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Sequence List Acetylome-Acetyltransferase JPT

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Acetylome - Acetyltransferase Microarray page 1 of 167 Sequence PEP_FLAG Protein name Uniprot IDs 1 AYGGLL-K(Ac)-DFTATD AC control peptide 3-ketoacyl-CoA thiolase, mitochondrial 2 SEDAVK-K(Ac)-HNFTPL AC control peptide 3-ketoacyl-CoA thiolase, mitochondrial 3 FVSFIS-K(Ac)-DSIQKS AC control peptide Enoyl-CoA delta isomerase 1, mitochondrial Q96DC0_HUMAN_00224;H3BP91_HUMAN_00275;ECI1_HUMAN_00266 4 EIFQHS-K(Ac)-YKVDFI AC control peptide 39S ribosomal protein L39, mitochondrial C9JG87_HUMAN_00224;RM39_HUMAN_00234 5 SMDALD-K(Ac)-VVQERE AC control peptide 39S ribosomal protein L47, mitochondrial RM47_HUMAN_00124;RM47_HUMAN_00034 6 NIGLGF-K(Ac)-TPKEAI AC control peptide 40S ribosomal protein S11 B7Z712_HUMAN_00082;C9JCQ4_HUMAN_00082;C9JL25_HUMAN_00124;E7ESH4_HUMAN_0008 7 DGVTVA-K(Ac)-SIDLKD AC control peptide 60 kDa heat shock protein, mitochondrial 2;E7EXB4_HUMAN_00082 8 EIIEGM-K(Ac)-FDRGYI AC control peptide 60 kDa heat shock protein, mitochondrial E7ESH4_HUMAN_00216;F5GWR2_HUMAN_00074 9 LNERLA-K(Ac)-LSDGVA AC control peptide 60 kDa heat shock protein, mitochondrial 10 YVLLSE-K(Ac)-KISSIQ AC control peptide 60 kDa heat shock protein, mitochondrial 11 VVTEIP-K(Ac)-EEKDPG AC control peptide 60 kDa heat shock protein, mitochondrial Q3B7A4_HUMAN_00077;F8VPE8_HUMAN_00063;F8VQY6_HUMAN_00077;F8VRK7_HUMAN_000 77;F8VS58_HUMAN_00077;F8VU65_HUMAN_00077;F8VW21_HUMAN_00057;F8VWS0_HUMAN_ 12 NNPALE-K(Ac)-LLPHIR AC control peptide 60S acidic ribosomal protein P0 00077;F8VWV4_HUMAN_00063;F8VZS0_HUMAN_00077;G3V210_HUMAN_00077 13 DKGALA-K(Ac)-LVEAIR AC control peptide 60S ribosomal protein L7a 14 IVKMLE-K(Ac)-YLKGED AC control peptide A-kinase anchor protein 8 15 NIEAMS-K(Ac)-LKPYFL AC control peptide Acetyl-CoA acetyltransferase, cytosolic 16 LEDLIV-K(Ac)-DGLTDV AC control peptide Acetyl-CoA acetyltransferase, mitochondrial 17 KRVDFS-K(Ac)-VPKLKT AC control peptide Acetyl-CoA acetyltransferase, mitochondrial F8W6G0_HUMAN_00328;ACACA_HUMAN_01522;ACACA_HUMAN_01502;ACACA_HUMAN_0161 18 NTPYVT-K(Ac)-DLLQSK AC control peptide Acetyl-CoA carboxylase 1 7 C9JZR4_HUMAN_00151;E9PB03_HUMAN_00179;F5GYF6_HUMAN_00150;H0Y6A0_HUMAN_000 19 KPNQAK-K(Ac)-GLGAKK AC control peptide ADP-ribosylation factor GTPase-activating protein 3 70 A6NCQ0_HUMAN_00042;A6NHE8_HUMAN_00042;A6NJU6_HUMAN_00042;C9JYY9_HUMAN_00 20 YMDPTG-K(Ac)-TRTWES AC control peptide ADP-sugar pyrophosphatase 042 21 GAKAFF-K(Ac)-GAWSNV AC control peptide ADP/ATP translocase 1 22 LGDCLV-K(Ac)-IYKSDG AC control peptide ADP/ATP translocase 2 23 GGKAFF-K(Ac)-GAWSNV AC control peptide ADP/ATP translocase 2 24 FLGGVD-K(Ac)-HTQFWR AC control peptide ADP/ATP translocase 3 25 VDSLYN-K(Ac)-AKKLTZ AC control peptide 26S proteasome non-ATPase regulatory subunit 11 26 TFEEIA-K(Ac)-SAKITV AC control peptide 26S proteasome non-ATPase regulatory subunit 13 B4DJ66_HUMAN_00233;PSD13_HUMAN_00300 27 