Product: Phospho-AKT1/2/3 (Ser473) Antibody
Catalog: AF0016
Description: Rabbit polyclonal antibody to Phospho-AKT1/2/3 (Ser473)
Application: WB IHC IF/ICC
Cited expt.: WB, IHC, IF/ICC
Reactivity: Human, Mouse, Rat, Monkey
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 60kDa; 56kD(Calculated).
Uniprot: P31749 | P31751 | Q9Y243
RRID: AB_2810275

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat,Monkey
Prediction:
Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%)
Clonality:
Polyclonal
Specificity:
Phospho-pan-AKT1/2/3 (Ser473) Antibody detects endogenous levels of pan-AKT1/2/3 only when phosphorylated at Sersine 473.
RRID:
AB_2810275
Cite Format: Affinity Biosciences Cat# AF0016, RRID:AB_2810275.
Conjugate:
Unconjugated.
Purification:
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

AKT 1; AKT; AKT1; AKT1_HUMAN; MGC99656; PKB; PKB-ALPHA; PRKBA; Protein Kinase B Alpha; Protein kinase B; Proto-oncogene c-Akt; RAC Alpha; RAC; RAC-alpha serine/threonine-protein kinase; RAC-PK-alpha; Akt2; AKT2_HUMAN; HIHGHH; murine thymoma viral (v-akt) homolog-2; PKB; PKB beta; PKBB; PKBBETA; PRKBB; Protein kinase Akt 2; Protein kinase Akt-2; Protein kinase B beta; rac protein kinase beta; RAC-BETA; RAC-beta serine/threonine-protein kinase; RAC-PK-beta; v akt murine thymoma viral oncogene homolog 2; Akt3; AKT3 kinase; AKT3_HUMAN; DKFZp434N0250; MPPH; PKB gamma; PKBG; PRKBG; Protein kinase Akt-3; Protein Kinase AKT3; Protein kinase B gamma; RAC gamma; RAC gamma serine/threonine protein kinase; RAC-gamma serine/threonine-protein kinase; RAC-PK-gamma; RACPK Gamma; Serine threonine protein kinase Akt 3; Serine threonine protein kinase Akt3; STK 2; STK-2; STK2; V akt murine thymoma viral oncogene homolog 3 (protein kinase B, gamma); V akt murine thymoma viral oncogene homolog 3; V akt murine thymoma viral oncogene homolog 3 protein kinase B gamma;

Immunogens

Immunogen:

A synthesized peptide derived from human Akt around the phosphorylation site of Ser473.

Uniprot:
Gene(ID):
Expression:
P31749 AKT1_HUMAN:

Expressed in prostate cancer and levels increase from the normal to the malignant state (at protein level). Expressed in all human cell types so far analyzed. The Tyr-176 phosphorylated form shows a significant increase in expression in breast cancers during the progressive stages i.e. normal to hyperplasia (ADH), ductal carcinoma in situ (DCIS), invasive ductal carcinoma (IDC) and lymph node metastatic (LNMM) stages.

P31751 AKT2_HUMAN:

Expressed in all cell types so far analyzed.

Q9Y243 AKT3_HUMAN:

In adult tissues, it is highly expressed in brain, lung and kidney, but weakly in heart, testis and liver. In fetal tissues, it is highly expressed in heart, liver and brain and not at all in kidney.

Description:
an AGC kinase that plays a critical role in controlling the balance between survival and AP0ptosis. Phosphorylated and activated by PDK1 in the PI3 kinase pathway. Mediates survival signals downstream of PI3 kinase and several growth factor receptors by phosphorylating AP0pototic proteins. First found in a mouse transforming retrovirus. Tumorigenic in a mouse lymphoma model and activated (by phospho-Akt staining) and/or overexpressed in a number of cancers including breast, prostate, lung, pancreatic, liver, ovarian and colorectal. Inhibitor: RX-0201. Substrates include tuberin, Bad, Forkhead transcription factors, caspase-9, and glycogen synthase kinase-3.
Sequence:
MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA

MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIRE

MSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Chicken
100
Rabbit
100
Xenopus
0
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

Research Backgrounds

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. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface (By similarity). Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling (By similarity). 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 (By similarity). Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven (By similarity). 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 (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 (By similarity). 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. 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 (By similarity). Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development (By similarity). 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.

