Ser51

Site Information
DQEWEsPsPPkPtVF SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 471098

In vivo Characterization
Methods used to characterize site in vivo:	electrophoretic mobility shift ( 23 ) , immunoprecipitation ( 23 ) , mass spectrometry ( 1 , 2 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 12 , 13 , 14 , 15 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 ) , mutation of modification site ( 23 ) , phospho-antibody ( 23 ) , western blotting ( 23 )
Disease tissue studied:	breast cancer ( 7 , 13 , 14 , 30 ) , breast adenocarcinoma ( 30 ) , breast ductal carcinoma ( 7 ) , HER2 positive breast cancer ( 2 ) , luminal A breast cancer ( 2 ) , luminal B breast cancer ( 2 ) , breast cancer, triple negative ( 2 , 7 , 30 ) , cervical cancer ( 25 ) , cervical adenocarcinoma ( 25 ) , leukemia ( 17 ) , acute myelogenous leukemia ( 17 ) , acute erythroid leukemias, including erythroleukemia (M6a) and very rare pure erythroid leukemia (M6b) ( 12 ) , acute megakaryoblastic leukemia (M7) ( 12 ) , acute monoblastic leukemia (M5a) or acute monocytic leukemia (M5b) ( 12 ) , acute myeloblastic leukemia, with granulocytic maturation (M2) ( 12 ) , acute myeloblastic leukemia, without maturation (M1) ( 12 ) , lung cancer ( 5 , 14 ) , non-small cell lung cancer ( 14 ) , non-small cell lung adenocarcinoma ( 5 ) , lymphoma ( 8 ) , B cell lymphoma ( 12 ) , Burkitt's lymphoma ( 8 ) , non-Hodgkin's lymphoma ( 12 ) , ovarian cancer ( 7 ) , multiple myeloma ( 12 )
Relevant cell line - cell type - tissue:	293 (epithelial) [AT1 (human), transfection, AT1R stable transfected HEK293] ( 22 ) , 293 (epithelial) ( 23 ) , 293E (epithelial) ( 19 ) , A498 (renal) ( 24 ) , AML-193 (monocyte) ( 12 ) , BJAB (B lymphocyte) ( 8 ) , breast ( 2 , 7 ) , BT-20 (breast cell) ( 14 ) , BT-549 (breast cell) ( 14 ) , Calu 6 (pulmonary) ( 14 ) , CMK (megakaryoblast) ( 12 ) , CTS (myeloid) ( 12 ) , DOHH2 ('B lymphocyte, precursor') ( 12 ) , 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) ( 4 , 23 ) , HEL (erythroid) ( 12 ) , HeLa (cervical) ( 1 , 6 , 18 , 21 , 23 , 26 , 27 , 28 , 29 ) , HeLa S3 (cervical) ( 25 ) , HOP62 (pulmonary) ( 14 ) , HUES-9 ('stem, embryonic') ( 20 ) , Jurkat (T lymphocyte) ( 10 ) , K562 (erythroid) ( 26 ) , Kasumi-1 (myeloid) ( 12 ) , KG-1 (myeloid) ( 12 , 17 ) , LCLC-103H (pulmonary) ( 14 ) , LOU-NH91 (squamous) ( 14 ) , MCF-7 (breast cell) ( 14 , 30 ) , MDA-MB-231 (breast cell) ( 14 ) , MDA-MB-468 (breast cell) ( 14 , 30 ) , MV4-11 (macrophage) ( 12 ) , 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 ) , OPM-2 (plasma cell) ( 12 ) , ovary ( 7 ) , P31/FUJ (erythroid) ( 12 ) , PC9 (pulmonary) ( 5 , 14 ) , RL ('B lymphocyte, precursor') ( 12 ) , RPMI-8266 (plasma cell) ( 12 ) , SH-SY5Y (neural crest) ( 9 ) , SKBr3 (breast cell) ( 13 , 30 ) , SU-DHL-6 (B lymphocyte) ( 12 ) , U266 (plasma cell) ( 12 )

Upstream Regulation
Kinases, in vitro:	mTOR (human) ( 23 )
Treatments:	amino_acid_starvation ( 23 ) , BI_4834 ( 18 ) , LRRK2-IN-1 ( 9 ) , nocodazole ( 25 ) , rapamycin ( 23 ) , refeeding ( 23 ) , Torin1 ( 23 )

Downstream Regulation
Effects of modification on DAP:	activity, inhibited ( 23 )
Effects of modification on biological processes:	autophagy, altered ( 23 )

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 27184836 Curated Info
4	Franchin C, et al. (2015) Quantitative analysis of a phosphoproteome readily altered by the protein kinase CK2 inhibitor quinalizarin in HEK-293T cells. Biochim Biophys Acta 1854, 609-23 25278378 Curated Info
5	Tsai CF, et al. (2015) Large-scale determination of absolute phosphorylation stoichiometries in human cells by motif-targeting quantitative proteomics. Nat Commun 6, 6622 25814448 Curated Info
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	Rolland D, et al. (2014) Global phosphoproteomic profiling reveals distinct signatures in B-cell non-Hodgkin lymphomas. Am J Pathol 184, 1331-42 24667141 Curated Info
9	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
10	Mertins P, et al. (2013) Integrated proteomic analysis of post-translational modifications by serial enrichment. Nat Methods 10, 634-7 23749302 Curated Info
11	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
12	Casado P, et al. (2013) Phosphoproteomics data classify hematological cancer cell lines according to tumor type and sensitivity to kinase inhibitors. Genome Biol 14, R37 23628362 Curated Info
13	Imami K, et al. (2012) Temporal profiling of lapatinib-suppressed phosphorylation signals in EGFR/HER2 pathways. Mol Cell Proteomics 11, 1741-57 22964224 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	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
19	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
20	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
21	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
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	Koren I, Reem E, Kimchi A (2010) DAP1, a novel substrate of mTOR, negatively regulates autophagy. Curr Biol 20, 1093-8 20537536 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 20071362 Curated Info
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	Chen RQ, et al. (2009) CDC25B mediates rapamycin-induced oncogenic responses in cancer cells. Cancer Res 69, 2663-8 19276368 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	Ruse CI, et al. (2008) Motif-specific sampling of phosphoproteomes. J Proteome Res 7, 2140-50 18452278 Curated Info
30	Zougman A, Wiśniewski JR (2006) Beyond linker histones and high mobility group proteins: global profiling of perchloric acid soluble proteins. J Proteome Res 5, 925-34 16602700 Curated Info