Ser2
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Home > Phosphorylation Site Page: > Ser2  -  eIF2-beta (human)

Site Information
______MsGDEMIFD   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 451805

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 36 ) , electrophoretic mobility shift ( 36 ) , mass spectrometry ( 1 , 2 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 35 ) , mutation of modification site ( 36 ) , phosphoamino acid analysis ( 36 )
Disease tissue studied:
breast cancer ( 7 , 12 ) , breast ductal carcinoma ( 7 ) , HER2 positive breast cancer ( 2 ) , luminal A breast cancer ( 2 ) , luminal B breast cancer ( 2 ) , breast cancer, surrounding tissue ( 2 ) , breast cancer, triple negative ( 2 , 7 ) , cervical cancer ( 25 ) , cervical adenocarcinoma ( 25 ) , leukemia ( 16 ) , acute myelogenous leukemia ( 16 ) , lung cancer ( 12 , 20 ) , non-small cell lung cancer ( 12 ) , ovarian cancer ( 7 ) , melanoma skin cancer ( 5 )
Relevant cell line - cell type - tissue:
'muscle, skeletal' ( 17 ) , 293 (epithelial) [AT1 (human), transfection, AT1R stable transfected HEK293] ( 22 ) , 293 (epithelial) ( 29 ) , 293GP (epithelial) [NPM-ALK (human), transfection] ( 21 ) , 786-O (renal) [VHL (human), transfection] ( 4 ) , 786-O (renal) ( 4 ) , A498 (renal) ( 24 ) , A549 (pulmonary) ( 9 ) , breast ( 2 , 7 ) , BT-20 (breast cell) ( 12 ) , BT-549 (breast cell) ( 12 ) , Calu 6 (pulmonary) ( 12 ) , CL1-0 (pulmonary) ( 20 ) , CL1-1 (pulmonary) ( 20 ) , CL1-2 (pulmonary) ( 20 ) , CL1-5 (pulmonary) ( 20 ) , endothelial-aorta ( 13 ) , Flp-In T-Rex-293 (epithelial) [PRKD1 (human), genetic knockin] ( 14 ) , Flp-In T-Rex-293 (epithelial) ( 14 ) , GM00130 (B lymphocyte) ( 23 ) , H2009 (pulmonary) ( 12 ) , H2077 (pulmonary) ( 12 ) , H2887 (pulmonary) ( 12 ) , H322M (pulmonary) ( 12 ) , HCC1359 (pulmonary) ( 12 ) , HCC1937 (breast cell) ( 12 ) , HCC2279 (pulmonary) ( 12 ) , HCC366 (pulmonary) ( 12 ) , HCC4006 (pulmonary) ( 12 ) , HCC78 (pulmonary) ( 12 ) , HCC827 (pulmonary) ( 12 ) , HCT116 (intestinal) ( 28 ) , HeLa (cervical) ( 1 , 6 , 11 , 26 , 33 , 35 , 36 ) , HeLa S3 (cervical) ( 18 , 25 , 31 ) , HOP62 (pulmonary) ( 12 ) , HUES-7 ('stem, embryonic') ( 27 ) , HUES-9 ('stem, embryonic') ( 19 ) , Jurkat (T lymphocyte) ( 10 ) , K562 (erythroid) ( 11 , 26 ) , KG-1 (myeloid) ( 16 ) , LCLC-103H (pulmonary) ( 12 ) , LOU-NH91 (squamous) ( 12 ) , MCF-7 (breast cell) ( 12 ) , MDA-MB-231 (breast cell) ( 12 ) , MDA-MB-435S (breast cell) ( 28 ) , MDA-MB-468 (breast cell) ( 12 ) , NCI-H1395 (pulmonary) ( 12 ) , NCI-H1568 (pulmonary) ( 12 ) , NCI-H157 (pulmonary) ( 12 ) , NCI-H1648 (pulmonary) ( 12 ) , NCI-H1666 (pulmonary) ( 12 ) , NCI-H2030 (pulmonary) ( 12 ) , NCI-H2172 (pulmonary) ( 12 ) , NCI-H322 (pulmonary) ( 12 ) , NCI-H460 (pulmonary) ( 12 , 30 ) , NCI-H520 (squamous) ( 12 ) , NCI-H647 (pulmonary) ( 12 ) , ovary ( 7 ) , PANC-1 (pancreatic) [PRP4 (human), knockdown, Lentiviral introduced doxycycline-inducible PRP4 shRNA] ( 8 ) , PANC-1 (pancreatic) ( 8 ) , PC9 (pulmonary) ( 12 ) , TERT20 ('stem, mesenchymal') ( 32 ) , WM239A (melanocyte) ( 5 )

Upstream Regulation
Regulatory protein:
PRP4 (human) ( 8 )
Putative in vivo kinases:
CK2A1 (human) ( 36 )
Kinases, in vitro:
CK2A1 (human) ( 36 )
Phosphatases, in vitro:
PPP1CA (rabbit) ( 34 )
Treatments:
metastatic potential ( 20 ) , nocodazole ( 25 ) , serum ( 36 )