PTMs:

O-GlcNAcylation at Thr-305 and Thr-312 inhibits activating phosphorylation at Thr-308 via disrupting the interaction between AKT1 and PDPK1. O-GlcNAcylation at Ser-473 also probably interferes with phosphorylation at this site.

Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity. Activated TNK2 phosphorylates it on Tyr-176 resulting in its binding to the anionic plasma membrane phospholipid PA. This phosphorylated form localizes to the cell membrane, where it is targeted by PDPK1 and PDPK2 for further phosphorylations on Thr-308 and Ser-473 leading to its activation. Ser-473 phosphorylation by mTORC2 favors Thr-308 phosphorylation by PDPK1. Phosphorylated at Thr-308 and Ser-473 by IKBKE and TBK1. Ser-473 phosphorylation is enhanced by interaction with AGAP2 isoform 2 (PIKE-A). Ser-473 phosphorylation is enhanced in focal cortical dysplasias with Taylor-type balloon cells. Ser-473 phosphorylation is enhanced by signaling through activated FLT3 (By similarity). Ser-473 is dephosphorylated by PHLPP. Dephosphorylated at Thr-308 and Ser-473 by PP2A phosphatase. The phosphorylated form of PPP2R5B is required for bridging AKT1 with PP2A phosphatase. Ser-473 is dephosphorylated by CPPED1, leading to termination of signaling.

Ubiquitinated via 'Lys-48'-linked polyubiquitination by ZNRF1, leading to its degradation by the proteasome (By similarity). Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT1 ubiquitination is critical for phosphorylation and activation. When ubiquitinated, it translocates to the plasma membrane, where it becomes phosphorylated. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome. Also ubiquitinated by TRIM13 leading to its proteasomal degradation. Phosphorylated, undergoes 'Lys-48'-linked polyubiquitination preferentially at Lys-284 catalyzed by MUL1, leading to its proteasomal degradation.

Acetylated on Lys-14 and Lys-20 by the histone acetyltransferases EP300 and KAT2B. Acetylation results in reduced phosphorylation and inhibition of activity. Deacetylated at Lys-14 and Lys-20 by SIRT1. SIRT1-mediated deacetylation relieves the inhibition.

Subcellular Location:

Cytoplasm. Nucleus. Cell membrane.
Note: Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A. Phosphorylation on Tyr-176 by TNK2 results in its localization to the cell membrane where it is targeted for further phosphorylations on Thr-308 and Ser-473 leading to its activation and the activated form translocates to the nucleus. Colocalizes with WDFY2 in intracellular vesicles (PubMed:16792529).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in prostate cancer and levels increase from the normal to the malignant state (at protein level). Expressed in all human cell types so far analyzed. The Tyr-176 phosphorylated form shows a significant increase in expression in breast cancers during the progressive stages i.e. normal to hyperplasia (ADH), ductal carcinoma in situ (DCIS), invasive ductal carcinoma (IDC) and lymph node metastatic (LNMM) stages.

Family&Domains:

Binding of the PH domain to phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) following phosphatidylinositol 3-kinase alpha (PIK3CA) activity results in its targeting to the plasma membrane. The PH domain mediates interaction with TNK2 and Tyr-176 is also essential for this interaction.

The AGC-kinase C-terminal mediates interaction with THEM4.

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

Function:

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 PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.

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 seems 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'.

PTMs:

Phosphorylation on Thr-309 and Ser-474 is required for full activity.

Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT2 ubiquitination. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome.

O-GlcNAcylation at Thr-306 and Thr-313 inhibits activating phosphorylation at Thr-309 via disrupting the interaction between AKT and PDK1.

Subcellular Location:

Cytoplasm. Nucleus. Cell membrane>Peripheral membrane protein. Early endosome.
Note: Localizes within both nucleus and cytoplasm of proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. By virtue of the N-terminal PH domain, is recruited to sites of the plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting is also facilitared by interaction with CLIP3. Colocalizes with WDFY2 in early endosomes (By similarity).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in all cell types so far analyzed.

Family&Domains:

Binding of the PH domain to phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) following phosphatidylinositol 3-kinase alpha (PIK3CA) activity results in its targeting to the plasma membrane.

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

Function:

AKT3 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. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis.

PTMs:

Phosphorylation on Thr-305 and Ser-472 is required for full activity.

