Enzymes
UniProtKB help_outline | 4 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
a 5'-end triphospho-guanosine-ribonucleotide-snRNA
Identifier
RHEA-COMP:15221
Reactive part
help_outline
- Name help_outline 5'-triphospho-guanosine-ribonucleotide residue Identifier CHEBI:138278 Charge -5 Formula C15H18N5O20P4R SMILEShelp_outline [C@@H]1(O[C@H]([C@@H]([C@@H]1O*)O)*)COP(O[C@@H]2[C@H](O[C@@H](N3C=4N=C(NC(=O)C4N=C3)N)[C@@H]2O)COP(=O)(OP(=O)(OP(=O)([O-])[O-])[O-])[O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 842 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
a 5'-end methyltriphosphate-guanosine-ribonucleotide-snRNA
Identifier
RHEA-COMP:15220
Reactive part
help_outline
- Name help_outline 5'-methyltriphosphate-guanosine-ribonucleotide residue Identifier CHEBI:142789 Charge -4 Formula C16H21N5O20P4R SMILEShelp_outline [C@@H]1(O[C@H]([C@@H]([C@@H]1OP(OC[C@H]2O[C@H]([C@@H]([C@@H]2O*)O)*)(=O)[O-])O)N3C=4N=C(NC(=O)C4N=C3)N)COP(OP(OP(OC)(=O)[O-])(=O)[O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-homocysteine Identifier CHEBI:57856 Charge 0 Formula C14H20N6O5S InChIKeyhelp_outline ZJUKTBDSGOFHSH-WFMPWKQPSA-N SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](CSCC[C@H]([NH3+])C([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 768 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:58780 | RHEA:58781 | RHEA:58782 | RHEA:58783 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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Publications
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Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme.
Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C., Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B., Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.
We have performed a survey of soluble human protein complexes containing components of the transcription and RNA processing machineries using protein affinity purification coupled to mass spectrometry. Thirty-two tagged polypeptides yielded a network of 805 high-confidence interactions. Remarkably ... >> More
We have performed a survey of soluble human protein complexes containing components of the transcription and RNA processing machineries using protein affinity purification coupled to mass spectrometry. Thirty-two tagged polypeptides yielded a network of 805 high-confidence interactions. Remarkably, the network is significantly enriched in proteins that regulate the formation of protein complexes, including a number of previously uncharacterized proteins for which we have inferred functions. The RNA polymerase II (RNAP II)-associated proteins (RPAPs) are physically and functionally associated with RNAP II, forming an interface between the enzyme and chaperone/scaffolding proteins. BCDIN3 is the 7SK snRNA methylphosphate capping enzyme (MePCE) present in an snRNP complex containing both RNA processing and transcription factors, including the elongation factor P-TEFb. Our results define a high-density protein interaction network for the mammalian transcription machinery and uncover multiple regulatory factors that target the transcription machinery. << Less
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Brd4 and JMJD6-associated anti-pause enhancers in regulation of transcriptional pause release.
Liu W., Ma Q., Wong K., Li W., Ohgi K., Zhang J., Aggarwal A., Rosenfeld M.G.
Distal enhancers characterized by the H3K4me(1) mark play critical roles in developmental and transcriptional programs. However, potential roles of specific distal regulatory elements in regulating RNA polymerase II (Pol II) promoter-proximal pause release remain poorly investigated. Here, we repo ... >> More
Distal enhancers characterized by the H3K4me(1) mark play critical roles in developmental and transcriptional programs. However, potential roles of specific distal regulatory elements in regulating RNA polymerase II (Pol II) promoter-proximal pause release remain poorly investigated. Here, we report that a unique cohort of jumonji C-domain-containing protein 6 (JMJD6) and bromodomain-containing protein 4 (Brd4) cobound distal enhancers, termed anti-pause enhancers (A-PEs), regulate promoter-proximal pause release of a large subset of transcription units via long-range interactions. Brd4-dependent JMJD6 recruitment on A-PEs mediates erasure of H4R3me(2(s)), which is directly read by 7SK snRNA, and decapping/demethylation of 7SK snRNA, ensuring the dismissal of the 7SK snRNA/HEXIM inhibitory complex. The interactions of both JMJD6 and Brd4 with the P-TEFb complex permit its activation and pause release of regulated coding genes. The functions of JMJD6/ Brd4-associated dual histone and RNA demethylase activity on anti-pause enhancers have intriguing implications for these proteins in development, homeostasis, and disease. << Less
Cell 155:1581-1595(2013) [PubMed] [EuropePMC]
This publication is cited by 6 other entries.