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DTSTAMP:20260716T152756Z
UID:71c7c15c-385c-4ad6-a210-20081b4b7eb6
DTSTART:20240306T090000Z
DTEND:20240306T170000Z
DESCRIPTION:A common mechanism for protein regulation is through post-trans
 lational modifications(PTMs)\, which can affect the activity\, subcellular
  localization\, and stability of proteins. Most of the available databases
  on protein PTMs collect and integrate PTM information from different reso
 urces\, but they provide very little or no information on the reliability 
 of the identified PTM sites\, experimental condition\, pathological status
  and their functional relevance. In order to remove the hidden layer on th
 e proteomics experiments using different versions of sequence databases wi
 th different search settings and FDR controls\, and to potentially look fo
 r additional modifications that could explain the identified spectra from 
 the original experiments\, we created Scop3PTM.\n\nScop3PTM is an interact
 ive knowledge-base on human PTMs built by reprocessing all available human
  proteomics experiments from PRIDE with the uniform and updated sequence d
 atabase\, search settings and FDR control.  Scop3PTM knowledgebase contain
 s 120 different biological modifications (phosphorylation\, acetylation et
 c) and more than 300 non-biological modifications (artefacts and chemical 
 derivatives).\n\nFurthermore\, PTM sites are put into sequence\, structura
 l and biophysical context by annotating every human protein with per-resid
 ue structural propensity\, solvent accessibility\, disordered probability\
 , backbone and sidechain dynamics\, and early folding information. Scop3PT
 M acts as a much-needed bridge between the fields of proteomics\, structur
 al bioinformatics and intrinsically disordered proteins (IDPs)\, and prese
 nts a unique resource for visualization\, and to understand the impact of 
 PTM-sites on structure-function relationship of proteins.\n\nA common mech
 anism for protein regulation is through post-translational modifications(P
 TMs)\, which can affect the activity\, subcellular localization\, and stab
 ility of proteins. Most of the available databases on protein PTMs collect
  and integrate PTM information from different resources\, but they provide
  very little or no information on the reliability of the identified PTM si
 tes\, experimental condition\, pathological status and their functional re
 levance. In order to remove the hidden layer on the proteomics experiments
  using different versions of sequence databases with different search sett
 ings and FDR controls\, and to potentially look for additional modificatio
 ns that could explain the identified spectra from the original experiments
 \, we created Scop3PTM. Scop3PTM is an interactive knowledge-base on human
  PTMs built by reprocessing all available human proteomics experiments fro
 m PRIDE with the uniform and updated sequence database\, search settings a
 nd FDR control. Scop3PTM knowledgebase contains 120 different biological m
 odifications (phosphorylation\, acetylation etc) and more than 300 non-bio
 logical modifications (artefacts and chemical derivatives). Furthermore\, 
 PTM sites are put into sequence\, structural and biophysical context by an
 notating every human protein with per-residue structural propensity\, solv
 ent accessibility\, disordered probability\, backbone and sidechain dynami
 cs\, and early folding information. Scop3PTM acts as a much-needed bridge 
 between the fields of proteomics\, structural bioinformatics and intrinsic
 ally disordered proteins (IDPs)\, and presents a unique resource for visua
 lization\, and to understand the impact of PTM-sites on structure-function
  relationship of proteins.
SUMMARY:Apply Scop3PTM web-interface to understand post-translational modif
 ications (PTMs) of proteins
URL;VALUE=URI:https://training.vib.be/all-trainings/apply-scop3ptm-web-inte
 rface-understand-post-translational-modifications-ptms
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