Ubiquitinated. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome.

O-GlcNAcylation at Thr-302 and Thr-309 inhibits activating phosphorylation at Thr-305 via disrupting the interaction between AKT and PDK1.

Subcellular Location:

Nucleus. Cytoplasm. Membrane>Peripheral membrane protein.
Note: Membrane-associated after cell stimulation leading to its translocation.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

In adult tissues, it is highly expressed in brain, lung and kidney, but weakly in heart, testis and liver. In fetal tissues, it is highly expressed in heart, liver and brain and not at all in kidney.

Family&Domains:

Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI(3)K) results in its targeting to the plasma membrane.

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

Research Fields

· Cellular Processes > Transport and catabolism > Autophagy - animal.   (View pathway)

· Cellular Processes > Cell growth and death > Apoptosis.   (View pathway)

· Cellular Processes > Cell growth and death > Cellular senescence.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Signaling pathways regulating pluripotency of stem cells.   (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > ErbB signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Ras signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Rap1 signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > cGMP-PKG signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > cAMP signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > HIF-1 signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > FoxO signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Sphingolipid signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Phospholipase D signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > mTOR signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > AMPK signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Apelin signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Jak-STAT signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > TNF signaling pathway.   (View pathway)

· Human Diseases > Drug resistance: Antineoplastic > EGFR tyrosine kinase inhibitor resistance.

· Human Diseases > Drug resistance: Antineoplastic > Endocrine resistance.

· Human Diseases > Drug resistance: Antineoplastic > Platinum drug resistance.

· Human Diseases > Endocrine and metabolic diseases > Insulin resistance.

· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).

· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).

· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

· Human Diseases > Infectious diseases: Viral > Hepatitis C.

· Human Diseases > Infectious diseases: Viral > Hepatitis B.

· Human Diseases > Infectious diseases: Viral > Measles.

· Human Diseases > Infectious diseases: Viral > Influenza A.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Cancers: Specific types > Colorectal cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Renal cell carcinoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Pancreatic cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Endometrial cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Glioma.   (View pathway)

· Human Diseases > Cancers: Specific types > Prostate cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Melanoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Chronic myeloid leukemia.   (View pathway)

· Human Diseases > Cancers: Specific types > Acute myeloid leukemia.   (View pathway)

· Human Diseases > Cancers: Specific types > Small cell lung cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Non-small cell lung cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Breast cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Gastric cancer.   (View pathway)

· Human Diseases > Cancers: Overview > Central carbon metabolism in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > Choline metabolism in cancer.   (View pathway)

· Organismal Systems > Immune system > Chemokine signaling pathway.   (View pathway)

· Organismal Systems > Aging > Longevity regulating pathway.   (View pathway)

· Organismal Systems > Aging > Longevity regulating pathway - multiple species.   (View pathway)

· Organismal Systems > Circulatory system > Adrenergic signaling in cardiomyocytes.   (View pathway)

· Organismal Systems > Development > Osteoclast differentiation.   (View pathway)

· Organismal Systems > Immune system > Platelet activation.   (View pathway)

· Organismal Systems > Immune system > Toll-like receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > T cell receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > B cell receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Fc epsilon RI signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Fc gamma R-mediated phagocytosis.   (View pathway)

· Organismal Systems > Nervous system > Neurotrophin signaling pathway.   (View pathway)

· Organismal Systems > Nervous system > Cholinergic synapse.

· Organismal Systems > Nervous system > Dopaminergic synapse.

· Organismal Systems > Endocrine system > Insulin signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Progesterone-mediated oocyte maturation.

· Organismal Systems > Endocrine system > Estrogen signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Prolactin signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Adipocytokine signaling pathway.

· Organismal Systems > Endocrine system > Glucagon signaling pathway.

· Organismal Systems > Endocrine system > Regulation of lipolysis in adipocytes.

· Organismal Systems > Endocrine system > Relaxin signaling pathway.

· Organismal Systems > Digestive system > Carbohydrate digestion and absorption.