KMHLAG-K(Ac)-TEQAKA AC control peptide 28 kDa heat- and acid-stable phosphoprotein 28 DIDKRG-K(Ac)-YDLLRS AC control peptide 28S ribosomal protein S22, mitochondrial G5E9V5_HUMAN_00257;G5E9W7_HUMAN_00217;H7C5L9_HUMAN_00087 29 QIKVQE-K(Ac)-YVWNKR AC control peptide 28S ribosomal protein S29, mitochondrial E7EM60_HUMAN_00173;RT29_HUMAN_00166 30 QSTLDA-K(Ac)-ATKAKS AC control peptide 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase 31 QRTKKN-K(Ac)-EEAAEY AC control peptide 40S ribosomal protein S6 32 IYIINL-K(Ac)-RTWEKL AC control peptide 40S ribosomal protein SA A6NE09_HUMAN_00052;C9J9K3_HUMAN_00052;C9JQR9_HUMAN_00052 33 SAVMDT-K(Ac)-KKKDVS AC control peptide 5-AMP-activated protein kinase subunit gamma-2 34 GNLNTY-K(Ac)-RLAIKL AC control peptide 6-phosphofructokinase type C Q5VSR7_HUMAN_00387;H0Y3P8_HUMAN_00384;B1APP6_HUMAN_00179 35 FNRTVS-K(Ac)-VDDFLA AC control peptide 6-phosphogluconate dehydrogenase, decarboxylating B4DQJ8_HUMAN_00025;F5H7U0_HUMAN_00038 B4DQJ8_HUMAN_00296;B4DV68_HUMAN_00125;F5H0L3_HUMAN_00255;F5H7U0_HUMAN_002 36 KLKGPQ-K(Ac)-FQFDGD AC control peptide 6-phosphogluconate dehydrogenase, decarboxylating 87 37 SGRLWS-K(Ac)-AIFAGY AC control peptide 60S ribosomal protein L35a C9K025_HUMAN_00008;F8WB72_HUMAN_00008;F8WBS5_HUMAN_00008 38 RKIEEI-K(Ac)-DFLLTA AC control peptide 60S ribosomal protein L38 B4DP82_HUMAN_00106;E7EWF1_HUMAN_00106;H3BM89_HUMAN_00012;H3BTP7_HUMAN_00 39 RMFAPT-K(Ac)-TWRRWH AC control peptide 60S ribosomal protein L4 106;H3BU31_HUMAN_00106 40 ZZMGFV-K(Ac)-VVKNKA AC control peptide 60S ribosomal protein L5 41 FDTEKE-K(Ac)-YEITEQ AC control peptide 60S ribosomal protein L6 42 FNGTFV-K(Ac)-LNKASI AC control peptide 60S ribosomal protein L7 A8MUD9_HUMAN_00084;C9JIJ5_HUMAN_00084 Acetylome - Acetyltransferase Microarray page 2 of 167 Sequence PEP_FLAG Protein name Uniprot IDs 43 NKVEEL-K(Ac)-KKYGIZ AC control peptide Acyl-CoA-binding protein ACBP_HUMAN_00099;ACBP_HUMAN_00083;ACBP_HUMAN_00124;ACBP_HUMAN_00143 44 PQVSES-K(Ac)-LZZZZZ AC control peptide Acyl-coenzyme A thioesterase 8 A6NDT2_HUMAN_00253;H7C5A7_HUMAN_00208 45 VPLVFP-K(Ac)-TYGESM AC control peptide Acyl-coenzyme A thioesterase 9, mitochondrial ACOT9_HUMAN_00374;ACOT9_HUMAN_00347;ACOT9_HUMAN_00416 46 EAVDIL-K(Ac)-TERLGH AC control peptide Adenosine deaminase E7EWH4_HUMAN_00014;F8VY04_HUMAN_00014;F8VZG5_HUMAN_00014;F8W1A4_HUMAN_00 014;G3V213_HUMAN_00014;F8VPP1_HUMAN_00014;KAD2_HUMAN_00014;KAD2_HUMAN_0001 47 AEPEYP-K(Ac)-GIRAVL AC control peptide Adenylate kinase 2, mitochondrial 4;KAD2_HUMAN_00014 Q5T0R1_HUMAN_00081;Q5T0R2_HUMAN_00081;Q5T0R3_HUMAN_00081;Q5T0R4_HUMAN_000 81;Q5T0R5_HUMAN_00081;Q5T0R6_HUMAN_00081;Q5T0R7_HUMAN_00081;Q5T0R9_HUMAN_ 48 MVHTGL-K(Ac)-LERALL AC control peptide Adenylyl cyclase-associated protein 1 00080;D3DPU2_HUMAN_00081;F5H6Z3_HUMAN_00058;CAP1_HUMAN_00080 49 KTELIQ-K(Ac)-AKLAEQ AC control peptide 14-3-3 protein theta B0AZS6_HUMAN_00038;E7EX29_HUMAN_00115;E7ESK7_HUMAN_00115;E7EX24_HUMAN_000 50 ASQAES-K(Ac)-VFYLKM AC control peptide 14-3-3 