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:
"Endonuclease/exonuclease/phosphatase
".
FunFam 9: DNA-(apurinic or apyrimidinic site) lyase
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 51 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 |
---|---|---|
Oxidoreductase activity GO:0016491
Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
|
14 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(4 more) |
Damaged DNA binding GO:0003684
Interacting selectively and non-covalently with damaged DNA.
|
13 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(3 more) |
DNA-(apurinic or apyrimidinic site) endonuclease activity GO:0003906
Catalysis of the cleavage of the C-O-P bond in the AP site created when DNA glycosylase removes a damaged base, involved in the DNA base excision repair pathway (BER).
|
13 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(3 more) |
3'-5' exonuclease activity GO:0008408
Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
|
13 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(3 more) |
Site-specific endodeoxyribonuclease activity, specific for altered base GO:0016890
Catalysis of the hydrolysis of ester linkages at specific sites within a deoxyribonucleic acid molecule by creating internal breaks.
|
13 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(3 more) |
Chromatin DNA binding GO:0031490
Interacting selectively and non-covalently with DNA that is assembled into chromatin.
|
13 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(3 more) |
DNA binding GO:0003677
Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
|
5 | P23196 (/ISS) P28352 (/ISS) P28352 (/ISS) P43138 (/ISS) Q9Z2J2 (/ISS) |
Transcription coactivator activity GO:0003713
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator.
|
5 | P23196 (/ISS) P28352 (/ISS) P28352 (/ISS) P43138 (/ISS) Q9Z2J2 (/ISS) |
Metal ion binding GO:0046872
Interacting selectively and non-covalently with any metal ion.
|
5 | P23196 (/ISS) P28352 (/ISS) P28352 (/ISS) P43138 (/ISS) Q9Z2J2 (/ISS) |
DNA-(apurinic or apyrimidinic site) endonuclease activity GO:0003906
Catalysis of the cleavage of the C-O-P bond in the AP site created when DNA glycosylase removes a damaged base, involved in the DNA base excision repair pathway (BER).
|
3 | P27695 (/IDA) P27695 (/IDA) P27864 (/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).
|
3 | P27695 (/IPI) P27695 (/IPI) P43138 (/IPI) |
3'-5' exonuclease activity GO:0008408
Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
|
3 | P27695 (/IDA) P27695 (/IDA) P27864 (/IDA) |
DNA binding GO:0003677
Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
|
2 | P27695 (/IDA) P27695 (/IDA) |
DNA binding GO:0003677
Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
|
2 | P28352 (/ISO) P28352 (/ISO) |
Damaged DNA binding GO:0003684
Interacting selectively and non-covalently with damaged DNA.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Damaged DNA binding GO:0003684
Interacting selectively and non-covalently with damaged DNA.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Double-stranded telomeric DNA binding GO:0003691
Interacting selectively and non-covalently with double-stranded telomere-associated DNA.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Double-stranded telomeric DNA binding GO:0003691
Interacting selectively and non-covalently with double-stranded telomere-associated DNA.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Transcription coactivator activity GO:0003713
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Transcription coactivator activity GO:0003713
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Transcription corepressor activity GO:0003714
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to repress the transcription of specific genes. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. A third class occludes DNA-binding transcription factor protein-protein interaction domains. A fourth class of corepressors prevents interactions of DNA bound DNA-binding transcription factor with coactivators.
|
2 | P27695 (/TAS) P27695 (/TAS) |
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
|
2 | P27695 (/HDA) P27695 (/HDA) |
DNA-(apurinic or apyrimidinic site) endonuclease activity GO:0003906
Catalysis of the cleavage of the C-O-P bond in the AP site created when DNA glycosylase removes a damaged base, involved in the DNA base excision repair pathway (BER).
|
2 | P28352 (/ISO) P28352 (/ISO) |
DNA-(apurinic or apyrimidinic site) endonuclease activity GO:0003906
Catalysis of the cleavage of the C-O-P bond in the AP site created when DNA glycosylase removes a damaged base, involved in the DNA base excision repair pathway (BER).
