ࡱ > Ms bjbjMFMF ' /, /, k ; p p 1! 1! 1! 1! 1! E! E! E! E! 8 }! " E! V 2 +3 ( S3 S3 S3 .4 .4 .4 h
h 1! .4 .4 .4 .4 24 > 1! 1! S3 S3 ̑ > > > 64 R 1! S3 1! S3 > .4 > > 9I h 1! 1! QJ 7 E! = H I mJ |B 0 I r > r QJ > 1! QJ .4 .4 .4 p :
Supplementary data
Table 1: Comparison between the aggregation parameters for short-living and long-living proteins. The analysed population is the group of short-living protein, the reference population are the long-living proteins. ++ and indicate that the population has a distribution significantly (p ( 0.001) shifted to respectively higher or lower values than the reference population in the performed statistical test, idem for + and where p ( 0.01.
Kolmogorov-SmirnovMann-Whitney testAverage aggregation propensity (total Tango/length)++++Number of aggregating segments----Number of aggregating segments/lengthn.s.n.s.Length of aggregating segments++++Aggregation propensity of aggregating segments++++
Table 2: Lifetime data for disease-associated proteins. We show the lifetime values of the proteins from the Yen dataset ADDIN EN.CITE Yen200822217Yen, H. C.Xu, Q.Chou, D. M.Zhao, Z.Elledge, S. J.Department of Genetics, Center for Genetics and Genomics, Brigham and Women's Hospital, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA.Global protein stability profiling in mammalian cellsScienceScience918-233225903Amino Acids/analysisCell CycleCell LineDNA, ComplementaryFlow CytometryGreen Fluorescent Proteins/analysis/metabolismHalf-LifeHumansLuminescent Proteins/analysis/metabolismOligonucleotide Array Sequence AnalysisOpen Reading FramesProteasome Endopeptidase Complex/*metabolismProtein Biosynthesis*Protein StabilityProteins/genetics/*metabolismRNA, Messenger/genetics/metabolismRecombinant Fusion Proteins/metabolismTranscription, Genetic2008Nov 718988847http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18988847[1] on protein lifetime that are associated with protein deposition diseases.
Protein NamePSI scoreAggregation propensityAmyloid beta A4 precursor proteina2.843.54Apolipoprotein A-I2.345.13Atrial natriuretic factor2.207.37Insulin1.567.43Lithostathine-1-alpha2.2710.9Lysozyme C1.968.37Lactadherin2.841.43Major prion protein2.219.60Serum amyloid A protein1.7910.74Superoxide dismutase5.60.61Transthyretin2.1510.02Lactotransferrin2.625.25Glucagon1.9812.21Transforming growth factor-beta-induced protein ig-h31.963.11Apolipoprotein A-II1.6415.83TAR DNA-binding protein 432.114.02a The clearance rate of the Abeta peptide in blood is even higher with a reported half life of approximately 5 mins ADDIN EN.CITE Ghersi-Egea199625302530253017Ghersi-Egea, J. F.Gorevic, P. D.Ghiso, J.Frangione, B.Patlak, C. S.Fenstermacher, J. D.Department of Neurosurgery, State University of New York, Stony Brook, USA.Fate of cerebrospinal fluid-borne amyloid beta-peptide: rapid clearance into blood and appreciable accumulation by cerebral arteriesJ NeurochemJ Neurochem880-36721996/08/01Amyloid beta-Peptides/blood/cerebrospinal fluid/*metabolismAnimalsCerebral Arteries/*metabolismHumansMaleMetabolic Clearance RatePeptide Fragments/blood/cerebrospinal fluid/metabolismRatsRats, Sprague-Dawley1996Aug0022-3042 (Print)
0022-3042 (Linking)8764620http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8764620eng[2].
