Post-translational modifications in proteins: resources, tools and prediction methods

Posttranslational modifications (PTMs) refer to amino acid side chain modification in some proteins after their biosynthesis. There are more than 400 different types of PTMs affecting many aspects of protein functions. Such modifications happen as crucial molecular regulatory mechanisms to regulate...

Full description

Saved in:
Bibliographic Details
Published inDatabase : the journal of biological databases and curation Vol. 2021
Main Authors Ramazi, Shahin, Zahiri, Javad
Format Journal Article
LanguageEnglish
Published UK Oxford University Press 07.04.2021
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Posttranslational modifications (PTMs) refer to amino acid side chain modification in some proteins after their biosynthesis. There are more than 400 different types of PTMs affecting many aspects of protein functions. Such modifications happen as crucial molecular regulatory mechanisms to regulate diverse cellular processes. These processes have a significant impact on the structure and function of proteins. Disruption in PTMs can lead to the dysfunction of vital biological processes and hence to various diseases. High-throughput experimental methods for discovery of PTMs are very laborious and time-consuming. Therefore, there is an urgent need for computational methods and powerful tools to predict PTMs. There are vast amounts of PTMs data, which are publicly accessible through many online databases. In this survey, we comprehensively reviewed the major online databases and related tools. The current challenges of computational methods were reviewed in detail as well.
AbstractList Posttranslational modifications (PTMs) refer to amino acid side chain modification in some proteins after their biosynthesis. There are more than 400 different types of PTMs affecting many aspects of protein functions. Such modifications happen as crucial molecular regulatory mechanisms to regulate diverse cellular processes. These processes have a significant impact on the structure and function of proteins. Disruption in PTMs can lead to the dysfunction of vital biological processes and hence to various diseases. High-throughput experimental methods for discovery of PTMs are very laborious and time-consuming. Therefore, there is an urgent need for computational methods and powerful tools to predict PTMs. There are vast amounts of PTMs data, which are publicly accessible through many online databases. In this survey, we comprehensively reviewed the major online databases and related tools. The current challenges of computational methods were reviewed in detail as well.
Author Zahiri, Javad
Ramazi, Shahin
Author_xml – sequence: 1
  givenname: Shahin
  surname: Ramazi
  fullname: Ramazi, Shahin
  organization: Bioinformatics and Computational Omics Lab (BioCOOL), Department of Biophysics, Faculty of Biological Sciences Tarbiat Modares University, Jalal Ale Ahmad Highway, P.O. Box: 14115-111, Tehran, Iran
– sequence: 2
  givenname: Javad
  orcidid: 0000-0002-8360-2458
  surname: Zahiri
  fullname: Zahiri, Javad
  organization: Bioinformatics and Computational Omics Lab (BioCOOL), Department of Biophysics, Faculty of Biological Sciences Tarbiat Modares University, Jalal Ale Ahmad Highway, P.O. Box: 14115-111, Tehran, Iran, Department of Neuroscience, University of California San Diego, La Jolla, CA, USA, Department of Pediatrics, University of California San Diego, La Jolla, CA, USA
BookMark eNpVkE1LAzEQhoNU7IfePe4PcG2ySXazHgQpfkFBD_a8TJJZG9kmZZMK_nu3VkXnMvPyzjww75SMfPBIyDmjl4zWfG4hgYaIcw2gKSuOyIRVUuVUlHz0Zx6TaYxvlJaVUuKEjDlXRVnW9YSsnkNMeerBxw6SCx66bBOsa535kjFzPtv2IaHz8SrrMYZdbzBeZCmELmbg7WCjdWa_nW0wrYONp-S4hS7i2XefkdXd7cviIV8-3T8ubpa5EbRMOTdKFHQoZtFqaRVSoVG2KBC1BK4tawtgtqwkGCZk0YKsrVJVZcAqU_MZuT5wtzu9QWvQD590zbZ3G-g_mgCu-e94t25ew3ujqKCFkAOAHgCmDzH22P7eMtrsI25-Im6-I-afpfV28A
CitedBy_id crossref_primary_10_3390_cancers15010138
crossref_primary_10_3390_ijms24076126
crossref_primary_10_1039_D2CP02883B
crossref_primary_10_1093_jxb_erad140
crossref_primary_10_1186_s11658_023_00529_7
crossref_primary_10_3390_ijms23158579
crossref_primary_10_1080_09537104_2023_2220046
crossref_primary_10_1155_2023_9705159
crossref_primary_10_3389_fneur_2023_1288740
crossref_primary_10_1111_tpj_16406
crossref_primary_10_1038_s41588_024_01686_x
crossref_primary_10_1172_jci_insight_170521
crossref_primary_10_3390_ijms24065350
crossref_primary_10_1016_j_trac_2024_117658
crossref_primary_10_1016_j_fsirep_2023_100120
crossref_primary_10_3389_fimmu_2022_898724
crossref_primary_10_1111_febs_17108
crossref_primary_10_1186_s13007_024_01201_7
crossref_primary_10_1042_BCJ20230420
crossref_primary_10_1161_ATVBAHA_122_318930
crossref_primary_10_3390_biom13050869
crossref_primary_10_1038_s41581_024_00837_x
crossref_primary_10_1016_j_ijbiomac_2023_126773
crossref_primary_10_1016_j_semcdb_2022_08_005
crossref_primary_10_3390_biom12081052
crossref_primary_10_1007_s40519_023_01618_4
crossref_primary_10_1016_j_ibneur_2022_03_002
crossref_primary_10_1101_cshperspect_a041417
crossref_primary_10_1093_bfgp_elad018
crossref_primary_10_14348_molcells_2023_0143
crossref_primary_10_1002_asia_202200197
crossref_primary_10_1002_ntls_20220006
crossref_primary_10_3390_ijms24119173
crossref_primary_10_1093_glycob_cwad094
crossref_primary_10_3390_biom13111564
crossref_primary_10_1007_s00018_022_04126_3
crossref_primary_10_1016_j_copbio_2023_103022
crossref_primary_10_1038_s41467_023_42940_w
crossref_primary_10_3390_ijms24119179
crossref_primary_10_1186_s12859_023_05581_w
crossref_primary_10_1021_acs_jpcb_2c03806
crossref_primary_10_1016_j_mib_2024_102425
crossref_primary_10_1016_j_jprot_2021_104279
crossref_primary_10_1016_j_rbc_2024_100032
crossref_primary_10_1002_ange_202313317
crossref_primary_10_1007_s11157_024_09688_1
crossref_primary_10_3390_cells11081279
crossref_primary_10_1016_j_autrev_2023_103393
crossref_primary_10_1016_j_gde_2022_101956
crossref_primary_10_1016_j_jbc_2023_104659
crossref_primary_10_1038_s41392_024_01800_9
crossref_primary_10_1186_s12967_023_04842_9
crossref_primary_10_3390_proteomes12020015
crossref_primary_10_1038_s12276_022_00883_0
crossref_primary_10_1016_j_bbcan_2023_189009
crossref_primary_10_1038_s41598_022_21366_2
crossref_primary_10_5564_pib_v39i1_3143
crossref_primary_10_1038_s41598_021_03624_x
crossref_primary_10_1093_database_baac072
crossref_primary_10_3389_fbioe_2023_1141272
crossref_primary_10_1111_ppl_14146
crossref_primary_10_1016_j_crmeth_2023_100430
crossref_primary_10_3390_cells12030387
crossref_primary_10_1016_j_toxicon_2024_107841
crossref_primary_10_1002_admi_202300021
crossref_primary_10_3390_v15040985
crossref_primary_10_1002_cbic_202300039
crossref_primary_10_1016_j_plantsci_2023_111843
crossref_primary_10_3389_fnano_2022_1047055
crossref_primary_10_1007_s12551_023_01088_z
crossref_primary_10_3390_biom12111590
crossref_primary_10_3390_ijms232012359
crossref_primary_10_1016_j_mam_2022_101099
crossref_primary_10_3389_fbioe_2022_835637
crossref_primary_10_1093_cercor_bhab430
crossref_primary_10_1093_biolre_ioac065
crossref_primary_10_1002_mco2_261
crossref_primary_10_3389_fphar_2023_1038457
crossref_primary_10_1186_s40364_023_00520_6
crossref_primary_10_1016_j_lfs_2024_122689
crossref_primary_10_1016_j_bbagrm_2023_194990
crossref_primary_10_1002_adma_202402871
crossref_primary_10_1186_s13045_024_01532_x
crossref_primary_10_1016_j_jff_2024_106052
crossref_primary_10_1039_D2CS00943A
crossref_primary_10_1021_acs_jproteome_2c00667
crossref_primary_10_1016_j_patter_2023_100758
crossref_primary_10_1042_BCJ20220251
crossref_primary_10_1016_j_jid_2023_03_1686
crossref_primary_10_1093_database_baac011
crossref_primary_10_3390_biology12101301
crossref_primary_10_1155_2021_4907167
crossref_primary_10_1016_j_bbagrm_2023_194983
crossref_primary_10_1016_j_str_2023_05_017
crossref_primary_10_3389_fimmu_2022_932525
crossref_primary_10_3390_biom13121704
crossref_primary_10_3390_cells11060955
crossref_primary_10_1016_j_molcel_2022_11_014
crossref_primary_10_3390_molecules28031476
crossref_primary_10_1038_s41598_023_42104_2
crossref_primary_10_1186_s13041_024_01088_4
crossref_primary_10_3390_pathogens12040629
crossref_primary_10_1016_j_bbadis_2024_167308
crossref_primary_10_1093_nargab_lqae011
crossref_primary_10_3390_ijms25126699
crossref_primary_10_1093_bioinformatics_btae005
crossref_primary_10_1016_j_bmc_2022_116918
crossref_primary_10_3748_wjg_v28_i29_3780
crossref_primary_10_1016_j_fsi_2023_109264
crossref_primary_10_1016_j_cellsig_2023_110682
crossref_primary_10_1016_j_plantsci_2023_111866
