PepCyber:P∼PEP: A database of human protein-protein interactions mediated by phosphoprotein-binding domains

Wuming Gong, Dihan Zhou, Yongliang Ren, Yejun Wang, Zhixiang Zuo, Yanping Shen, Feifei Xiao, Qi Zhu, Ailing Hong, Xiaochuan Zhou, Xiaolian Gao, Tongbin Li

Research output: Contribution to journalArticlepeer-review

42 Scopus citations


Phosphoprotein-binding domains (PPBDs) mediate many important cellular and molecular processes. Ten PPBDs have been known to exist in the human proteome, namely, 14-3-3, BRCT, C2, FHA, MH2, PBD, PTB, SH2, WD-40 and WW. PepCyber:P∼PEP is a newly constructed database specialized in documenting human PPBD-containing proteins and PPBD-mediated interactions. Our motivation is to provide the research community with a rich information source emphasizing the reported, experimentally validated data for specific PPBD-PPEP interactions. This information is not only useful for designing, comparing and validating the relevant experiments, but it also serves as a knowledge-base for computationally constructing systems signaling pathways and networks. PepCyber:P∼PEP is accessible through the URL, The current release of the database contains 7044 PPBD-mediated interactions involving 337 PPBD-containing proteins and 1123 substrate proteins.

Original languageEnglish (US)
Pages (from-to)D679-D683
JournalNucleic acids research
Issue numberSUPPL. 1
StatePublished - Jan 2008

Bibliographical note

Funding Information:
We thank the Supercomputing Institute, University of Minnesota for computational resources and Dr K. Cassidy for reviewing the database and the manuscript. We also acknowledge the support of NIH (1R21CA126209 to X.G. and T.L.), Minnesota Medical Foundation (to T.L.), NIH/GM/AI (R43 GM076941 to X.G.) and the R. A. Welch Foundation (E-1270 to X.G.). Funding to pay the Open Access publication charges for this article was provided by NIH/NCI.


Dive into the research topics of 'PepCyber:P∼PEP: A database of human protein-protein interactions mediated by phosphoprotein-binding domains'. Together they form a unique fingerprint.

Cite this