Ser129
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Home > Phosphorylation Site Page: > Ser129  -  Akt1 (human)

Site Information
sGsPsDNsGAEEMEV   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 450019

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 30 , 31 ) , immunoprecipitation ( 2 ) , mass spectrometry ( 1 , 3 , 5 , 6 , 7 , 8 , 9 , 11 , 13 , 14 , 15 , 17 , 18 , 21 , 22 , 24 , 25 , 26 , 27 , 28 , 29 ) , microscopy-colocalization with upstream kinase ( 4 ) , mutation of modification site ( 4 , 19 , 30 ) , phospho-antibody ( 2 , 4 , 20 , 23 , 30 , 31 ) , phosphopeptide mapping ( 31 ) , western blotting ( 4 , 19 , 20 , 23 , 31 )
Disease tissue studied:
breast cancer ( 6 , 7 , 14 , 23 ) , breast ductal carcinoma ( 6 ) , HER2 positive breast cancer ( 1 ) , luminal A breast cancer ( 1 ) , luminal B breast cancer ( 1 ) , breast cancer, surrounding tissue ( 1 ) , breast cancer, triple negative ( 1 , 6 ) , leukemia ( 17 , 29 ) , acute myelogenous leukemia ( 17 ) , chronic myelogenous leukemia ( 29 ) , hepatocellular carcinoma, surrounding tissue ( 27 ) , lung cancer ( 14 , 21 ) , non-small cell lung cancer ( 14 ) , non-small cell lung adenocarcinoma ( 21 ) , ovarian cancer ( 6 ) , pancreatic cancer ( 23 ) , pancreatic carcinoma ( 23 ) , pancreatic ductal adenocarcinoma ( 9 ) , prostate cancer ( 20 ) , melanoma skin cancer ( 3 )
Relevant cell line - cell type - tissue:
'muscle, skeletal' ( 18 ) , 'pancreatic, ductal'-pancreas ( 9 ) , 293 (epithelial) [AT1 (human), transfection, AT1R stable transfected HEK293] ( 25 ) , 293 (epithelial) [AT1 (human), transfection] ( 24 ) , 293 (epithelial) ( 2 ) , A498 (renal) ( 26 ) , breast ( 1 , 6 ) , BT-474 (breast cell) ( 23 ) , BT-549 (breast cell) ( 14 ) , BxPC-3 (pancreatic) ( 23 ) , C2C12 (myoblast) ( 4 ) , Calu 6 (pulmonary) ( 14 ) , COS (fibroblast) ( 31 ) , Flp-In T-Rex-293 (epithelial) [PRKD1 (human), genetic knockin] ( 15 ) , Flp-In T-Rex-293 (epithelial) ( 15 ) , H2009 (pulmonary) ( 14 ) , H2077 (pulmonary) ( 14 ) , H2887 (pulmonary) ( 14 ) , H322M (pulmonary) ( 14 ) , HCC1359 (pulmonary) ( 14 ) , HCC1937 (breast cell) ( 14 ) , HCC2279 (pulmonary) ( 14 ) , HCC366 (pulmonary) ( 14 ) , HCC4006 (pulmonary) ( 14 ) , HCC78 (pulmonary) ( 14 ) , HCC827 (pulmonary) ( 14 ) , HEK293T (epithelial) [Akt1 (human), transfection] ( 4 ) , HEK293T (epithelial) ( 30 ) , HeLa (cervical) ( 4 , 5 , 13 , 22 , 28 ) , hepatocyte-liver ( 27 ) , HMLER ('stem, breast cancer') [CXCR4 (human), knockdown] ( 7 ) , HMLER ('stem, breast cancer') ( 7 ) , HOP62 (pulmonary) ( 14 ) , HUVEC (endothelial) ( 23 ) , Jurkat (T lymphocyte) ( 11 ) , K562 (erythroid) ( 13 , 29 ) , KG-1 (myeloid) ( 17 ) , LCLC-103H (pulmonary) ( 14 ) , liver ( 8 ) , LOU-NH91 (squamous) ( 14 ) , MCF-7 (breast cell) ( 14 ) , MDA-MB-231 (breast cell) ( 14 ) , NCI-H1395 (pulmonary) ( 14 ) , NCI-H1568 (pulmonary) ( 14 ) , NCI-H157 (pulmonary) ( 14 ) , NCI-H1648 (pulmonary) ( 14 ) , NCI-H1666 (pulmonary) ( 14 ) , NCI-H2030 (pulmonary) ( 14 ) , NCI-H2172 (pulmonary) ( 14 ) , NCI-H322 (pulmonary) ( 14 ) , NCI-H460 (pulmonary) ( 14 ) , NCI-H520 (squamous) ( 14 ) , NCI-H647 (pulmonary) ( 14 ) , ovary ( 6 ) , PC3 (prostate cell) ( 20 ) , PC9 (pulmonary) ( 14 ) , SKOV-3 (ovarian) ( 31 ) , U-1810 (pulmonary) [EFNB3 (human), knockdown] ( 21 ) , U-1810 (pulmonary) ( 21 ) , WM239A (melanocyte) ( 3 )

Upstream Regulation
Regulatory protein:
Akt1 (human) ( 4 ) , Akt2 (human) ( 4 )
Putative in vivo kinases:
CK2A1 (human) ( 23 )
Kinases, in vitro:
CK2A1 (human) ( 30 )
Treatments:
insulin ( 4 ) , okadaic_acid ( 4 ) , quinalizarin ( 2 ) , SII_angiotensin_2 ( 24 ) , silmitasertib ( 2 , 20 , 23 ) , TBB ( 30 )

Downstream Regulation
Effects of modification on Akt1:
enzymatic activity, induced ( 30 ) , molecular association, regulation ( 4 ) , phosphorylation ( 4 )
Effects of modification on biological processes:
apoptosis, inhibited ( 19 , 23 ) , carcinogenesis, induced ( 23 ) , cell cycle regulation ( 23 ) , cell growth, induced ( 23 ) , cell motility, induced ( 23 ) , signaling pathway regulation ( 23 ) , transcription, induced ( 19 )
Induce interaction with:
palladin (human) ( 4 )

References 

1

Mertins P, et al. (2016) Proteogenomics connects somatic mutations to signalling in breast cancer. Nature 534, 55-62
27251275   Curated Info

2

Borgo C, et al. (2015) Protein kinase CK2 potentiates translation efficiency by phosphorylating eIF3j at Ser127. Biochim Biophys Acta 1853, 1693-701
25887626   Curated Info

3

Stuart SA, et al. (2015) A Phosphoproteomic Comparison of B-RAFV600E and MKK1/2 Inhibitors in Melanoma Cells. Mol Cell Proteomics 14, 1599-615
25850435   Curated Info

4

Girardi C, et al. (2014) Differential phosphorylation of Akt1 and Akt2 by protein kinase CK2 may account for isoform specific functions. Biochim Biophys Acta 1843, 1865-74
24769357   Curated Info

5

Sharma K, et al. (2014) Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. Cell Rep 8, 1583-94
25159151   Curated Info

6

Mertins P, et al. (2014) Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels. Mol Cell Proteomics 13, 1690-704
24719451   Curated Info

7

Yi T, et al. (2014) Quantitative phosphoproteomic analysis reveals system-wide signaling pathways downstream of SDF-1/CXCR4 in breast cancer stem cells. Proc Natl Acad Sci U S A 111, E2182-90
24782546   Curated Info

8

Bian Y, et al. (2014) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics 96, 253-62
24275569   Curated Info

9

Britton D, et al. (2014) Quantification of pancreatic cancer proteome and phosphorylome: indicates molecular events likely contributing to cancer and activity of drug targets. PLoS One 9, e90948
24670416   Curated Info

10

Nguyen le XT, Mitchell BS (2013) Akt activation enhances ribosomal RNA synthesis through casein kinase II and TIF-IA. Proc Natl Acad Sci U S A 110, 20681-6
24297901   Curated Info