crossref_primary_10_1002_pmic_202100389
crossref_primary_10_1016_j_jim_2023_113540
crossref_primary_10_3390_biology12101311
crossref_primary_10_1016_j_addr_2024_115386
crossref_primary_10_3390_medicina59101722
crossref_primary_10_1016_j_freeradbiomed_2024_04_005
crossref_primary_10_1152_physrev_00026_2023
crossref_primary_10_3390_ijms25116099
crossref_primary_10_2144_btn_2022_0003
crossref_primary_10_3390_cells13050426
crossref_primary_10_1042_BST20221147
crossref_primary_10_1530_VB_22_0003
crossref_primary_10_1016_j_xpro_2023_102682
crossref_primary_10_1158_1541_7786_MCR_23_0976
crossref_primary_10_1002_elsc_202300003
crossref_primary_10_1016_j_tranon_2023_101673
crossref_primary_10_1021_acs_analchem_3c05891
crossref_primary_10_1021_jasms_2c00249
crossref_primary_10_3390_ijms25084340
crossref_primary_10_1039_D3CB00018D
crossref_primary_10_1093_bioinformatics_btad046
crossref_primary_10_1016_j_bbagrm_2023_194968
crossref_primary_10_1016_j_coviro_2022_101291
crossref_primary_10_1002_ctd2_163
crossref_primary_10_3390_ijms23169299
crossref_primary_10_1002_pmic_202100230
crossref_primary_10_1042_EBC20210068
crossref_primary_10_35534_sbe_2023_10011
crossref_primary_10_3390_biom13081221
crossref_primary_10_1002_elps_202400043
crossref_primary_10_1371_journal_pone_0271995
crossref_primary_10_1007_s42485_023_00108_6
crossref_primary_10_1038_s41598_023_43521_z
crossref_primary_10_3389_fmolb_2022_906437
crossref_primary_10_1021_acs_analchem_3c01618
crossref_primary_10_1152_physrev_00017_2022
crossref_primary_10_1071_RD23082
crossref_primary_10_1016_j_drudis_2024_103891
crossref_primary_10_1002_jccs_202400136
crossref_primary_10_1021_acsinfecdis_3c00566
crossref_primary_10_3390_jof8111179
crossref_primary_10_1016_j_trac_2024_117725
crossref_primary_10_1002_jcb_30330
crossref_primary_10_1093_nar_gkab1017
crossref_primary_10_1007_s11104_024_06745_0
crossref_primary_10_1128_spectrum_03010_23
crossref_primary_10_3390_jpm11121373
crossref_primary_10_1159_000531352
crossref_primary_10_2174_0113892037291318240130103348
crossref_primary_10_1038_s41598_023_49665_2
crossref_primary_10_1186_s10020_023_00684_9
crossref_primary_10_1007_s00299_023_03016_7
crossref_primary_10_1016_j_cobme_2023_100496
crossref_primary_10_3390_cells11081330
crossref_primary_10_1021_acs_chemrev_4c00112
crossref_primary_10_1021_acs_chemrev_4c00110
crossref_primary_10_3390_proteomes11040038
crossref_primary_10_3389_fpls_2023_1098401
crossref_primary_10_1002_cm_21857
crossref_primary_10_1016_j_phrs_2023_106712
crossref_primary_10_3390_molecules27248859
crossref_primary_10_1016_j_tifs_2024_104570
crossref_primary_10_1080_02770903_2021_2020815
crossref_primary_10_1083_jcb_202307103
crossref_primary_10_1016_j_sajb_2023_04_022
crossref_primary_10_1016_j_bbcan_2022_188736
crossref_primary_10_1007_s00438_023_02013_5
crossref_primary_10_34133_research_0011
crossref_primary_10_1016_j_tetlet_2023_154602
crossref_primary_10_1080_07388551_2023_2283376
crossref_primary_10_1016_j_biopha_2023_115859
crossref_primary_10_1038_s41392_023_01439_y
crossref_primary_10_3390_ijms232012093
crossref_primary_10_1016_j_heares_2023_108823
crossref_primary_10_3390_ijms25126408
crossref_primary_10_1186_s12885_023_10916_0
crossref_primary_10_3390_nu16050699
crossref_primary_10_1093_database_baad094
crossref_primary_10_3389_fnmol_2023_1133271
crossref_primary_10_1242_jcs_259618
crossref_primary_10_3390_ijms24076742
crossref_primary_10_1039_D3RA06476J
crossref_primary_10_1111_pce_14926
crossref_primary_10_1186_s13287_024_03778_1
crossref_primary_10_1016_j_tranon_2022_101556
crossref_primary_10_1016_j_lfs_2024_122868
crossref_primary_10_1002_btpr_3392
crossref_primary_10_1016_j_jprot_2022_104488
crossref_primary_10_1016_j_molbiopara_2024_111633
crossref_primary_10_1007_s12551_021_00849_y
crossref_primary_10_1038_s41598_024_58450_8
crossref_primary_10_1080_07391102_2023_2231553
crossref_primary_10_1126_science_adg3925
crossref_primary_10_1089_gen_43_02_13
crossref_primary_10_1021_acsptsci_3c00076
crossref_primary_10_3390_foods11243993
crossref_primary_10_3390_ijms232214285
crossref_primary_10_1042_BCJ20230223
crossref_primary_10_1016_j_chemolab_2023_105019
crossref_primary_10_1021_acs_chemrev_3c00850
crossref_primary_10_1042_BST20221194
crossref_primary_10_1016_j_xphs_2023_12_018
crossref_primary_10_3389_fnmol_2022_931301
crossref_primary_10_1021_acs_jafc_3c00886
crossref_primary_10_3389_fmicb_2023_1245805
crossref_primary_10_3390_biom12030443
crossref_primary_10_1186_s43897_022_00038_9
crossref_primary_10_1021_acsmeasuresciau_3c00068
crossref_primary_10_1002_pro_4618
crossref_primary_10_3389_fmicb_2022_935735
crossref_primary_10_1002_bies_202300178
crossref_primary_10_1002_pro_4979
crossref_primary_10_1007_s10725_024_01163_9
crossref_primary_10_1093_plphys_kiae200
crossref_primary_10_3389_fnmol_2023_1271226
crossref_primary_10_1016_j_ymeth_2024_04_007
crossref_primary_10_3390_cells11030581
crossref_primary_10_1111_tpj_16206
crossref_primary_10_7554_eLife_82819
crossref_primary_10_1002_jmv_27845
crossref_primary_10_1016_j_jphotobiol_2024_112867
crossref_primary_10_1007_s11154_023_09834_0
crossref_primary_10_1007_s41061_024_00469_6
crossref_primary_10_3390_ijms25010405
crossref_primary_10_1016_j_compbiolchem_2023_107962
crossref_primary_10_1016_j_mcpro_2024_100723
crossref_primary_10_1016_j_mattod_2023_01_018
crossref_primary_10_3390_biom14010118
crossref_primary_10_1021_acs_jafc_2c09094
crossref_primary_10_1016_j_compbiolchem_2022_107669
crossref_primary_10_1002_anie_202313317
crossref_primary_10_1093_bib_bbac015
crossref_primary_10_1021_acsomega_3c04592
crossref_primary_10_1126_science_adl2528
crossref_primary_10_1016_j_microb_2024_100121
crossref_primary_10_3390_ijms25073813
crossref_primary_10_1016_j_bej_2022_108612
crossref_primary_10_1016_j_biopha_2023_114329
crossref_primary_10_1016_j_jhazmat_2023_132211
crossref_primary_10_1016_j_addr_2023_114992
crossref_primary_10_1080_13543784_2023_2288075
crossref_primary_10_3390_antib13010017
crossref_primary_10_3390_pharmaceutics14010010
crossref_primary_10_3390_jof7090700
crossref_primary_10_3390_molecules28031083
crossref_primary_10_1016_j_gene_2023_147730
crossref_primary_10_1002_pmic_202300011
crossref_primary_10_3389_fcimb_2024_1408947
crossref_primary_10_1007_s13205_021_03038_6
crossref_primary_10_1039_D3CC02909C
crossref_primary_10_2174_0929866529666220318152509
crossref_primary_10_1016_j_nbd_2023_106342
crossref_primary_10_1093_pcp_pcae040
crossref_primary_10_3390_genes15040393
crossref_primary_10_1186_s12864_024_10298_y
crossref_primary_10_1016_j_bbadva_2022_100050
crossref_primary_10_1128_jvi_01192_23
crossref_primary_10_1016_j_chroma_2022_463352
crossref_primary_10_3389_fnmol_2024_1405415
crossref_primary_10_1007_s12272_022_01409_y
crossref_primary_10_1016_j_gpb_2023_03_007
crossref_primary_10_1093_jxb_erad354
crossref_primary_10_1016_j_tips_2023_01_002
crossref_primary_10_3390_biom14040409
crossref_primary_10_1242_jeb_243271
crossref_primary_10_3390_ijms232415803
crossref_primary_10_3390_ijms25073958
crossref_primary_10_3390_molecules27082411
crossref_primary_10_1002_jcp_30954
crossref_primary_10_1016_j_heares_2022_108625
crossref_primary_10_1111_imm_13822
crossref_primary_10_3389_fmolb_2022_928287
Cites_doi 10.1074/jbc.M115.675488
10.1165/rcmb.2007-0118OC
10.1371/journal.pgen.1003225
10.1007/s12038-020-00099-2
10.1038/ncomms5919
10.1093/nar/gky1079
10.3390/molecules20022138
10.1016/S0955-0674(99)00085-X
10.1016/j.biochi.2019.06.005
10.1038/nrc3151
10.1186/1471-2105-8-438
10.1038/nature17888
10.1038/cdd.2016.53
10.1093/bioinformatics/btl013
10.1093/hmg/11.18.2119
10.3390/molecules24244604
10.1042/BST20160236
10.1016/j.cell.2006.08.019
10.1093/glycob/3.2.97
10.1080/10409238.2017.1287161
10.1371/journal.pone.0179529
10.1038/nrm.2017.35
10.1016/S0021-9258(17)46054-6
10.1111/febs.13378
10.1126/science.3340856
10.1042/BST20160233
10.1016/j.molcel.2008.07.002
10.1002/prca.201400037
10.2217/epi.11.23
10.1007/s12017-013-8258-6
10.1002/0471142956.cy0936s56
10.1007/s00018-005-5298-6
10.1007/s12035-013-8627-z
10.1074/jbc.271.18.10897
10.1038/nrd4360
10.1126/science.1164097
10.1093/bioinformatics/btl158
10.1016/j.tibs.2005.04.013
10.1098/rsob.170024
10.1007/s00018-017-2515-z
10.1109/TCBB.2017.2670558
10.1016/j.molcel.2006.11.019
10.1093/bioinformatics/btv403
10.1200/JCO.2012.44.0958
10.1093/emboj/19.6.1176
10.7150/ijbs.24121
10.1021/cb500791f
10.1681/ASN.2006010083
10.1007/s12035-015-9594-3
10.1093/nar/gky1052
10.1093/nar/gky1159
10.12688/f1000research.6464.1
10.1016/S0092-8674(00)81862-0
10.1016/j.biochi.2010.10.018
10.1007/s12154-009-0032-8
doi:10.1136/jmedgenet-2013-102138.
