Ser102

Site Information
sREPAPAsPAPAGVE SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 4033178

In vivo Characterization
Methods used to characterize site in vivo:	mass spectrometry ( 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 )
Disease tissue studied:	breast cancer ( 5 , 10 ) , 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 ) , lung cancer ( 9 , 10 , 21 ) , non-small cell lung cancer ( 10 , 21 ) , non-small cell lung adenocarcinoma ( 9 ) , ovarian cancer ( 4 ) , pancreatic ductal adenocarcinoma ( 8 ) , melanoma skin cancer ( 3 )
Relevant cell line - cell type - tissue:	'muscle, skeletal' ( 13 ) , 'pancreatic, ductal'-pancreas ( 8 ) , 293 (epithelial) [AT1 (human), transfection, AT1R stable transfected HEK293] ( 17 ) , 786-O (renal) [VHL (human), transfection] ( 2 ) , 786-O (renal) ( 2 ) , A498 (renal) ( 18 ) , breast ( 1 ) , Flp-In T-Rex-293 (epithelial) [PRKD1 (human), genetic knockin] ( 11 ) , Flp-In T-Rex-293 (epithelial) ( 11 ) , H2009 (pulmonary) ( 10 ) , H2887 (pulmonary) ( 10 ) , HCC1937 (breast cell) ( 10 ) , HCC2279 (pulmonary) ( 10 ) , HeLa (cervical) ( 14 , 16 , 19 , 22 ) , HMLER ('stem, breast cancer') [CXCR4 (human), knockdown] ( 5 ) , HMLER ('stem, breast cancer') ( 5 ) , HUES-9 ('stem, embryonic') ( 15 ) , liver ( 7 ) , lung ( 9 ) , MCF-7 (breast cell) ( 10 ) , NCI-H1299 (pulmonary) ( 21 ) , NCI-H157 (pulmonary) ( 10 ) , NCI-H1666 (pulmonary) ( 10 ) , NCI-H2172 (pulmonary) ( 10 ) , NCI-H520 (squamous) ( 10 ) , ovary ( 4 ) , PC9 (pulmonary) ( 10 ) , SH-SY5Y (neural crest) [LRRK2 (human), transfection, over-expression of LRRK2(G2019S)] ( 6 ) , WM115 (melanocyte) ( 20 ) , WM239A (melanocyte) ( 3 )

Upstream Regulation
Treatments:	angiotensin_2 ( 17 ) , LRRK2-IN-1 ( 6 ) , selumetinib ( 3 ) , vemurafenib ( 3 )

References
1	Mertins P, et al. (2016) Proteogenomics connects somatic mutations to signalling in breast cancer. Nature 534, 55-62 27251275 Curated Info
2	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
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	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
5	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
6	Luerman GC, et al. (2014) Phosphoproteomic evaluation of pharmacological inhibition of leucine-rich repeat kinase 2 reveals significant off-target effects of LRRK-2-IN-1. J Neurochem 128, 561-76 24117733 Curated Info
7	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
8	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
9	Schweppe DK, Rigas JR, Gerber SA (2013) Quantitative phosphoproteomic profiling of human non-small cell lung cancer tumors. J Proteomics 91, 286-96 23911959 Curated Info
10	Klammer M, et al. (2012) Phosphosignature predicts dasatinib response in non-small cell lung cancer. Mol Cell Proteomics 11, 651-68 22617229 Curated Info
11	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
12	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
13	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
14	Grosstessner-Hain K, et al. (2011) Quantitative phospho-proteomics to investigate the polo-like kinase 1-dependent phospho-proteome. Mol Cell Proteomics 10, M111.008540 21857030 Curated Info
15	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
16	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
17	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
18	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
19	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
20	Old WM, et al. (2009) Functional proteomics identifies targets of phosphorylation by B-Raf signaling in melanoma. Mol Cell 34, 115-31 19362540 Curated Info
21	Tsai CF, et al. (2008) Immobilized metal affinity chromatography revisited: pH/acid control toward high selectivity in phosphoproteomics. J Proteome Res 7, 4058-69 18707149 Curated Info
22	Cantin GT, et al. (2008) Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res 7, 1346-51 18220336 Curated Info