The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Poly(ADP-ribose) polymerase, regulatory domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 1: Poly [ADP-ribose] polymerase

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 39 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
NAD+ ADP-ribosyltransferase activity GO:0003950
Catalysis of the reaction: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
5 P09874 (/IDA) P09874 (/IDA) P11103 (/IDA) P27008 (/IDA) P35875 (/IDA)
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
5 P09874 (/IPI) P09874 (/IPI) P11103 (/IPI) P27008 (/IPI) P35875 (/IPI)
Protein ADP-ribosylase activity GO:1990404
The transfer, from NAD, of ADP-ribose to a protein amino acid residue.
5 P18493 (/ISS) P26446 (/ISS) P27008 (/ISS) P31669 (/ISS) Q9R152 (/ISS)
NAD+ ADP-ribosyltransferase activity GO:0003950
Catalysis of the reaction: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
4 P09874 (/IMP) P09874 (/IMP) P11103 (/IMP) P27008 (/IMP)
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
3 P09874 (/IPI) P09874 (/IPI) P27008 (/IPI)
Protein ADP-ribosylase activity GO:1990404
The transfer, from NAD, of ADP-ribose to a protein amino acid residue.
3 P09874 (/IDA) P09874 (/IDA) P11103 (/IDA)
RNA polymerase II regulatory region sequence-specific DNA binding GO:0000977
Interacting selectively and non-covalently with a specific sequence of DNA that is part of a regulatory region that controls the transcription of a gene or cistron by RNA polymerase II.
2 P09874 (/IDA) P09874 (/IDA)
DNA-binding transcription activator activity, RNA polymerase II-specific GO:0001228
A protein or a member of a complex that interacts selectively and non-covalently with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a RNA polymerase II-transcribed gene to activate or increase transcription. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units.
2 P09874 (/IDA) P09874 (/IDA)
DNA binding GO:0003677
Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
2 P09874 (/TAS) P09874 (/TAS)
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
2 P09874 (/HDA) P09874 (/HDA)
NAD+ ADP-ribosyltransferase activity GO:0003950
Catalysis of the reaction: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
2 P09874 (/TAS) P09874 (/TAS)
Transcription factor binding GO:0008134
Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.
2 P09874 (/IPI) P09874 (/IPI)
Protein kinase binding GO:0019901
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
2 P09874 (/IPI) P09874 (/IPI)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
2 P09874 (/IPI) P09874 (/IPI)
Protein N-terminus binding GO:0047485
Interacting selectively and non-covalently with a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
2 P09874 (/IPI) P09874 (/IPI)
NAD DNA ADP-ribosyltransferase activity GO:0140294
Catalysis of the transfer of the ADP-ribose group of NAD+ to a residue in double-stranded DNA.
2 P09874 (/IDA) P09874 (/IDA)
RNA polymerase II regulatory region sequence-specific DNA binding GO:0000977
Interacting selectively and non-covalently with a specific sequence of DNA that is part of a regulatory region that controls the transcription of a gene or cistron by RNA polymerase II.
1 P11103 (/ISO)
DNA-binding transcription activator activity, RNA polymerase II-specific GO:0001228
A protein or a member of a complex that interacts selectively and non-covalently with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a RNA polymerase II-transcribed gene to activate or increase transcription. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units.
1 P11103 (/ISO)
Chromatin binding GO:0003682
Interacting selectively and non-covalently with chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
1 P11103 (/IDA)
NAD+ ADP-ribosyltransferase activity GO:0003950
Catalysis of the reaction: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
1 P11103 (/ISO)
Transcription factor binding GO:0008134
Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.
1 P11103 (/ISO)
Transferase activity, transferring pentosyl groups GO:0016763
Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
1 P27008 (/NAS)
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
1 P11103 (/ISO)
Protein kinase binding GO:0019901
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
1 P11103 (/ISO)
Estrogen receptor binding GO:0030331
Interacting selectively and non-covalently with an estrogen receptor.
1 P27008 (/IPI)
Estrogen receptor binding GO:0030331
Interacting selectively and non-covalently with an estrogen receptor.
1 P11103 (/ISO)
Histone binding GO:0042393
Interacting selectively and non-covalently with a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity.
1 P35875 (/IPI)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
1 P11103 (/ISO)
Histone deacetylase binding GO:0042826
Interacting selectively and non-covalently with the enzyme histone deacetylase.
1 P27008 (/IPI)
Histone deacetylase binding GO:0042826
Interacting selectively and non-covalently with the enzyme histone deacetylase.
1 P11103 (/ISO)
SMAD binding GO:0046332
Interacting selectively and non-covalently with a SMAD signaling protein.
1 P27008 (/IPI)
SMAD binding GO:0046332
Interacting selectively and non-covalently with a SMAD signaling protein.