Table 3: Overview of the protein set used. From the Yen dataset ADDIN EN.CITE Yen200822217Yen, H. C.Xu, Q.Chou, D. M.Zhao, Z.Elledge, S. J.Department of Genetics, Center for Genetics and Genomics, Brigham and Women's Hospital, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA.Global protein stability profiling in mammalian cellsScienceScience918-233225903Amino Acids/analysisCell CycleCell LineDNA, ComplementaryFlow CytometryGreen Fluorescent Proteins/analysis/metabolismHalf-LifeHumansLuminescent Proteins/analysis/metabolismOligonucleotide Array Sequence AnalysisOpen Reading FramesProteasome Endopeptidase Complex/*metabolismProtein Biosynthesis*Protein StabilityProteins/genetics/*metabolismRNA, Messenger/genetics/metabolismRecombinant Fusion Proteins/metabolismTranscription, Genetic2008Nov 718988847http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18988847[1] on protein lifetime, we here show the lifetime values for the 611 proteins that fall in the extreme categories (longest and shortest lifetimes respectively). Where high resolution structural information is available in the Protein Structure Databank (PDB) ( HYPERLINK "http://www.pdb.org" http://www.pdb.org) ADDIN EN.CITE Berman200077717Berman, H. M.Westbrook, J.Feng, Z.Gilliland, G.Bhat, T. N.Weissig, H.Shindyalov, I. N.Bourne, P. E.Research Collaboratory for Structural Bioinformatics (RCSB), Rutgers University, Piscataway, NJ 08854-8087, USA. berman@rcsb.rutgers.eduThe Protein Data BankNucleic Acids ResNucleic Acids Res235-422811999/12/11*Databases, FactualInformation Storage and RetrievalInternetMagnetic Resonance SpectroscopyProtein ConformationProteins/*chemistry2000Jan 10305-1048 (Print)
0305-1048 (Linking)10592235http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10592235gkd090 [pii]eng[3] we indicate the PDBID.
gene_namePSIPDBID1433E_HUMAN6.492br91433G_HUMAN6.091433S_HUMAN5.881yz52AAA_HUMAN5.163k7w2B32_HUMAN1.852B51_HUMAN1.861zgl2DMB_HUMAN1.642bc42DOB_HUMAN1.983MG_HUMAN5.086PGD_HUMAN5.68ACO11_HUMAN1.88ACSF4_HUMAN1.60ADRM1_HUMAN1.84AER61_HUMAN1.72AMY2B_HUMAN1.65AMYP_HUMAN1.591b2yANFB_HUMAN1.781yk1ANGL7_HUMAN1.75ANKR1_HUMAN1.89ANR22_HUMAN1.77APOA2_HUMAN1.642ou1APOC2_HUMAN1.751sohAPOC3_HUMAN1.80APOL1_HUMAN1.50APOL4_HUMAN2.00ARH_HUMAN5.042g30ASPX_HUMAN1.76B2LA1_HUMAN1.623i1hB2MG_HUMAN1.593kyoC1QT6_HUMAN1.84CA109_HUMAN1.91CA128_HUMAN1.97CAH6_HUMAN1.75CAPZB_HUMAN1.66CATB_HUMAN1.783pbhCCKN_HUMAN1.36CCL21_HUMAN1.92CG034_HUMAN1.98CH004_HUMAN1.99CH059_HUMAN1.72CHD9_HUMAN1.37CHP1_HUMAN2.002e30CIDEA_HUMAN1.892eelCIDEC_HUMAN1.77CMTA2_HUMAN1.94CN128_HUMAN1.69CNOT7_HUMAN1.832d5rCOAC_HUMAN5.49CP052_HUMAN1.62CPSF5_HUMAN5.283bapCRIS2_HUMAN1.88CSH_HUMAN1.77CT024_HUMAN1.73CTRB1_HUMAN1.76CXCL6_HUMAN1.58CXL11_HUMAN1.601rjtCYHR1_HUMAN1.60CYTF_HUMAN1.612ch9DCUP_HUMAN5.643gvrDEF1_HUMAN1.553hjdDEXI_HUMAN1.36DHPR_HUMAN6.15DHRS7_HUMAN1.91DHX37_HUMAN1.97DJB11_HUMAN1.64DJC10_HUMAN1.93DNJB9_HUMAN1.58DNJC3_HUMAN1.55DPH5_HUMAN1.70DPYD_HUMAN1.85DSCR8_HUMAN1.74DUS22_HUMAN1.881wrmDYDC1_HUMAN1.76EGLN1_HUMAN1.553hquELAF_HUMAN1.852relEMAL4_HUMAN1.91F10A1_HUMAN1.55F19A4_HUMAN1.60FAM3A_HUMAN1.79FBX15_HUMAN1.94FIBG_HUMAN1.732a45FKBP7_HUMAN1.73FOSL2_HUMAN2.00GAGC1_HUMAN5.23GALA_HUMAN1.711smzGATA2_HUMAN1.53GGEE1_HUMAN5.42GHRL_HUMAN1.66GLHA_HUMAN1.851xwdGLUC_HUMAN1.983iolGLYC_HUMAN5.11GP175_HUMAN1.58GRAB_HUMAN1.761fq3HA2Q_HUMAN1.81HB25_HUMAN1.91HB2B_HUMAN1.821a6aHB2X_HUMAN1.91HES2_HUMAN1.70HIS3_HUMAN1.77HMGB4_HUMAN1.90HNMT_HUMAN1.932aoxHNRPG_HUMAN5.33IGF2_HUMAN1.80IL15_HUMAN1.57IL32_HUMAN1.66ILEU_HUMAN5.36ILF2_HUMAN5.58ILKAP_HUMAN5.92IMDH2_HUMAN6.181nfbIMPA1_HUMAN5.221imfING3_HUMAN1.971x4iING5_HUMAN1.993c6wINO1_HUMAN5.02INS_HUMAN1.565aiyIPP2_HUMAN5.45ISK1_HUMAN1.77ISK2_HUMAN1.392jxdISLR_HUMAN1.66K1609_HUMAN5.12K1C23_HUMAN5.99K6PF_HUMAN5.50K6PP_HUMAN6.04KATL2_HUMAN5.63KHDR2_HUMAN5.08KHDR3_HUMAN5.35KIME_HUMAN6.04KLK1_HUMAN1.71KLK10_HUMAN1.64KPCZ_HUMAN5.34KPYM_HUMAN5.033h6oKSYK_HUMAN6.283fqsLACB2_HUMAN5.32LBH_HUMAN1.79LC7L2_HUMAN5.29LCHN_HUMAN1.68LDOC1_HUMAN1.61LEG3_HUMAN5.042nn8LEGL_HUMAN1.542jj6LICH_HUMAN1.72LIPR1_HUMAN1.88LMCD1_HUMAN5.76LMNA_HUMAN5.091ivtLPXN_HUMAN5.14LRC28_HUMAN1.94LRSM1_HUMAN6.10LXN_HUMAN5.88LYPA1_HUMAN5.071fj2LYPA2_HUMAN5.35LYSC_HUMAN1.961c46LZTL1_HUMAN5.68M3K3_HUMAN1.732o2vM6PBP_HUMAN6.35MAGA8_HUMAN5.11MAGA9_HUMAN5.01MARE2_HUMAN5.94MATK_HUMAN1.671jwoMCH_HUMAN1.76MDM1_HUMAN1.75MGLL_HUMAN5.76MGMT_HUMAN5.58MIA_HUMAN1.701k0xMINA_HUMAN5.05MK_HUMAN1.741mknMK12_HUMAN5.811cm8MKNK2_HUMAN1.86MNDA_HUMAN6.212dbgMP2K2_HUMAN5.36MP2K3_HUMAN5.60MP2K6_HUMAN5.96MPPD2_HUMAN5.16MRE11_HUMAN1.92MRP_HUMAN6.34MT1E_HUMAN5.39MT1H_HUMAN5.39MT1M_HUMAN5.33MT1X_HUMAN5.44MT3_HUMAN5.48MTF1_HUMAN5.40MTG8_HUMAN5.322knhMTHFS_HUMAN5.14MYCT1_HUMAN1.70MYEOV_HUMAN1.97MYOME_HUMAN1.94NADK_HUMAN5.61NASP_HUMAN5.65NCALD_HUMAN5.121bjfNCK2_HUMAN5.661u5sNDKA_HUMAN5.642hvdNDRG4_HUMAN5.02NEIL1_HUMAN5.46NF2L2_HUMAN2.002fluNMB_HUMAN1.981c9aNNAT_HUMAN1.71NOE1_HUMAN1.95NP1L1_HUMAN5.50NPC2_HUMAN1.53NPY_HUMAN1.631ronNRF1_HUMAN5.28NSF1C_HUMAN5.181ss6NTF2_HUMAN5.621ounNTKL_HUMAN5.11NUD11_HUMAN5.45NUDC_HUMAN5.17NUDT3_HUMAN5.09NXF1_HUMAN5.361oaiOCAD2_HUMAN1.92OGT1_HUMAN5.38OXSR1_HUMAN5.012vwiP2R3B_HUMAN1.89P53_HUMAN5.112ocjP5CR3_HUMAN5.38PA1B2_HUMAN5.301vyhPA1B3_HUMAN5.60PA21B_HUMAN1.48PA2GD_HUMAN1.61PACN1_HUMAN5.78PACN2_HUMAN5.15PAK7_HUMAN5.20PANK2_HUMAN1.84PAPS2_HUMAN5.312ax4PCGF3_HUMAN2.00PCY2_HUMAN5.313elbPDCD5_HUMAN5.022cruPDCL2_HUMAN5.46PDCL3_HUMAN5.65PDE1B_HUMAN6.14PDLI1_HUMAN5.11PDYN_HUMAN1.95PENK_HUMAN1.82PEPD_HUMAN6.04PFD2_HUMAN5.17PFD4_HUMAN5.35PG12A_HUMAN1.92PGAM2_HUMAN6.36PGM1_HUMAN6.04PIP_HUMAN1.913es6PIPNB_HUMAN5.08PMM2_HUMAN5.552q4rPP1R8_HUMAN5.16PP2BA_HUMAN5.311auiPPCT_HUMAN5.141ln3PPIL1_HUMAN5.09PPIP1_HUMAN5.92PPM1A_HUMAN5.97PPM1G_HUMAN5.13PPR1A_HUMAN5.82PPR1B_HUMAN5.69PROF1_HUMAN5.55PROSC_HUMAN5.53PRP4_HUMAN5.23PRPS1_HUMAN5.653efhPRS7_HUMAN5.23PSD10_HUMAN5.581uohPSME2_HUMAN5.14PSPC_HUMAN1.84PTBP2_HUMAN6.092cq1PTN7_HUMAN5.27PUR6_HUMAN6.062h31PURA2_HUMAN1.492v40PYGB_HUMAN5.44R3GEF_HUMAN5.36RAB7B_HUMAN1.94RAF1_HUMAN5.573lb7RAN_HUMAN5.603ch5RB15B_HUMAN5.02RBBP9_HUMAN5.54RBM3_HUMAN5.28RBM5_HUMAN5.34RBMS1_HUMAN5.05RCC1_HUMAN5.68REG3A_HUMAN1.781uv0RFA2_HUMAN5.382pqaRFA3_HUMAN1.312z6kRIFK_HUMAN6.12RIR1_HUMAN5.132wghRL10L_HUMAN1.68RL13A_HUMAN1.95RL23_HUMAN1.78RL23A_HUMAN1.692zkrRL27_HUMAN1.63RL28_HUMAN1.83RL30_HUMAN5.402zkrRL5_HUMAN1.76RL8_HUMAN1.59RLA1_HUMAN5.032jdlRLBP1_HUMAN5.66RM33_HUMAN1.923iy9RM42_HUMAN1.96RN111_HUMAN1.49RNF26_HUMAN1.91RNF32_HUMAN1.72RNPS1_HUMAN5.42RNS11_HUMAN1.62RNT2_HUMAN1.77ROP1B_HUMAN1.93RPE_HUMAN5.26RPIA_HUMAN5.21RS12_HUMAN5.48RS4Y1_HUMAN1.91RSPO2_HUMAN1.77RUSD2_HUMAN5.52RWDD1_HUMAN5.212ebmS10A7_HUMAN5.00SAA_HUMAN1.79SAPS3_HUMAN6.47SCLY_HUMAN6.36SCRG1_HUMAN1.66SDCG3_HUMAN5.29SDSL_HUMAN5.20SELT_HUMAN1.48SENP8_HUMAN5.431xt9SERC_HUMAN5.88SF3B4_HUMAN5.02SFRS4_HUMAN5.28SFRS7_HUMAN5.132hvzSHC1_HUMAN6.531shcSHLB2_HUMAN5.09SIAS_HUMAN5.471wvoSIL1_HUMAN1.53SMAD4_HUMAN6.30SMR3B_HUMAN1.64SNRPA_HUMAN5.451oiaSNURF_HUMAN5.71SNX16_HUMAN5.57SNX17_HUMAN5.323luiSNX9_HUMAN5.502rakSODC_HUMAN5.603ecuSPB6_HUMAN5.46SPB9_HUMAN6.13SPI2_HUMAN1.77SPIR1_HUMAN1.97SPOP_HUMAN1.753ivvSPS1_HUMAN5.653fd6SSA27_HUMAN5.17SSBP3_HUMAN5.15ST2B1_HUMAN5.921q22ST32B_HUMAN5.03STIP1_HUMAN5.931elrSTMN1_HUMAN6.31STRAP_HUMAN5.22STUB1_HUMAN5.20SUMO2_HUMAN6.122awtSUMO3_HUMAN5.462io1SURF2_HUMAN5.13SUV91_HUMAN5.22SYAP1_HUMAN5.151x3aSYNC_HUMAN6.06SYTC_HUMAN5.291wwtSYUG_HUMAN5.94SYWC_HUMAN5.662qukTALDO_HUMAN5.131f05TBB3_HUMAN5.05TBB4_HUMAN5.05TBB5_HUMAN5.19TBB6_HUMAN5.04TBCC_HUMAN5.332yuhTBCE_HUMAN5.81TBE_HUMAN5.19TBRG1_HUMAN1.66TCTA_HUMAN1.69TEBP_HUMAN5.771ejfTETN_HUMAN1.841tn3TEX12_HUMAN1.83TFF1_HUMAN1.751hi7TFF2_HUMAN1.59TFG_HUMAN5.14TFIP8_HUMAN5.13TFPI1_HUMAN1.781adzTGFA1_HUMAN5.11THOC3_HUMAN5.12THOP1_HUMAN5.36THTPA_HUMAN6.07THUM1_HUMAN5.732dirTHUM3_HUMAN5.13TKN1_HUMAN1.712b19TNF13_HUMAN1.88TPD52_HUMAN5.54TPD54_HUMAN6.07TPIS_HUMAN6.442jk2TRBP2_HUMAN5.362cpnTRI38_HUMAN5.57TSG6_HUMAN1.752pf5TTC19_HUMAN1.88TTC4_HUMAN5.67TXD12_HUMAN1.861senTXND3_HUMAN5.94TYB10_HUMAN5.90U2AF2_HUMAN5.081u2fUAP1_HUMAN6.001jvgUB2Q1_HUMAN1.832qgxUB2Q2_HUMAN1.86UB2R2_HUMAN1.69UBE2U_HUMAN1.581yrvUBP12_HUMAN1.92UCHL1_HUMAN5.75UCHL3_HUMAN6.111xd3UFM1_HUMAN5.261wxsUROK_HUMAN2.003ig6UTP11_HUMAN1.56VIME_HUMAN5.161gk4VINEX_HUMAN5.492ct3WD51A_HUMAN5.41WDR33_HUMAN1.70WDR5_HUMAN5.522gnqWDR62_HUMAN5.40WIBG_HUMAN5.82WIF1_HUMAN1.72WWP2_HUMAN5.34XRCC4_HUMAN5.39ZBP1_HUMAN1.933eyiZC3HA_HUMAN5.38ZCH10_HUMAN5.08ZCH12_HUMAN1.90ZCH13_HUMAN5.62ZG16_HUMAN1.79ZMAT5_HUMAN1.84ZMY10_HUMAN5.332d8qZN616_HUMAN1.69ZNF18_HUMAN5.06ZNF85_HUMAN1.82Table 4: Overview of the chaperone set. This table contains the chaperones used in the IntAct ADDIN EN.CITE ADDIN EN.CITE.DATA [4] interaction study, represented by their accession number, entry name and UniProt comment.
