Ser2

Site Information
______MsDNDDIEV SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 449307

In vivo Characterization
Methods used to characterize site in vivo:	[32P] bio-synthetic labeling ( 22 ) , immunoprecipitation ( 22 ) , mass spectrometry ( 1 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 ) , mutation of modification site ( 22 ) , phosphopeptide mapping ( 22 )
Disease tissue studied:	breast cancer ( 7 , 9 ) , breast ductal carcinoma ( 7 ) , 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 , 7 ) , cervical cancer ( 19 ) , cervical adenocarcinoma ( 19 ) , leukemia ( 12 ) , acute myelogenous leukemia ( 12 ) , lung cancer ( 9 ) , non-small cell lung cancer ( 9 ) , ovarian cancer ( 7 ) , melanoma skin cancer ( 5 )
Relevant cell line - cell type - tissue:	'muscle, skeletal' ( 13 ) , 293 (epithelial) [AT1 (human), transfection, AT1R stable transfected HEK293] ( 16 ) , 786-O (renal) [VHL (human), transfection] ( 4 ) , 786-O (renal) ( 4 ) , breast ( 1 , 7 ) , COS (fibroblast) ( 22 ) , Flp-In T-Rex-293 (epithelial) [PRKD1 (human), genetic knockin] ( 10 ) , Flp-In T-Rex-293 (epithelial) ( 10 ) , GM00130 (B lymphocyte) ( 18 ) , H2009 (pulmonary) ( 9 ) , H2077 (pulmonary) ( 9 ) , H2887 (pulmonary) ( 9 ) , H322M (pulmonary) ( 9 ) , HCC1359 (pulmonary) ( 9 ) , HCC1937 (breast cell) ( 9 ) , HCC2279 (pulmonary) ( 9 ) , HCC366 (pulmonary) ( 9 ) , HCC4006 (pulmonary) ( 9 ) , HCC78 (pulmonary) ( 9 ) , HCC827 (pulmonary) ( 9 ) , HeLa (cervical) ( 6 , 20 ) , HeLa S3 (cervical) ( 14 , 19 , 21 ) , HeLa_Meta (cervical) ( 17 ) , HeLa_Pro (cervical) ( 17 ) , HeLa_Telo (cervical) ( 17 ) , HOP62 (pulmonary) ( 9 ) , HUES-9 ('stem, embryonic') ( 15 ) , Jurkat (T lymphocyte) ( 8 ) , K562 (erythroid) ( 20 ) , KG-1 (myeloid) ( 12 ) , LCLC-103H (pulmonary) ( 9 ) , LOU-NH91 (squamous) ( 9 ) , MCF-7 (breast cell) ( 3 , 9 ) , MEF (fibroblast) ( 22 ) , NCI-H1395 (pulmonary) ( 9 ) , NCI-H1568 (pulmonary) ( 9 ) , NCI-H2030 (pulmonary) ( 9 ) , NCI-H2172 (pulmonary) ( 9 ) , NCI-H322 (pulmonary) ( 9 ) , NCI-H460 (pulmonary) ( 9 ) , NCI-H647 (pulmonary) ( 9 ) , ovary ( 7 ) , WM239A (melanocyte) ( 5 )

Upstream Regulation
Treatments:	metformin ( 3 ) , MG132_withdrawal ( 17 )

Downstream Regulation
Effects of modification on MAX iso2:	activity, inhibited ( 22 )
Effects of modification on biological processes:	transcription, altered ( 22 )

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	Sacco F, et al. (2016) Deep Proteomics of Breast Cancer Cells Reveals that Metformin Rewires Signaling Networks Away from a Pro-growth State. Cell Syst 2, 159-71 27135362 Curated Info
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 25850435 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	Mertins P, et al. (2013) Integrated proteomic analysis of post-translational modifications by serial enrichment. Nat Methods 10, 634-7 23749302 Curated Info
9	Klammer M, et al. (2012) Phosphosignature predicts dasatinib response in non-small cell lung cancer. Mol Cell Proteomics 11, 651-68 22617229 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	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	Santamaria A, et al. (2011) The Plk1-dependent phosphoproteome of the early mitotic spindle. Mol Cell Proteomics 10, M110.004457 20860994 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	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
17	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
18	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
19	Olsen JV, et al. (2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal 3, ra3 20068231 Curated Info
20	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
21	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
22	Koskinen PJ, et al. (1994) Max activity is affected by phosphorylation at two NH2-terminal sites. Cell Growth Differ 5, 313-20 8018564 Curated Info