|
2 | P27695 (/TAS) P27695 (/TAS) |
Endonuclease activity GO:0004519
Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Endodeoxyribonuclease activity GO:0004520
Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
|
2 | P27695 (/TAS) P27695 (/TAS) |
Endoribonuclease activity GO:0004521
Catalysis of the hydrolysis of ester linkages within ribonucleic acid by creating internal breaks.
|
2 | P28352 (/ISO) P28352 (/ISO) |
RNA-DNA hybrid ribonuclease activity GO:0004523
Catalysis of the endonucleolytic cleavage of RNA in RNA-DNA hybrids to 5'-phosphomonoesters.
|
2 | P27695 (/TAS) P27695 (/TAS) |
Phosphodiesterase I activity GO:0004528
Catalysis of the sequential hydrolytic removal of 5'-nucleotides from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
|
2 | P27695 (/TAS) P27695 (/TAS) |
Uracil DNA N-glycosylase activity GO:0004844
Catalysis of the cleavage of the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar, releasing a free base and leaving an apyrimidinic (AP) site. Enzymes with this activity recognize and remove uracil bases in DNA that result from the deamination of cytosine or the misincorporation of dUTP opposite an adenine.
|
2 | P27695 (/TAS) P27695 (/TAS) |
Phosphoric diester hydrolase activity GO:0008081
Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Phosphoric diester hydrolase activity GO:0008081
Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Double-stranded DNA exodeoxyribonuclease activity GO:0008309
Catalysis of the sequential cleavage of mononucleotides from a free 5' or 3' terminus of a double-stranded DNA molecule.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Double-stranded DNA exodeoxyribonuclease activity GO:0008309
Catalysis of the sequential cleavage of mononucleotides from a free 5' or 3' terminus of a double-stranded DNA molecule.
|
2 | P28352 (/ISO) P28352 (/ISO) |
3'-5' exonuclease activity GO:0008408
Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
|
2 | P28352 (/ISO) P28352 (/ISO) |
3'-5' exonuclease activity GO:0008408
Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
|
2 | P27695 (/TAS) P27695 (/TAS) |
Oxidoreductase activity GO:0016491
Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Oxidoreductase activity GO:0016491
Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Site-specific endodeoxyribonuclease activity, specific for altered base GO:0016890
Catalysis of the hydrolysis of ester linkages at specific sites within a deoxyribonucleic acid molecule by creating internal breaks.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Site-specific endodeoxyribonuclease activity, specific for altered base GO:0016890
Catalysis of the hydrolysis of ester linkages at specific sites within a deoxyribonucleic acid molecule by creating internal breaks.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Chromatin DNA binding GO:0031490
Interacting selectively and non-covalently with DNA that is assembled into chromatin.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Chromatin DNA binding GO:0031490
Interacting selectively and non-covalently with DNA that is assembled into chromatin.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Metal ion binding GO:0046872
Interacting selectively and non-covalently with any metal ion.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Metal ion binding GO:0046872
Interacting selectively and non-covalently with any metal ion.
|
2 | P28352 (/ISO) P28352 (/ISO) |
NF-kappaB binding GO:0051059
Interacting selectively and non-covalently with NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Endoribonuclease activity GO:0004521
Catalysis of the hydrolysis of ester linkages within ribonucleic acid by creating internal breaks.
|
1 | P43138 (/IDA) |
Phosphoric diester hydrolase activity GO:0008081
Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.
|
1 | P23196 (/ISS) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
1 | P43138 (/IPI) |
NF-kappaB binding GO:0051059
Interacting selectively and non-covalently with NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters.
|
1 | P43138 (/IDA) |
Class II DNA-(apurinic or apyrimidinic site) endonuclease activity GO:0052720
Catalysis of the hydrolysis of ester linkages immediately 5' to an apurinic/apyrimidinic (AP; also called abasic) site within a deoxyribonucleic acid molecule by creating internal breaks, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends.
|
1 | P27864 (/IDA) |
There are 39 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 |
---|---|---|
DNA demethylation GO:0080111
The removal of a methyl group from one or more nucleotides within an DNA molecule.