protein zeta/delta 40 51 CIFFEP-K(Ac)-ILYRAA AC control peptide 2-oxoisovalerate dehydrogenase subunit beta, mitochondria 52 ERHKIV-K(Ac)-EIHEQL AC control peptide 2-5-oligoadenylate synthase 2 53 LAKDFE-K(Ac)-AYKTVI AC control peptide 26S protease regulatory subunit 6B H0YJC0_HUMAN_00020;H0YJD2_HUMAN_00017;H0YJE9_HUMAN_00024;H0YJS8_HUMAN_000 54 KKLLEH-K(Ac)-EIDGRL AC control peptide 26S protease regulatory subunit 10B 21;H0YJT1_HUMAN_00030;H0YJY8_HUMAN_00026 55 LPKLYV-K(Ac)-LHYCVS AC control peptide 40S ribosomal protein S26 F8VZW7_HUMAN_00070;RS26L_HUMAN_00070 56 KVDENG-K(Ac)-ISRLRR AC control peptide Ubiquitin-40S ribosomal protein S27a UBC_HUMAN_00048;RS27A_HUMAN_00048;RL40_HUMAN_00048;B2RDW1_HUMAN_00048;B4 DV12_HUMAN_00048;Q96C32_HUMAN_00048;F5GXK7_HUMAN_00048;F5GYU3_HUMAN_00048 ;F5GYX6_HUMAN_00048;F5GZ39_HUMAN_00048;F5H041_HUMAN_00048;F5H265_HUMAN_000 48;F5H2Z3_HUMAN_00048;F5H388_HUMAN_00048;F5H4D8_HUMAN_00048;F5H6Q2_HUMAN_0 57 RLIFAG-K(Ac)-QLEDGR AC control peptide Polyubiquitin-B 0048;F5H747_HUMAN_00048;F5H7K6_HUMAN_00048;F5H7Y5_HUMAN_00048 58 GDETGA-K(Ac)-VERADG AC control peptide 40S ribosomal protein S3a D6RAT0_HUMAN_00212;D6R9B6_HUMAN_00130;H0Y9Y4_HUMAN_00193 59 ITPEEA-K(Ac)-YKLCKV AC control peptide 40S ribosomal protein S4, X isoform 60 VKEKYA-K(Ac)-YLPHSA AC control peptide 40S ribosomal protein S5 61 LADIMA-K(Ac)-RNQKPE AC control peptide 60S ribosomal protein L24 C9JNW5_HUMAN_00093;C9JXB8_HUMAN_00093 62 RREAKV-K(Ac)-FEERYK AC control peptide 60S ribosomal protein L27 63 HPGYFG-K(Ac)-VGMKHY AC control peptide 60S ribosomal protein L27a 64 VKPKEV-K(Ac)-PKIPKG AC control peptide 60S ribosomal protein L29 65 LVMKSG-K(Ac)-YVLGYK AC control peptide 60S ribosomal protein L30 E5RI99_HUMAN_00026;E5RJH3_HUMAN_00026 66 KKEELL-K(Ac)-QLDDLK AC control peptide 60S ribosomal protein L35 F2Z388_HUMAN_00019;H0Y3A0_HUMAN_00019 ACTA_HUMAN_00193;ACTG_HUMAN_00191;ACTH_HUMAN_00192;ACTC_HUMAN_00193;ACTS _HUMAN_00193;ACTBL_HUMAN_00192;B4DUI8_HUMAN_00148;B4DW52_HUMAN_00163;B4E33 5_HUMAN_00167;Q5T8M7_HUMAN_00158;E9PG30_HUMAN_00149;F5GYT4_HUMAN_00110;F5 H0N0_HUMAN_00149;F5H1C1_HUMAN_00158;POTEI_HUMAN_00891;POTEJ_HUMAN_00854;A 67 LTDYLM-K(Ac)-ILTERG AC control peptide Actin, cytoplasmic 1 CTBM_HUMAN_00191 68 NMFQIG-K(Ac)-MRYVSV AC control peptide Activated RNA polymerase II transcriptional coactivator p15 69 KNSSYG-K(Ac)-VEGFWS AC control peptide Activity-dependent neuroprotector homeobox protein B7TY16_HUMAN_00676;H0YJ11_HUMAN_00116;H0YJW3_HUMAN_00062;H7C5W8_HUMAN_00 70 HLRQYE-K(Ac)-SIVNYK AC control peptide Alpha-actinin-1 205;H9KV75_HUMAN_00611;ACTN1_HUMAN_00676;ACTN1_HUMAN_00676 71 SQQILE-K(Ac)-RAYICA AC control peptide Acyl-CoA dehydrogenase family member 9, mitochondria F8WAN8_HUMAN_00475;H0Y8Z9_HUMAN_00371 72 VRHLKT-K(Ac)-PSDEEM AC control peptide Acyl-CoA-binding protein ACBP_HUMAN_00036;ACBP_HUMAN_00020;ACBP_HUMAN_00061;ACBP_HUMAN_00080 [3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, Q96G95_HUMAN_00184;A8MY43_HUMAN_00184;E9PF13_HUMAN_00184;H3BS02_HUMAN_001 