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 26: Heat shock protein 70
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 22 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 |
---|---|---|
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).
|
37 |
G3I8R9 (/IPI)
G3I8R9 (/IPI)
G3I8R9 (/IPI)
P06761 (/IPI)
P07823 (/IPI)
P07823 (/IPI)
P07823 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
(27 more) |
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
|
25 |
P06761 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
(15 more) |
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
|
20 |
G3I8R9 (/IDA)
G3I8R9 (/IDA)
G3I8R9 (/IDA)
P07823 (/IDA)
P07823 (/IDA)
P07823 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(10 more) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
17 |
P07823 (/IPI)
P07823 (/IPI)
P07823 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
(7 more) |
Misfolded protein binding GO:0051787
Interacting selectively and non-covalently with a misfolded protein.
|
17 |
P06761 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(7 more) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
14 |
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
(4 more) |
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
|
14 |
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
(4 more) |
Cadherin binding GO:0045296
Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.
|
14 |
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
(4 more) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Chaperone binding GO:0051087
Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
3 | G3I8R9 (/NAS) G3I8R9 (/NAS) G3I8R9 (/NAS) |
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
|
3 | P20029 (/ISO) P20029 (/ISO) P36604 (/ISO) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
3 | P20029 (/ISO) P20029 (/ISO) P36604 (/ISO) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Ribosome binding GO:0043022
Interacting selectively and non-covalently with any part of a ribosome.
|
2 | P20029 (/IDA) P20029 (/IDA) |
Misfolded protein binding GO:0051787
Interacting selectively and non-covalently with a misfolded protein.
|
2 | P20029 (/ISO) P20029 (/ISO) |
RNA polymerase II transcription factor binding GO:0001085
Interacting selectively and non-covalently with an RNA polymerase II transcription factor, any protein required to initiate or regulate transcription by RNA polymerase II.
|
1 | P20163 (/IPI) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
1 | P36604 (/IC) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
1 | P06761 (/IPI) |
There are 82 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 |
---|---|---|
Negative regulation of protein homodimerization activity GO:0090074
Any process that decreases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.
|
27 |
P06761 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
(17 more) |
Negative regulation of IRE1-mediated unfolded protein response GO:1903895
Any process that stops, prevents or reduces the frequency, rate or extent of the IRE1-mediated unfolded protein response.
|
27 |
P06761 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
(17 more) |
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.
|
17 |
G3I8R9 (/IMP)
G3I8R9 (/IMP)
G3I8R9 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(7 more) |
Substantia nigra development GO:0021762
The progression of the substantia nigra over time from its initial formation until its mature state. The substantia nigra is the layer of gray substance that separates the posterior parts of the cerebral peduncles (tegmentum mesencephali) from the anterior parts; it normally includes a posterior compact part with many pigmented cells (pars compacta) and an anterior reticular part whose cells contain little pigment (pars reticularis).
|
14 |
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
(4 more) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
14 |
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(4 more) |
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
14 |
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(4 more) |
Protein folding in endoplasmic reticulum GO:0034975
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Maintenance of protein localization in endoplasmic reticulum GO:0035437
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
|
14 |
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(4 more) |
IRE1-mediated unfolded protein response GO:0036498
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
PERK-mediated unfolded protein response GO:0036499
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
ATF6-mediated unfolded protein response GO:0036500
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Cellular response to glucose starvation GO:0042149
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 deprivation of glucose.
|
14 |
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(4 more) |
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.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Regulation of protein folding in endoplasmic reticulum GO:0060904
Any process that modulates the rate, frequency or extent of the protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Negative regulation of protein homodimerization activity GO:0090074
Any process that decreases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Regulation of ATF6-mediated unfolded protein response GO:1903891
Any process that modulates the frequency, rate or extent of the ATF6-mediated unfolded protein response.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Regulation of IRE1-mediated unfolded protein response GO:1903894
Any process that modulates the frequency, rate or extent of the IRE1-mediated unfolded protein response.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Regulation of PERK-mediated unfolded protein response GO:1903897
Any process that modulates the frequency, rate or extent of the PERK-mediated unfolded protein response.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress GO:1990440
Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of an endoplasmic reticulum stress.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
12 |
G3I8R9 (/ISS)
G3I8R9 (/ISS)
G3I8R9 (/ISS)
P06761 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P20029 (/ISS)
P20029 (/ISS)
Q0VCX2 (/ISS)
(2 more) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
9 | P06761 (/ISS) P07823 (/ISS) P07823 (/ISS) P07823 (/ISS) P20029 (/ISS) P20029 (/ISS) Q0VCX2 (/ISS) Q3S4T7 (/ISS) Q5R4P0 (/ISS) |
Maintenance of protein localization in endoplasmic reticulum GO:0035437
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
|
9 | P06761 (/ISS) P07823 (/ISS) P07823 (/ISS) P07823 (/ISS) P20029 (/ISS) P20029 (/ISS) Q0VCX2 (/ISS) Q3S4T7 (/ISS) Q5R4P0 (/ISS) |
Protein folding in endoplasmic reticulum GO:0034975
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
|
8 | Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
3 | P06761 (/IEP) Q39043 (/IEP) Q39043 (/IEP) |
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process GO:0043154
Any process that stops, prevents, or reduces the frequency, rate or extent of a cysteine-type endopeptidase activity involved in the apoptotic process.