|
14 |
A0MTA1 (/ISS)
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
(4 more) |
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.
|
13 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(3 more) |
Regulation of apoptotic process GO:0042981
Any process that modulates the occurrence or rate of cell death by apoptotic process.
|
13 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(3 more) |
Regulation of mRNA stability GO:0043488
Any process that modulates the propensity of mRNA molecules to degradation. Includes processes that both stabilize and destabilize mRNAs.
|
13 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(3 more) |
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 | P27695 (/IDA) P27695 (/IDA) |
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 | P28352 (/ISO) P28352 (/ISO) |
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.
|
2 | P27695 (/IDA) P27695 (/IDA) |
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.
|
2 | P28352 (/ISO) P28352 (/ISO) |
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.
|
2 | P27695 (/IDA) P27695 (/IDA) |
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.
|
2 | P28352 (/ISO) P28352 (/ISO) |
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.
|
2 | P27695 (/TAS) P27695 (/TAS) |
Base-excision repair, base-free sugar-phosphate removal GO:0006286
Excision of the sugar phosphate residue at an AP site, i.e. a deoxyribose sugar with a missing base, by a phosphodiesterase enzyme.
|
2 | P27695 (/TAS) P27695 (/TAS) |
Aging GO:0007568
A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
|
2 | P28352 (/ISO) P28352 (/ISO) |
Negative regulation of smooth muscle cell migration GO:0014912
Any process that stops, prevents, or reduces the frequency, rate or extent of smooth muscle cell migration.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Regulation of apoptotic process GO:0042981
Any process that modulates the occurrence or rate of cell death by apoptotic process.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Regulation of apoptotic process GO:0042981
Any process that modulates the occurrence or rate of cell death by apoptotic process.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Regulation of mRNA stability GO:0043488
Any process that modulates the propensity of mRNA molecules to degradation. Includes processes that both stabilize and destabilize mRNAs.
|
2 | P27695 (/IMP) P27695 (/IMP) |
Regulation of mRNA stability GO:0043488
Any process that modulates the propensity of mRNA molecules to degradation. Includes processes that both stabilize and destabilize mRNAs.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Cell redox homeostasis GO:0045454
Any process that maintains the redox environment of a cell or compartment within a cell.
|
2 | P28352 (/IDA) P28352 (/IDA) |
Cellular response to hydrogen peroxide GO:0070301
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 hydrogen peroxide (H2O2) stimulus.
|
2 | P28352 (/ISO) P28352 (/ISO) |
DNA demethylation GO:0080111
The removal of a methyl group from one or more nucleotides within an DNA molecule.
|
2 | P27695 (/IDA) P27695 (/IDA) |
DNA demethylation GO:0080111
The removal of a methyl group from one or more nucleotides within an DNA molecule.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Telomere maintenance via base-excision repair GO:0097698
A telomere maintenance process that occurs by base-excision repair of telomeric DNA in response to DNA damage. Telomeric sequences are particularly susceptible to oxidative DNA damage, due to their G-rich nature.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Telomere maintenance via base-excision repair GO:0097698
A telomere maintenance process that occurs by base-excision repair of telomeric DNA in response to DNA damage. Telomeric sequences are particularly susceptible to oxidative DNA damage, due to their G-rich nature.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Positive regulation of G1/S transition of mitotic cell cycle GO:1900087
Any signalling pathway that increases or activates a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the mitotic cell cycle.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Heart looping GO:0001947
The tube morphogenesis process in which the primitive heart tube loops asymmetrically. This looping brings the primitive heart chambers into alignment preceding their future integration. Heart looping begins with dextral-looping and ends when the main regional divisions of the mature heart and primordium of the great arterial trunks become established preceeding septation.
|
1 | A0MTA1 (/IMP) |
Aging GO:0007568
A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
|
1 | P43138 (/IDA) |
Response to organonitrogen compound GO:0010243
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 organonitrogen stimulus. An organonitrogen compound is formally a compound containing at least one carbon-nitrogen bond.
|
1 | P43138 (/IEP) |
Positive regulation of gene expression GO:0010628
Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form.