sHSPAccession Entry name Uniprot commentsP04792HSPB1_HUMANHeat shock protein beta-1 (HspB1) (Heat shock 27 kDa protein) (HSP 27) (Stress-responsive protein 27) (SRP27) (Estrogen-regulated 24 kDa protein) (28 kDa heat shock protein)A8KAH6A8KAH6_HUMANHeat shock 27kDa protein 2, isoform CRA_a (Heat-shock protein beta-2) (cDNA FLJ77220, highly similar to Homo sapiens heat shock 27kDa protein 2 (HSPB2), mRNA)Q6ICS9Q6ICS9_HUMANHSPB3 protein (Heat shock 27kDa protein 3) (cDNA, FLJ94950, Homo sapiens heat shock 27kDa protein 3 (HSPB3), mRNA) (Fragment)P02489CRYAA_HUMANAlpha-crystallin A chain (Heat shock protein beta-4) (HspB4) [Cleaved into: Alpha-crystallin A chain, short form]P02511CRYAB_HUMANAlpha-crystallin B chain (Alpha(B)-crystallin) (Rosenthal fiber component) (Heat shock protein beta-5) (HspB5) (Renal carcinoma antigen NY-REN-27)O14558HSPB6_HUMANHeat shock protein beta-6 (HspB6) (Heat shock 20 kDa-like protein p20)Q9UBY9HSPB7_HUMANHeat shock protein beta-7 (HspB7) (Cardiovascular heat shock protein) (cvHsp)Q9UJY1HSPB8_HUMANHeat shock protein beta-8 (HspB8) (Alpha-crystallin C chain) (Small stress protein-like protein HSP22) (E2-induced gene 1 protein) (Protein kinase H11)Q9BQS6HSPB9_HUMANHeat shock protein beta-9 (HspB9) (Cancer/testis antigen 51) (CT51)Q9Y547HSB11_HUMANHeat shock protein beta-11 (Hspb11) (Placental protein 25) (PP25)
Hsp40AccessionEntryUniprot commentsP31689DNJA1_HUMANDnaJ homolog subfamily A member 1 (Heat shock 40 kDa protein 4) (DnaJ protein homolog 2) (HDJ-2) (HSJ-2) (HSDJ)O60884DNJA2_HUMANDnaJ homolog subfamily A member 2 (HIRA-interacting protein 4) (Cell cycle progression restoration gene 3 protein) (Dnj3) (Dj3) (Renal carcinoma antigen NY-REN-14)Q96EY1DNJA3_HUMANDnaJ homolog subfamily A member 3, mitochondrial (Tumorous imaginal discs protein Tid56 homolog) (DnaJ protein Tid-1) (hTid-1) (Hepatocellular carcinoma-associated antigen 57)Q6AW87Q6AW87_HUMANPutative uncharacterized protein DKFZp686G2074 (DnaJ (Hsp40) homolog, subfamily A, member 4, isoform CRA_b)Q5F1R6DJC21_HUMANDnaJ homolog subfamily C member 21 (DnaJ homolog subfamily A member 5) (Protein GS3)P25685DNJB1_HUMANDnaJ homolog subfamily B member 1 (Heat shock 40 kDa protein 1) (Heat shock protein 40) (HSP40) (DnaJ protein homolog 1) (HDJ-1)P25686DNJB2_HUMANDnaJ homolog subfamily B member 2 (Heat shock 40 kDa protein 3) (DnaJ protein homolog 1) (HSJ-1)Q9UDY4DNJB4_HUMANDnaJ homolog subfamily B member 4 (Heat shock 40 kDa protein 1 homolog) (Heat shock protein 40 homolog) (HSP40 homolog) (Human liver DnaJ-like protein)O75953DNJB5_HUMANDnaJ homolog subfamily B member 5 (Heat shock protein Hsp40-3) (Heat shock protein cognate 40) (Hsc40) (Hsp40-2)O75190DNJB6_HUMANDnaJ homolog subfamily B member 6 (Heat shock protein J2) (HSJ-2) (MSJ-1) (HHDJ1) (MRJ)Q7Z6W7DNJB7_HUMANDnaJ homolog subfamily B member 7Q8NHS0DNJB8_HUMANDnaJ homolog subfamily B member 8Q9UBS3DNJB9_HUMANDnaJ homolog subfamily B member 9 (Microvascular endothelial differentiation gene 1 protein) (Mdg-1)Q9UBS4DJB11_HUMANDnaJ homolog subfamily