10.1038/nbt0303-255
10.1002/mas.20164
10.1021/bi00250a003
10.1016/S0021-9258(18)73846-5
10.1007/s12017-013-8266-6
10.1039/C5MB00384A
10.1042/BJ20121201
10.1038/cr.2011.22
10.1007/s11030-009-9149-5
10.1038/nrg1655
10.1093/database/bav037
10.1016/S0955-0674(00)00208-8
10.1016/S0021-9258(18)55985-8
10.1128/MCB.19.10.6775
10.1038/cr.2016.39
10.1016/j.autrev.2014.02.005
10.2144/000112201
10.1038/cr.2013.151
10.1021/bi991454f
10.1016/j.nbt.2009.03.011
10.1093/nar/gkm854
10.1021/acs.jcim.5b00276
10.1146/annurev.biochem.73.011303.074043
10.1093/bioinformatics/btr525
10.1128/JVI.01888-06
10.1007/s11427-015-4836-1
10.1210/me.2012-1404
10.2174/1568026615666150819110421
10.1038/srep00090
10.1070/RC2014v083n02ABEH004377
10.1038/nchembio.509
10.1016/j.pneurobio.2011.11.002
10.1146/annurev-biochem-061909-093311
10.1083/jcb.201202056
10.1073/pnas.51.5.786
10.1126/science.1175371
10.1038/nm.3739
10.1111/j.1399-0004.2011.01724.x
10.1002/prot.22555
10.1038/nrn940
10.1371/journal.pone.0078235
10.2174/1389202911314060004
10.1523/JNEUROSCI.4436-10.2010
10.1093/nar/gky1074
10.4061/2011/207691
10.1073/pnas.72.1.11
10.1146/annurev-genet-111212-133453
10.1042/bj1950639
10.1152/physrev.00012.2016
10.1371/journal.pone.0136360
10.1186/1471-2105-7-82
10.1371/journal.pcbi.1004049
10.3389/fpls.2020.590529
10.1002/pmic.200300771
10.1098/rstb.2012.0106
10.1016/j.csbj.2017.03.004
10.1016/j.jprot.2013.03.025
10.1016/0006-291X(78)91505-X
10.1042/BSR20150295
10.1016/0014-5793(82)80759-X
10.1126/science.8456312
10.1093/oxfordjournals.jbchem.a123780
10.1016/j.bbamem.2011.07.009
10.1002/mrr.20228
10.1016/j.bmc.2015.04.056
10.1007/978-1-4614-7138-7
10.1016/j.csbj.2015.03.001
10.1042/BJ20121375
ContentType Journal Article
Copyright The Author(s) 2021. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com 2021
Copyright_xml – notice: The Author(s) 2021. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com 2021
DBID AAYXX
CITATION
5PM
DOI 10.1093/database/baab012
DatabaseName CrossRef
PubMed Central (Full Participant titles)
DatabaseTitle CrossRef
DatabaseTitleList CrossRef

DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1758-0463
ExternalDocumentID 10_1093_database_baab012
GroupedDBID ---
.I3
0R~
18M
53G
5VS
5WA
70E
AAHBH
AAMVS
AAPPN
AAPXW
AAVAP
AAYXX
ABDBF
ABEJV
ABPTD
ABXVV
ACGFO
ACGFS
ACPRK
ADBBV
ADHZD
ADRAZ
AENZO
AFULF
AHMBA
AIAGR
ALMA_UNASSIGNED_HOLDINGS
ALUQC
AOIJS
BAWUL
BAYMD
BCNDV
BTTYL
CIDKT
CITATION
CZ4
DIK
D~K
E3Z
EBD
EBS
EMOBN
ESX
GROUPED_DOAJ
GX1
H13
HYE
HZ~
KSI
M48
MK~
M~E
O5R
O5S
OAWHX
OJQWA
OK1
O~Y
P2P
PEELM
PQQKQ
RD5
ROX
RPM
RXO
SV3
TOX
TR2
TUS
X7H
ZBA
~91
~D7
~S-
5PM
ID FETCH-LOGICAL-c406t-3c84200001dedb5d8e04be5fe4eeb5a3bd1f2a1d675ac1452fa59d8877cad8c93
IEDL.DBID RPM
ISSN 1758-0463
IngestDate Tue Sep 17 21:03:04 EDT 2024
Fri Dec 06 05:33:19 EST 2024
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Language English
License https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model
This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c406t-3c84200001dedb5d8e04be5fe4eeb5a3bd1f2a1d675ac1452fa59d8877cad8c93
Notes Shahin Ramazi and Javad Zahiri contributed equally to this work.
ORCID 0000-0002-8360-2458
OpenAccessLink https://academic.oup.com/database/article-pdf/doi/10.1093/database/baab012/37044588/baab012.pdf
PMID 33826699
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_8040245
crossref_primary_10_1093_database_baab012
PublicationCentury 2000
PublicationDate 2021-04-07
PublicationDateYYYYMMDD 2021-04-07
PublicationDate_xml – month: 04
  year: 2021
  text: 2021-04-07
  day: 07
PublicationDecade 2020
PublicationPlace UK
PublicationPlace_xml – name: UK
PublicationTitle Database : the journal of biological databases and curation
PublicationYear 2021
Publisher Oxford University Press
Publisher_xml – name: Oxford University Press
References Wellen (2021041314334196800_R57) 2009; 324
Kanan (2021041314334196800_R30) 2013; 1
Resh (2021041314334196800_R105) 2017; 45
Wesche (2021041314334196800_R76) 2017; 74
Gao (2021041314334196800_R119) 2016; 53
Suresh (2021041314334196800_R65) 2016; 23
Eifler (2021041314334196800_R87) 2015; 282
Blanc (2021041314334196800_R100) 2015; 4
Hasan (2021041314334196800_R23) 2018; 2
Wang (2021041314334196800_R4) 2014; 24
Strumillo (2021041314334196800_R18) 2015; 23
Fuchs (2021041314334196800_R21) 2011; 3
Meckler (2021041314334196800_R104) 2010; 30
Yu (2021041314334196800_R128) 2019; 47
Roosing (2021041314334196800_R118) 2014; 51
Wright (2021041314334196800_R109) 2010; 3
Haltiwanger (2021041314334196800_R11) 2004; 73
Young (2021041314334196800_R98) 2012; 97
Audagnotto (2021041314334196800_R16) 2017; 15
Wang (2021041314334196800_R17) 2015; 11
Radivojac (2021041314334196800_R68) 2010; 78
Blom (2021041314334196800_R5) 2004; 4
Ohtsubo (2021041314334196800_R13) 2006; 126
Bause (2021041314334196800_R37) 1981; 195
Kumar (2021041314334196800_R91) 2015; 13
Goulabchand (2021041314334196800_R14) 2014; 13
Temporini (2021041314334196800_R53) 2008; 27
Murn (2021041314334196800_R75) 2017; 18
Stone (2021041314334196800_R121) 2009; 25
Palsuledesai (2021041314334196800_R112) 2014; 10
Caragea (2021041314334196800_R9) 2007; 8
Panni (2021041314334196800_R46) 2019; 163
Sobolev (2021041314334196800_R25) 2014; 83
Levene (2021041314334196800_R28) 1906; 2
Pawson (2021041314334196800_R43) 2005; 30
Rice (2021041314334196800_R77) 2001; 13
Alonso (2021041314334196800_R66) 2013; 27
Duan (2021041314334196800_R48) 2015; 11
Gong (2021041314334196800_R51) 2008; 36
Lin (2021041314334196800_R125) 2020; 2020
Agola (2021041314334196800_R116) 2011; 80
Jin (2021041314334196800_R49) 2012; 367
Nickchi (2021041314334196800_R26) 2015; 2015
Li (2021041314334196800_R102) 2015; 55
Khoury (2021041314334196800_R27) 2011; 1
Sun (2021041314334196800_R79) 2014; 2014
Park (2021041314334196800_R61) 2016; 291
Skamnaki (2021041314334196800_R47) 1999; 38
Xia (2021041314334196800_R55) 2020; 20
Xu (2021041314334196800_R115) 2015; 58
Cundy (2021041314334196800_R10) 2002; 11
Oman (2021041314334196800_R40) 2011; 7
Edwards (2021041314334196800_R45) 2000; 12
Xie (2021041314334196800_R74) 2007; 81
Hottman (2021041314334196800_R117) 2014; 50
Ferguson (2021041314334196800_R42) 1988; 239
Choudhary (2021041314334196800_R56) 2009; 325
Lu (2021041314334196800_R93) 2010; 14
Yang (2021041314334196800_R54) 2008; 31
Mehta (2021041314334196800_R41) 1996; 271
Del Monte (2021041314334196800_R15) 2014; 8
Goldstein (2021041314334196800_R32) 1975; 72
Folch (2021041314334196800_R94) 1951; 191
Zhang (2021041314334196800_R97) 2017; 45
Nsiah-Sefaa (2021041314334196800_R52) 2016; 36
Marshall (2021041314334196800_R8) 1993; 259
Wei (2021041314334196800_R19) 2017; 16
Xiong (2021041314334196800_R59) 2012; 198