1 P11103 (/ISO)
Protein N-terminus binding GO:0047485
Interacting selectively and non-covalently with a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
1 P11103 (/ISO)
NAD binding GO:0051287
Interacting selectively and non-covalently with nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
1 P27008 (/IDA)
NAD binding GO:0051287
Interacting selectively and non-covalently with nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
1 P11103 (/ISO)
R-SMAD binding GO:0070412
Interacting selectively and non-covalently with a receptor-regulated SMAD signaling protein.
1 P27008 (/IPI)
R-SMAD binding GO:0070412
Interacting selectively and non-covalently with a receptor-regulated SMAD signaling protein.
1 P11103 (/ISO)
NAD DNA ADP-ribosyltransferase activity GO:0140294
Catalysis of the transfer of the ADP-ribose group of NAD+ to a residue in double-stranded DNA.
1 P11103 (/ISO)
Protein ADP-ribosylase activity GO:1990404
The transfer, from NAD, of ADP-ribose to a protein amino acid residue.
1 P11103 (/ISO)

There are 138 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Peptidyl-serine ADP-ribosylation GO:0018312
The transfer, from NAD, of ADP-ribose to peptidyl-serine to form peptidyl-O-(ADP-ribosyl)-L-serine.
6 P11103 (/ISS) P18493 (/ISS) P26446 (/ISS) P27008 (/ISS) P31669 (/ISS) Q9R152 (/ISS)
Peptidyl-glutamic acid poly-ADP-ribosylation GO:0018424
This modification produces peptidyl-glutamic acid poly-ADP-ribose found in a number of nuclear proteins under certain conditions including the repair of single strand DNA breaks. The activated form of the generating enzyme poly(ADP-ribose) polymerase is itself modified in this way.
6 P11103 (/ISS) P18493 (/ISS) P26446 (/ISS) P27008 (/ISS) P31669 (/ISS) Q9R152 (/ISS)
DNA ADP-ribosylation GO:0030592
The covalent attachment of an ADP-ribosyl group to a residue in double-stranded DNA.
6 P11103 (/ISS) P18493 (/ISS) P26446 (/ISS) P27008 (/ISS) P31669 (/ISS) Q9R152 (/ISS)
Protein auto-ADP-ribosylation GO:0070213
The ADP-ribosylation by a protein of one or more of its own amino acid residues, or residues on an identical protein.
6 P11103 (/ISS) P18493 (/ISS) P26446 (/ISS) P27008 (/ISS) P31669 (/ISS) Q9R152 (/ISS)
Positive regulation of double-strand break repair via homologous recombination GO:1905168
Any process that activates or increases the frequency, rate or extent of double-strand break repair via homologous recombination.
6 P11103 (/ISS) P18493 (/ISS) P26446 (/ISS) P27008 (/ISS) P31669 (/ISS) Q9R152 (/ISS)
ATP generation from poly-ADP-D-ribose GO:1990966
The process of generating ATP in the nucleus from poly-ADP-D-ribose. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.
6 P11103 (/ISS) P18493 (/ISS) P26446 (/ISS) P27008 (/ISS) P31669 (/ISS) Q9R152 (/ISS)
Positive regulation of cardiac muscle hypertrophy GO:0010613
Any process that increases the rate, frequency or extent of the enlargement or overgrowth of all or part of the heart due to an increase in size (not length) of individual cardiac muscle fibers, without cell division.
5 P09874 (/ISS) P09874 (/ISS) P11103 (/ISS) P18493 (/ISS) Q9R152 (/ISS)
Double-strand break repair GO:0006302
The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
4 P11103 (/ISS) P18493 (/ISS) P27008 (/ISS) Q9R152 (/ISS)
Protein ADP-ribosylation GO:0006471
The transfer, from NAD, of ADP-ribose to protein amino acids.
4 P09874 (/IMP) P09874 (/IMP) P27008 (/IMP) P35875 (/IMP)
Cellular response to DNA damage stimulus GO:0006974
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
4 P11103 (/ISS) P18493 (/ISS) P27008 (/ISS) Q9R152 (/ISS)
Protein poly-ADP-ribosylation GO:0070212
The transfer of multiple ADP-ribose residues from NAD to a protein amino acid, forming a poly(ADP-ribose) chain.
4 P09874 (/IDA) P09874 (/IDA) P11103 (/IDA) P26446 (/IDA)
Protein poly-ADP-ribosylation GO:0070212
The transfer of multiple ADP-ribose residues from NAD to a protein amino acid, forming a poly(ADP-ribose) chain.
