742-16] Zimmermann, S; Moelling K (Novembro de 1999). «Phosphorylation and regulation of Raf by Akt (protein kinase B)». UNITED STATES. Science. 286 (5445): 1741–4. ISSN 0036-8075. PMID 10576742. doi:10.1126/science.286.5445.1741

[pmid11042204-17] Rane, M J; Coxon P Y, Powell D W, Webster R, Klein J B, Pierce W, Ping P, McLeish K R (Fevereiro de 2001). «p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils». United States. J. Biol. Chem. 276 (5): 3517–23. ISSN 0021-9258. PMID 11042204. doi:10.1074/jbc.M005953200

[pmid18292230-18] Dickey, Chad A; Koren John, Zhang Yong-Jie, Xu Ya-Fei, Jinwal Umesh K, Birnbaum Morris J, Monks Bobby, Sun Mei, Cheng Jin Q, Patterson Cam, Bailey Rachel M, Dunmore Judith, Soresh Sareh, Leon Carlos, Morgan Dave, Petrucelli Leonard (Março de 2008). «Akt and CHIP coregulate tau degradation through coordinated interactions». United States. Proc. Natl. Acad. Sci. U.S.A. 105 (9): 3622–7. PMC 2265134. PMID 18292230. doi:10.1073/pnas.0709180105

[pmid11707464-19] Park, Hee-Sae; Kim Mi-Sung, Huh Sung-Ho, Park Jihyun, Chung Jongkyeong, Kang Sang Sun, Choi Eui-Ju (Janeiro de 2002). «Akt (protein kinase B) negatively regulates SEK1 by means of protein phosphorylation». United States. J. Biol. Chem. 277 (4): 2573–8. ISSN 0021-9258. PMID 11707464. doi:10.1074/jbc.M110299200

[pmid11707444-20] Laine, Jarmo; Künstle Gerald, Obata Toshiyuki, Noguchi Masayuki (Fevereiro de 2002). «Differential regulation of Akt kinase isoforms by the members of the TCL1 oncogene family». United States. J. Biol. Chem. 277 (5): 3743–51. ISSN 0021-9258. PMID 11707444. doi:10.1074/jbc.M107069200

[pmid10983986-21] Laine, J; Künstle G, Obata T, Sha M, Noguchi M (Agosto de 2000). «The protooncogene TCL1 is an Akt kinase coactivator». UNITED STATES. Mol. Cell. 6 (2): 395–407. ISSN 1097-2765. PMID 10983986. doi:10.1016/S1097-2765(00)00039-3

[pmid12009899-22] French, Samuel W; Shen Rhine R, Koh Patricia J, Malone Cindy S, Mallick Parag, Teitell Michael A (Maio de 2002). «A modeled hydrophobic domain on the TCL1 oncoprotein mediates association with AKT at the cytoplasmic membrane». United States. Biochemistry. 41 (20): 6376–82. ISSN 0006-2960. PMID 12009899. doi:10.1021/bi016068o

[pmid11274386-23] Pekarsky, Y; Hallas C, Palamarchuk A, Koval A, Bullrich F, Hirata Y, Bichi R, Letofsky J, Croce C M (Março de 2001). «Akt phosphorylates and regulates the orphan nuclear receptor Nur77». United States. Proc. Natl. Acad. Sci. U.S.A. 98 (7): 3690–4. ISSN 0027-8424. PMC 31113. PMID 11274386. doi:10.1073/pnas.051003198

[pmid11410591-24] Bauer, B; Krumböck N, Fresser F, Hochholdinger F, Spitaler M, Simm A, Uberall F, Schraven B, Baier G (Agosto de 2001). «Complex formation and cooperation of protein kinase C theta and Akt1/protein kinase B alpha in the NF-kappa B transactivation cascade in Jurkat T cells». United States. J. Biol. Chem. 276 (34): 31627–34. ISSN 0021-9258. PMID 11410591. doi:10.1074/jbc.M103098200

[pmid11404460-25] Lin, H K; Yeh S, Kang H Y, Chang C (Junho de 2001). «Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor». United States. Proc. Natl. Acad. Sci. U.S.A. 98 (13): 7200–5. ISSN 0027-8424. PMC 34646. PMID 11404460. doi:10.1073/pnas.121173298

[pmid12586360-26] Haendeler, Judith; Hoffmann Jörg, Rahman Sandy, Zeiher Andreas M, Dimmeler Stefanie (Fevereiro de 2003). «Regulation of telomerase activity and anti-apoptotic function by protein-protein interaction and phosphorylation». Netherlands. FEBS Lett. 536 (1-3): 180–6. ISSN 0014-5793. PMID 12586360. doi:10.1016/S0014-5793(03)00058-9