B member 11 (ER-associated dnaJ protein 3) (ERj3p) (ERdj3) (ER-associated Hsp40 co-chaperone) (ER-associated DNAJ) (HEDJ) (hDj9) (PWP1-interacting protein 4) (APOBEC1-binding protein 2) (ABBP-2)Q9NXW2DJB12_HUMANDnaJ homolog subfamily B member 12Q8TBM8DJB14_HUMANDnaJ homolog subfamily B member 14Q5T1X3Q5T1X3_HUMANDnaJ (Hsp40) homolog, subfamily C, member 1 (Fragment)Q99543DNJC2_HUMANDnaJ homolog subfamily C member 2 (Zuotin-related factor 1) (M-phase phosphoprotein 11)Q13217DNJC3_HUMANDnaJ homolog subfamily C member 3 (Interferon-induced, double-stranded RNA-activated protein kinase inhibitor) (Protein kinase inhibitor of 58 kDa) (Protein kinase inhibitor p58)Q9NNZ3DNJC4_HUMANDnaJ homolog subfamily C member 4 (Multiple endocrine neoplasia type 1 candidate protein number 18) (DnaJ-like protein HSPF2)Q9H3Z4DNJC5_HUMANDnaJ homolog subfamily C member 5 (Cysteine string protein) (CSP)Q9UF47DNJ5B_HUMANDnaJ homolog subfamily C member 5B (Beta cysteine string protein) (Beta-CSP)Q8N7S2DNJ5G_HUMANDnaJ homolog subfamily C member 5G (Gamma-cysteine string protein) (Gamma-CSP)O75061AUXI_HUMANPutative tyrosine-protein phosphatase auxilin (EC 3.1.3.48) (DnaJ homolog subfamily C member 6)Q99615DNJC7_HUMANDnaJ homolog subfamily C member 7 (Tetratricopeptide repeat protein 2) (TPR repeat protein 2)O75937DNJC8_HUMANDnaJ homolog subfamily C member 8 (Splicing protein spf31)Q8WXX5DNJC9_HUMANDnaJ homolog subfamily C member 9 (DnaJ protein SB73)Q8IXB1DJC10_HUMANDnaJ homolog subfamily C member 10 (ER-resident protein ERdj5) (Macrothioredoxin) (MTHr)Q9NVH1DJC11_HUMANDnaJ homolog subfamily C member 11Q5JVQ1Q5JVQ1_HUMANJ domain containing protein 1 (JDP1) (DnaJ (Hsp40) homolog, subfamily C, member 12, isoform CRA_c)O75165DJC13_HUMANDnaJ homolog subfamily C member 13 (Required for receptor-mediated endocytosis 8) (RME-8)Q6Y2X3DJC14_HUMANDnaJ homolog subfamily C member 14 (Dopamine receptor-interacting protein of 78 kDa) (DRiP78) (DnaJ protein homolog 3) (HDJ-3)Q9Y5T4DJC15_HUMANDnaJ homolog subfamily C member 15 (Methylation-controlled J protein) (MCJ) (Cell growth-inhibiting gene 22 protein)Q5TDH4Q5TDH4_HUMANDnaJ (Hsp40) homolog, subfamily C, member 16Q9NVM6DJC17_HUMANDnaJ homolog subfamily C member 17Q9H819DJC18_HUMANDnaJ homolog subfamily C member 18Q96DA6TIM14_HUMANMitochondrial import inner membrane translocase subunit TIM14 (DnaJ homolog subfamily C member 19)Q8IWL3HSC20_HUMANCo-chaperone protein HscB, mitochondrial (DnaJ homolog subfamily C member 20) (Hsc20)Q5F1R6DJC21_HUMANDnaJ homolog subfamily C member 21 (DnaJ homolog subfamily A member 5) (Protein GS3)Q8N4W6DJC22_HUMANDnaJ homolog subfamily C member 22Q9H1X3DJC25_HUMANDnaJ homolog subfamily C member 25Q9NX36DJC28_HUMANDnaJ homolog subfamily C member 28