4 P18493 (/ISS) P27008 (/ISS) P31669 (/ISS) Q9R152 (/ISS)
DNA repair GO:0006281
The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
3 P09874 (/TAS) P09874 (/TAS) P11103 (/TAS)
Protein ADP-ribosylation GO:0006471
The transfer, from NAD, of ADP-ribose to protein amino acids.
3 P09874 (/IDA) P09874 (/IDA) P27008 (/IDA)
Protein ADP-ribosylation GO:0006471
The transfer, from NAD, of ADP-ribose to protein amino acids.
3 P18493 (/ISS) P31669 (/ISS) Q9R152 (/ISS)
Protein ADP-ribosylation GO:0006471
The transfer, from NAD, of ADP-ribose to protein amino acids.
3 P09874 (/TAS) P09874 (/TAS) P35875 (/TAS)
Mitochondrion organization GO:0007005
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
3 P09874 (/IMP) P09874 (/IMP) P11103 (/IMP)
Positive regulation of single strand break repair GO:1903518
Any process that activates or increases the frequency, rate or extent of single strand break repair.
3 P09874 (/IGI) P09874 (/IGI) P11103 (/IGI)
Negative regulation of transcription by RNA polymerase II GO:0000122
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II.
2 P09874 (/TAS) P09874 (/TAS)
Nucleotide-excision repair, DNA damage recognition GO:0000715
The identification of lesions in DNA, such as pyrimidine-dimers, intrastrand cross-links, and bulky adducts. The wide range of substrate specificity suggests the repair complex recognizes distortions in the DNA helix.
2 P09874 (/TAS) P09874 (/TAS)
Nucleotide-excision repair, DNA duplex unwinding GO:0000717
The unwinding, or local denaturation, of the DNA duplex to create a bubble around the site of the DNA damage.
2 P09874 (/TAS) P09874 (/TAS)
Telomere maintenance GO:0000723
Any process that contributes to the maintenance of proper telomeric length and structure by affecting and monitoring the activity of telomeric proteins, the length of telomeric DNA and the replication and repair of the DNA. These processes includes those that shorten, lengthen, replicate and repair the telomeric DNA sequences.
2 P09874 (/TAS) P09874 (/TAS)
Double-strand break repair via homologous recombination GO:0000724
The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule.
2 P09874 (/TAS) P09874 (/TAS)
Nucleotide-excision repair, preincision complex stabilization GO:0006293
The stabilization of the multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage as well as the unwound DNA. The stabilization of the protein-DNA complex ensures proper positioning of the preincision complex before the phosphodiester backbone of the damaged strand is cleaved 3' and 5' of the site of DNA damage.
2 P09874 (/TAS) P09874 (/TAS)
Nucleotide-excision repair, preincision complex assembly GO:0006294
The aggregation, arrangement and bonding together of proteins on DNA to form the multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage. This assembly occurs before the phosphodiester backbone of the damaged strand is cleaved 3' and 5' of the site of DNA damage.
2 P09874 (/TAS) P09874 (/TAS)
Nucleotide-excision repair, DNA incision, 3'-to lesion GO:0006295
The endonucleolytic cleavage of the damaged strand of DNA 3' to the site of damage. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The incision precedes the incision formed 5' to the site of damage.
2 P09874 (/TAS) P09874 (/TAS)
Nucleotide-excision repair, DNA incision, 5'-to lesion GO:0006296
The endonucleolytic cleavage of the damaged strand of DNA 5' to the site of damage. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The incision follows the incision formed 3' to the site of damage.
2 P09874 (/TAS) P09874 (/TAS)
Double-strand break repair GO:0006302
The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
2 P09874 (/IMP) P09874 (/IMP)
Transcription by RNA polymerase II GO:0006366
The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs).
2 P09874 (/TAS) P09874 (/TAS)
Apoptotic process GO:0006915
A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
2 P09874 (/IDA) P09874 (/IDA)
Cellular response to DNA damage stimulus GO:0006974
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
2 P09874 (/IMP) P09874 (/IMP)
Peptidyl-serine ADP-ribosylation GO:0018312
The transfer, from NAD, of ADP-ribose to peptidyl-serine to form peptidyl-O-(ADP-ribosyl)-L-serine.
2 P09874 (/IDA) P09874 (/IDA)
Peptidyl-glutamic acid poly-ADP-ribosylation GO:0018424
This modification produces peptidyl-glutamic acid poly-ADP-ribose found in a number of nuclear proteins under certain conditions including the repair of single strand DNA breaks. The activated form of the generating enzyme poly(ADP-ribose) polymerase is itself modified in this way.
2 P09874 (/IDA) P09874 (/IDA)
Macrophage differentiation GO:0030225
The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage.
2 P09874 (/TAS) P09874 (/TAS)
DNA ADP-ribosylation GO:0030592
The covalent attachment of an ADP-ribosyl group to a residue in double-stranded DNA.