Beauclair (2021041314334196800_R89) 2015; 31
Takamitsu (2021041314334196800_R108) 2015; 10
Liu (2021041314334196800_R122) 2008; 38
Sedek (2021041314334196800_R85) 2013; 453
Varki (2021041314334196800_R81) 1993; 3
Xu (2021041314334196800_R130) 2018; 8
Allfrey (2021041314334196800_R31) 1964; 51
El-Husseini (2021041314334196800_R96) 2002; 3
Leuchowius (2021041314334196800_R20) 2011; 56
Wang (2021041314334196800_R80) 2019; 24
James (2021041314334196800_R131) 2013
Robertson (2021041314334196800_R78) 2005; 6
Hofsteenge (2021041314334196800_R39) 1994; 33
Bhogaraju (2021041314334196800_R63) 2016; 533
Bartels (2021041314334196800_R36) 1999; 19
Falkenberg (2021041314334196800_R60) 2014; 13
Liu (2021041314334196800_R124) 2018; 14
McTaggart (2021041314334196800_R113) 2006; 63
Yang (2021041314334196800_R123) 2015; 20
Lauc (2021041314334196800_R82) 2013; 9
Kouzarides (2021041314334196800_R58) 2000; 19
Zahiri (2021041314334196800_R132) 2013; 14
Kamiya (2021041314334196800_R33) 1978; 83
Feligioni (2021041314334196800_R83) 2013; 15
Larsen (2021041314334196800_R22) 2006; 40
Swatek (2021041314334196800_R64) 2016; 26
Weng (2021041314334196800_R103) 2017; 12
Khalili (2021041314334196800_R133) 2020; 11
Martin (2021041314334196800_R106) 2011; 93
Flotho (2021041314334196800_R90) 2013; 82
Turkina (2021041314334196800_R44) 2008
Popovic (2021041314334196800_R70) 2014; 20
Ryšlavá (2021041314334196800_R7) 2013; 92
Cheng (2021041314334196800_R73) 2007; 25
Mustfa (2021041314334196800_R86) 2017; 7
Trost (2021041314334196800_R24) 2011; 27
Schoenheimer (2021041314334196800_R29) 1939; 127
Jentsch (2021041314334196800_R84) 2013; 47
Aicart-Ramos (2021041314334196800_R99) 2011; 1808
Hornbeck (2021041314334196800_R127) 2019; 47
Mahajan (2021041314334196800_R35) 1997; 88
Micel (2021041314334196800_R67) 2013; 31
Foot (2021041314334196800_R69) 2017; 97
Xu (2021041314334196800_R3) 2016; 16
Bannister (2021041314334196800_R72) 2011; 21
Moriya (2021041314334196800_R107) 2013; 8
Li (2021041314334196800_R129) 2006; 22
Mann (2021041314334196800_R2) 2003; 21
Li (2021041314334196800_R71) 2012; 32
Karve (2021041314334196800_R12) 2011; 2011
Aitken (2021041314334196800_R34) 1982; 150
Ramazi (2021041314334196800_R1) 2020; 45
Nishimura (2021041314334196800_R38) 1992; 111
Chida (2021041314334196800_R110) 2013; 449
Zhou (2021041314334196800_R95) 2006; 22
Droescher (2021041314334196800_R92) 2013; 15
Lecker (2021041314334196800_R62) 2006; 17
Huang (2021041314334196800_R6) 2018; 47
Brown (2021041314334196800_R101) 2017; 52
Ramazi (2021041314334196800_R88) 2016; 3
Forrest (2021041314334196800_R50) 2006; 7
Thinon (2021041314334196800_R111) 2014; 5
Kanan (2021041314334196800_R120) 2013; 1
Berndt (2021041314334196800_R114) 2011; 11
Oughtred (2021041314334196800_R126) 2019; 47
References_xml – volume: 291
  start-page: 3531
  year: 2016
  ident: 2021041314334196800_R61
  article-title: Regulation of histone acetylation by autophagy in Parkinson disease
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M115.675488
  contributor:
    fullname: Park
– volume: 38
  start-page: 738
  year: 2008
  ident: 2021041314334196800_R122
  article-title: Tyrosine sulfation is prevalent in human chemokine receptors important in lung disease
  publication-title: Am. J. Respir. Cell Mol. Biol.
  doi: 10.1165/rcmb.2007-0118OC
  contributor:
    fullname: Liu
– volume: 9
  year: 2013
  ident: 2021041314334196800_R82
  article-title: Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers
  publication-title: PLoS Genet.
  doi: 10.1371/journal.pgen.1003225
  contributor:
    fullname: Lauc
– volume: 45
  year: 2020
  ident: 2021041314334196800_R1
  article-title: Evaluation of post-translational modifications in histone proteins: a review on histone modification defects in developmental and neurological disorders
  publication-title: J. Biosci.
  doi: 10.1007/s12038-020-00099-2
  contributor:
    fullname: Ramazi
– volume: 5
  start-page: 1
  year: 2014
  ident: 2021041314334196800_R111
  article-title: Global profiling of co-and post-translationally N-myristoylated proteomes in human cells
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms5919
  contributor:
    fullname: Thinon
– volume: 47
  start-page: D529
  year: 2019
  ident: 2021041314334196800_R126
  article-title: The BioGRID interaction database: 2019 update
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gky1079
  contributor:
    fullname: Oughtred
– volume: 20
  start-page: 2138
  year: 2015
  ident: 2021041314334196800_R123
  article-title: Tyrosine sulfation as a protein post-translational modification
  publication-title: Molecules
  doi: 10.3390/molecules20022138
  contributor:
    fullname: Yang
– volume: 12
  start-page: 217
  year: 2000
  ident: 2021041314334196800_R45
  article-title: A-kinase anchoring proteins: protein kinase A and beyond
  publication-title: Curr. Opin. Cell Biol.
  doi: 10.1016/S0955-0674(99)00085-X
  contributor:
    fullname: Edwards
– volume: 163
  start-page: 117
  year: 2019
  ident: 2021041314334196800_R46
  article-title: Phospho-peptide binding domains in S. cerevisiae model organism
  publication-title: Biochimie.
  doi: 10.1016/j.biochi.2019.06.005
  contributor:
    fullname: Panni
– volume: 11
  year: 2011
  ident: 2021041314334196800_R114
  article-title: Targeting protein prenylation for cancer therapy
  publication-title: Nat. Rev. Cancer
  doi: 10.1038/nrc3151
  contributor:
    fullname: Berndt
– volume: 8
  year: 2007
  ident: 2021041314334196800_R9
  article-title: Glycosylation site prediction using ensembles of Support Vector Machine classifiers
  publication-title: BMC Bioinform.
  doi: 10.1186/1471-2105-8-438
  contributor:
    fullname: Caragea
– volume: 533
  year: 2016
  ident: 2021041314334196800_R63
  article-title: Cell biology: ubiquitination without E1 and E2 enzymes
  publication-title: Nature
  doi: 10.1038/nature17888
  contributor:
    fullname: Bhogaraju
– volume: 23
  start-page: 1257
  year: 2016
  ident: 2021041314334196800_R65
  article-title: Regulation of pluripotency and differentiation by deubiquitinating enzymes
  publication-title: Cell Death Differ.
  doi: 10.1038/cdd.2016.53
  contributor:
    fullname: Suresh
– volume: 22
  start-page: 894
  year: 2006
  ident: 2021041314334196800_R95
  article-title: CSS-Palm: palmitoylation site prediction with a clustering and scoring strategy (CSS)
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btl013
  contributor:
    fullname: Zhou
– volume: 11
  start-page: 2119
  year: 2002
  ident: 2021041314334196800_R10
  article-title: A mutation in the gene TNFRSF11B encoding osteoprotegerin causes an idiopathic hyperphosphatasia phenotype
  publication-title: Hum. Mol. Genet.
