|Affiliation||Harvard Medical School, Department of Biological Chemistry and Molecular Pharmacology|
|Author of summation(s)||A highly conserved lysine within the guanylyltransferase (GT...
After the capping complex is formed, the RNA triphosphatase ...
GMP capped mRNA transcript dissociates from GT for further m...
In the final step of the capping reaction, the methyltransfe...
Phosphorylation of serine 5 residue at the CTD of pol II la...
The cap binding complex binds to the methylated GMP cap on t...
The capping enzyme binds the 5'-end of the nascent transcrip...
The capping enzyme interacts with the Spt5 subunit of trans...
The diphosphate 5'-end of the mRNA is joined to the GMP, rel...
|Author of entries||Activation of GT [Homo sapiens]
Capping complex formation [Homo sapiens]
CE:Pol II CTD:Spt5 complex [nucleoplasm]
Dissociation of transcript with 5'-GMP from GT [Homo sapiens]
Extrusion of 5'-end of 30 nt long transcript through the pore in Pol II complex [Homo sapiens]
Formation of cap binding complex (CBC) [Homo sapiens]
Formation of the CE:GMP intermediate complex [Homo sapiens]
Hydrolysis of the 5'-end of the nascent transcript by the capping enzyme [Homo sapiens]
Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex [Homo sapiens]
Methylation of GMP-cap by RNA Methyltransferase [Homo sapiens]
mRNA Capping [Homo sapiens]
Phosphorylation (Ser5) of RNA pol II CTD [Homo sapiens]
Recognition and binding of the HIV-1 mRNA cap by the cap-binding complex [Homo sapiens]
Recognition and binding of the mRNA cap by the cap-binding complex [Homo sapiens]
RNA Pol II CTD phosphorylation and interaction with CE [Homo sapiens]
RNA Pol II with phosphorylated CTD: CE complex [nucleoplasm]
RNA Pol II with phosphorylated CTD: CE complex with activated GT [nucleoplasm]
RNA Polymerase II CTD (phosphorylated) binds to CE [Homo sapiens]
SPT5 subunit of Pol II binds the RNA triphosphatase (RTP) [Homo sapiens]
Transfer of GMP from the capping enzyme GT site to 5'-end of mRNA [Homo sapiens]
|Publication(s)||Komarnitsky, P, Cho, EJ, Buratowski, S Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription. 2000 Genes Dev PubMed
Wada, T, Takagi, T, Yamaguchi, Y, Ferdous, A, Imai, T, Hirose, S, Sugimoto, S, Yano, K, Hartzog, GA, Winston, F, Buratowski, S, Handa, H DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs. 1998 Genes Dev PubMed