2 P09874 (/IDA) P09874 (/IDA)
Mitochondrial DNA metabolic process GO:0032042
The chemical reactions and pathways involving mitochondrial DNA.
2 P09874 (/IMP) P09874 (/IMP)
Cellular response to insulin stimulus GO:0032869
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
2 P09874 (/IDA) P09874 (/IDA)
Nucleotide-excision repair, DNA incision GO:0033683
A process that results in the endonucleolytic cleavage of the damaged strand of DNA. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound.
2 P09874 (/TAS) P09874 (/TAS)
Cellular response to oxidative stress GO:0034599
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
2 P09874 (/IMP) P09874 (/IMP)
Cellular response to UV GO:0034644
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
2 P09874 (/IMP) P09874 (/IMP)
Protein modification process GO:0036211
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
2 P09874 (/IMP) P09874 (/IMP)
Mitochondrial DNA repair GO:0043504
The process of restoring mitochondrial DNA after damage.
2 P09874 (/IMP) P09874 (/IMP)
Positive regulation of transcription by RNA polymerase II GO:0045944
Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.
2 P09874 (/IDA) P09874 (/IDA)
Regulation of catalytic activity GO:0050790
Any process that modulates the activity of an enzyme.
2 P09874 (/IDA) P09874 (/IDA)
Protein auto-ADP-ribosylation GO:0070213
The ADP-ribosylation by a protein of one or more of its own amino acid residues, or residues on an identical protein.
2 P09874 (/IDA) P09874 (/IDA)
Global genome nucleotide-excision repair GO:0070911
The nucleotide-excision repair process in which DNA lesions are removed from nontranscribed strands and from transcriptionally silent regions over the entire genome.
2 P09874 (/TAS) P09874 (/TAS)
Positive regulation of protein localization to nucleus GO:1900182
Any process that activates or increases the frequency, rate or extent of protein localization to nucleus.
2 P27008 (/IMP) P35875 (/IMP)
Regulation of cellular protein localization GO:1903827
Any process that modulates the frequency, rate or extent of cellular protein localization. Cellular protein localization is any process in which a protein is transported to, and/or maintained in, a specific location and encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell.
2 P09874 (/IMP) P09874 (/IMP)
Negative regulation of telomere maintenance via telomere lengthening GO:1904357
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance via telomere lengthening.
2 P09874 (/ISS) P09874 (/ISS)
Positive regulation of double-strand break repair via homologous recombination GO:1905168
Any process that activates or increases the frequency, rate or extent of double-strand break repair via homologous recombination.
2 P09874 (/IDA) P09874 (/IDA)
ATP generation from poly-ADP-D-ribose GO:1990966
The process of generating ATP in the nucleus from poly-ADP-D-ribose. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.
2 P09874 (/IDA) P09874 (/IDA)
Negative regulation of ATP biosynthetic process GO:2001170
Any process that stops, prevents or reduces the frequency, rate or extent of ATP biosynthetic process.
2 P09874 (/IMP) P09874 (/IMP)
Telomere maintenance GO:0000723
Any process that contributes to the maintenance of proper telomeric length and structure by affecting and monitoring the activity of telomeric proteins, the length of telomeric DNA and the replication and repair of the DNA. These processes includes those that shorten, lengthen, replicate and repair the telomeric DNA sequences.
1 P11103 (/IMP)
DNA metabolic process GO:0006259
Any cellular metabolic process involving deoxyribonucleic acid. This is one of the two main types of nucleic acid, consisting of a long, unbranched macromolecule formed from one, or more commonly, two, strands of linked deoxyribonucleotides.
1 P11103 (/IMP)
Base-excision repair GO:0006284
In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.
1 P11103 (/IMP)
Double-strand break repair GO:0006302
The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
1 P11103 (/IGI)
Double-strand break repair GO:0006302
The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
1 P11103 (/ISO)
Regulation of transcription, DNA-templated GO:0006355
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
1 P35875 (/TAS)
Protein ADP-ribosylation GO:0006471
The transfer, from NAD, of ADP-ribose to protein amino acids.
1 P11103 (/ISO)
Apoptotic process GO:0006915
A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
1 P11103 (/ISO)
Positive regulation of antibacterial peptide biosynthetic process GO:0006963
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide biosynthesis.
1 P35875 (/IMP)
Cellular response to DNA damage stimulus GO:0006974
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
1 P11103 (/ISO)
Nucleolus organization GO:0007000
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleolus.