  doi: 10.1093/hmg/11.18.2119
  contributor:
    fullname: Cundy
– volume: 24
  year: 2019
  ident: 2021041314334196800_R80
  article-title: Glycan mimetics from natural products: new therapeutic opportunities for neurodegenerative disease
  publication-title: Molecules
  doi: 10.3390/molecules24244604
  contributor:
    fullname: Wang
– volume: 45
  start-page: 275
  year: 2017
  ident: 2021041314334196800_R97
  article-title: Protein S-palmitoylation in cellular differentiation
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST20160236
  contributor:
    fullname: Zhang
– volume: 126
  start-page: 855
  year: 2006
  ident: 2021041314334196800_R13
  article-title: Glycosylation in cellular mechanisms of health and disease
  publication-title: Cell
  doi: 10.1016/j.cell.2006.08.019
  contributor:
    fullname: Ohtsubo
– volume: 3
  start-page: 97
  year: 1993
  ident: 2021041314334196800_R81
  article-title: Biological roles of oligosaccharides: all of the theories are correct
  publication-title: Glycobiology
  doi: 10.1093/glycob/3.2.97
  contributor:
    fullname: Varki
– volume: 52
  start-page: 145
  year: 2017
  ident: 2021041314334196800_R101
  article-title: Dynamic protein S-palmitoylation mediates parasite life cycle progression and diverse mechanisms of virulence
  publication-title: Crit. Rev. Biochem. Mol. Biol.
  doi: 10.1080/10409238.2017.1287161
  contributor:
    fullname: Brown
– volume: 12
  year: 2017
  ident: 2021041314334196800_R103
  article-title: MDD-Palm: identification of protein S-palmitoylation sites with substrate motifs based on maximal dependence decomposition
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0179529
  contributor:
    fullname: Weng
– volume: 18
  start-page: 517
  year: 2017
  ident: 2021041314334196800_R75
  article-title: The winding path of protein methylation research: milestones and new frontiers
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/nrm.2017.35
  contributor:
    fullname: Murn
– volume: 2
  start-page: 127
  year: 1906
  ident: 2021041314334196800_R28
  article-title: The cleavage products of vitellin
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(17)46054-6
  contributor:
    fullname: Levene
– volume: 282
  start-page: 3669
  year: 2015
  ident: 2021041314334196800_R87
  article-title: Mapping the SUMOylated landscape
  publication-title: FEBS J.
  doi: 10.1111/febs.13378
  contributor:
    fullname: Eifler
– volume: 1
  year: 2013
  ident: 2021041314334196800_R120
  article-title: Tyrosine O sulfation: an overview
  publication-title: JSM Biotechnol. Bioeng.
  contributor:
    fullname: Kanan
– volume: 239
  start-page: 753
  year: 1988
  ident: 2021041314334196800_R42
  article-title: Glycosyl-phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane
  publication-title: Science
  doi: 10.1126/science.3340856
  contributor:
    fullname: Ferguson
– volume: 45
  start-page: 409
  year: 2017
  ident: 2021041314334196800_R105
  article-title: Palmitoylation of proteins in cancer
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST20160233
  contributor:
    fullname: Resh
– volume: 31
  start-page: 449
  year: 2008
  ident: 2021041314334196800_R54
  article-title: Lysine acetylation: codified crosstalk with other posttranslational modifications
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2008.07.002
  contributor:
    fullname: Yang
– volume: 8
  start-page: 534
  year: 2014
  ident: 2021041314334196800_R15
  article-title: Protein post-translational modifications and misfolding: new concepts in heart failure
  publication-title: Proteomics Clin. Appl.
  doi: 10.1002/prca.201400037
  contributor:
    fullname: Del Monte
– volume: 3
  start-page: 247
  year: 2011
  ident: 2021041314334196800_R21
  article-title: Antibody recognition of histone post-translational modifications: emerging issues and future prospects
  publication-title: Epigenomics
  doi: 10.2217/epi.11.23
  contributor:
    fullname: Fuchs
– volume: 15
  start-page: 639
  year: 2013
  ident: 2021041314334196800_R92
  article-title: SUMO rules: regulatory concepts and their implication in neurologic functions
  publication-title: Neuromolecular Med.
  doi: 10.1007/s12017-013-8258-6
  contributor:
    fullname: Droescher
– volume: 56
  start-page: 9.36.1
  year: 2011
  ident: 2021041314334196800_R20
  article-title: In situ proximity ligation assay for microscopy and flow cytometry
  publication-title: Curr. Protoc. Cytometry
  doi: 10.1002/0471142956.cy0936s56
  contributor:
    fullname: Leuchowius
– volume: 63
  start-page: 255
  year: 2006
  ident: 2021041314334196800_R113
  article-title: Isoprenylated proteins
  publication-title: Cell. Mol. Life Sci. CMLS
  doi: 10.1007/s00018-005-5298-6
  contributor:
    fullname: McTaggart
– volume: 50
  start-page: 177
  year: 2014
  ident: 2021041314334196800_R117
  article-title: Protein prenylation and synaptic plasticity: implications for Alzheimer’s disease
  publication-title: Mol. Neurobiol.
  doi: 10.1007/s12035-013-8627-z
  contributor:
    fullname: Hottman
– volume: 271
  start-page: 10897
  year: 1996
  ident: 2021041314334196800_R41
  article-title: A lysosomal cysteine proteinase from Dictyostelium discoideum contains N-acetylglucosamine-1-phosphate bound to serine but not mannose-6-phosphate on N-linked oligosaccharides
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.271.18.10897
  contributor:
    fullname: Mehta
– volume: 13
  year: 2014
  ident: 2021041314334196800_R60
  article-title: Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
  publication-title: Nat. Rev. Drug Discov.
  doi: 10.1038/nrd4360
  contributor:
    fullname: Falkenberg
– volume: 324
  start-page: 1076
  year: 2009
  ident: 2021041314334196800_R57
  article-title: ATP-citrate lyase links cellular metabolism to histone acetylation
  publication-title: Science.
  doi: 10.1126/science.1164097
  contributor:
    fullname: Wellen
– volume: 3
  year: 2016
  ident: 2021041314334196800_R88
  article-title: Computational prediction of proteins sumoylation: a review on the methods and databases
  publication-title: J. Nanomed. Res.
  contributor:
    fullname: Ramazi
– volume: 22
  start-page: 1658
  year: 2006
  ident: 2021041314334196800_R129
  article-title: Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btl158
  contributor:
    fullname: Li
– volume: 30
  start-page: 286
  year: 2005
  ident: 2021041314334196800_R43
  article-title: Protein phosphorylation in signaling–50 years and counting
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2005.04.013
  contributor:
    fullname: Pawson
– volume: 7
  year: 2017
  ident: 2021041314334196800_R86
  article-title: SUMOylation pathway alteration coupled with downregulation of SUMO E2 enzyme at mucosal epithelium modulates inflammation in inflammatory bowel disease
  publication-title: Open Biol.
  doi: 10.1098/rsob.170024
  contributor:
    fullname: Mustfa
– volume: 74
  start-page: 3305
  year: 2017
  ident: 2021041314334196800_R76
  article-title: Protein arginine methylation: a prominent modification and its demethylation
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-017-2515-z
  contributor:
    fullname: Wesche
– volume: 16
  start-page: 1264
  year: 2017
  ident: 2021041314334196800_R19
  article-title: Fast prediction of protein methylation sites using a sequence-based feature selection technique
  publication-title: IEEE/ACM Trans. Comput. Biol.Bioinf
  doi: 10.1109/TCBB.2017.2670558
  contributor:
    fullname: Wei
– volume: 25
  start-page: 71
  year: 2007
  ident: 2021041314334196800_R73
  article-title: The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2006.11.019
  contributor:
    fullname: Cheng
– volume: 31
  start-page: 3483
  year: 2015
  ident: 2021041314334196800_R89
  article-title: JASSA: a comprehensive tool for prediction of SUMOylation sites and SIMs
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btv403
  contributor:
    fullname: Beauclair
– volume: 31
  year: 2013
  ident: 2021041314334196800_R67
  article-title: Role of ubiquitin ligases and the proteasome in oncogenesis: novel targets for anticancer therapies
  publication-title: J. Clin. Oncol.
  doi: 10.1200/JCO.2012.44.0958
  contributor:
    fullname: Micel
– volume: 19
  start-page: 1176
  year: 2000
  ident: 2021041314334196800_R58
  article-title: Acetylation: a regulatory modification to rival phosphorylation?
  publication-title: Embo J.
  doi: 10.1093/emboj/19.6.1176
  contributor:
    fullname: Kouzarides
– volume: 14
  start-page: 946
  year: 2018
  ident: 2021041314334196800_R124
  article-title: PTM-ssMP: a web server for predicting different types of post-translational modification sites using novel site-specific modification profile
  publication-title: Int. J. Biol. Sci.
  doi: 10.7150/ijbs.24121
  contributor:
    fullname: Liu
– volume: 10
  start-page: 51
  year: 2014
  ident: 2021041314334196800_R112
  article-title: Protein prenylation: enzymes, therapeutics, and biotechnology applications
  publication-title: ACS Chem. Biol.
  doi: 10.1021/cb500791f
  contributor:
    fullname: Palsuledesai
– volume: 17
  start-page: 1807
  year: 2006
  ident: 2021041314334196800_R62
  article-title: Protein degradation by the ubiquitin–proteasome pathway in normal and disease states
  publication-title: J. Am. Soc. Nephrol.
  doi: 10.1681/ASN.2006010083
  contributor:
    fullname: Lecker
– volume: 53
  start-page: 6925
  year: 2016
  ident: 2021041314334196800_R119
  article-title: The role of geranylgeranyltransferase I-mediated protein prenylation in the brain
  publication-title: Mol. Neurobiol.