[pmid15843522-27] Kawauchi, Kiyotaka; Ihjima Kimiko, Yamada Osamu (Maio de 2005). «IL-2 increases human telomerase reverse transcriptase activity transcriptionally and posttranslationally through phosphatidylinositol 3'-kinase/Akt, heat shock protein 90, and mammalian target of rapamycin in transformed NK cells». United States. J. Immunol. 174 (9): 5261–9. ISSN 0022-1767. PMID 15843522

[pmid10995457-28] Sato, S; Fujita N, Tsuruo T (Setembro de 2000). «Modulation of Akt kinase activity by binding to Hsp90». UNITED STATES. Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10832–7. ISSN 0027-8424. PMC 27109. PMID 10995457. doi:10.1073/pnas.170276797

[pmid15187088-29] Turner, Laura J; Nicholls Sarah, Hall Alan (Agosto de 2004). «The activity of the plexin-A1 receptor is regulated by Rac». United States. J. Biol. Chem. 279 (32): 33199–205. ISSN 0021-9258. PMID 15187088. doi:10.1074/jbc.M402943200

[pmid12458207-30] Barthwal, Manoj K; Sathyanarayana Pradeep, Kundu Chanakya N, Rana Basabi, Pradeep Anamika, Sharma Chandan, Woodgett James R, Rana Ajay (Fevereiro de 2003). «Negative regulation of mixed lineage kinase 3 by protein kinase B/AKT leads to cell survival». United States. J. Biol. Chem. 278 (6): 3897–902. ISSN 0021-9258. PMID 12458207. doi:10.1074/jbc.M211598200

[pmid12138205-31] Kane, Lawrence P; Mollenauer Marianne N, Xu Zheng, Turck Christoph W, Weiss Arthur (Agosto de 2002). «Akt-dependent phosphorylation specifically regulates Cot induction of NF-kappa B-dependent transcription». United States. Mol. Cell. Biol. 22 (16): 5962–74. ISSN 0270-7306. PMC 133991. PMID 12138205. doi:10.1128/MCB.22.16.5962-5974.2002

[pmid15718470-32] Sarbassov, D D; Guertin David A, Ali Siraj M, Sabatini David M (Fevereiro de 2005). «Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex». United States. Science. 307 (5712): 1098–101. PMID 15718470. doi:10.1126/science.1106148

[pmid10910062-33] Sekulić, A; Hudson C C, Homme J L, Yin P, Otterness D M, Karnitz L M, Abraham R T (Julho de 2000). «A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells». UNITED STATES. Cancer Res. 60 (13): 3504–13. ISSN 0008-5472. PMID 10910062

[pmid14970221-34] Cheng, Susan W Y; Fryer Lee G D, Carling David, Shepherd Peter R (Abril de 2004). «Thr2446 is a novel mammalian target of rapamycin (mTOR) phosphorylation site regulated by nutrient status». United States. J. Biol. Chem. 279 (16): 15719–22. ISSN 0021-9258. PMID 14970221. doi:10.1074/jbc.C300534200

[pmid10926925-35] Koh, H; Lee K H, Kim D, Kim S, Kim J W, Chung J (Novembro de 2000). «Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage». UNITED STATES. J. Biol. Chem. 275 (44): 34451–8. ISSN 0021-9258. PMID 10926925. doi:10.1074/jbc.M001753200

[pmid14749367-36] Remy, Ingrid; Michnick Stephen W (Fevereiro de 2004). «Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt». United States. Mol. Cell. Biol. 24 (4): 1493–504. ISSN 0270-7306. PMC 344167. PMID 14749367. doi:10.1128/MCB.24.4.1493-1504.2004

[pmid11956222-37] Powell, David W; Rane Madhavi J, Chen Qingdan, Singh Saurabh, McLeish Kenneth R (Junho de 2002). «Identification of 14-3-3zeta as a protein kinase B/Akt substrate». United States. J. Biol. Chem. 277 (24): 21639–42. ISSN 0021-9258. PMID 11956222. doi:10.1074/jbc.M203167200

[pmid10485710-38] Ozes, O N; Mayo L D, Gustin J A, Pfeffer S R, Pfeffer L M, Donner D B (Setembro de 1999). «NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase». ENGLAND. Nature. 401 (6748): 82–5. ISSN 0028-0836. PMID 10485710. doi:10.1038/43466

[pmid10485711-39] Romashkova, J A; Makarov S S (Setembro de 1999). «NF-kappaB is a target of AKT in anti-apoptotic PDGF signalling». ENGLAND. Nature. 401 (6748): 86–90. ISSN 0028-0836. PMID 10485711. doi:10.1038/43474

[pmid12042314-40] Fujita, Naoya; Sato Saori, Katayama Kazuhiro, Tsuruo Takashi (Agosto de 2002). «Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization». United States. J. Biol. Chem. 277 (32): 28706–13. ISSN 0021-9258. PMID 12042314. doi:10.1074/jbc.M203668200

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]

[21]

[22]

[23]

[24]

[25]

[26]

[27]

[28]

[29]

[30]

[31]

[32]

[33]

[34]

[35]

[36]

[37]

[38]

[39]

[40]