References

1). CircVAPA promotes small cell lung cancer progression by modulating the miR-377-3p and miR-494-3p/IGF1R/AKT axis. Molecular Cancer, 2022 (PubMed: 35668527) [IF=37.3]

Application: WB    Species: Human    Sample: SCLC cells

Fig. 6 circVAPA promotes the progression of SCLC through the miR-377-3p and miR-494-3p/IGF1R/AKT axis. a and b Western blot analysis of the effects of circVAPA or miR-377-3p/miR-494-3p on IGF1R, AKT, and its downstream protein expression in SCLC cells. 377 inhi, miR-377 inhibitor, 494 inhi, miR-494 inhibitor; 377 mimic, miR-377 mimic; 494 mimic, miR-494 mimic. c Western blot analysis of the effect of overexpressing circVAPA or silencing IGF1R on AKT and its downstream protein expression in SCLC cells. d Western blot analysis of the effect of overexpressing circVAPA or IGF1R inhibitor (drug BMS-536924) on AKT and its downstream protein expression in SCLC cells. e The relative luciferase activities were detected in 293T cells after co-transfection with Lu-IGF1R-WT and mimic-NC or the circVAPA overexpression plasmid or miR-377-3p/miR-494-3p mimics, respectively. The firefly luciferase activities were measured and normalized to renilla luciferase activities (F/R). f-g Representative images of immunohistochemistry analysis of IGF1R (f) and p-AKT (g) in three independent SCLC cases. Scale bar, 50 μm. SCR, siRNA with scrambled sequences; si-circVAPA, the co-transfection of two independent siRNAs target circVAPA; EV, the empty vector; circVAPA, the circVAPA overexpression plasmid; miR-377 mimic/miR-494 mimic, transiently overexpressing miR-377-3p/miR-494-3p, respectively; miR-377 inhibitor/miR-494 inhibitor, transiently suppressing miR-377-3p/miR-494-3p, respectively; si-IGF1R, an independent siRNA targeting IGF1R; IGF1Ri, the addition of IGF1R inhibitor (drug BMS-536924). (All data are presented as the mean ± SD; ns, no significance; *P < 0.05; **P < 0.01; ***P < 0.001 by two-tailed Student’s t-test). Three independent assays were performed in the above assays. *** miR-377/miR-494 in this article represents miR-377-3p/miR-494-3p, respectively

Application: IHC    Species: Human    Sample: SCLC cells

Fig. 6 circVAPA promotes the progression of SCLC through the miR-377-3p and miR-494-3p/IGF1R/AKT axis. a and b Western blot analysis of the effects of circVAPA or miR-377-3p/miR-494-3p on IGF1R, AKT, and its downstream protein expression in SCLC cells. 377 inhi, miR-377 inhibitor, 494 inhi, miR-494 inhibitor; 377 mimic, miR-377 mimic; 494 mimic, miR-494 mimic. c Western blot analysis of the effect of overexpressing circVAPA or silencing IGF1R on AKT and its downstream protein expression in SCLC cells. d Western blot analysis of the effect of overexpressing circVAPA or IGF1R inhibitor (drug BMS-536924) on AKT and its downstream protein expression in SCLC cells. e The relative luciferase activities were detected in 293T cells after co-transfection with Lu-IGF1R-WT and mimic-NC or the circVAPA overexpression plasmid or miR-377-3p/miR-494-3p mimics, respectively. The firefly luciferase activities were measured and normalized to renilla luciferase activities (F/R). f-g Representative images of immunohistochemistry analysis of IGF1R (f) and p-AKT (g) in three independent SCLC cases. Scale bar, 50 μm. SCR, siRNA with scrambled sequences; si-circVAPA, the co-transfection of two independent siRNAs target circVAPA; EV, the empty vector; circVAPA, the circVAPA overexpression plasmid; miR-377 mimic/miR-494 mimic, transiently overexpressing miR-377-3p/miR-494-3p, respectively; miR-377 inhibitor/miR-494 inhibitor, transiently suppressing miR-377-3p/miR-494-3p, respectively; si-IGF1R, an independent siRNA targeting IGF1R; IGF1Ri, the addition of IGF1R inhibitor (drug BMS-536924). (All data are presented as the mean ± SD; ns, no significance; *P < 0.05; **P < 0.01; ***P < 0.001 by two-tailed Student’s t-test). Three independent assays were performed in the above assays. *** miR-377/miR-494 in this article represents miR-377-3p/miR-494-3p, respectively

2). Aberrant translation regulated by METTL1/WDR4‐mediated tRNA N7‐methylguanosine modification drives head and neck squamous cell carcinoma progression. Cancer Communications, 2022 (PubMed: 35179319) [IF=16.2]