1 P35875 (/IMP)
Mitochondrion organization GO:0007005
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
1 P11103 (/ISO)
Transforming growth factor beta receptor signaling pathway GO:0007179
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
1 P27008 (/IMP)
Transforming growth factor beta receptor signaling pathway GO:0007179
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
1 P11103 (/ISO)
Metamorphosis GO:0007552
A biological process in which an animal physically develops after birth or hatching, involving a conspicuous and relatively abrupt change in the animal's form or structure. Examples include the change from tadpole to frog, and the change from larva to adult. An example of this is found in Drosophila melanogaster.
1 P35875 (/TAS)
Dorsal/ventral axis specification, ovarian follicular epithelium GO:0008069
Polarization of the ovarian follicle cells along the dorsal/ventral axis. An example of this process is found in Drosophila melanogaster.
1 P35875 (/IGI)
RRNA transcription GO:0009303
The synthesis of ribosomal RNA (rRNA), any RNA that forms part of the ribosomal structure, from a DNA template.
1 P35875 (/TAS)
Response to gamma radiation GO:0010332
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gamma radiation stimulus. Gamma radiation is a form of electromagnetic radiation (EMR) or light emission of a specific frequency produced from sub-atomic particle interaction, such as electron-positron annihilation and radioactive decay. Gamma rays are generally characterized as EMR having the highest frequency and energy, and also the shortest wavelength, within the electromagnetic radiation spectrum.
1 P27008 (/IEP)
Positive regulation of cardiac muscle hypertrophy GO:0010613
Any process that increases the rate, frequency or extent of the enlargement or overgrowth of all or part of the heart due to an increase in size (not length) of individual cardiac muscle fibers, without cell division.
1 P27008 (/IMP)
Positive regulation of cardiac muscle hypertrophy GO:0010613
Any process that increases the rate, frequency or extent of the enlargement or overgrowth of all or part of the heart due to an increase in size (not length) of individual cardiac muscle fibers, without cell division.
1 P11103 (/ISO)
Regulation of SMAD protein complex assembly GO:0010990
Any process that modulates the rate, frequency, or extent of SMAD protein complex assembly. SMAD protein complex assembly is the aggregation, arrangement and bonding together of a set of components to form a protein complex that contains SMAD proteins.
1 P27008 (/IMP)
Regulation of SMAD protein complex assembly GO:0010990
Any process that modulates the rate, frequency, or extent of SMAD protein complex assembly. SMAD protein complex assembly is the aggregation, arrangement and bonding together of a set of components to form a protein complex that contains SMAD proteins.
1 P11103 (/ISO)
Protein autoprocessing GO:0016540
Processing which a protein carries out itself. This involves actions such as the autolytic removal of residues to generate the mature form of the protein.
1 P27008 (/IDA)
Protein autoprocessing GO:0016540
Processing which a protein carries out itself. This involves actions such as the autolytic removal of residues to generate the mature form of the protein.
1 P11103 (/ISO)
Peptidyl-serine ADP-ribosylation GO:0018312
The transfer, from NAD, of ADP-ribose to peptidyl-serine to form peptidyl-O-(ADP-ribosyl)-L-serine.
1 P11103 (/ISO)
Peptidyl-glutamic acid poly-ADP-ribosylation GO:0018424
This modification produces peptidyl-glutamic acid poly-ADP-ribose found in a number of nuclear proteins under certain conditions including the repair of single strand DNA breaks. The activated form of the generating enzyme poly(ADP-ribose) polymerase is itself modified in this way.
1 P11103 (/ISO)
Signal transduction involved in regulation of gene expression GO:0023019
Any process that modulates the frequency, rate or extent of gene expression as a consequence of a process in which a signal is released and/or conveyed from one location to another.
1 P27008 (/IMP)
Signal transduction involved in regulation of gene expression GO:0023019
Any process that modulates the frequency, rate or extent of gene expression as a consequence of a process in which a signal is released and/or conveyed from one location to another.
1 P11103 (/ISO)
Cajal body organization GO:0030576
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of Cajal bodies, nuclear bodies that appear ultrastructurally as a tangle of coiled, electron-dense threads roughly 0.5 micrometers in diameter and are enriched in ribonucleoproteins, and certain general RNA polymerase II transcription factors.
1 P35875 (/IMP)
DNA ADP-ribosylation GO:0030592
The covalent attachment of an ADP-ribosyl group to a residue in double-stranded DNA.
1 P11103 (/ISO)
Mitochondrial DNA metabolic process GO:0032042
The chemical reactions and pathways involving mitochondrial DNA.
1 P11103 (/ISO)
Cellular response to insulin stimulus GO:0032869
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
1 P11103 (/ISO)
Positive regulation of intracellular estrogen receptor signaling pathway GO:0033148
Any process that activates or increases the frequency, rate or extent of the activity of an intracellular estrogen receptor signaling pathway.
