Ser39

Site Information
TTsTRTysLGsALRP SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 451766

In vivo Characterization
Methods used to characterize site in vivo:	mass spectrometry ( 4 , 5 , 6 , 8 , 9 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 20 , 21 , 22 , 23 , 24 ) , mutation of modification site ( 7 , 10 , 25 ) , phospho-antibody ( 1 , 7 , 19 , 26 ) , western blotting ( 1 , 7 , 19 , 26 )
Disease tissue studied:	adrenal cancer ( 7 ) , bladder cancer ( 25 ) , neuroblastoma ( 18 , 26 ) , melanoma skin cancer ( 23 )
Relevant cell line - cell type - tissue:	'3T3-L1, differentiated' (adipocyte) ( 5 , 8 , 12 ) , 'fat, brown' ( 21 ) , 3T3 (fibroblast) ( 19 ) , BaF3 ('B lymphocyte, precursor') [JAK3 (human), transfection] ( 4 ) , brain ( 21 ) , epithelial-lens [Vimentin (mouse), genetic knockin] ( 10 ) , heart ( 13 , 21 ) , Hepa 1-6 (epithelial) ( 24 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 9 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 9 ) , HL-1 (myocyte) ( 9 ) , kidney ( 21 ) , liver ( 11 , 15 , 21 ) , liver [leptin (mouse), homozygous knockout] ( 15 ) , lung ( 21 ) , macrophage-bone marrow ( 1 , 22 ) , macrophage-bone marrow [DUSP1 (mouse), homozygous knockout] ( 22 ) , macrophage-peritoneum ( 1 , 14 ) , MC3T3-E1 (preosteoblast) ( 6 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 16 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 17 ) , N1E-115 (neuron) ( 18 ) , Neuro-2a (neuron) ( 26 ) , pancreas ( 21 ) , skin [mGluR1 (mouse), transgenic, TG mutant mice] ( 23 ) , spleen ( 21 ) , SW13 (adrenal) ( 7 ) , T lymphocyte-spleen ( 20 ) , T24 (bladder cell) ( 25 ) , testis ( 21 )

Upstream Regulation
Regulatory protein:	RAC1 (mouse) ( 19 ) , Vimentin (human) ( 7 )
Kinases, in vitro:	AurB (mouse) ( 25 ) , CAMK2A (rat) ( 27 ) , PKACA (mouse) ( 28 ) , PKCA (mouse) ( 28 )
Treatments:	calyculin_A ( 7 ) , insulin ( 12 ) , LDL_oxidized ( 1 ) , LPA ( 18 ) , LPS ( 22 ) , LY294002 ( 12 ) , MK-2206 ( 12 ) , okadaic_acid ( 26 ) , PTH(1-34) ( 6 ) , serum ( 19 ) , serum_withdrawal ( 19 )

Downstream Regulation
Effects of modification on Vimentin:	intracellular localization ( 1 )
Effects of modification on biological processes:	cell motility, altered ( 19 ) , cytoskeletal reorganization ( 19 , 25 )

