CATH Superfamily 2.60.40.790
The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was: waiting to be named.
FunFam 3: prostaglandin E synthase 3
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 20 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 |
---|---|---|
DNA polymerase binding GO:0070182
Interacting selectively and non-covalently with a DNA polymerase.
|
84 |
G1TGF1 (/IPI)
G1TGF1 (/IPI)
G1TGF1 (/IPI)
G1TGF1 (/IPI)
G1TGF1 (/IPI)
G1TGF1 (/IPI)
G1TGF1 (/IPI)
G1TGF1 (/IPI)
G1TGF1 (/IPI)
G1TGF1 (/IPI)
(74 more) |
Prostaglandin-E synthase activity GO:0050220
Catalysis of the reaction: prostaglandin H(2) = prostaglandin E(2).
|
44 |
P83868 (/IDA)
P83868 (/IDA)
P83868 (/IDA)
P83868 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
(34 more) |
Telomerase activity GO:0003720
Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Catalyzes extension of the 3'- end of a DNA strand by one deoxynucleotide at a time using an internal RNA template that encodes the telomeric repeat sequence.
|
40 |
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
(30 more) |
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).
|
40 |
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
(30 more) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
40 |
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
(30 more) |
Hsp90 protein binding GO:0051879
Interacting selectively and non-covalently with Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size.
|
40 |
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
Q15185 (/IPI)
(30 more) |
Prostaglandin-E synthase activity GO:0050220
Catalysis of the reaction: prostaglandin H(2) = prostaglandin E(2).
|
27 |
P83868 (/ISS)
P83868 (/ISS)
P83868 (/ISS)
P83868 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
(17 more) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
27 |
P83868 (/ISS)
P83868 (/ISS)
P83868 (/ISS)
P83868 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
(17 more) |
Telomerase activity GO:0003720
Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Catalyzes extension of the 3'- end of a DNA strand by one deoxynucleotide at a time using an internal RNA template that encodes the telomeric repeat sequence.
|
19 |
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
(9 more) |
Progesterone receptor binding GO:0033142
Interacting selectively and non-covalently with a progesterone receptor.
|
19 |
Q90955 (/IPI)
Q90955 (/IPI)
Q90955 (/IPI)
Q90955 (/IPI)
Q90955 (/IPI)
Q90955 (/IPI)
Q90955 (/IPI)
Q90955 (/IPI)
Q90955 (/IPI)
Q90955 (/IPI)
(9 more) |
P53 binding GO:0002039
Interacting selectively and non-covalently with one of the p53 family of proteins.
|
4 | P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) |
P53 binding GO:0002039
Interacting selectively and non-covalently with one of the p53 family of proteins.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Telomerase activity GO:0003720
Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Catalyzes extension of the 3'- end of a DNA strand by one deoxynucleotide at a time using an internal RNA template that encodes the telomeric repeat sequence.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
4 | P83868 (/IPI) P83868 (/IPI) P83868 (/IPI) P83868 (/IPI) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Prostaglandin-E synthase activity GO:0050220
Catalysis of the reaction: prostaglandin H(2) = prostaglandin E(2).
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Hsp90 protein binding GO:0051879
Interacting selectively and non-covalently with Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size.
|
4 | P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) |
Hsp90 protein binding GO:0051879
Interacting selectively and non-covalently with Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
DNA polymerase binding GO:0070182
Interacting selectively and non-covalently with a DNA polymerase.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
There are 38 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 |
---|---|---|
Telomere maintenance via telomerase GO:0007004
The maintenance of proper telomeric length by the addition of telomeric repeats by telomerase.
|
84 |
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
(74 more) |
Positive regulation of telomerase activity GO:0051973
Any process that activates or increases the frequency, rate or extent of telomerase activity, the catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
|
84 |
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
(74 more) |
Telomerase holoenzyme complex assembly GO:1905323
The aggregation, arrangement and bonding together of a set of components to form a telomerase holoenzyme complex.
|
84 |
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
G1TGF1 (/IDA)
(74 more) |
Prostaglandin biosynthetic process GO:0001516
The chemical reactions and pathways resulting in the formation of prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring.