1 P27008 (/IMP)
Positive regulation of intracellular estrogen receptor signaling pathway GO:0033148
Any process that activates or increases the frequency, rate or extent of the activity of an intracellular estrogen receptor signaling pathway.
1 P11103 (/ISO)
Cellular response to oxidative stress GO:0034599
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
1 P11103 (/ISO)
Cellular response to UV GO:0034644
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
1 P11103 (/ISO)
Polytene chromosome puffing GO:0035079
The decondensing (loosening) and swelling of the chromosomal sites of target genes on polytene chromosomes following response to a stimulus, to facilitate sudden bursts of transcriptional activity in response to transient environmental signals.
1 P35875 (/TAS)
Heat shock-mediated polytene chromosome puffing GO:0035080
The decondensing (loosening) and swelling of the chromosomal sites of heat shock genes on polytene chromosomes in response to a heat shock stimulus.
1 P35875 (/IEP)
Heat shock-mediated polytene chromosome puffing GO:0035080
The decondensing (loosening) and swelling of the chromosomal sites of heat shock genes on polytene chromosomes in response to a heat shock stimulus.
1 P35875 (/IMP)
Protein modification process GO:0036211
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
1 P11103 (/ISO)
Regulation of growth rate GO:0040009
Any process that modulates the rate of growth of all or part of an organism.
1 P11103 (/IMP)
DNA damage response, detection of DNA damage GO:0042769
The series of events required to receive a stimulus indicating DNA damage has occurred and convert it to a molecular signal.
1 P27008 (/IDA)
DNA damage response, detection of DNA damage GO:0042769
The series of events required to receive a stimulus indicating DNA damage has occurred and convert it to a molecular signal.
1 P11103 (/ISO)
Regulation of RNA splicing GO:0043484
Any process that modulates the frequency, rate or extent of RNA splicing, the process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA.
1 P35875 (/IMP)
Mitochondrial DNA repair GO:0043504
The process of restoring mitochondrial DNA after damage.
1 P11103 (/ISO)
Regulation of DNA methylation GO:0044030
Any process that modulates the frequency, rate or extent of the covalent transfer of a methyl group to either N-6 of adenine or C-5 or N-4 of cytosine.
1 P27008 (/IMP)
Regulation of DNA methylation GO:0044030
Any process that modulates the frequency, rate or extent of the covalent transfer of a methyl group to either N-6 of adenine or C-5 or N-4 of cytosine.
1 P11103 (/ISO)
Innate immune response GO:0045087
Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens.
1 P35875 (/IMP)
Positive regulation of transcription by RNA polymerase II GO:0045944
Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.
1 P27008 (/IMP)
Positive regulation of transcription by RNA polymerase II GO:0045944
Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.
1 P11103 (/ISO)
Behavioral response to cocaine GO:0048148
Any process that results in a change in the behavior of an organism as a result of a cocaine stimulus.
1 P11103 (/IMP)
Regulation of catalytic activity GO:0050790
Any process that modulates the activity of an enzyme.
1 P11103 (/ISO)
Voluntary musculoskeletal movement GO:0050882
The movement of an organism or part of an organism using mechanoreceptors, the nervous system, striated muscle and/or the skeletal system that can be controlled at will.
1 P11103 (/IGI)
Chromosome organization GO:0051276
A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of chromosomes, structures composed of a very long molecule of DNA and associated proteins that carries hereditary information. This term covers covalent modifications at the molecular level as well as spatial relationships among the major components of a chromosome.
1 P35875 (/TAS)
Maintenance of protein location in nucleus GO:0051457
Any process in which a protein is maintained in the nucleus and prevented from moving elsewhere. These include sequestration within the nucleus, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the nucleus.
1 P35875 (/IMP)
Positive regulation of mitochondrial depolarization GO:0051901
Any process that activates, maintains or increases the frequency, rate or extent of the change in the membrane potential of the mitochondria from negative to positive.
1 P27008 (/IMP)
Positive regulation of mitochondrial depolarization GO:0051901
Any process that activates, maintains or increases the frequency, rate or extent of the change in the membrane potential of the mitochondria from negative to positive.
1 P11103 (/ISO)
Positive regulation of SMAD protein signal transduction GO:0060391
Any process that increases the rate, frequency or extent of SMAD protein signal transduction. Pathway-restricted SMAD proteins and common-partner SMAD proteins are involved in the transforming growth factor beta receptor signaling pathways.
1 P27008 (/IMP)
Positive regulation of SMAD protein signal transduction GO:0060391
Any process that increases the rate, frequency or extent of SMAD protein signal transduction. Pathway-restricted SMAD proteins and common-partner SMAD proteins are involved in the transforming growth factor beta receptor signaling pathways.
