دورية أكاديمية

A resource database for protein kinase substrate sequence-preference motifs based on large-scale mass spectrometry data

التفاصيل البيبلوغرافية
العنوان: A resource database for protein kinase substrate sequence-preference motifs based on large-scale mass spectrometry data
المؤلفون: Brian G. Poll, Kirby T. Leo, Venky Deshpande, Nipun Jayatissa, Trairak Pisitkun, Euijung Park, Chin-Rang Yang, Viswanathan Raghuram, Mark A. Knepper
المصدر: Cell Communication and Signaling, Vol 22, Iss 1, Pp 1-12 (2024)
بيانات النشر: BMC, 2024.
سنة النشر: 2024
المجموعة: LCC:Medicine
LCC:Cytology
مصطلحات موضوعية: Phosphorylation, Protein kinases, Kinase prediction, Medicine, Cytology, QH573-671
الوصف: Abstract Background Protein phosphorylation is one of the most prevalent posttranslational modifications involved in molecular control of cellular processes, and is mediated by over 520 protein kinases in humans and other mammals. Identification of the protein kinases responsible for phosphorylation events is key to understanding signaling pathways. Unbiased phosphoproteomics experiments have generated a wealth of data that can be used to identify protein kinase targets and their preferred substrate sequences. Methods This study utilized prior data from mass spectrometry-based studies identifying sites of protein phosphorylation after in vitro incubation of protein mixtures with recombinant protein kinases. PTM-Logo software was used with these data to generate position-dependent Shannon information matrices and sequence motif ‘logos’. Webpages were constructed for facile access to logos for each kinase and a new stand-alone application was written in Python that uses the position-dependent Shannon information matrices to identify kinases most likely to phosphorylate a particular phosphorylation site. Results A database of kinase substrate target preference logos allows browsing, searching, or downloading target motif data for each protein kinase ( https://esbl.nhlbi.nih.gov/Databases/Kinase_Logos/ ). These logos were combined with phylogenetic analysis of protein kinase catalytic sequences to reveal substrate preference patterns specific to particular groups of kinases ( https://esbl.nhlbi.nih.gov/Databases/Kinase_Logos/KinaseTree.html ). A stand-alone program, KinasePredictor, is provided ( https://esbl.nhlbi.nih.gov/Databases/Kinase_Logos/KinasePredictor.html ). It takes as input, amino-acid sequences surrounding a given phosphorylation site and generates a ranked list of protein kinases most likely to phosphorylate that site. Conclusions This study provides three new resources for protein kinase characterization. It provides a tool for prediction of kinase-substrate interactions, which in combination with other types of data (co-localization, etc.), can predict which kinases are likely responsible for a given phosphorylation event in a given tissue. Video Abstract
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1478-811X
Relation: https://doaj.org/toc/1478-811X
DOI: 10.1186/s12964-023-01436-2
URL الوصول: https://doaj.org/article/58a7eaa096d5461f9c37d64fd8eca33d
رقم الأكسشن: edsdoj.58a7eaa096d5461f9c37d64fd8eca33d
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:1478811X
DOI:10.1186/s12964-023-01436-2