References
1	Kim SY, et al. (2022) Plasma Membrane Localization of CD36 Requires Vimentin Phosphorylation; A Mechanism by Which Macrophage Vimentin Promotes Atherosclerosis. Front Cardiovasc Med 9, 792717 35656400 Curated Info
2	Ding I, et al. (2020) Cooperative roles of PAK1 and filamin A in regulation of vimentin assembly and cell extension formation. Biochim Biophys Acta Mol Cell Res 32389644 Curated Info
3	Yang CY, et al. (2019) Src and SHP2 coordinately regulate the dynamics and organization of vimentin filaments during cell migration. Oncogene 38 30696956 Curated Info
4	Degryse S, et al. (2017) Mutant JAK3 phosphoproteomic profiling predicts synergism between JAK3 inhibitors and MEK/BCL2 inhibitors for the treatment of T-cell acute lymphoblastic leukemia. Leukemia 32 28852199 Curated Info
5	Minard AY, et al. (2016) mTORC1 Is a Major Regulatory Node in the FGF21 Signaling Network in Adipocytes. Cell Rep 17, 29-36 27681418 Curated Info
6	Williams GR, et al. (2016) Exploring G protein-coupled receptor signaling networks using SILAC-based phosphoproteomics. Methods 92, 36-50 26160508 Curated Info
7	Robert A, et al. (2015) Vimentin filament precursors exchange subunits in an ATP-dependent manner. Proc Natl Acad Sci U S A 112, E3505-14 26109569 Curated Info
8	Parker BL, et al. (2015) Targeted phosphoproteomics of insulin signaling using data-independent acquisition mass spectrometry. Sci Signal 8, rs6 26060331 Curated Info
9	Reinartz M, Raupach A, Kaisers W, Gödecke A (2014) AKT1 and AKT2 induce distinct phosphorylation patterns in HL-1 cardiac myocytes. J Proteome Res 13, 4232-45 25162660 Curated Info
10	Matsuyama M, et al. (2013) Defect of mitotic vimentin phosphorylation causes microophthalmia and cataract via aneuploidy and senescence in lens epithelial cells. J Biol Chem 288, 35626-35 24142690 Curated Info
11	Wilson-Grady JT, Haas W, Gygi SP (2013) Quantitative comparison of the fasted and re-fed mouse liver phosphoproteomes using lower pH reductive dimethylation. Methods 61, 277-86 23567750 Curated Info
12	Humphrey SJ, et al. (2013) Dynamic Adipocyte Phosphoproteome Reveals that Akt Directly Regulates mTORC2. Cell Metab 17, 1009-20 23684622 Curated Info
13	Lundby A, et al. (2013) In vivo phosphoproteomics analysis reveals the cardiac targets of β-adrenergic receptor signaling. Sci Signal 6, rs11 23737553 Curated Info
14	Wu X, et al. (2012) Investigation of receptor interacting protein (RIP3)-dependent protein phosphorylation by quantitative phosphoproteomics. Mol Cell Proteomics 11, 1640-51 22942356 Curated Info
15	Grimsrud PA, et al. (2012) A quantitative map of the liver mitochondrial phosphoproteome reveals posttranslational control of ketogenesis. Cell Metab 16, 672-83 23140645 Curated Info
16	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
17	Yu Y, et al. (2011) Phosphoproteomic analysis identifies Grb10 as an mTORC1 substrate that negatively regulates insulin signaling. Science 332, 1322-6 21659605 Curated Info
18	Wang Y, et al. (2011) Spatial phosphoprotein profiling reveals a compartmentalized extracellular signal-regulated kinase switch governing neurite growth and retraction. J Biol Chem 286, 18190-201 21454597 Curated Info
19	Helfand BT, et al. (2011) Vimentin organization modulates the formation of lamellipodia. Mol Biol Cell 22, 1274-1289 21346197 Curated Info
20	Navarro MN, et al. (2011) Phosphoproteomic analysis reveals an intrinsic pathway for the regulation of histone deacetylase 7 that controls the function of cytotoxic T lymphocytes. Nat Immunol 12, 352-61 21399638 Curated Info
21	Huttlin EL, et al. (2010) A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 143, 1174-89 21183079 Curated Info
22	Weintz G, et al. (2010) The phosphoproteome of toll-like receptor-activated macrophages. Mol Syst Biol 6, 371 20531401 Curated Info
23	Zanivan S, et al. (2008) Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry. J Proteome Res 7, 5314-26 19367708 Curated Info
24	Pan C, Gnad F, Olsen JV, Mann M (2008) Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors. Proteomics 8, 4534-46 18846507 Curated Info
25	Goto H, et al. (2003) Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process. J Biol Chem 278, 8526-30 12458200 Curated Info
26	Nakamura Y, et al. (2000) Localized phosphorylation of vimentin by rho-kinase in neuroblastoma N2a cells. Genes Cells 5, 823-37 11029658 Curated Info
27	Ando S, et al. (1991) Evidence that Ser-82 is a unique phosphorylation site on vimentin for Ca2(+)-calmodulin-dependent protein kinase II. Biochem Biophys Res Commun 175, 955-62 1850997 Curated Info
28	Ando S, et al. (1989) Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. Biochemistry 28, 2974-9 2500966 Curated Info