Ser923
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Home > Phosphorylation Site Page: > Ser923  -  MEKK1 (human)

Site Information
CATkLsAsSEDIsER   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 3195236

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 1 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 )
Disease tissue studied:
breast cancer ( 5 ) , breast ductal carcinoma ( 5 ) , 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 , 5 ) , leukemia ( 12 ) , acute myelogenous leukemia ( 12 ) , neuroblastoma ( 9 ) , pancreatic ductal adenocarcinoma ( 6 ) , melanoma skin cancer ( 3 )
Relevant cell line - cell type - tissue:
'pancreatic, ductal'-pancreas ( 6 ) , 'stem, embryonic' ( 18 ) , 293 (epithelial) ( 20 ) , 293E (epithelial) ( 13 ) , A498 (renal) ( 16 ) , breast ( 1 , 5 ) , DG75 (B lymphocyte) ( 14 ) , Flp-In T-Rex-293 (epithelial) [PRKD1 (human), genetic knockin] ( 10 ) , Flp-In T-Rex-293 (epithelial) ( 10 ) , HCT116 (intestinal) ( 19 ) , HeLa (cervical) ( 4 , 8 , 23 ) , HeLa S3 (cervical) ( 22 ) , HeLa_Meta (cervical) ( 15 ) , HeLa_Pro (cervical) ( 15 ) , HeLa_Telo (cervical) ( 15 ) , HUES-7 ('stem, embryonic') ( 17 ) , Jurkat (T lymphocyte) ( 7 , 21 ) , K562 (erythroid) ( 8 ) , KG-1 (myeloid) ( 12 ) , MDA-MB-435S (breast cell) ( 19 ) , MV4-11 (macrophage) ( 19 ) , NB10 (neural crest) ( 9 ) , NPC (neural crest) ( 9 ) , WM239A (melanocyte) ( 3 )

Upstream Regulation
Treatments:
MG132_withdrawal ( 15 )

References 

1

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

2

Boeing S, et al. (2016) Multiomic Analysis of the UV-Induced DNA Damage Response. Cell Rep 15, 1597-1610
27184836   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

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

5

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

6

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

7

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

8

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

9

DeNardo BD, et al. (2013) Quantitative phosphoproteomic analysis identifies activation of the RET and IGF-1R/IR signaling pathways in neuroblastoma. PLoS One 8, e82513
24349301   Curated Info

10

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

11

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

12

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

13

Hsu PP, et al. (2011) The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling. Science 332, 1317-22
21659604   Curated Info

14

Iliuk AB, et al. (2010) In-depth analyses of kinase-dependent tyrosine phosphoproteomes based on metal ion-functionalized soluble nanopolymers. Mol Cell Proteomics 9, 2162-72
20562096   Curated Info

15

Dulla K, et al. (2010) Quantitative site-specific phosphorylation dynamics of human protein kinases during mitotic progression. Mol Cell Proteomics 9, 1167-81
20097925   Curated Info

16

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

17

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

18

Brill LM, et al. (2009) Phosphoproteomic analysis of human embryonic stem cells. Cell Stem Cell 5, 204-13
19664994   Curated Info

19

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

20

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

21

Mayya V, et al. (2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal 2, ra46
19690332   Curated Info

22

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

23

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