1 P11103 (/ISO)
Protein poly-ADP-ribosylation GO:0070212
The transfer of multiple ADP-ribose residues from NAD to a protein amino acid, forming a poly(ADP-ribose) chain.
1 P27008 (/IMP)
Protein poly-ADP-ribosylation GO:0070212
The transfer of multiple ADP-ribose residues from NAD to a protein amino acid, forming a poly(ADP-ribose) chain.
1 P11103 (/ISO)
Protein auto-ADP-ribosylation GO:0070213
The ADP-ribosylation by a protein of one or more of its own amino acid residues, or residues on an identical protein.
1 P11103 (/ISO)
Cellular response to zinc ion GO:0071294
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a zinc ion stimulus.
1 P27008 (/IEP)
Cellular response to superoxide GO:0071451
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a superoxide stimulus. Superoxide is the anion, oxygen-, formed by addition of one electron to dioxygen (O2) or any compound containing the superoxide anion.
1 P11103 (/IDA)
Cellular response to transforming growth factor beta stimulus GO:0071560
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a transforming growth factor beta stimulus.
1 P27008 (/IMP)
Cellular response to transforming growth factor beta stimulus GO:0071560
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a transforming growth factor beta stimulus.
1 P11103 (/ISO)
Positive regulation of protein localization to nucleus GO:1900182
Any process that activates or increases the frequency, rate or extent of protein localization to nucleus.
1 P11103 (/ISO)
Positive regulation of neuron death GO:1901216
Any process that activates or increases the frequency, rate or extent of neuron death.
1 P27008 (/IMP)
Positive regulation of neuron death GO:1901216
Any process that activates or increases the frequency, rate or extent of neuron death.
1 P11103 (/ISO)
Regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway GO:1903376
Any process that modulates the frequency, rate or extent of oxidative stress-induced neuron intrinsic apoptotic signaling pathway.
1 P27008 (/IMP)
Regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway GO:1903376
Any process that modulates the frequency, rate or extent of oxidative stress-induced neuron intrinsic apoptotic signaling pathway.
1 P11103 (/ISO)
Regulation of single strand break repair GO:1903516
Any process that modulates the frequency, rate or extent of single strand break repair.
1 P11103 (/IMP)
Positive regulation of single strand break repair GO:1903518
Any process that activates or increases the frequency, rate or extent of single strand break repair.
1 P11103 (/ISO)
Regulation of cellular protein localization GO:1903827
Any process that modulates the frequency, rate or extent of cellular protein localization. Cellular protein localization is any process in which a protein is transported to, and/or maintained in, a specific location and encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell.
1 P11103 (/ISO)
Response to aldosterone GO:1904044
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an aldosterone stimulus.
1 P27008 (/IEP)
Negative regulation of telomere maintenance via telomere lengthening GO:1904357
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance via telomere lengthening.
1 P11103 (/IMP)
Cellular response to amyloid-beta GO:1904646
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a amyloid-beta stimulus.
1 P27008 (/IMP)
Cellular response to amyloid-beta GO:1904646
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a amyloid-beta stimulus.
1 P11103 (/ISO)
Positive regulation of myofibroblast differentiation GO:1904762
Any process that activates or increases the frequency, rate or extent of myofibroblast differentiation.
1 P27008 (/IMP)
Positive regulation of myofibroblast differentiation GO:1904762
Any process that activates or increases the frequency, rate or extent of myofibroblast differentiation.
1 P11103 (/ISO)
Negative regulation of interleukin-17 secretion GO:1905077
Any process that stops, prevents or reduces the frequency, rate or extent of interleukin-17 secretion.
1 P11103 (/IMP)
Positive regulation of double-strand break repair via homologous recombination GO:1905168
Any process that activates or increases the frequency, rate or extent of double-strand break repair via homologous recombination.
1 P11103 (/ISO)
ATP generation from poly-ADP-D-ribose GO:1990966
The process of generating ATP in the nucleus from poly-ADP-D-ribose. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.
1 P11103 (/ISO)
Positive regulation of transcription regulatory region DNA binding GO:2000679
Any process that activates or increases the frequency, rate or extent of transcription regulatory region DNA binding.
1 P27008 (/IMP)
Positive regulation of transcription regulatory region DNA binding GO:2000679
Any process that activates or increases the frequency, rate or extent of transcription regulatory region DNA binding.
1 P11103 (/ISO)
Negative regulation of ATP biosynthetic process GO:2001170
Any process that stops, prevents or reduces the frequency, rate or extent of ATP biosynthetic process.