Hsp70AccesionEntry_nameUniprot commentsP08107HSP71_HUMANHeat shock 70 kDa protein 1 (HSP70.1) (HSP70-1/HSP70-2)P34931HS71L_HUMANHeat shock 70 kDa protein 1L (Heat shock 70 kDa protein 1-like) (Heat shock 70 kDa protein 1-Hom) (HSP70-Hom)P54652HSP72_HUMANHeat shock-related 70 kDa protein 2 (Heat shock 70 kDa protein 2)P34932HSP74_HUMANHeat shock 70 kDa protein 4 (Heat shock 70-related protein APG-2) (HSP70RY)P11021GRP78_HUMAN78 kDa glucose-regulated protein (GRP 78) (Heat shock 70 kDa protein 5) (Immunoglobulin heavy chain-binding protein) (BiP) (Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78)P17066HSP76_HUMANHeat shock 70 kDa protein 6 (Heat shock 70 kDa protein B')P48741HSP77_HUMANPutative heat shock 70 kDa protein 7 (Heat shock 70 kDa protein B)P11142HSP7C_HUMANHeat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8)P38646GRP75_HUMANStress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP 75) (Heat shock 70 kDa protein 9) (Peptide-binding protein 74) (PBP74) (Mortalin) (MOT)P48723HSP13_HUMANHeat shock 70 kDa protein 13 (Stress 70 protein chaperone microsome-associated 60 kDa protein) (Microsomal stress 70 protein ATPase core)
Hsp90AccessionEntryUniprot commentsP07900HS90A_HUMANHeat shock protein HSP 90-alpha (HSP 86) (Renal carcinoma antigen NY-REN-38)Q14568HS902_HUMANPutative heat shock protein HSP 90-alpha A2 (Heat shock 90 kDa protein 1 alpha-like 3)Q58FG1HS904_HUMANPutative heat shock protein HSP 90-alpha A4 (Heat shock protein 90-alpha D) (Heat shock protein 90Ad) (Heat shock 90 kDa protein 1 alpha-like 2)Q58FG0HS905_HUMANPutative heat shock protein HSP 90-alpha A5 (Heat shock protein 90-alpha E) (Heat shock protein 90Ae)O75322O75322_HUMANRaf activator, no geldanamycin binding region, overexpressed in pancreatic carcinomasP08238HS90B_HUMANHeat shock protein HSP 90-beta (HSP 90) (HSP 84)Q58FF8H90B2_HUMANPutative heat shock protein HSP 90-beta 2 (Heat shock protein 90-beta b) (Heat shock protein 90Bb)Q58FF7H90B3_HUMANPutative heat shock protein HSP 90-beta-3 (Heat shock protein 90-beta c) (Heat shock protein 90Bc)Q58FF6H90B4_HUMANPutative heat shock protein HSP 90-beta 4P14625ENPL_HUMANEndoplasmin (Heat shock protein 90 kDa beta member 1) (94 kDa glucose-regulated protein) (GRP94) (gp96 homolog) (Tumor rejection antigen 1)Q96GW1Q96GW1_HUMANHSP90B1 proteinQ58FF3ENPLL_HUMANPutative endoplasmin-like protein (Putative heat shock protein 90 kDa beta member 2)Q58FF2Q58FF2_HUMANHeat shock protein 94cQ12931TRAP1_HUMANHeat shock protein 75 kDa, mitochondrial (HSP 75) (Tumor necrosis factor type 1 receptor-associated protein) (TRAP-1) (TNFR-associated protein 1)
ADDIN EN.REFLIST 1. Yen HC, Xu Q, Chou DM, Zhao Z, Elledge SJ (2008) Global protein stability profiling in mammalian cells. Science 322: 918-923.
2. Ghersi-Egea JF, Gorevic PD, Ghiso J, Frangione B, Patlak CS, et al. (1996) Fate of cerebrospinal fluid-borne amyloid beta-peptide: rapid clearance into blood and appreciable accumulation by cerebral arteries. J Neurochem 67: 880-883.
3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, et al. (2000) The Protein Data Bank. Nucleic Acids Res 28: 235-242.
4. Aranda B, Achuthan P, Alam-Faruque Y, Armean I, Bridge A, et al. (2010) The IntAct molecular interaction database in 2010. Nucleic Acids Res 38: D525-531.
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