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OGT Protein Interaction Network (OGT-PIN): A Curated Database of Experimentally Identified Interaction Proteins of OGT.
Ma, Junfeng; Hou, Chunyan; Li, Yaoxiang; Chen, Shufu; Wu, Ci.
Affiliation
  • Ma J; Lombardi Comprehensive Cancer Center, Department of Oncology, Georgetown University Medical Center, Washington, DC 20057, USA.
  • Hou C; Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
  • Li Y; Lombardi Comprehensive Cancer Center, Department of Oncology, Georgetown University Medical Center, Washington, DC 20057, USA.
  • Chen S; School of Engineering, Pennsylvania State University Behrend, Erie, PA 16563, USA.
  • Wu C; Lombardi Comprehensive Cancer Center, Department of Oncology, Georgetown University Medical Center, Washington, DC 20057, USA.
Int J Mol Sci ; 22(17)2021 Sep 06.
Article in En | MEDLINE | ID: mdl-34502531
Interactions between proteins are essential to any cellular process and constitute the basis for molecular networks that determine the functional state of a cell. With the technical advances in recent years, an astonishingly high number of protein-protein interactions has been revealed. However, the interactome of O-linked N-acetylglucosamine transferase (OGT), the sole enzyme adding the O-linked ß-N-acetylglucosamine (O-GlcNAc) onto its target proteins, has been largely undefined. To that end, we collated OGT interaction proteins experimentally identified in the past several decades. Rigorous curation of datasets from public repositories and O-GlcNAc-focused publications led to the identification of up to 929 high-stringency OGT interactors from multiple species studied (including Homo sapiens, Mus musculus, Rattus norvegicus, Drosophila melanogaster, Arabidopsis thaliana, and others). Among them, 784 human proteins were found to be interactors of human OGT. Moreover, these proteins spanned a very diverse range of functional classes (e.g., DNA repair, RNA metabolism, translational regulation, and cell cycle), with significant enrichment in regulating transcription and (co)translation. Our dataset demonstrates that OGT is likely a hub protein in cells. A webserver OGT-Protein Interaction Network (OGT-PIN) has also been created, which is freely accessible.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Acetylglucosamine / Protein Processing, Post-Translational / N-Acetylglucosaminyltransferases / Databases, Protein / Protein Interaction Maps / Data Curation Limits: Animals / Humans Language: En Journal: Int J Mol Sci Year: 2021 Document type: Article Affiliation country: Estados Unidos Country of publication: Suiza

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Acetylglucosamine / Protein Processing, Post-Translational / N-Acetylglucosaminyltransferases / Databases, Protein / Protein Interaction Maps / Data Curation Limits: Animals / Humans Language: En Journal: Int J Mol Sci Year: 2021 Document type: Article Affiliation country: Estados Unidos Country of publication: Suiza