|
44 |
P83868 (/IDA)
P83868 (/IDA)
P83868 (/IDA)
P83868 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
(34 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.
|
40 |
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
(30 more) |
Xenobiotic metabolic process GO:0006805
The chemical reactions and pathways involving a xenobiotic compound, a compound foreign to living organisms. Used of chemical compounds, e.g. a xenobiotic chemical, such as a pesticide.
|
40 |
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
(30 more) |
Telomere maintenance via telomerase GO:0007004
The maintenance of proper telomeric length by the addition of telomeric repeats by telomerase.
|
40 |
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
(30 more) |
Signal transduction GO:0007165
The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
|
40 |
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
(30 more) |
Cyclooxygenase pathway GO:0019371
The chemical reactions and pathways by which prostaglandins are formed from arachidonic acid, and in which prostaglandin-endoperoxide synthase (cyclooxygenase) catalyzes the committed step in the conversion of arachidonic acid to the prostaglandin-endoperoxides PGG2 and PGH2.
|
40 |
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
(30 more) |
Positive regulation of phosphorylation GO:0042327
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to a molecule.
|
40 |
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
(30 more) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
40 |
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
(30 more) |
Chaperone cofactor-dependent protein refolding GO:0051085
The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.
|
40 |
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
(30 more) |
Chaperone-mediated protein complex assembly GO:0051131
The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
|
40 |
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
(30 more) |
Positive regulation of telomerase activity GO:0051973
Any process that activates or increases the frequency, rate or extent of telomerase activity, the catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
|
40 |
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
(30 more) |
Regulation of cellular response to heat GO:1900034
Any process that modulates the frequency, rate or extent of cellular response to heat.
|
40 |
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
(30 more) |
Prostaglandin biosynthetic process GO:0001516
The chemical reactions and pathways resulting in the formation of prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring.
|
27 |
P83868 (/ISS)
P83868 (/ISS)
P83868 (/ISS)
P83868 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
(17 more) |
Prostaglandin biosynthetic process GO:0001516
The chemical reactions and pathways resulting in the formation of prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring.
|
8 | P83868 (/IMP) P83868 (/IMP) P83868 (/IMP) P83868 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) |
Prostaglandin biosynthetic process GO:0001516
The chemical reactions and pathways resulting in the formation of prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Glycogen biosynthetic process GO:0005978
The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
|
4 | Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) |
Prostaglandin metabolic process GO:0006693
The chemical reactions and pathways involving prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring due to the formation of a bond between two carbons of a fatty acid. They have a wide range of biological activities.
|
4 | P83868 (/IMP) P83868 (/IMP) P83868 (/IMP) P83868 (/IMP) |
Prostaglandin metabolic process GO:0006693
The chemical reactions and pathways involving prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring due to the formation of a bond between two carbons of a fatty acid. They have a wide range of biological activities.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Telomere maintenance via telomerase GO:0007004
The maintenance of proper telomeric length by the addition of telomeric repeats by telomerase.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Cell population proliferation GO:0008283
The multiplication or reproduction of cells, resulting in the expansion of a cell population.
|
4 | Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) |
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.
|
4 | P83868 (/IMP) P83868 (/IMP) P83868 (/IMP) P83868 (/IMP) |
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.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Sensory perception of pain GO:0019233
The series of events required for an organism to receive a painful stimulus, convert it to a molecular signal, and recognize and characterize the signal. Pain is medically defined as the physical sensation of discomfort or distress caused by injury or illness, so can hence be described as a harmful stimulus which signals current (or impending) tissue damage. Pain may come from extremes of temperature, mechanical damage, electricity or from noxious chemical substances. This is a neurological process.
|
4 | P83868 (/IMP) P83868 (/IMP) P83868 (/IMP) P83868 (/IMP) |
Sensory perception of pain GO:0019233
The series of events required for an organism to receive a painful stimulus, convert it to a molecular signal, and recognize and characterize the signal. Pain is medically defined as the physical sensation of discomfort or distress caused by injury or illness, so can hence be described as a harmful stimulus which signals current (or impending) tissue damage. Pain may come from extremes of temperature, mechanical damage, electricity or from noxious chemical substances. This is a neurological process.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Positive regulation of phosphorylation GO:0042327
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to a molecule.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Glucocorticoid receptor signaling pathway GO:0042921
Any series of molecular signals generated as a consequence of a glucocorticoid binding to its receptor.
