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View Protein Complex Details

Complex Overview

From Publication: Krogan N. J. et al. (2006) Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature. 2006 Mar 30;440(7084):637-43. Epub 2006 Mar 22.
Notes: From the published set of core protein complex predictions.
Complex Size: 3 proteins

Complex Member Proteins

Cellular Component Analysis

Given the number of proteins in the complex (A), total proteins annotated with a given GO term (B), and the total number of annotated proteins (T); the p-value represents the chances of randomly having the number of proteins in the complex annotated with a specific GO term (I).

Only showing terms with a p-value less than or equal to 0.01.

GO Term

P-value

A

B

I

T

F-actin capping protein complex 9.5344E-4 3 2 1 6292
actin filament 4.2857E-3 3 9 1 6292

Biological Process Analysis

Given the number of proteins in the complex (A), total proteins annotated with a given GO term (B), and the total number of annotated proteins (T); the p-value represents the chances of randomly having the number of proteins in the complex annotated with a specific GO term (I).

Only showing terms with a p-value less than or equal to 0.01.

GO Term

P-value

A

B

I

T

barbed-end actin filament capping 9.5344E-4 3 2 1 6292
actin filament capping 9.5344E-4 3 2 1 6292
negative regulation of actin filament depolymerization 9.5344E-4 3 2 1 6292
regulation of actin filament depolymerization 9.5344E-4 3 2 1 6292
regulation of actin polymerization or depolymerization 1.4299E-3 3 3 1 6292
protein polymerization 1.4299E-3 3 3 1 6292
regulation of actin cytoskeleton organization 1.4299E-3 3 3 1 6292
regulation of protein polymerization 1.4299E-3 3 3 1 6292
negative regulation of protein polymerization 1.4299E-3 3 3 1 6292
negative regulation of protein complex assembly 1.4299E-3 3 3 1 6292
actin filament polymerization 1.4299E-3 3 3 1 6292
regulation of actin filament polymerization 1.4299E-3 3 3 1 6292
regulation of actin filament length 1.4299E-3 3 3 1 6292
negative regulation of actin filament polymerization 1.4299E-3 3 3 1 6292
regulation of actin filament-based process 1.4299E-3 3 3 1 6292
actin filament depolymerization 1.9063E-3 3 4 1 6292
phosphoinositide dephosphorylation 3.3344E-3 3 7 1 6292
negative regulation of protein complex disassembly 3.3344E-3 3 7 1 6292
phospholipid dephosphorylation 3.3344E-3 3 7 1 6292
negative regulation of cytoskeleton organization 3.8101E-3 3 8 1 6292
folic acid and derivative metabolic process 4.2857E-3 3 9 1 6292
actin polymerization or depolymerization 4.2857E-3 3 9 1 6292
protein depolymerization 4.7611E-3 3 10 1 6292
regulation of protein complex disassembly 4.7611E-3 3 10 1 6292
regulation of protein complex assembly 5.2364E-3 3 11 1 6292
phosphoinositide-mediated signaling 7.6106E-3 3 16 1 6292
inositol lipid-mediated signaling 7.6106E-3 3 16 1 6292
regulation of cellular component biogenesis 8.5592E-3 3 18 1 6292
regulation of cytoskeleton organization 9.5071E-3 3 20 1 6292

Molecular Function Analysis

Given the number of proteins in the complex (A), total proteins annotated with a given GO term (B), and the total number of annotated proteins (T); the p-value represents the chances of randomly having the number of proteins in the complex annotated with a specific GO term (I).

Only showing terms with a p-value less than or equal to 0.01.

GO Term

P-value

A

B

I

T

dihydrofolate reductase activity 4.768E-4 3 1 1 6292
phosphoinositide 5-phosphatase activity 1.9063E-3 3 4 1 6292
phosphatidylinositol bisphosphate phosphatase activity 1.9063E-3 3 4 1 6292
phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity 1.9063E-3 3 4 1 6292
inositol or phosphatidylinositol phosphatase activity 4.2857E-3 3 9 1 6292
oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor 5.7116E-3 3 12 1 6292
actin filament binding 5.7116E-3 3 12 1 6292
oxidoreductase activity, acting on the CH-NH group of donors 6.6614E-3 3 14 1 6292
actin binding 9.9809E-3 3 21 1 6292

YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle