Inventory of Supplemental information Supplementary table I related to figure 4. Supplementary figure 1 related to figure 1. Supplementary figure 2 related to figure 2. Supplementary figure 3 related to figure 3. Supplementary figure 4 related to figure 4. Supplementary figure 5 related to figure 4. Supplementary figure 6 related to figure 4. Supplementary figure 7 related to figure 5. Supplementary figure 8 related to figure 6. Supplementary figure 9 related to figure 7. Supplementary figure 10 related to figure 8. Supplementary figure 11 related to discussion. Supplementary experimental procedures. Supplementary table I. Senescence associated phosphoprotein degradation (SAPD) Peptide/ Protein Fold Functions (Phospho SitePlus) AF4 SSSPGKPQAVSSLNSSHSR 3.03 RNA pol II transcription (P(PMIDMID 21574958). Calcium and PKC signaling (PMID: 19497879) TVIRLPSGSGAASPTGSAVDIR (S210-p) 14 Actin cytoskeleton dynamics and pseudopodia AHNAK LKSEDGVEGDLGETQSR (S135-p) formation (PMID: 20388789). AKT1S1 SSDEENGPPSSPDLDR (S212-p) 2.36 AKT/Tor signaling, (PMID: 18372248) IYLEENPEKSETIQDTDTQSLVGSPSTR (S341-p) 1.4 Cell motility and invasion, (PMID: 17575049) ARHGEF12 HLSTPSSVSPEPQDSAK (S637) ARHGAP1 SSSPELVTHLK (S51-p) 1.8 Cdc42 and Rho signaling, (PMID: 16157885) ARHGAP17 SPSPPTQHTGQPPGQPSAPSQLSAPR (S676) 2.3 Rho signaling and cell polarity, (PMID: 16678097) VPPAPVPCPPPSPGPSAVPSSPKSVATEER (S377-p, S386-p) Chaperone in complex with Hsp70, (PMID: BAG3 SSTPLHSPSPIR (T285-p, S291) 9.2 12750378), mediates ERK inactivation by DUSP6, AASPFR (S264) (PMID: 22310281) Bind acetylated histones and stimulate transcription KADTTTPTPTAILAPGSPASPPGSLEPK (S298-p) * BRD2 (PMID: 18406326) CALD1 RGSIGENQGEEK (S202-p) 1.9 Cell migration and lamellipodia (PMID:16800003) Genomic stability, (PMID: 22363533). ERK target at ILQEKLDQPVSAPPSPR (S240-p, S244-p) 2.9 CCDC6 S244) (PMID: 14712216) ALVEFESNPEETREPGSPPSVQR (S47-p) RLGGLRPESPESLTSVSR (S18-p) 6.2 Nucleolar protein with coiled coil domain, (PMID: CCDC86 AGLGSPERPPK (S58-p) 17300783) LVINSGNGAVEDR (S686-p) LVINSGNGAVEDRKPSGLNGEASK (S697-p) Cell migration and lamellipodia component PMID: CD44 LVINSGNGAVEDRKPSGLNGEASK (S704-p) 9 12145196 KPSGLNGEASKSQEMVHLVNK (S706-p) KPSGLNGEASKSQEMVHLVNK (S697-p, S706-p) Cytoskeletal protein, cell motility, (PMID: Cortactin TQTPPVSPAPQPTEERLPSSPVYEDAASFK (T401-p, S405-p) 4.4 18406052), ERK1/2 target (S405), lamellipodia and N-WASP regulator, (PMID: 21079800) CYBRD1 NLALDEAGQRSTM (T285-p) 3.0 Iron metabolism (PMID: 18194661). LKNGFPHPEPDCNPSEAASEESNSEIEQEIPVEQK (S171-p) 12.3 Nucleolar RNA helicase, pre-rRNA processing, DDX21 VTKNEEPSEEEIDAPKPK (S121-p) (PMID: 19106111) SPGKAEAESDALPDDTVIESEALPSDIAAEAR (S287-p) 13.0 RNA helicase DDX24 AQAVSEEEEEEEGK (S82-p) DDX42 YMAENPTAGVVQEEEEDNLEYDSDGNPIAPTKK (S185-p) 1.7 RNA helicase Nucleolar component. Ribosomal RNA maturation, RVNDAEPGSPEAPQGK (S83-p) 2.6 DDX51 (PMID: 20404093) MHLPSPTDSNFYR (S991-p), EGFR GSHQISLDNPDYQQDFFPK (S1166-p) 10 Growth factor signaling GSHQISLDNPDYQQDFFPK (S1162-p) EIF3G GIPLATGDTSPEPELLPGAPLPPPKEVINGNIK (S42-p) 3.9 Translation initiation, (PMID: 17094969) TEPAAEAEAASGPSESPSPPAAEELPGSHAEPPVPAQGEAPGE QARDER (S85-p) 10 Translation