73 KHIEDE-K(Ac)-LVRYFL AC control peptide mitochondrial 84;H3BTL2_HUMAN_00175 [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, 74 PNDYFS-K(Ac)-EASKLY AC control peptide mitochondrial 75 GSGSKG-K(Ac)-GGEIQP AC control peptide 10 kDa heat shock protein, mitochondrial Acetylome - Acetyltransferase Microarray page 3 of 167 Sequence PEP_FLAG Protein name Uniprot IDs 76 ISSIEQ-K(Ac)-TERNEK AC control peptide 14-3-3 protein beta/alpha Q4VY19_HUMAN_00070;1433B_HUMAN_00068 77 ANTGES-K(Ac)-VFYYKM AC control peptide 14-3-3 protein epsilon 78 LLSVAY-K(Ac)-NVVGGR AC control peptide 14-3-3 protein theta 79 DLYHLI-K(Ac)-KAVAVR AC control peptide 40S ribosomal protein S13 H0YK46_HUMAN_00019;H0YN88_HUMAN_00019;RS17L_HUMAN_00019;H0YN73_HUMAN_0001
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    Table S2. List of proteins detected in anterior and posterior intestine pooled samples. Data on protein expression are mean ± SEM of 4 pools fed the experimental diets. The number of the contig in the Sea Bream Database (http://nutrigroup-iats.org/seabreamdb) is indicated. Contig Protein Description Symbol Anterior Posterior Ratio Ant/Pos C2_6629 1,4-alpha-glucan-branching enzyme GBE1 0.88±0.1 0.91±0.03 0.98 C2_4764 116 kDa U5 small nuclear ribonucleoprotein component EFTUD2 0.74±0.09 0.71±0.05 1.03 C2_299 14-3-3 protein beta/alpha-1 YWHAB 1.45±0.23 2.18±0.09 0.67 C2_268 14-3-3 protein epsilon YWHAE 1.28±0.2 2.01±0.13 0.63 C2_2474 14-3-3 protein gamma-1 YWHAG 1.8±0.41 2.72±0.09 0.66 C2_1017 14-3-3 protein zeta YWHAZ 1.33±0.14 4.41±0.38 0.30 C2_34474 14-3-3-like protein 2 YWHAQ 1.3±0.11 1.85±0.13 0.70 C2_4902 17-beta-hydroxysteroid dehydrogenase 14 HSD17B14 0.93±0.05 2.33±0.09 0.40 C2_3100 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 ABHD5 0.85±0.07 0.78±0.13 1.10 C2_15440 1-phosphatidylinositol phosphodiesterase PLCD1 0.65±0.12 0.4±0.06 1.65 C2_12986 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1 PLCD1 0.76±0.08 1.15±0.16 0.66 C2_4412 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 PLCG2 1.13±0.08 2.08±0.27 0.54 C2_3170 2,4-dienoyl-CoA reductase, mitochondrial DECR1 1.16±0.1 0.83±0.03 1.39 C2_1520 26S protease regulatory subunit 10B PSMC6 1.37±0.21 1.43±0.04 0.96 C2_4264 26S protease regulatory subunit 4 PSMC1 1.2±0.2 1.78±0.08 0.68 C2_1666 26S protease regulatory subunit 6A PSMC3 1.44±0.24 1.61±0.08
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus

    A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus

    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
  • 1 Metabolic Dysfunction Is Restricted to the Sciatic Nerve in Experimental

    1 Metabolic Dysfunction Is Restricted to the Sciatic Nerve in Experimental