Downstream Regulation
Effects of modification on biological processes:
cell growth, altered ( 36 ) , translation, altered ( 36 )

References 

1

Huang H, et al. (2016) Simultaneous Enrichment of Cysteine-containing Peptides and Phosphopeptides Using a Cysteine-specific Phosphonate Adaptable Tag (CysPAT) in Combination with titanium dioxide (TiO2) Chromatography. Mol Cell Proteomics 15, 3282-3296
27281782   Curated Info

2

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

3

Boeing S, et al. (2016) Multiomic Analysis of the UV-Induced DNA Damage Response. Cell Rep 15, 1597-1610
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4

Malec V, Coulson JM, Urbé S, Clague MJ (2015) Combined Analyses of the VHL and Hypoxia Signaling Axes in an Isogenic Pairing of Renal Clear Cell Carcinoma Cells. J Proteome Res 14, 5263-72
26506913   Curated Info

5

Stuart SA, et al. (2015) A Phosphoproteomic Comparison of B-RAFV600E and MKK1/2 Inhibitors in Melanoma Cells. Mol Cell Proteomics 14, 1599-615
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6

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

7

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

8

Gao Q, et al. (2013) Evaluation of cancer dependence and druggability of PRP4 kinase using cellular, biochemical, and structural approaches. J Biol Chem 288, 30125-38
24003220   Curated Info

9

Kim JY, et al. (2013) Dissection of TBK1 signaling via phosphoproteomics in lung cancer cells. Proc Natl Acad Sci U S A 110, 12414-9
23836654   Curated Info

10

Mertins P, et al. (2013) Integrated proteomic analysis of post-translational modifications by serial enrichment. Nat Methods 10, 634-7
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11

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

12

Klammer M, et al. (2012) Phosphosignature predicts dasatinib response in non-small cell lung cancer. Mol Cell Proteomics 11, 651-68
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13

Verano-Braga T, et al. (2012) Time-resolved quantitative phosphoproteomics: new insights into Angiotensin-(1-7) signaling networks in human endothelial cells. J Proteome Res 11, 3370-81
22497526   Curated Info

14

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

15

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
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16

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
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17

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

18

Santamaria A, et al. (2011) The Plk1-dependent phosphoproteome of the early mitotic spindle. Mol Cell Proteomics 10, M110.004457
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19

Rigbolt KT, et al. (2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal 4, rs3
21406692   Curated Info

20

Wang YT, et al. (2010) An informatics-assisted label-free quantitation strategy that depicts phosphoproteomic profiles in lung cancer cell invasion. J Proteome Res 9, 5582-97
20815410   Curated Info

21

Wu F, et al. (2010) Studies of phosphoproteomic changes induced by nucleophosmin-anaplastic lymphoma kinase (ALK) highlight deregulation of tumor necrosis factor (TNF)/Fas/TNF-related apoptosis-induced ligand signaling pathway in ALK-positive anaplastic large cell lymphoma. Mol Cell Proteomics 9, 1616-32
20393185   Curated Info

22

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

23

Bennetzen MV, et al. (2010) Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response. Mol Cell Proteomics 9, 1314-23
20164059   Curated Info

24

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
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25

Olsen JV, et al. (2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal 3, ra3
20068231   Curated Info

26

Pan C, Olsen JV, Daub H, Mann M (2009) Global effects of kinase inhibitors on signaling networks revealed by quantitative phosphoproteomics. Mol Cell Proteomics 8, 2796-808
19651622   Curated Info

27

Van Hoof D, et al. (2009) Phosphorylation dynamics during early differentiation of human embryonic stem cells. Cell Stem Cell 5, 214-26
19664995   Curated Info

28

Oppermann FS, et al. (2009) Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics 8, 1751-64
19369195   Curated Info

29

Gauci S, et al. (2009) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem 81, 4493-501
19413330   Curated Info

30

Nagano K, et al. (2009) Phosphoproteomic analysis of distinct tumor cell lines in response to nocodazole treatment. Proteomics 9, 2861-74
19415658   Curated Info

31

Daub H, et al. (2008) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell 31, 438-48
18691976   Curated Info

32

Thingholm TE, et al. (2008) TiO2-Based Phosphoproteomic Analysis of the Plasma Membrane and the Effects of Phosphatase Inhibitor Treatment. J Proteome Res 7, 3304-3313
18578522   Curated Info

33

Ruse CI, et al. (2008) Motif-specific sampling of phosphoproteomes. J Proteome Res 7, 2140-50
18452278   Curated Info

34

Wakula P, et al. (2006) The translation initiation factor eIF2beta is an interactor of protein phosphatase-1. Biochem J 400, 377-83
16987104   Curated Info

35

Olsen JV, et al. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-48
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36

Llorens F, et al. (2006) The N-terminal domain of the human eIF2beta subunit and the CK2 phosphorylation sites are required for its function. Biochem J 394, 227-36
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