All terms in GO
| Label | Id | Description |
|---|---|---|
| autophagy of mitochondrion | GO_0000422 |
The autophagic process in which mitochondria are delivered to a type of vacuole and degraded in response to changing cellular conditions.
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| micromitophagy | GO_0000424 |
Degradation of a mitochondrion by lysosomal microautophagy.
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| autophagosome membrane | GO_0000421 |
The lipid bilayer surrounding an autophagosome, a double-membrane-bounded vesicle in which endogenous cellular material is sequestered.
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| mitochondrion disassembly | GO_0061726 |
The disaggregation of a mitochondrion into its constituent components.
|
| GO_0000420 | GO_0000420 | |
| RNA polymerase IV complex | GO_0000418 |
RNA polymerase IV is a multisubunit RNA polymerase complex found in the nucleus of plants and involved in accumulation of siRNAs and in DNA methylation-dependent silencing of endogenous repeated sequences. Pol IV is composed of subunits that are paralogous or identical to the 12 subunits of Pol II. The largest and second-largest subunits of Pol IV are the catalytic subunits and share similarity with the corresponding subunits of other eukaryotic and bacterial multisubunit RNA polymerases. The second largest subunit is also found in RNA polymerase V, while the largest subunit is found only in RNAP IV complex.
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| nuclear DNA-directed RNA polymerase complex | GO_0055029 |
A protein complex, located in the nucleus, that possesses DNA-directed RNA polymerase activity.
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| axial mesoderm morphogenesis | GO_0048319 |
The process in which the anatomical structures of the axial mesoderm are generated and organized.
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| mesoderm morphogenesis | GO_0048332 |
The process in which the anatomical structures of the mesoderm are generated and organized.
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| RNA polymerase V complex | GO_0000419 |
RNA polymerase V is a multisubunit RNA polymerase complex found in the nucleus of plants and involved in accumulation of siRNAs and in DNA methylation-dependent silencing of endogenous repeated sequences. Pol V is composed of subunits that are paralogous or identical to the 12 subunits of Pol II. Two large subunits comprise the most conserved portion including the catalytic site and share similarity with other eukaryotic and bacterial multisubunit RNA polymerases. The second largest subunit is also found in RNA polymerase IVa, while the largest subunit is found only in the IVa complex and contains an extended C-terminal domain (CTD) that includes multiple repeats of a 16 amino-acid consensus sequence as well as other sequences. The remainder of the complex is composed of smaller subunits.
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| positive regulation of histone H3-K36 methylation | GO_0000416 |
Any process that activates or increases the frequency, rate or extent of the covalent addition of a methyl group to the lysine at position 36 of histone H3.
|
| regulation of histone H3-K36 methylation | GO_0000414 |
Any process that modulates the frequency, rate or extent of the covalent addition of a methyl group to the lysine at position 36 of histone H3.
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| positive regulation of histone methylation | GO_0031062 |
Any process that activates or increases the frequency, rate or extent of the covalent addition of methyl groups to histones.
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| HIR complex | GO_0000417 |
A protein complex proposed to be involved in replication-independent nucleosome assembly, by promoting histone deposition onto DNA. For example, in Saccharomyces, the complex contains Hir1p, Hir2p, Hir3p, and Hpc2p.
|
| regulation of histone methylation | GO_0031060 |
Any process that modulates the frequency, rate or extent of the covalent addition of methyl groups to histones.
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| negative regulation of histone H3-K36 methylation | GO_0000415 |
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent addition of a methyl group to the lysine at position 36 of histone H3.
|
| negative regulation of histone methylation | GO_0031061 |
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent addition of methyl groups to histones.
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| histone peptidyl-prolyl isomerization | GO_0000412 |
The modification of a histone by cis-trans isomerization of a proline residue.
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| protein peptidyl-prolyl isomerization | GO_0000413 |
The modification of a protein by cis-trans isomerization of a proline residue.
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| histone modification | GO_0016570 |
The covalent alteration of one or more amino acid residues within a histone protein.
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