  doi: 10.1007/s12035-015-9594-3
  contributor:
    fullname: Gao
– volume: 47
  start-page: D451
  year: 2019
  ident: 2021041314334196800_R128
  article-title: qPhos: a database of protein phosphorylation dynamics in humans
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gky1052
  contributor:
    fullname: Yu
– volume: 47
  start-page: D433
  year: 2019
  ident: 2021041314334196800_R127
  article-title: 15 years of PhosphoSitePlus®: integrating post-translationally modified sites, disease variants and isoforms
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gky1159
  contributor:
    fullname: Hornbeck
– volume: 4
  year: 2015
  ident: 2021041314334196800_R100
  article-title: SwissPalm: protein palmitoylation database
  publication-title: F1000Research
  doi: 10.12688/f1000research.6464.1
  contributor:
    fullname: Blanc
– volume: 88
  start-page: 97
  year: 1997
  ident: 2021041314334196800_R35
  article-title: A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81862-0
  contributor:
    fullname: Mahajan
– volume: 93
  start-page: 18
  year: 2011
  ident: 2021041314334196800_R106
  article-title: Post-translational myristoylation: fat matters in cellular life and death
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2010.10.018
  contributor:
    fullname: Martin
– volume: 3
  start-page: 19
  year: 2010
  ident: 2021041314334196800_R109
  article-title: Protein myristoylation in health and disease
  publication-title: J. Chem. Biol.
  doi: 10.1007/s12154-009-0032-8
  contributor:
    fullname: Wright
– volume: 51
  start-page: 143
  year: 2014
  ident: 2021041314334196800_R118
  article-title: Prenylation defects in inherited retinal diseases
  publication-title: J. Med. Genet.
  doi: doi:10.1136/jmedgenet-2013-102138.
  contributor:
    fullname: Roosing
– volume: 21
  start-page: 255
  year: 2003
  ident: 2021041314334196800_R2
  article-title: Proteomic analysis of post-translational modifications
  publication-title: Nat. Biotechnol.
  doi: 10.1038/nbt0303-255
  contributor:
    fullname: Mann
– volume: 8
  year: 2018
  ident: 2021041314334196800_R130
  article-title: PhosContext2vec: a distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction
  publication-title: Sci. Rep.
  contributor:
    fullname: Xu
– volume: 27
  start-page: 207
  year: 2008
  ident: 2021041314334196800_R53
  article-title: Integrated analytical strategies for the study of phosphorylation and glycosylation in proteins
  publication-title: Mass Spectrom. Rev.
  doi: 10.1002/mas.20164
  contributor:
    fullname: Temporini
– volume: 33
  start-page: 13524
  year: 1994
  ident: 2021041314334196800_R39
  article-title: New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us
  publication-title: Biochemistry
  doi: 10.1021/bi00250a003
  contributor:
    fullname: Hofsteenge
– volume: 127
  start-page: 333
  year: 1939
  ident: 2021041314334196800_R29
  article-title: Studies in protein metabolism VII. The metabolism of tyrosine
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)73846-5
  contributor:
    fullname: Schoenheimer
– volume: 15
  start-page: 707
  year: 2013
  ident: 2021041314334196800_R83
  article-title: SUMO: a (oxidative) stressed protein
  publication-title: Neuromolecular Med.
  doi: 10.1007/s12017-013-8266-6
  contributor:
    fullname: Feligioni
– volume: 11
  start-page: 3092
  year: 2015
  ident: 2021041314334196800_R17
  article-title: A novel method for predicting post-translational modifications on serine and threonine sites by using site-modification network profiles
  publication-title: Mol. Biosyst.
  doi: 10.1039/C5MB00384A
  contributor:
    fullname: Wang
– volume: 449
  start-page: 741
  year: 2013
  ident: 2021041314334196800_R110
  article-title: N-Myristoylation is essential for protein phosphatases PPM1A and PPM1B to dephosphorylate their physiological substrates in cells
  publication-title: Biochem. J.
  doi: 10.1042/BJ20121201
  contributor:
    fullname: Chida
– volume: 21
  year: 2011
  ident: 2021041314334196800_R72
  article-title: Regulation of chromatin by histone modifications
  publication-title: Cell Res.
  doi: 10.1038/cr.2011.22
  contributor:
    fullname: Bannister
– volume: 14
  start-page: 81
  year: 2010
  ident: 2021041314334196800_R93
  article-title: Protein sumoylation sites prediction based on two-stage feature selection
  publication-title: Mol. Divers.
  doi: 10.1007/s11030-009-9149-5
  contributor:
    fullname: Lu
– volume: 6
  year: 2005
  ident: 2021041314334196800_R78
  article-title: DNA methylation and human disease
  publication-title: Nat. Rev. Genet.
  doi: 10.1038/nrg1655
  contributor:
    fullname: Robertson
– volume: 2015
  start-page: 1
  year: 2015
  ident: 2021041314334196800_R26
  article-title: PEIMAN 1.0: post-translational modification enrichment, integration and matching analysis
  publication-title: Database
  doi: 10.1093/database/bav037
  contributor:
    fullname: Nickchi
– volume: 13
  start-page: 263
  year: 2001
  ident: 2021041314334196800_R77
  article-title: Histone methylation versus histone acetylation: new insights into epigenetic regulation
  publication-title: Curr. Opin. Cell Biol.
  doi: 10.1016/S0955-0674(00)00208-8
  contributor:
    fullname: Rice
– volume: 191
  start-page: 807
  year: 1951
  ident: 2021041314334196800_R94
  article-title: Proteolipides, a new type of tissue lipoproteins their isolation from brain
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)55985-8
  contributor:
    fullname: Folch
– volume: 19
  start-page: 6775
  year: 1999
  ident: 2021041314334196800_R36
  article-title: Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.19.10.6775
  contributor:
    fullname: Bartels
– volume: 26
  start-page: 399
  year: 2016
  ident: 2021041314334196800_R64
  article-title: Ubiquitin modifications
  publication-title: Cell Res.
  doi: 10.1038/cr.2016.39
  contributor:
    fullname: Swatek
– volume: 13
  start-page: 742
  year: 2014
  ident: 2021041314334196800_R14
  article-title: Impact of autoantibody glycosylation in autoimmune diseases
  publication-title: Autoimmun. Rev.
  doi: 10.1016/j.autrev.2014.02.005
  contributor:
    fullname: Goulabchand
– volume: 40
  start-page: 790
  year: 2006
  ident: 2021041314334196800_R22
  article-title: Analysis of posttranslational modifications of proteins by tandem mass spectrometry: mass spectrometry for proteomics analysis
  publication-title: Biotechniques
  doi: 10.2144/000112201
  contributor:
    fullname: Larsen
– volume: 24
  year: 2014
  ident: 2021041314334196800_R4
  article-title: Protein post-translational modifications and regulation of pluripotency in human stem cells
  publication-title: Cell Res.
  doi: 10.1038/cr.2013.151
  contributor:
    fullname: Wang
– volume: 38
  start-page: 14718
  year: 1999
  ident: 2021041314334196800_R47
  article-title: Catalytic mechanism of phosphorylase kinase probed by mutational studies
  publication-title: Biochemistry
  doi: 10.1021/bi991454f
  contributor:
    fullname: Skamnaki
– volume: 25
  start-page: 299
  year: 2009
  ident: 2021041314334196800_R121
  article-title: Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins
  publication-title: N. Biotechnol.
  doi: 10.1016/j.nbt.2009.03.011
  contributor:
    fullname: Stone
– volume: 36
  start-page: D679
  year: 2008
  ident: 2021041314334196800_R51
  article-title: PepCyber: P∼PEP: a database of human protein–protein interactions mediated by phosphoprotein-binding domains
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkm854
  contributor:
    fullname: Gong
– volume: 55
  start-page: 2015
  year: 2015
  ident: 2021041314334196800_R102
  article-title: In silico identification of protein S-palmitoylation sites and their involvement in human inherited disease
  publication-title: J. Chem. Inf. Model
  doi: 10.1021/acs.jcim.5b00276
  contributor:
    fullname: Li
– volume: 73
  start-page: 491
  year: 2004
  ident: 2021041314334196800_R11
  article-title: Role of glycosylation in development
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.73.011303.074043
  contributor:
    fullname: Haltiwanger
– volume: 27
  start-page: 2927
  year: 2011
  ident: 2021041314334196800_R24
  article-title: Computational prediction of eukaryotic phosphorylation sites
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btr525
  contributor:
    fullname: Trost
– volume: 81
  start-page: 4226
  year: 2007
  ident: 2021041314334196800_R74
  article-title: Arginine methylation of the human immunodeficiency virus type 1 Tat protein by PRMT6 negatively affects Tat interactions with both cyclin T1 and the Tat transactivation region
  publication-title: J. Virol.
  doi: 10.1128/JVI.01888-06
  contributor:
    fullname: Xie
– volume: 58
  start-page: 328
  year: 2015
  ident: 2021041314334196800_R115
  article-title: Protein prenylation and human diseases: a balance of protein farnesylation and geranylgeranylation
  publication-title: Sci. China Life Sci.
  doi: 10.1007/s11427-015-4836-1
  contributor:
    fullname: Xu
– volume: 27
  start-page: 558
  year: 2013
  ident: 2021041314334196800_R66
  article-title: Minireview: ubiquitination-regulated G protein-coupled receptor signaling and trafficking
  publication-title: Mol. Endocrinol.
  doi: 10.1210/me.2012-1404
  contributor:
    fullname: Alonso
– volume: 16
  start-page: 591
  year: 2016
  ident: 2021041314334196800_R3
  article-title: Recent progress in predicting posttranslational modification sites in proteins
  publication-title: Curr. Top. Med. Chem.