initiation EIF3B TEPAAEAEAASGPSESPSPPAAEELPGSHAEPPVPAQGEAPGE QARDER (S81-p) SFSKEVEER (S1185-p), SFSKEVEER (S1187-p) EAALPPVSPLK 2.4 Protein synthesis (PMID: 9418880). EIF4G1 (S1231-p) EIF4G2 TQTPPLGQTPQLGLK (T506-p) 1.3 Protein synthesis Signaling and cell motility, S910 is phosphorylated FAK/PTK2 LQPQEISPPPTANLDR (S910-p) 2.3 by ERK, (PMID: 12692126), pseudopodia protein (PMID: 15985431) KMEESDEEAVQAK (S692-p) 9.5 Histone demethylase of K36H3, knockdown induces FBXL11 SCDEPLTPPPHSPTSMLQLIHDPVSPR (T713-p, S718-p) senescence (PMID: 18836456) Actin binding protein, RalA effector to induce LVSPGSANETSSILVESVTR (S-2478-p) 12 FLNB filopodia, (PMID: 10051605) hnRNA-binding protein, Ras and NF-kB signaling NLEELEEKSTTPPPAEPVSLPQEPPKPR (T227-p) 12 G3BP2 (PMID: 10969074) Nuclear protein, Methyl lysine histone binding ARGDSEALDEES (S664-p) 1.7 HDGF2 (PMID: 19162039) Stabilizes proteins against aggregation during cellular stress and mediate the folding of newly GGSGSGPTIEEVD (S631-p) 14.8 HSPA1A translated polypeptides (PMID: 21874533). Controls OIS (PMID: 19001088). Involved in stress resistance, actin organization AQLGGPEAAKSDETAAK (S199-p) (PMID: 19593530) and mitochondrial quality control QLSSGVSEIR (S82-p) 48.2 HSPB1 (PMID: 21641551). Phosphorylated by MAPKAP GPSWDPFRDWYPHSR (S15-p) kinase 2 at S15 and S82, (PMID: 1332886) Involved in translational control, mRNA localization QGSPVAAGAPAK (S181-p) 1.5 IGF2BP1 and cell migration (PMID: 22279049 RNA binding protein, nucleolar protein, CDK2 target DSSKGEDSAEETEAKPAVVAPAPVVEAVSTPSAAFPSDATAE at S382) (PMID: 18847512), regulates DNA damage QGPILTK (S482-p) 2.3 ILF3/NF90 repair and non-homologous end joining, (PMID: RPMEEDGEEKSPSK (S382-p) 21969602) Involved in the transport of phosphorylated LVSFHDDSDEDLLHI (S2484-p) lysosomal enzymes from the Golgi and the cell IGF2R/M6PR 2.6 TVSSTKLVSFHDDSDEDLLHI (S2484-p) surface to lysosomes (PMID: 20615935, 11058096, 2541923). Transcriptional repressor of IRF-2, (PMID: RKPSPEPEGEVGPPK (S360-p) IRF2BP2 12799427) Involved in cell adhesion to collagens, modulation of collagen and collagenase gene expression. It ITGA2 NPDEIDETTELSS (S1180-p) 1.7 regulates generation and organization of newly synthesized extracellular matrix (PMID: 2545729). JUN LASPELER (S73-p) 25 Transcription factor (PMID: 20132737). JunB SRDATPPVSPINMEDQER (T255-p) 1.4 Transcription factor (PMID: 20132737). Heterochromatin and gene repression (PMID: SRSGEGEVSGLMR (S473-p) 7 KAP1 STAPSAAASASASAAASSPAGGGAEALELLEHCGVCR (S50-p) 8769649). ETPHSPGVEDAPIAK (S490-p) Cystoskeletal protein, ERK target at S360, cell SEVQQPVHPKPLSPDSR (S362-p) 5 LIMA1/EPLIN motility, (PMID: 17875928) ASSLSESSPPK (S374-p) Nucleocytoplasmic shuttling protein (PMID: LMO7 ATLSSTSGLDLMSESGEGEISPQREVSR (S1026-p) 15 EVAATEEDVTRLPSPTSPFSSLSQDQAATSK (T990-p, S991-p) 17067998), cell migration, (PMID: 21670154) EVAATEEDVTRLPSPTSPFSSLSQDQAATSK (S988) SHSPSASQSGSQLR (S1593-p) LRWD1 ANSPEKPPEAGAAHKPR (S212-p) * Origin of replication, (PMID: 20932478) CLSPDDSTVK (S986-p) MASPPPSGPPSATHTPFHQSPVEEKSEPQDFQEADSWGDTK (S1013-p) WPEVSPEDTQSLSLSEESPSKETSLDVSSK (S1203-p) QLSPESLGTLQFGELNLGK (S1218-p) YLPGAITSPDEHILTPDSSFSK (S1311-p) WLAESPVGLPPEEEDKLTR (S1776-p) Structural protein that interacts with MAPK (PMID: 14 MAP1A SPFEIISPPASPPEMVGQR (S1797-p, S1801-p) 20936779). SPFEIISPPASPPEMVGQRVPSAPGQESPIPDPK (S1801-p) VPSAPGQESPIPDPK (S1818) NTSAEKELSSPISPK (S2019-p, S2022-p) GELSPSFLNPPLPPSIDDR (S2449-p) SPTPGKGPADR (S2629-p) DVMSDETNNEETESPSQEFVNITK (S1154-p) SPSLSPSPPSPLEK (S1262-p) SPSLSPSPPSPLEK (S1265-p) VSAEAEVAPVSPEVTQEVVEEHCASPEDK (S1298-p) ASVSPMDEPVPDSESPIEK (S1378-p, S1389-p) GAESPFEEKSGK (S1427) MAP1B QGSPDQVSPVSEMTSTSLYQDKQEGK (S1438-p, S1443-p) 6 Cytoskeleton (PMID: 17292797) KLGDVSPTQIDVSQFGSFK (S1501) VQSLEGEKLSPK (S1779-p) SDISPLTPR (S185) ESSPLYSPTFSDSTSAVKEK (S1793-p) ESSPLYSPTFSDSTSAVKEK (S1797-p) TATCHSSSSPPIDAASAEPYGFR (S1819-p) DMESPTKLDVTLAK (S280-p) DMESPTKLDVTLAK (T282-p) DMSPLSETEMALGKDVTPPPETEVVLIK (S507-p) DMSPLSETEMALGKDVTPPPETEVVLIK (S510-p) 29 Microtubules dynamics, (PMID:15840946) MAP4 DVTPPPETEVVLIK (T521-p) GISEDSHLESLQDVGQSAAPTFMISPETITGTGKK (S624-p) KCSLPAEEDSVLEK (S636-p) RASPSKPASAPASR (S793-p, S797-p) VGSTENIKHQPGGGR (S941-p) AAATPESQEPQAK (T148-p) 15 PKC signaling MARCKSL1 GDVTAEEAAGASPAKANGQENGHVK (S22-p) RVASGPSPGEGISPQSAQAPQAPGDNHVVPVLR (S873-p) MVP RVASGPSPGEGISPQSAQAPQAPGDNHVVPVLR (S867-p, S876- 3 Vault ribonucleoproteins p) TLLEAENSRLQTPGGGSK (T315-p) QEASTGQSPEDHASLAPPLSPDHSSLEAK (S471-p) Nestin 19 Cancer Stem cell marker (PMID: 20429619) TPTLASTPIPPTPQAPSPAVDAEIR (S398-p) ENQEPLRSPEVGDEEALRPLTK (S680-p) WEDTVEKDQELAQESPPGMAGVENEDEAELNLR (S965-p) EAARSPDKPGGSPSASR (S49-p) 10 Nucleolar protein, p53 inhibitor, (PMID: 16322561) NOC2L EAARSPDKPGGSPSASR (S49-p, S56-p) NOLC1 GGSISVQVNSIKFDSE (S698-p) 28 Pol1 coactivator, nucleologenesis (PMID: 7657714) NOL6/NRAP GQSPAGDGSPEPPTPR (S283-p) 7.5 Nucleolar protein (PMID: 11895476) Nucleolar protein, 60S biogenesis, (PMID: HIKEEPLSEEEPCTSTAIASPEK (S502-p) 23 NOP5 11583964) Nucleolar protein, 60S biogenesis, snoRNP FSKEEPVSSGPEEAVGK (S570-p) 21 NOP56 biogenesis, (PMID: 19620283) VVVSPTKK (S67-p) 20 Nucleolar protein and pol I cofactor, (PMID: Nucleolin LELQGPRGSPNAR (S563-p) 17130237), p53 inhibitor, (PMID: 22013067) NUP188 GAPSSPATGVLPSPQGK (S1708-p, S1717-p) 1.5 Nuclear pore, (PMID: 20566687) ODZ2 SLMYWMTVQYDSMGRVIK (S2181) 54 Tenascin family PDLIM4 IHIDPEIQDGSPTTSR (S112-p) 22 Cytoskeletal protein. Competes with other PH domain-containing proteins TAPAAPAEDAVAAAAAAPSEPSEPSRPSPQPKPRTP (S144-p) 9.6 to prevent their binding to membrane lipids (PMID: PHLDA2 TAPAAPAEDAVAAAAAAPSEPSEPSRPSPQPKPRTP (T160-p) 9403053). VADAKGDSESEEDEDLEVPVPSR (S78-p, S80-p) 11 Regulatory subunit of cAMP-regulated kinase PRKAR2A RVSVCAETYNPDEEEEDTDPR (S99-p) KEESEESDDDMGFGLFD (S104-p) 3.4 Structural component of ribosome (PMID: RPLP1 KEESEESDDDMGFGLFD (S101-p) 54.7 16572171), bypass senescence (PMID: 19233166). Ribosomal protein RPL23 IRTSPTFR (S43-p) 35 Actin cytoskeleton dynamics and pseudopodia formation (PMID: 20388789). RRBP1 SHVEDGDIAGAPASSPEAPPAEQDPVQLK (S1277-p) 6 Binding of ribosomes to the ER, (PMID: 22156060) Nucleolar protein. Inhibits PTEN and p27 and is RSL1D1 (CSIG) downregulated in replicative senescence (PMID: ATNESEDEIPQLVPIGK (S361-p) 2.4 IPI00642046 18678645). Regulates nucleostemin localization (PMID: 17158916). SCAMP2