1 P11103 (/ISO)

There are 37 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
6 A0A024R3T8 (/IDA) A0A024R3T8 (/IDA) P09874 (/IDA) P09874 (/IDA) P11103 (/IDA) P27008 (/IDA)
Nucleolus GO:0005730
A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
4 P09874 (/IDA) P09874 (/IDA) P11103 (/IDA) P35875 (/IDA)
Site of DNA damage GO:0090734
A region of a chromosome at which DNA damage has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
4 P11103 (/ISS) P18493 (/ISS) P27008 (/ISS) Q9R152 (/ISS)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
3 P09874 (/TAS) P09874 (/TAS) P11103 (/TAS)
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
3 P09874 (/IDA) P09874 (/IDA) P11103 (/IDA)
Nuclear chromosome, telomeric region GO:0000784
The terminal region of a linear nuclear chromosome that includes the telomeric DNA repeats and associated proteins.
2 P09874 (/HDA) P09874 (/HDA)
Nuclear envelope GO:0005635
The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
2 P09874 (/IDA) P09874 (/IDA)
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
2 P09874 (/TAS) P09874 (/TAS)
Transcription factor complex GO:0005667
A protein complex that is capable of associating with DNA by direct binding, or via other DNA-binding proteins or complexes, and regulating transcription.
2 P09874 (/IDA) P09874 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
2 P11103 (/IDA) P27008 (/IDA)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
2 P09874 (/IDA) P09874 (/IDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
2 P09874 (/HDA) P09874 (/HDA)
Protein-DNA complex GO:0032993
A macromolecular complex containing both protein and DNA molecules.
2 P09874 (/IDA) P09874 (/IDA)
Site of double-strand break GO:0035861
A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
2 P09874 (/IDA) P09874 (/IDA)
Site of DNA damage GO:0090734
A region of a chromosome at which DNA damage has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
2 P09874 (/IMP) P09874 (/IMP)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 P11103 (/ISO)
Nuclear envelope GO:0005635
The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
1 P11103 (/ISO)
Nuclear envelope GO:0005635
The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
1 P18493 (/ISS)
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
1 P11103 (/IDA)
Transcription factor complex GO:0005667
A protein complex that is capable of associating with DNA by direct binding, or via other DNA-binding proteins or complexes, and regulating transcription.
1 P11103 (/ISO)
Chromosome GO:0005694
A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
1 P35875 (/IDA)
Polytene chromosome GO:0005700
A type of chromosome in a polyploid cell, formed when multiple copies of homologous chromosomes are aligned side by side to give a giant chromosome in which distinct chromosome bands are readily visible.
1 P35875 (/IDA)
Polytene chromosome GO:0005700
A type of chromosome in a polyploid cell, formed when multiple copies of homologous chromosomes are aligned side by side to give a giant chromosome in which distinct chromosome bands are readily visible.
1 P35875 (/TAS)
Polytene chromosome puff GO:0005703
A swelling at a site along the length of a polytene chromosome, thought to be the site of active transcription.
1 P35875 (/IDA)
Polytene chromosome puff GO:0005703
A swelling at a site along the length of a polytene chromosome, thought to be the site of active transcription.
1 P35875 (/TAS)
Nuclear euchromatin GO:0005719
The dispersed less dense form of chromatin in the interphase nucleus. It exists in at least two forms, a some being in the form of transcriptionally active chromatin which is the least condensed, while the rest is inactive euchromatin which is more condensed than active chromatin but less condensed than heterochromatin.
1 P35875 (/IDA)
Nucleolus GO:0005730
A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
1 P11103 (/ISO)
Nucleolus GO:0005730
A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
1 P18493 (/ISS)
Nucleolus GO:0005730
A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
1 P35875 (/TAS)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P11103 (/ISO)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
1 P11103 (/ISO)
Cajal body GO:0015030
A class of nuclear body, first seen after silver staining by Ramon y Cajal in 1903, enriched in small nuclear ribonucleoproteins, and certain general RNA polymerase II transcription factors; ultrastructurally, they appear as a tangle of coiled, electron-dense threads roughly 0.5 micrometers in diameter; involved in aspects of snRNP biogenesis; the protein coilin serves as a marker for Cajal bodies. Some argue that Cajal bodies are the sites for preassembly of transcriptosomes, unitary particles involved in transcription and processing of RNA.
1 P35875 (/IDA)
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
1 P11103 (/ISO)
Protein-DNA complex GO:0032993
A macromolecular complex containing both protein and DNA molecules.
1 P11103 (/ISO)
Histone locus body GO:0035363
A nuclear body associated with the histone gene locus that is thought to contain all of the factors necessary for histone mRNA transcription and pre-mRNA processing. In Drosophila, U7 snRNP is located in the histone locus body rather than the distinct Cajal body.
1 P35875 (/IDA)
Site of double-strand break GO:0035861
A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
1 P11103 (/ISO)
Site of DNA damage GO:0090734
A region of a chromosome at which DNA damage has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
1 P11103 (/ISO)