  doi: 10.2174/1568026615666150819110421
  contributor:
    fullname: Xu
– volume: 2
  start-page: 049
  year: 2018
  ident: 2021041314334196800_R23
  article-title: Prediction of protein post-translational modification sites: an overview
  publication-title: Ann. Proteom. Bioinform.
  contributor:
    fullname: Hasan
– volume: 1
  year: 2011
  ident: 2021041314334196800_R27
  article-title: Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database
  publication-title: Sci. Rep.
  doi: 10.1038/srep00090
  contributor:
    fullname: Khoury
– volume: 83
  year: 2014
  ident: 2021041314334196800_R25
  article-title: Prediction of protein post-translational modifications: main trends and methods
  publication-title: Russ. Chem. Rev.
  doi: 10.1070/RC2014v083n02ABEH004377
  contributor:
    fullname: Sobolev
– volume: 7
  year: 2011
  ident: 2021041314334196800_R40
  article-title: Sublancin is not a lantibiotic but an S-linked glycopeptide
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/nchembio.509
  contributor:
    fullname: Oman
– year: 2008
  ident: 2021041314334196800_R44
  article-title: Functional proteomics of protein phosphorylation in algal photosynthetic membranes
  contributor:
    fullname: Turkina
– volume: 97
  start-page: 220
  year: 2012
  ident: 2021041314334196800_R98
  article-title: Putting proteins in their place: palmitoylation in Huntington disease and other neuropsychiatric diseases
  publication-title: Prog. Neurobiol.
  doi: 10.1016/j.pneurobio.2011.11.002
  contributor:
    fullname: Young
– volume: 82
  start-page: 357
  year: 2013
  ident: 2021041314334196800_R90
  article-title: Sumoylation: a regulatory protein modification in health and disease
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev-biochem-061909-093311
  contributor:
    fullname: Flotho
– volume: 20
  start-page: 2923
  year: 2020
  ident: 2021041314334196800_R55
  article-title: Protein acetylation and deacetylation: an important regulatory modification in gene transcription
  publication-title: Exp. Ther. Med.
  contributor:
    fullname: Xia
– volume: 198
  start-page: 155
  year: 2012
  ident: 2021041314334196800_R59
  article-title: Mechanistic insights into the regulation of metabolic enzymes by acetylation
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.201202056
  contributor:
    fullname: Xiong
– volume: 51
  year: 1964
  ident: 2021041314334196800_R31
  article-title: Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.51.5.786
  contributor:
    fullname: Allfrey
– volume: 325
  start-page: 834
  year: 2009
  ident: 2021041314334196800_R56
  article-title: Lysine acetylation targets protein complexes and co-regulates major cellular functions
  publication-title: Science
  doi: 10.1126/science.1175371
  contributor:
    fullname: Choudhary
– volume: 20
  start-page: 1242
  year: 2014
  ident: 2021041314334196800_R70
  article-title: Ubiquitination in disease pathogenesis and treatment
  publication-title: Nat. Med.
  doi: 10.1038/nm.3739
  contributor:
    fullname: Popovic
– volume: 80
  start-page: 305
  year: 2011
  ident: 2021041314334196800_R116
  article-title: Rab GTPases as regulators of endocytosis, targets of disease and therapeutic opportunities
  publication-title: Clin. Genet.
  doi: 10.1111/j.1399-0004.2011.01724.x
  contributor:
    fullname: Agola
– volume: 78
  start-page: 365
  year: 2010
  ident: 2021041314334196800_R68
  article-title: Identification, analysis, and prediction of protein ubiquitination sites
  publication-title: Proteins Struct. Funct. Bioinf.
  doi: 10.1002/prot.22555
  contributor:
    fullname: Radivojac
– volume: 3
  year: 2002
  ident: 2021041314334196800_R96
  article-title: Protein palmitoylation: a regulator of neuronal development and function
  publication-title: Nat. Rev. Neurosci.
  doi: 10.1038/nrn940
  contributor:
    fullname: El-Husseini
– volume: 8
  year: 2013
  ident: 2021041314334196800_R107
  article-title: Protein N-myristoylation plays a critical role in the endoplasmic reticulum morphological change induced by overexpression of protein Lunapark, an integral membrane protein of the endoplasmic reticulum
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0078235
  contributor:
    fullname: Moriya
– volume: 1
  year: 2013
  ident: 2021041314334196800_R30
  article-title: Tyrosine-O-sulfation: an overview
  publication-title: JSM Biotechnol. Bioeng.
  contributor:
    fullname: Kanan
– volume: 14
  start-page: 397
  year: 2013
  ident: 2021041314334196800_R132
  article-title: Computational prediction of protein–protein interaction networks: algorithms and resources
  publication-title: Curr. Genomics
  doi: 10.2174/1389202911314060004
  contributor:
    fullname: Zahiri
– volume: 30
  start-page: 16160
  year: 2010
  ident: 2021041314334196800_R104
  article-title: Reduced Alzheimer’s disease β-amyloid deposition in transgenic mice expressing S-palmitoylation-deficient APH1aL and nicastrin
  publication-title: J. Neurosci.
  doi: 10.1523/JNEUROSCI.4436-10.2010
  contributor:
    fullname: Meckler
– volume: 47
  start-page: D298
  year: 2018
  ident: 2021041314334196800_R6
  article-title: dbPTM in 2019: exploring disease association and cross-talk of post-translational modifications
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gky1074
  contributor:
    fullname: Huang
– volume: 2011
  start-page: 1
  year: 2011
  ident: 2021041314334196800_R12
  article-title: Small changes huge impact: the role of protein posttranslational modifications in cellular homeostasis and disease
  publication-title: J. Amino Acids
  doi: 10.4061/2011/207691
  contributor:
    fullname: Karve
– volume: 72
  start-page: 11
  year: 1975
  ident: 2021041314334196800_R32
  article-title: Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells
  publication-title: Proc. Natl. Acad. Sci.
  doi: 10.1073/pnas.72.1.11
  contributor:
    fullname: Goldstein
– volume: 47
  start-page: 167
  year: 2013
  ident: 2021041314334196800_R84
  article-title: Control of nuclear activities by substrate-selective and protein-group SUMOylation
  publication-title: Annu. Rev. Genet.
  doi: 10.1146/annurev-genet-111212-133453
  contributor:
    fullname: Jentsch
– volume: 195
  start-page: 639
  year: 1981
  ident: 2021041314334196800_R37
  article-title: The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr (Ser) for the N-glycosylation step during glycoprotein biosynthesis
  publication-title: Biochem. J.
  doi: 10.1042/bj1950639
  contributor:
    fullname: Bause
– volume: 97
  start-page: 253
  year: 2017
  ident: 2021041314334196800_R69
  article-title: Ubiquitination and the regulation of membrane proteins
  publication-title: Physiol. Rev.
  doi: 10.1152/physrev.00012.2016
  contributor:
    fullname: Foot
– volume: 2020
  start-page: 1
  year: 2020
  ident: 2021041314334196800_R125
  article-title: EPSD: a well-annotated data resource of protein phosphorylation sites in eukaryotes
  publication-title: Brief. Bioinformatics
  contributor:
    fullname: Lin
– volume: 10
  year: 2015
  ident: 2021041314334196800_R108
  article-title: Identification of human N-myristoylated proteins from human complementary DNA resources by cell-free and cellular metabolic labeling analyses
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0136360
  contributor:
    fullname: Takamitsu
– volume: 7
  year: 2006
  ident: 2021041314334196800_R50
  article-title: PhosphoregDB: the tissue and sub-cellular distribution of mammalian protein kinases and phosphatases
  publication-title: BMC Bioinform.
  doi: 10.1186/1471-2105-7-82
  contributor:
    fullname: Forrest
– volume: 11
  year: 2015
  ident: 2021041314334196800_R48
  article-title: The roles of post-translational modifications in the context of protein interaction networks
  publication-title: PLoS Comput. Biol.
  doi: 10.1371/journal.pcbi.1004049
  contributor:
    fullname: Duan
– volume: 11
  year: 2020
  ident: 2021041314334196800_R133
  article-title: Machine learning techniques for soybean charcoal rot disease prediction
  publication-title: Front. Plant Sci.
  doi: 10.3389/fpls.2020.590529
  contributor:
    fullname: Khalili
– volume: 4
  start-page: 1633
  year: 2004
  ident: 2021041314334196800_R5
  article-title: Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
  publication-title: Proteomics
  doi: 10.1002/pmic.200300771
  contributor:
    fullname: Blom
– volume: 367
  start-page: 2540
  year: 2012
  ident: 2021041314334196800_R49
  article-title: Modular evolution of phosphorylation-based signalling systems
  publication-title: Philos. Trans. R. Soc. B Biol. Sci.
  doi: 10.1098/rstb.2012.0106
  contributor:
    fullname: Jin
– volume: 15
  start-page: 307
  year: 2017
  ident: 2021041314334196800_R16
  article-title: Protein post-translational modifications: in silico prediction tools and molecular modeling
  publication-title: Comput. Struct. Biotechnol. J.
  doi: 10.1016/j.csbj.2017.03.004
  contributor:
    fullname: Audagnotto
– volume: 92
  start-page: 80
  year: 2013
  ident: 2021041314334196800_R7
  article-title: Effect of posttranslational modifications on enzyme function and assembly
  publication-title: J. Proteomics
  doi: 10.1016/j.jprot.2013.03.025
  contributor:
    fullname: Ryšlavá
– volume: 83
  start-page: 1077
  year: 1978
  ident: 2021041314334196800_R33
  article-title: Structure of rhodotorucine A, a novel lipopeptide, inducing mating tube formation in Rhodosporidium toruloides
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/0006-291X(78)91505-X
  contributor:
    fullname: Kamiya
– volume: 36
  year: 2016
  ident: 2021041314334196800_R52
  article-title: Combined defects in oxidative phosphorylation and fatty acid β-oxidation in mitochondrial disease
  publication-title: Biosci. Rep.
