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LLPSDB: a database of proteins undergoing liquid–liquid phase separation in vitro

Liquid-liquid phase separation (LLPS) leads to a conversion of homogeneous solution into a dense phase that often resembles liquid droplets, and a dilute phase. An increasing number of investigations have shown that biomolecular condensates formed by LLPS play important roles in both physiology and...

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Detalles Bibliográficos
Autores principales: Li, Qian, Peng, Xiaojun, Li, Yuanqing, Tang, Wenqin, Zhu, Jia’an, Huang, Jing, Qi, Yifei, Zhang, Zhuqing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6943074/
https://www.ncbi.nlm.nih.gov/pubmed/31906602
http://dx.doi.org/10.1093/nar/gkz778
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author Li, Qian
Peng, Xiaojun
Li, Yuanqing
Tang, Wenqin
Zhu, Jia’an
Huang, Jing
Qi, Yifei
Zhang, Zhuqing
author_facet Li, Qian
Peng, Xiaojun
Li, Yuanqing
Tang, Wenqin
Zhu, Jia’an
Huang, Jing
Qi, Yifei
Zhang, Zhuqing
author_sort Li, Qian
collection PubMed
description Liquid-liquid phase separation (LLPS) leads to a conversion of homogeneous solution into a dense phase that often resembles liquid droplets, and a dilute phase. An increasing number of investigations have shown that biomolecular condensates formed by LLPS play important roles in both physiology and pathology. It has been suggested the phase behavior of proteins would be not only determined by sequences, but controlled by micro-environmental conditions. Here, we introduce LLPSDB (http://bio-comp.ucas.ac.cn/llpsdb or http://bio-comp.org.cn/llpsdb), a web-accessible database providing comprehensive, carefully curated collection of proteins involved in LLPS as well as corresponding experimental conditions in vitro from published literatures. The current release of LLPSDB incorporates 1182 entries with 273 independent proteins and 2394 specific conditions. The database provides a variety of data including biomolecular information (protein sequence, protein modification, nucleic acid, etc.), specific phase separation information (experimental conditions, phase behavior description, etc.) and comprehensive annotations. To our knowledge, LLPSDB is the first available database designed for LLPS related proteins specifically. It offers plenty of valuable resources for exploring the relationship between protein sequence and phase behavior, and will enhance the development of phase separation prediction methods, which may further provide more insights into a comprehensive understanding of LLPS in cellular function and related diseases.
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spelling pubmed-69430742020-01-08 LLPSDB: a database of proteins undergoing liquid–liquid phase separation in vitro Li, Qian Peng, Xiaojun Li, Yuanqing Tang, Wenqin Zhu, Jia’an Huang, Jing Qi, Yifei Zhang, Zhuqing Nucleic Acids Res Database Issue Liquid-liquid phase separation (LLPS) leads to a conversion of homogeneous solution into a dense phase that often resembles liquid droplets, and a dilute phase. An increasing number of investigations have shown that biomolecular condensates formed by LLPS play important roles in both physiology and pathology. It has been suggested the phase behavior of proteins would be not only determined by sequences, but controlled by micro-environmental conditions. Here, we introduce LLPSDB (http://bio-comp.ucas.ac.cn/llpsdb or http://bio-comp.org.cn/llpsdb), a web-accessible database providing comprehensive, carefully curated collection of proteins involved in LLPS as well as corresponding experimental conditions in vitro from published literatures. The current release of LLPSDB incorporates 1182 entries with 273 independent proteins and 2394 specific conditions. The database provides a variety of data including biomolecular information (protein sequence, protein modification, nucleic acid, etc.), specific phase separation information (experimental conditions, phase behavior description, etc.) and comprehensive annotations. To our knowledge, LLPSDB is the first available database designed for LLPS related proteins specifically. It offers plenty of valuable resources for exploring the relationship between protein sequence and phase behavior, and will enhance the development of phase separation prediction methods, which may further provide more insights into a comprehensive understanding of LLPS in cellular function and related diseases. Oxford University Press 2020-01-08 2019-09-06 /pmc/articles/PMC6943074/ /pubmed/31906602 http://dx.doi.org/10.1093/nar/gkz778 Text en © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Database Issue
Li, Qian
Peng, Xiaojun
Li, Yuanqing
Tang, Wenqin
Zhu, Jia’an
Huang, Jing
Qi, Yifei
Zhang, Zhuqing
LLPSDB: a database of proteins undergoing liquid–liquid phase separation in vitro
title LLPSDB: a database of proteins undergoing liquid–liquid phase separation in vitro
title_full LLPSDB: a database of proteins undergoing liquid–liquid phase separation in vitro
title_fullStr LLPSDB: a database of proteins undergoing liquid–liquid phase separation in vitro
title_full_unstemmed LLPSDB: a database of proteins undergoing liquid–liquid phase separation in vitro
title_short LLPSDB: a database of proteins undergoing liquid–liquid phase separation in vitro
title_sort llpsdb: a database of proteins undergoing liquid–liquid phase separation in vitro
topic Database Issue
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6943074/
https://www.ncbi.nlm.nih.gov/pubmed/31906602
http://dx.doi.org/10.1093/nar/gkz778
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