All terms in GO

Label Id Description
obsolete histone ubiquitination GO_0016574 [OBSOLETE. The modification of histones by addition of ubiquitin groups.]
obsolete histone acetylation GO_0016573 [OBSOLETE. The modification of a histone by the addition of an acetyl group.]
obsolete histone phosphorylation GO_0016572 [OBSOLETE. The modification of histones by addition of phosphate groups.]
obsolete histone methylation GO_0016571 [OBSOLETE. The modification of histones by addition of methyl groups.]
obsolete histone modification GO_0016570 [OBSOLETE. The covalent alteration of one or more amino acid residues within a histone protein.]
NURF complex GO_0016589 [An ISWI complex that contains an ATPase subunit of the ISWI family (SNF2L in mammals), a NURF301 homolog (BPTF in humans), and additional subunits, though the composition of these additional subunits varies slightly with species. NURF is involved in regulation of transcription from TRNA polymerase II promoters.]
GO_0016588 GO_0016588
RSC-type complex GO_0016586 [A SWI/SNF-type complex that contains a bromodomain containing-protein, such as yeast Rsc1 or Rsc4 or mammalian PB1/BAF180. The RSC complex is generally recruited to RNA polymerase III promoters and is specifically recruited to RNA polymerase II promoters by transcriptional activators and repressors; it is also involved in non-homologous end joining.]
obsolete chromatin remodeling complex GO_0016585 [OBSOLETE. Any complex that mediates dynamic changes in eukaryotic chromatin.]
obsolete nucleosome positioning GO_0016584 [OBSOLETE. Ordering of successions of nucleosomes into regular arrays so that nucleosomes are positioned at defined distances from one another.]
obsolete nucleosome modeling GO_0016583 [OBSOLETE. (Was not defined before being made obsolete).]
obsolete non-covalent chromatin modification GO_0016582 [OBSOLETE. The alteration of DNA or protein in chromatin by the non-covalent addition or removal of chemical groups.]
obsolete Sin3 complex GO_0016580 [OBSOLETE. A multiprotein complex that functions broadly in eukaryotic organisms as a transcriptional repressor of protein-coding genes, through the gene-specific deacetylation of histones. Amongst its subunits, the Sin3 complex contains Sin3-like proteins, and a number of core proteins that are shared with the NuRD complex (including histone deacetylases and histone binding proteins). The Sin3 complex does not directly bind DNA itself, but is targeted to specific genes through protein-protein interactions with DNA-binding proteins.]
GO_0016599 GO_0016599
protein arginylation GO_0016598 [The conjugation of arginine to the N-terminal aspartate or glutamate of a protein; required for the degradation of the protein via the ubiquitin pathway.]
thienylcyclohexylpiperidine binding GO_0016596 [Binding to thienylcyclohexylpiperidine.]
glutamate binding GO_0016595 [Binding to glutamate, the anion of 2-aminopentanedioic acid.]
glycine binding GO_0016594 [Binding to glycine, aminoethanoic acid.]
Cdc73/Paf1 complex GO_0016593 [A multiprotein complex that associates with RNA polymerase II and general RNA polymerase II transcription factor complexes and may be involved in both transcriptional initiation and elongation. In Saccharomyces the complex contains Paf1p, Cdc73p, Ctr9p, Rtf1p, and Leo1p.]
mediator complex GO_0016592 [A protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The mediator complex is required for activation of transcription of most protein-coding genes, but can also act as a transcriptional corepressor. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins.]