  doi: 10.1042/BSR20150295
  contributor:
    fullname: Nsiah-Sefaa
– volume: 150
  start-page: 314
  year: 1982
  ident: 2021041314334196800_R34
  article-title: Identification of the NH2-terminal blocking group of calcineurin B as myristic acid
  publication-title: FEBS Lett.
  doi: 10.1016/0014-5793(82)80759-X
  contributor:
    fullname: Aitken
– volume: 259
  start-page: 1865
  year: 1993
  ident: 2021041314334196800_R8
  article-title: Protein prenylation: a mediator of protein-protein interactions
  publication-title: Science
  doi: 10.1126/science.8456312
  contributor:
    fullname: Marshall
– volume: 111
  start-page: 460
  year: 1992
  ident: 2021041314334196800_R38
  article-title: Evidence for the existence of O-linked sugar chains consisting of glucose and xylose in bovine thrombospondin
  publication-title: J. Biochem.
  doi: 10.1093/oxfordjournals.jbchem.a123780
  contributor:
    fullname: Nishimura
– volume: 1808
  start-page: 2981
  year: 2011
  ident: 2021041314334196800_R99
  article-title: Protein palmitoylation and subcellular trafficking
  publication-title: Biochim. Biophys. Acta (BBA) Biomembr.
  doi: 10.1016/j.bbamem.2011.07.009
  contributor:
    fullname: Aicart-Ramos
– volume: 32
  start-page: 815
  year: 2012
  ident: 2021041314334196800_R71
  article-title: Chemical and biochemical approaches in the study of histone methylation and demethylation
  publication-title: Med. Res. Rev.
  doi: 10.1002/mrr.20228
  contributor:
    fullname: Li
– volume: 2014
  start-page: 1
  year: 2014
  ident: 2021041314334196800_R79
  article-title: Histone lysine methylation in diabetic nephropathy
  publication-title: J. Diabetes Res.
  contributor:
    fullname: Sun
– volume: 23
  start-page: 2877
  year: 2015
  ident: 2021041314334196800_R18
  article-title: Towards the computational design of protein post-translational regulation
  publication-title: Bioorg. Med. Chem.
  doi: 10.1016/j.bmc.2015.04.056
  contributor:
    fullname: Strumillo
– volume-title: An Introduction to Statistical Learning
  year: 2013
  ident: 2021041314334196800_R131
  doi: 10.1007/978-1-4614-7138-7
  contributor:
    fullname: James
– volume: 13
  start-page: 204
  year: 2015
  ident: 2021041314334196800_R91
  article-title: Advances in the development of SUMO specific protease (SENP) inhibitors
  publication-title: Comput. Struct. Biotechnol. J.
  doi: 10.1016/j.csbj.2015.03.001
  contributor:
    fullname: Kumar
– volume: 453
  start-page: 231
  year: 2013
  ident: 2021041314334196800_R85
  article-title: SUMOylation is a regulator of the translocation of Jak2 between nucleus and cytosol
  publication-title: Biochem. J.
  doi: 10.1042/BJ20121375
  contributor:
    fullname: Sedek
SSID ssj0067884
Score 2.6906924
Snippet Posttranslational modifications (PTMs) refer to amino acid side chain modification in some proteins after their biosynthesis. There are more than 400 different...
SourceID pubmedcentral
crossref
SourceType Open Access Repository
Aggregation Database
SubjectTerms Review
SummonAdditionalLinks – databaseName: Scholars Portal Journals: Open Access
  dbid: M48
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1bS8MwFA4yEXwRrzhv5MEXwbi1TdpMEBFxDGE-WdhbyRUHs9W1gvv35rTZtLAXn9MLnLTnS8758n0IXTIrdcw1J8YySqhKIsIDZUkomdJUiFjWWnrjl3iU0ucJm_wej_YBLNdu7cBPKp3Pbr4_F_fuh7_zYkg94FJCzu9JIWQfLIc3Q4eLQPAa01VPwWXl2n_Y4SUHQmPkm5brntACqTZZ8g_6DHfRjl824odmnvfQhsn30VZjJLk4QCl47pIKcGfmq3v4vdBAA2oqcnia41qSYZqXt3jua_blNa6KYlZikWs3DD0buBo3ttLlIUqHT6-PI-INE4hyuFyRSHEa1vV6bbRkmps-lYZZQ42RTERSBzYUgXabBKECykIr2EC7NJMoobkaREeokxe5OUbYclCOdPPnVkhUCSVsoIwLlcsARut-3EVXywhlH40uRtb0s6NsGc3MR7OLklYIVzeAtHV7JJ--1RLX3OWWkLKTf7zlFG2HwDcBVk1yhjrV_MucuwVDJS_q7-AHUCDHwA
  priority: 102
  providerName: Scholars Portal
Title Post-translational modifications in proteins: resources, tools and prediction methods
URI https://pubmed.ncbi.nlm.nih.gov/PMC8040245
Volume 2021
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV07a8MwEBZJoCVL6ZOmj6ChS6GOY1uylW6lJIRCSocGshm9TA2JHGJ36L_vSbbbZu3iRRaY0_k-3enTdwjd0UyomCnm6YwSj8gk8lggMy8UVCrCeSyclt7iNZ4vycuKrjqItndhHGlfinxk1puRyT8ct3K7kX7LE_PfFs8MPC8k1O-iLsBvm6LX4ReCLyPNeSRk674lWlpA8AXnAqJxHx1CVgaw5NRef6FonxL5B2Nmx-io2Rzip_ojTlBHm1N0ULeL_DpDS9tZ16ssuqybGh7eFMqSfeq6G84NdsILuSkf8a6pzJcPuCqKdYm5UTBsT2bs27huHl2eo-Vs-v4895q2CJ4E9K28SDISuqq80kpQxfSYCE0zTbQWlEdCBVnIAwWpAJcBoWHG6URBMEkkV0xOogvUM4XRlwhnzOpDwirBPohILnkWSA1Wg_9cKzWOB-i-tVC6rdUv0vrUOkpbw6aNYQco2TPhzwQrYL0_AuvqhKybdbz698xr1A8tx8QyaZIb1Kt2n_oWNgmVGIJrjKdDl2LDc0HY0LnJN8HDx30
link.rule.ids 230,314,727,780,784,864,885,24318,27924,27925,53791,53793
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT8JAEJ4gRuVifEZ87sGLibW03W0Xb4ZIUIF4gIRbs8_YBAqh9eC_d7cPlavn7SbNzHa-mdmv3wDcEs1lSCV1lCbYwSIKHOoJ7ficCIkZC3mhpTcah4Mpfp2RWQNI_S9MQdoXPHlI54uHNPkouJWrhXBrnpj7PupRc_J8TNwt2CZB1PXqIr0MwCb8UlzdSJp63bVUSwsJLmeMm3jcgl1TlxlgKvRef8FokxT5B2X6B7BfpYfoqXyNQ2io9Ah2yoGRX8cwtbN1ndziy7zq4qHFUlq6T9l5Q0mKCumFJM0e0brqzWf3KF8u5xliqTTL9m7GPo3K8dHZCUz7z5PewKkGIzjC4G_uBIJiv-jLSyU5kVR1MFdEK6wUJyzg0tM-86QpBpjwMPE1I11pwkkkmKSiG5xCM12m6gyQplYh0vjJZEJYMMG0J5SxmvnSlZSdsA13tYXiVal_EZf31kFcGzauDNuGaMOEPxushPXmivFsIWVdefL83ztvYG8wGQ3j4cv47QJavmWcWF5NdAnNfP2prkzKkPPr4oB8A1hUyDY
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1JT8JAFJ4oRsPFuEZc5-DFxFLazrSDN4MSXCAcJOHWzBqbQCG0Hvz3vumicPU8naR5781bv3wPoVtqhAqZYo42lDhERoHDPGkcX1CpCOehKLj0hqNwMCGvUzpdW_VVgPalSNrpbN5Ok88CW7mcS7fGibnjYY-B5fmEuktl3G20QwMwsrpQL50wuGBGqqkk1OyuhVvasOAKzgX45Cbag9oMglPB-foXkDaBkWuRpn-A9qsUET-Wv3KItnR6hHbLpZHfx2hi9-s6uY0xs6qTh-cLZSE_ZfcNJyku6BeSNHvAq6o_n93jfLGYZZinCo7tfMZ-jcsV0tkJmvSfP3oDp1qO4EiIwbkTSEb8ojevtBJUMd0hQlOjidaC8kAoz_jcU1AQcOkR6htOuwpcSiS5YrIbnKJGukj1GcKGWZZI0BVkQ0RyyY0nNUgNXrtWqhO20F0toXhZcmDE5ew6iGvBxpVgWyjaEOHvBUtjvXkC2i3orCttnv_75g3aGz_14_eX0dsFavoWdGKhNdElauSrL30FWUMurgv7-AEseslJ
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Post-translational+modifications+in+proteins%3A+resources%2C+tools+and+prediction+methods&rft.jtitle=Database+%3A+the+journal+of+biological+databases+and+curation&rft.au=Ramazi%2C+Shahin&rft.au=Zahiri%2C+Javad&rft.date=2021-04-07&rft.issn=1758-0463&rft.eissn=1758-0463&rft.volume=2021&rft_id=info:doi/10.1093%2Fdatabase%2Fbaab012&rft.externalDBID=n%2Fa&rft.externalDocID=10_1093_database_baab012
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1758-0463&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1758-0463&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1758-0463&client=summon