11

Mertins P, et al. (2013) Integrated proteomic analysis of post-translational modifications by serial enrichment. Nat Methods 10, 634-7
23749302   Curated Info

12

Shiromizu T, et al. (2013) Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res 12, 2414-21
23312004   Curated Info

13

Zhou H, et al. (2013) Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res 12, 260-71
23186163   Curated Info

14

Klammer M, et al. (2012) Phosphosignature predicts dasatinib response in non-small cell lung cancer. Mol Cell Proteomics 11, 651-68
22617229   Curated Info

15

Franz-Wachtel M, et al. (2012) Global detection of protein kinase D-dependent phosphorylation events in nocodazole-treated human cells. Mol Cell Proteomics 11, 160-70
22496350   Curated Info

16

Beli P, et al. (2012) Proteomic Investigations Reveal a Role for RNA Processing Factor THRAP3 in the DNA Damage Response. Mol Cell 46, 212-25
22424773   Curated Info

17

Weber C, Schreiber TB, Daub H (2012) Dual phosphoproteomics and chemical proteomics analysis of erlotinib and gefitinib interference in acute myeloid leukemia cells. J Proteomics 75, 1343-56
22115753   Curated Info

18

Lundby A, et al. (2012) Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun 3, 876
22673903   Curated Info

19

Ponce DP, et al. (2011) CK2 functionally interacts with AKT/PKB to promote the β-catenin-dependent expression of survivin and enhance cell survival. Mol Cell Biochem 356, 127-32
21735093   Curated Info

20

Pierre F, et al. (2011) Pre-clinical characterization of CX-4945, a potent and selective small molecule inhibitor of CK2 for the treatment of cancer. Mol Cell Biochem 356, 37-43
21755459   Curated Info

21

Ståhl S, et al. (2011) Phosphoproteomic profiling of NSCLC cells reveals that ephrin B3 regulates pro-survival signaling through Akt1-mediated phosphorylation of the EphA2 receptor. J Proteome Res 10, 2566-78
21413766   Curated Info

22

Kettenbach AN, et al. (2011) Quantitative phosphoproteomics identifies substrates and functional modules of aurora and polo-like kinase activities in mitotic cells. Sci Signal 4, rs5
21712546   Curated Info

23

Siddiqui-Jain A, et al. (2010) CX-4945, an orally bioavailable selective inhibitor of protein kinase CK2, inhibits prosurvival and angiogenic signaling and exhibits antitumor efficacy. Cancer Res 70, 10288-98
21159648   Curated Info

24

Xiao K, et al. (2010) Global phosphorylation analysis of beta-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR). Proc Natl Acad Sci U S A 107, 15299-304
20686112   Curated Info

25

Christensen GL, et al. (2010) Quantitative phosphoproteomics dissection of seven-transmembrane receptor signaling using full and biased agonists. Mol Cell Proteomics 9, 1540-53
20363803   Curated Info

26

Schreiber TB, et al. (2010) An integrated phosphoproteomics work flow reveals extensive network regulation in early lysophosphatidic acid signaling. Mol Cell Proteomics 9, 1047-62
20071362   Curated Info

27

Han G, et al. (2010) Phosphoproteome analysis of human liver tissue by long-gradient nanoflow LC coupled with multiple stage MS analysis. Electrophoresis 31, 1080-9
20166139   Curated Info

28

Dephoure N, et al. (2008) A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A 105, 10762-7
18669648   Curated Info

29

Stokes M (2008) CST Curation Set: 4392; Year: 2008; Biosample/Treatment: cell line, K562/untreated; Disease: chronic myelogenous leukemia; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: p[STY])
Curated Info

30

Di Maira G, et al. (2005) Protein kinase CK2 phosphorylates and upregulates Akt/PKB. Cell Death Differ 12, 668-77
15818404   Curated Info

31

Conus NM, et al. (2002) Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase. J Biol Chem 277, 38021-8
12149249   Curated Info