Application: WB    Species: Human    Sample: METTL1‐KO cells

FIGURE 4 METTL1‐mediated m7G tRNA modification regulates the activity of the PI3K/AKT/mTOR signaling pathway. (A) Scatterplot of the TRs in METTL1‐WT and METTL1‐KO SCC15 cells. TRs were calculated by dividing the ribosome‐binding transcript signals by input RNA‐seq signals. (B) KEGG pathway analysis of the genes with decreased TRs upon METTL1 knockout. (C) The PI3K/AKT/mTOR signaling pathway was enriched in RNC‐seq datasets by GSEA (NES = 1.64, FDR = 0.165, P < 0.001). (D) Western blotting of PI3K/AKT/mTOR signaling pathway proteins and downstream proteins using the indicated antibodies. (E) qRT‐PCR analysis of PIK3CA with RNC and input samples in SCC9 and SCC15 cells. (F) The protein levels of PI3K, AKT, and p‐AKT in METTL1‐WT, METTL1‐KO, PI3K‐transfected METTL1‐KO cells (KO + PIK3CA) and 5 μg/mL SC79‐treated METTL1‐KO cells cultured with (KO + SC79). (G‐I) The proliferation (G), migration (H) and invasion abilities (I) were partially restored after transfecting METTL1‐KO cells with the PI3K plasmid or activating AKT. Data are presented as the mean ± SD and analyzed by Student's t‐test. *, P < 0.05, **, P < 0.01, ***, P < 0.001. Abbreviations: PI3K/AKT/mTOR: phosphatidylinositol‐3‐kinase/protein kinase B/mammalian target of rapamycin; METTL1: Methyltransferase‐like 1; WT: wild‐type; KO: knockout; TRs: translation ratios; KEGG: Koto Encyclopedia of Genes and Genomes; GSEA: gene set enrichment analysis; NES: normalized enrichment score; FDR: false discovery rate; qRT‐PCR: quantitative real‐time PCR; RNC: Ribosome nascent‐chain complex‐bound; MMP9: matrix metalloprotein 9; Bcl‐2: B‐cell lymphoma‐2; P‐S6K: phosphorylation of S6 kinase; BAX: Bcl‐2‐associated X protein; PIK3CA: phosphatidylinositol‐4,5‐bisphosphate 3‐kinase, catalytic subunit alpha; SD: standard deviation

3). The combination of CUDC-907 and gilteritinib shows promising in vitro and in vivo antileukemic activity against FLT3-ITD AML. Blood Cancer Journal, 2021 (PubMed: 34099621) [IF=12.9]

Application: WB    Species: Human    Sample: MV4-11 cells

Fig. 5 CUDC-907 and gilteritinib induce complimentary and cooperatively altered activity within the MAPK/ERK and JAK2/STAT5 pathways. A MV4-11 cells were treated with gilteritinib, CUDC-907, both, or neither for 4, 8, 12, or 24 h. Western blots were generated utilizing whole-cell lysates, with representative blots shown, and densitometry displayed below each blot. Densitometry was assessed via comparison to vehicle control and normalized to β-actin. B A primary FLT3-ITD positive AML patient sample was treated with gilteritinib and/or CUDC-907 for 24 h. Densitometry was assessed via comparison to vehicle control and normalized to β-actin. C, D MOLM-13 and MV4-11 cells were treated using CUDC- 907 either with or without AZD1480, a selective JAK2 inhibitor, for 24 h. Flow cytometry analysis of annexin V/PI stained cells is shown in the upper panels and western blot analyses of phosphorylated STAT5 are shown in the lower panels. ***p < 0.001 compared to single-drug treatments. E MOLM-13, MV4-11, and primary patient sample AML#213 were treated with gilteritinib, CUDC-907, both, or vehicle control for 24 h. Western blotting was performed to analyze expression of members of the Bcl-2 family. Densitometry was measured via comparison to vehicle control and normalized to β-actin. F Mcl-1 overexpression and red fluorescent protein (RFP) control MV4-11 cells were generated using lentivirus particles as described in the “Methods” section. Whole-cell lysates were subjected to western blotting to confirm overexpression (upper panel). The cells were then treated with vehicle control, gilteritinib, CUDC-907, or in combination for 24 h, and then annexin V/PI staining and flow cytometry analysis were performed (lower panel). ***p < 0.001 compared to RFP under the same drug treatment. G, H shRNA knockdown of Bim, Bak, and Bax, or nontemplate control (NTC) was performed in MV4-11 cells. Whole-cell lysates were subjected to western blotting (upper panels). Cells were treated with vehicle control, gilteritinib, CUDC-907, or in combination for 24 h. Annexin V/PI staining and flow cytometry analysis results are shown (lower panels). ***p < 0.001 compared to NTC for the same drug treatment.