|
1 | A0MTA1 (/IMP) |
Negative regulation of smooth muscle cell migration GO:0014912
Any process that stops, prevents, or reduces the frequency, rate or extent of smooth muscle cell migration.
|
1 | P43138 (/IMP) |
Response to drug GO:0042493
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 drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
|
1 | P43138 (/IEP) |
Negative regulation of apoptotic process GO:0043066
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
|
1 | A0MTA1 (/IMP) |
Heart contraction GO:0060047
The multicellular organismal process in which the heart decreases in volume in a characteristic way to propel blood through the body.
|
1 | A0MTA1 (/IMP) |
Cellular response to hydrogen peroxide GO:0070301
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 hydrogen peroxide (H2O2) stimulus.
|
1 | P43138 (/IDA) |
Cellular response to hydrogen peroxide GO:0070301
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 hydrogen peroxide (H2O2) stimulus.
|
1 | P43138 (/IEP) |
Cellular response to cAMP GO:0071320
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 cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus.
|
1 | P43138 (/IEP) |
Cellular response to peptide hormone stimulus GO:0071375
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 peptide hormone stimulus. A peptide hormone is any of a class of peptides that are secreted into the blood stream and have endocrine functions in living animals.
|
1 | P43138 (/IEP) |
Cellular response to organonitrogen compound GO:0071417
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 organonitrogen stimulus. An organonitrogen compound is formally a compound containing at least one carbon-nitrogen bond.
|
1 | P43138 (/IEP) |
Positive regulation of G1/S transition of mitotic cell cycle GO:1900087
Any signalling pathway that increases or activates a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the mitotic cell cycle.
|
1 | P43138 (/IMP) |
There are 29 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.
|
14 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(4 more) |
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.
|
13 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(3 more) |
Nuclear speck GO:0016607
A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
|
13 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(3 more) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
12 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(2 more) |
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.
|
12 |
A1YES6 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A1YFZ3 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T6Y4 (/ISS)
A2T7I6 (/ISS)
A2T7I6 (/ISS)
P23196 (/ISS)
(2 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
10 | A1YES6 (/ISS) A1YFZ3 (/ISS) A1YFZ3 (/ISS) A1YFZ3 (/ISS) A2T6Y4 (/ISS) A2T6Y4 (/ISS) A2T6Y4 (/ISS) A2T7I6 (/ISS) A2T7I6 (/ISS) P23196 (/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.
|
8 | G3V3M6 (/IDA) P27695 (/IDA) P27695 (/IDA) P28352 (/IDA) P28352 (/IDA) P43138 (/IDA) Q5TZP7 (/IDA) Q5TZP7 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
5 | P27695 (/IDA) P27695 (/IDA) P28352 (/IDA) P28352 (/IDA) P43138 (/IDA) |
Centrosome GO:0005813
A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
|
5 | G3V3M6 (/IDA) P27695 (/IDA) P27695 (/IDA) Q5TZP7 (/IDA) Q5TZP7 (/IDA) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
5 | P23196 (/ISS) P28352 (/ISS) P28352 (/ISS) P43138 (/ISS) Q9Z2J2 (/ISS) |
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.
|
3 | P27695 (/IDA) P27695 (/IDA) P43138 (/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 | P27695 (/IC) P27695 (/IC) |
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.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
2 | P27695 (/TAS) P27695 (/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 | P28352 (/ISO) P28352 (/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.
|
2 | P27695 (/IDA) P27695 (/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.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | P28352 (/ISO) P28352 (/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.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
2 | P27695 (/TAS) P27695 (/TAS) |
Centrosome GO:0005813
A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Ribosome GO:0005840
An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
|
2 | P27695 (/TAS) P27695 (/TAS) |
Nuclear speck GO:0016607
A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Nuclear speck GO:0016607
A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
|
2 | P28352 (/ISO) P28352 (/ISO) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
2 | P27695 (/IDA) P27695 (/IDA) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
2 | P28352 (/ISO) P28352 (/ISO) |
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 | P43138 (/IDA) |