Limits...
dbSNO 2.0: a resource for exploring structural environment, functional and disease association and regulatory network of protein S-nitrosylation.

Chen YJ, Lu CT, Su MG, Huang KY, Ching WC, Yang HH, Liao YC, Chen YJ, Lee TY - Nucleic Acids Res. (2014)

Bottom Line: Given the increasing number of proteins reported to be regulated by S-nitrosylation (SNO), it is considered to act, in a manner analogous to phosphorylation, as a pleiotropic regulator that elicits dual effects to regulate diverse pathophysiological processes by altering protein function, stability, and conformation change in various cancers and human disorders.Additionally, the annotations of protein molecular functions, biological processes, functional domains and human diseases are integrated to explore the functional and disease associations for S-nitrosoproteome.In this update, users are allowed to search a group of interested proteins/genes and the system reconstructs the SNO regulatory network based on the information of metabolic pathways and protein-protein interactions.

View Article: PubMed Central - PubMed

Affiliation: Institute of Chemistry, Academia Sinica, Taipei 115, Taiwan.

Show MeSH

Related in: MedlinePlus

Protein–protein interaction network of all human S-nitrosylated proteins with the annotations of GO molecular function (marked in different colors) and KEGG metabolic pathways (clustered in different pathway groups).
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4383970&req=5

Figure 3: Protein–protein interaction network of all human S-nitrosylated proteins with the annotations of GO molecular function (marked in different colors) and KEGG metabolic pathways (clustered in different pathway groups).

Mentions: Based on the annotations of GO database, the distributions of the biological process, molecular function and cellular component for human and mouse general and SNO proteins are presented in Supplementary Tables S5–S8, respectively. According to the annotations of KEGG pathways, the distributions of pathway annotations for human and mouse SNO proteins are provided in Supplementary Tables S9–S12, respectively. Figure 3 provides a global network view for PPI of all 720 human SNO proteins with the annotations of GO molecular function and KEGG metabolic pathways. The result could provide a preview of the SNO protein family clustering involving in what major functional annotation and biological pathway, such as RNA binding family in ribosome and spliceosome, structural molecule activity family in focal adhesion and adherens junction and enzymes in glycolysis/gluconeogenesis, cancer and disease regulation.


dbSNO 2.0: a resource for exploring structural environment, functional and disease association and regulatory network of protein S-nitrosylation.

Chen YJ, Lu CT, Su MG, Huang KY, Ching WC, Yang HH, Liao YC, Chen YJ, Lee TY - Nucleic Acids Res. (2014)

Protein–protein interaction network of all human S-nitrosylated proteins with the annotations of GO molecular function (marked in different colors) and KEGG metabolic pathways (clustered in different pathway groups).
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4383970&req=5

Figure 3: Protein–protein interaction network of all human S-nitrosylated proteins with the annotations of GO molecular function (marked in different colors) and KEGG metabolic pathways (clustered in different pathway groups).
Mentions: Based on the annotations of GO database, the distributions of the biological process, molecular function and cellular component for human and mouse general and SNO proteins are presented in Supplementary Tables S5–S8, respectively. According to the annotations of KEGG pathways, the distributions of pathway annotations for human and mouse SNO proteins are provided in Supplementary Tables S9–S12, respectively. Figure 3 provides a global network view for PPI of all 720 human SNO proteins with the annotations of GO molecular function and KEGG metabolic pathways. The result could provide a preview of the SNO protein family clustering involving in what major functional annotation and biological pathway, such as RNA binding family in ribosome and spliceosome, structural molecule activity family in focal adhesion and adherens junction and enzymes in glycolysis/gluconeogenesis, cancer and disease regulation.

Bottom Line: Given the increasing number of proteins reported to be regulated by S-nitrosylation (SNO), it is considered to act, in a manner analogous to phosphorylation, as a pleiotropic regulator that elicits dual effects to regulate diverse pathophysiological processes by altering protein function, stability, and conformation change in various cancers and human disorders.Additionally, the annotations of protein molecular functions, biological processes, functional domains and human diseases are integrated to explore the functional and disease associations for S-nitrosoproteome.In this update, users are allowed to search a group of interested proteins/genes and the system reconstructs the SNO regulatory network based on the information of metabolic pathways and protein-protein interactions.

View Article: PubMed Central - PubMed

Affiliation: Institute of Chemistry, Academia Sinica, Taipei 115, Taiwan.

Show MeSH
Related in: MedlinePlus