|
3 | G3I8R9 (/IMP) G3I8R9 (/IMP) G3I8R9 (/IMP) |
Negative regulation of protein homodimerization activity GO:0090074
Any process that decreases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.
|
3 | G3I8R9 (/IDA) G3I8R9 (/IDA) G3I8R9 (/IDA) |
Negative regulation of IRE1-mediated unfolded protein response GO:1903895
Any process that stops, prevents or reduces the frequency, rate or extent of the IRE1-mediated unfolded protein response.
|
3 | G3I8R9 (/IDA) G3I8R9 (/IDA) G3I8R9 (/IDA) |
Response to hypoxia GO:0001666
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 stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
|
2 | Q6P3L3 (/IDA) Q7SZD3 (/IDA) |
Response to yeast GO:0001878
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 stimulus from a yeast species.
|
2 | Q6P3L3 (/IDA) Q7SZD3 (/IDA) |
ER overload response GO:0006983
The series of molecular signals generated by the accumulation of normal or misfolded proteins in the endoplasmic reticulum and leading to activation of transcription by NF-kappaB.
|
2 | P20029 (/IDA) P20029 (/IDA) |
Response to cytokinin GO:0009735
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 cytokinin stimulus.
|
2 | Q39043 (/IDA) Q39043 (/IDA) |
Positive regulation of neuron projection development GO:0010976
Any process that increases the rate, frequency or extent of neuron projection development. Neuron projection development is the process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
|
2 | P20029 (/ISO) P20029 (/ISO) |
RNA interference GO:0016246
The process in which double-stranded RNAs silence cognate genes. Involves posttranscriptional gene inactivation ('silencing') both of transgenes or dsRNA introduced into a germline, and of the host gene(s) homologous to the transgenes or dsRNA. This silencing is triggered by the introduction of transgenes or double-stranded RNA (dsRNA), and can occur through a specific decrease in the level of mRNA, or by negative regulation of translation, of both host genes and transgenes.
|
2 | P29844 (/IMP) P29844 (/IMP) |
Cerebellum structural organization GO:0021589
The process that contributes to the act of creating the structural organization of the cerebellum. This process pertains to the physical shaping of a rudimentary structure. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. The cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
|
2 | P20029 (/IMP) P20029 (/IMP) |
Cerebellar Purkinje cell layer development GO:0021680
The process whose specific outcome is the progression of the cerebellar Purkinje cell layer over time, from its formation to the mature structure. The Purkinje cell layer lies just underneath the molecular layer of the cerebellar cortex. It contains the neuronal cell bodies of the Purkinje cells that are arranged side by side in a single layer. Candelabrum interneurons are vertically oriented between the Purkinje cells. Purkinje neurons are inhibitory and provide the output of the cerebellar cortex through axons that project into the white matter. Extensive dendritic trees from the Purkinje cells extend upward in a single plane into the molecular layer where they synapse with parallel fibers of granule cells.
|
2 | P20029 (/IMP) P20029 (/IMP) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Sleep GO:0030431
Any process in which an organism enters and maintains a periodic, readily reversible state of reduced awareness and metabolic activity. Usually accompanied by physical relaxation, the onset of sleep in humans and other mammals is marked by a change in the electrical activity of the brain.
|
2 | P29844 (/TAS) P29844 (/TAS) |
Negative regulation of transforming growth factor beta receptor signaling pathway GO:0030512
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
|
2 | P20029 (/IGI) P20029 (/IGI) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
2 | P20163 (/HEP) P27420 (/HEP) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
2 | P20163 (/IEP) P27420 (/IEP) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
2 | P20029 (/IMP) P20029 (/IMP) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Positive regulation of protein ubiquitination GO:0031398
Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein.
|
2 | P20029 (/IMP) P20029 (/IMP) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
2 | P29844 (/IMP) P29844 (/IMP) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Maintenance of protein localization in endoplasmic reticulum GO:0035437
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Intestinal stem cell homeostasis GO:0036335
Any biological process involved in the maintenance of the steady-state number of intestinal stem cells within a population of cells.