|
4 | Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) |
Skin development GO:0043588
The process whose specific outcome is the progression of the skin over time, from its formation to the mature structure. The skin is the external membranous integument of an animal. In vertebrates the skin generally consists of two layers, an outer nonsensitive and nonvascular epidermis (cuticle or skarfskin) composed of cells which are constantly growing and multiplying in the deeper, and being thrown off in the superficial layers, as well as an inner vascular dermis (cutis, corium or true skin) composed mostly of connective tissue.
|
4 | Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Chaperone cofactor-dependent protein refolding GO:0051085
The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Chaperone-mediated protein complex assembly GO:0051131
The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Positive regulation of telomerase activity GO:0051973
Any process that activates or increases the frequency, rate or extent of telomerase activity, the catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Lung saccule development GO:0060430
The biological process whose specific outcome is the progression of a lung saccule from an initial condition to its mature state. The lung saccule is the primitive gas exchange portion of the lung composed of type I and type II cells.
|
4 | Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) Q9R0Q7 (/IMP) |
Negative regulation of cell death GO:0060548
Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.
|
4 | P83868 (/IMP) P83868 (/IMP) P83868 (/IMP) P83868 (/IMP) |
Negative regulation of cell death GO:0060548
Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Telomerase holoenzyme complex assembly GO:1905323
The aggregation, arrangement and bonding together of a set of components to form a telomerase holoenzyme complex.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
There are 26 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 |
---|---|---|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
105 |
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
(95 more) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
86 |
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
A0A024RB32 (/IDA)
(76 more) |
Chromosome, telomeric region GO:0000781
The terminal region of a linear chromosome that includes the telomeric DNA repeats and associated proteins.
|
40 |
Q15185 (/IC)
Q15185 (/IC)
Q15185 (/IC)
Q15185 (/IC)
Q15185 (/IC)
Q15185 (/IC)
Q15185 (/IC)
Q15185 (/IC)
Q15185 (/IC)
Q15185 (/IC)
(30 more) |
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.
|
40 |
Q15185 (/HDA)
Q15185 (/HDA)
Q15185 (/HDA)
Q15185 (/HDA)
Q15185 (/HDA)
Q15185 (/HDA)
Q15185 (/HDA)
Q15185 (/HDA)
Q15185 (/HDA)
Q15185 (/HDA)
(30 more) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
40 |
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
(30 more) |
Telomerase holoenzyme complex GO:0005697
Telomerase is a ribonucleoprotein enzyme complex, with a minimal catalytic core composed of a catalytic reverse transcriptase subunit and an RNA subunit that provides the template for telomeric DNA addition. In vivo, the holoenzyme complex often contains additional subunits.
|
40 |
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
(30 more) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
40 |
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
Q15185 (/TAS)
(30 more) |
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.
|
40 |
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
Q15185 (/IMP)
(30 more) |
Chaperone complex GO:0101031
A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins.
|
40 |
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
Q15185 (/IDA)
(30 more) |
Telomerase holoenzyme complex GO:0005697
Telomerase is a ribonucleoprotein enzyme complex, with a minimal catalytic core composed of a catalytic reverse transcriptase subunit and an RNA subunit that provides the template for telomeric DNA addition. In vivo, the holoenzyme complex often contains additional subunits.
|
19 |
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
Q90955 (/ISS)
(9 more) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Telomerase holoenzyme complex GO:0005697
Telomerase is a ribonucleoprotein enzyme complex, with a minimal catalytic core composed of a catalytic reverse transcriptase subunit and an RNA subunit that provides the template for telomeric DNA addition. In vivo, the holoenzyme complex often contains additional subunits.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Actin filament GO:0005884
A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
|
4 | P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) |
Actin filament GO:0005884
A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
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.
|
4 | P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) P83868 (/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.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
|
4 | P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) |
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
4 | P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
4 | P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) |
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
4 | P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) P83868 (/IDA) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |
Chaperone complex GO:0101031
A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins.
|
4 | Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) Q9R0Q7 (/ISO) |