4). Arsenic induces hepatic insulin resistance via mtROS-NLRP3 inflammasome pathway. JOURNAL OF HAZARDOUS MATERIALS, 2020 (PubMed: 32544768) [IF=12.2]

Application: WB    Species: rat    Sample: liver

Fig.2 The effect of NaAsO2 on mitophagy, ox-mtDNA and NLRP3 inflammation in rats liver. Male SD rats were treated with 2.5, 5 mg/kg of NaAsO2 for 3 months. Liver coefficient (A). The level of serum ALT and AST were determined by commercial reagent kits (B-C). H&E staining of liver sections after NaAsO2 administration (D). scale bar = 500 μm. NAS in rat liver (E). Cytosolic fractions were analyzed by Western blot analysis. GAPDH was used as an internal control. The relative expression of MPO was shown as the percentage of GAPDH (F-G). The level of ox￾mtDNA was measured with an ELISA kit (H). Mitochondria fractions were analyzed by Western blot analysis. VDAC1, mitochondria marker protein, was used as an Journal Pre-proof internal control. The protein level and densitometric analyses of PINK1, Parkin, LC3B in rats liver tissues (I-L). The protein level and densitometric analyses of NLRP3, IL-1β, IL-18 expressed in rat liver tissues (M-T). Results are mean ± SEM of 5 rats. *P < 0.05 compare with the control group.

5). High yield engineered nanovesicles from ADSC with enriched miR-21-5p promote angiogenesis in adipose tissue regeneration. Biomaterials Research, 2022 (PubMed: 36528594) [IF=11.3]

Application: WB    Species: Human    Sample: HUVECs

Fig. 6 miR-21-5p abundant in ADSC-NVs inhibits PTEN and activates PI3K/AKT signaling in HUVECs. First, HUVECs were transfected with miR-21-5p mimic or inhibitor. qRT-PCR assay was then conducted to determine the relative expression level of miR-21-5p (A) and PTEN (B) in the mimic, mimic negative control (mimic NC), inhibitor, and inhibitor negative control (inhibitor NC) groups (n = 3 per group). qRT-PCR assay of the relative expression level of angiogenetic VEGF and Ang-1 mRNA (C), and apoptosis associated mRNA expression of Bax and Bcl-2 (D) in the mimic, mimic NC, inhibitor, and inhibitor NC groups (n = 3 per group). E Western blot assay for protein level of PTEN. F-G Western blot assay for protein level of VEGF, Ang-1, Bax, and Bcl-2. H Western blot assay of PI3K, Akt, and p-Akt protein level. Next, HUVECs were treated with/without ADSC-NVs for 24 h and collected for analysis. I qRT-PCR analysis of the relative expression level of miR-21-5p (n = 3 per group). J qRT-PCR analysis of relative expression level of PTEN and PI3K (n = 3 per group). K Western blot assay for protein levels of PTEN and PI3K. L Western blot assay for protein levels of Akt and p-Akt. ns, no significant difference, *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001

6). LncRNA AK023391 promotes tumorigenesis and invasion of gastric cancer through activation of the PI3K/Akt signaling pathway. Journal of Experimental & Clinical Cancer Research, 2017 (PubMed: 29282102) [IF=11.3]

Application: IHC    Species: human    Sample: xenograft tumor

Fig. 9 | Knockdown of AK023391 inhibited tumor growth in vivo. d IHC analysis of the expression levels of Ki-67, p-FOXO3a, p-PI3K, p-Akt, and p-NF-κB in xenograft tumor tissues treated with si-AK023391 and in the NC group (original magnification, ×200).