    Page 1 of 255 Diabetes Metabolic dysfunction is restricted to the sciatic nerve in experimental diabetic neuropathy Oliver J. Freeman1,2, Richard D. Unwin2,3, Andrew W. Dowsey2,3, Paul Begley2,3, Sumia Ali1, Katherine A. Hollywood2,3, Nitin Rustogi2,3, Rasmus S. Petersen1, Warwick B. Dunn2,3†, Garth J.S. Cooper2,3,4,5* & Natalie J. Gardiner1* 1 Faculty of Life Sciences, University of Manchester, UK 2 Centre for Advanced Discovery and Experimental Therapeutics (CADET), Central Manchester University Hospitals NHS Foundation Trust, Manchester Academic Health Sciences Centre, Manchester, UK 3 Centre for Endocrinology and Diabetes, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK 4 School of Biological Sciences, University of Auckland, New Zealand 5 Department of Pharmacology, Medical Sciences Division, University of Oxford, UK † Present address: School of Biosciences, University of Birmingham, UK *Joint corresponding authors: Natalie J. Gardiner and Garth J.S. Cooper Email: [email protected]; [email protected] Address: University of Manchester, AV Hill Building, Oxford Road, Manchester, M13 9PT, United Kingdom Telephone: +44 161 275 5768; +44 161 701 0240 Word count: 4,490 Number of tables: 1, Number of figures: 6 Running title: Metabolic dysfunction in diabetic neuropathy 1 Diabetes Publish Ahead of Print, published online October 15, 2015 Diabetes Page 2 of 255 Abstract High glucose levels in the peripheral nervous system (PNS) have been implicated in the pathogenesis of diabetic neuropathy (DN). However our understanding of the molecular mechanisms which cause the marked distal pathology is incomplete. Here we performed a comprehensive, system-wide analysis of the PNS of a rodent model of DN.
  • Supplementary Materials

    Supplementary Materials

    1 Supplementary Materials: Supplemental Figure 1. Gene expression profiles of kidneys in the Fcgr2b-/- and Fcgr2b-/-. Stinggt/gt mice. (A) A heat map of microarray data show the genes that significantly changed up to 2 fold compared between Fcgr2b-/- and Fcgr2b-/-. Stinggt/gt mice (N=4 mice per group; p<0.05). Data show in log2 (sample/wild-type). 2 Supplemental Figure 2. Sting signaling is essential for immuno-phenotypes of the Fcgr2b-/-lupus mice. (A-C) Flow cytometry analysis of splenocytes isolated from wild-type, Fcgr2b-/- and Fcgr2b-/-. Stinggt/gt mice at the age of 6-7 months (N= 13-14 per group). Data shown in the percentage of (A) CD4+ ICOS+ cells, (B) B220+ I-Ab+ cells and (C) CD138+ cells. Data show as mean ± SEM (*p < 0.05, **p<0.01 and ***p<0.001). 3 Supplemental Figure 3. Phenotypes of Sting activated dendritic cells. (A) Representative of western blot analysis from immunoprecipitation with Sting of Fcgr2b-/- mice (N= 4). The band was shown in STING protein of activated BMDC with DMXAA at 0, 3 and 6 hr. and phosphorylation of STING at Ser357. (B) Mass spectra of phosphorylation of STING at Ser357 of activated BMDC from Fcgr2b-/- mice after stimulated with DMXAA for 3 hour and followed by immunoprecipitation with STING. (C) Sting-activated BMDC were co-cultured with LYN inhibitor PP2 and analyzed by flow cytometry, which showed the mean fluorescence intensity (MFI) of IAb expressing DC (N = 3 mice per group). 4 Supplemental Table 1. Lists of up and down of regulated proteins Accession No.