http://www.reactome.org/bio... | rdf:type | biopax3:BiochemicalReaction | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:comment | Full activity of most CDKs is dependent on CAK mediated phosphorylation at a conserved residue (Thr 161 in Cdc2). This modification is thought to improve substrate binding. Cyclin B:Cdc2 complexes have considerably low activity in the absence of CAK mediated phosphorylation (Desai et al 1995). | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:xref | urn:biopax:UnificationXref:... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:xref | http://identifiers.org/pubm... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:xref | urn:biopax:UnificationXref:... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:dataSource | urn:biopax:Provenance:react... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:dataSource | http://www.reactome.org/bio... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:displayName | CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:left | http://www.reactome.org/bio... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:left | http://www.reactome.org/bio... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:right | http://www.reactome.org/bio... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:right | http://www.reactome.org/bio... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:stepProcess | http://www.reactome.org/bio... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:controlled | http://www.reactome.org/bio... | lld:biopax3 |
http://www.reactome.org/bio... | biopax3:pathwayComponent | http://www.reactome.org/bio... | lld:biopax3 |