Application: WB    Species: human    Sample: Gastric cancer cells

Fig. 8 | LncRNA AK023391 was involved in the regulation of the PI3K/Akt signaling pathway.e-f Western blotting validation of the effects of AK023391 knockdown on the expression of PI3K/Akt, NF-κB, p53, and FOXO3a pathways, and their downstream transcription factors c-myb, cyclinB1/G2, and BCL-6 in HGC 27, AGS, and SGC-7901 cells

7). Particulate Matter Exposure History Affects Antioxidant Defense Response of Mouse Lung to Haze Episodes. ENVIRONMENTAL SCIENCE & TECHNOLOGY, 2019 (PubMed: 31328514) [IF=10.8]

Application: WB    Species:    Sample:

Figure 6.| Activated signaling pathways before and after haze exposure. Western blot analysis of the Erk and Akt signaling pathways related to oxidative stress (A) and mRNA expression detections of P38 (B), Nf r2 (C), and P21 (D) were conducted at the moment pre-exposure terminated (PE) and at the moment haze exposure terminated (HE).

8). Breaking the vicious loop between inflammation, oxidative stress and coagulation, a novel anti-thrombus insight of nattokinase by inhibiting LPS-induced inflammation and oxidative stress. Redox Biology, 2020 (PubMed: 32193146) [IF=10.7]

Application: WB    Species: Mice    Sample: RAW264.7 cells

Fig. 4. NK suppressed the LPS-induced ROS generation and NOX2 activation in RAW264.7 cells. (A) Effect of NK on LPS-induced ROS generation in RAW 264.7 cells. Cells were pretreated with NK (0.30 FU/ml) for 1 h and then exposed to LPS (0.1 μg/mL) for 24 h. Intracellular ROS appeared green under a confocal microscopy (Scale bar is 40 μm), and the green fluorescent intensity was quantified by Image Pro Plus. Data represent the mean ± SD from three independent experiments. The mean fluorescence intensity were standardized to LPS treatment cells. **P < 0.01, vs. control; ##P < 0.01, ###P < 0.001, vs. LPS-stimulated cells. (B) Effect of NK on LPS-induced Nrf2 and AKT activation in RAW264.7 cells. Cells were pretreated with NK (0.08, 0.15, 0.30 FU/mL) for 1 h and then were stimulated with LPS (0.1 μg/mL) for 6 h. Equal amounts of total cell lysates were loaded and subjected to immunoblot analysis. β-actin was used as the control for equal protein loading and protein integrity. Data represent the mean ± SD from three independent experiments. *P < 0.01, vs. control; #P < 0.05, ##P < 0.05, vs. LPS-stimulated cells. (C) Effect of NK on LPS-induced P47 translocation via immunofluorescence assay. Cells were pretreated with NK (0.30 FU/ml) for 1 h before LPS (0.1 μg/mL) stimulation for 2 h. Double immunostainings were performed with anti-NOX2 (in green) and anti-p47phox (in red); nuclei were stained with Hochest (blue). Scale bars: 40 μm. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

9). Environmental endocrine disruptor Bisphenol A induces metabolic derailment and obesity via upregulating IL-17A in adipocytes. ENVIRONMENT INTERNATIONAL, 2023 (PubMed: 36696794) [IF=10.3]

10). MiR-146b-5p enriched bioinspired exosomes derived from fucoidan-directed induction mesenchymal stem cells protect chondrocytes in osteoarthritis by targeting TRAF6. Journal of nanobiotechnology, 2023 (PubMed: 38105181) [IF=10.2]

Application: WB    Species: Rat    Sample: chondrocytes

Fig. 7 Enriched miR-146b-5p in F-MSCs-Exo inhibits PI3K/AKT/mTOR pathway by targeting TRAF6. (A, B) Western blot analysis was performed to detect the impact of F-MSCs-Exo on TRAF6 and the PI3K/AKT/mTOR pathway in rat chondrocytes. (C, D) The expression of TRAF6 was quantitatively analyzed using immunofluorescence staining and ImageJ software (scale bar = 10 μm). (E, F) Direct visualization of chondrocytes treated with nc-inhibitor and miR-146b-5p-inhibitor was performed using Alcian blue staining and safranin staining. (G, H) Western blot analysis was conducted to examine the expressions of TRAF6 and the PI3K/AKT/mTOR pathway in chondrocytes after treatment with nc-inhibitor and miR-146b-5p-inhibitor. (ns, no significant difference; *p 

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