|
2 | P29844 (/IMP) P29844 (/IMP) |
Positive regulation of embryonic development GO:0040019
Any process that activates or increases the frequency, rate or extent of embryonic development.
|
2 | P20029 (/TAS) P20029 (/TAS) |
Cellular response to glucose starvation GO:0042149
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 deprivation of glucose.
|
2 | P20029 (/ISO) P20029 (/ISO) |
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.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Response to cadmium ion GO:0046686
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 cadmium (Cd) ion stimulus.
|
2 | Q39043 (/IEP) Q39043 (/IEP) |
Proteolysis involved in cellular protein catabolic process GO:0051603
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
|
2 | P20029 (/IDA) P20029 (/IDA) |
Cellular response to interleukin-4 GO:0071353
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 interleukin-4 stimulus.
|
2 | P20029 (/IDA) P20029 (/IDA) |
Toxin transport GO:1901998
The directed movement of a toxin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
|
2 | P20029 (/IMP) P20029 (/IMP) |
Luteolysis GO:0001554
The lysis or structural demise of the corpus luteum. During normal luteolysis, two closely related events occur. First, there is loss of the capacity to synthesize and secrete progesterone (functional luteolysis) followed by loss of the cells that comprise the corpus luteum (structural luteolysis). Preventing luteolysis is crucial to maintain pregnancy.
|
1 | P06761 (/IEP) |
Translation GO:0006412
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
|
1 | Q5A397 (/IGI) |
Response to radiation GO:0009314
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 electromagnetic radiation stimulus. Electromagnetic radiation is a propagating wave in space with electric and magnetic components. These components oscillate at right angles to each other and to the direction of propagation.
|
1 | P06761 (/IEP) |
Pollen tube growth GO:0009860
Growth of pollen via tip extension of the intine wall.
|
1 | Q8H1B3 (/IEP) |
Positive regulation of neuron projection development GO:0010976
Any process that increases the rate, frequency or extent of neuron projection development. Neuron projection development is the process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
|
1 | P06761 (/IMP) |
Neuron differentiation GO:0030182
The process in which a relatively unspecialized cell acquires specialized features of a neuron.
|
1 | P06761 (/IEP) |
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
|
1 | Q9LKR3 (/IMP) |
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
|
1 | P36604 (/ISO) |
Filamentous growth GO:0030447
The process in which a multicellular organism, a unicellular organism or a group of unicellular organisms grow in a threadlike, filamentous shape.
|
1 | Q5A397 (/IMP) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
1 | P06761 (/IDA) |
Cellular response to drug GO:0035690
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 drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
|
1 | P06761 (/IEP) |
IRE1-mediated unfolded protein response GO:0036498
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
|
1 | P36604 (/IMP) |
Response to cocaine GO:0042220
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 cocaine stimulus. Cocaine is a crystalline alkaloid obtained from the leaves of the coca plant.
|
1 | P06761 (/IEP) |
Filamentous growth of a population of unicellular organisms GO:0044182
The process in which a group of unicellular organisms grow in a threadlike, filamentous shape.
|
1 | Q5A397 (/IMP) |
Induction by symbiont of host defense response GO:0044416
The activation by an organism of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
|
1 | Q5A397 (/IDA) |
Response to mercury ion GO:0046689
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 mercury ion stimulus.
|
1 | Q8T869 (/IDA) |
Neuron apoptotic process GO:0051402
Any apoptotic process in a neuron, the basic cellular unit of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the nervous system.
|
1 | P06761 (/IEP) |
Cellular response to antibiotic GO:0071236
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 antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
|
1 | P06761 (/IEP) |
Cellular response to calcium ion GO:0071277
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 calcium ion stimulus.
|
1 | P06761 (/IEP) |
Cellular response to manganese ion GO:0071287
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 manganese ion stimulus.
|
1 | P06761 (/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 | P06761 (/IEP) |
Cellular response to interferon-gamma GO:0071346
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 interferon-gamma stimulus. Interferon gamma is the only member of the type II interferon found so far.
|
1 | B5X397 (/IMP) |
Cellular response to gamma radiation GO:0071480
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 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 | P06761 (/IEP) |
Stress response to metal ion GO:0097501
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 disturbance in organismal or cellular homeostasis caused by a metal ion stimulus.
|
1 | P06761 (/IEP) |
Response to methamphetamine hydrochloride GO:1904313
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 methamphetamine hydrochloride stimulus.
|
1 | P06761 (/IEP) |
Cellular response to nerve growth factor stimulus GO:1990090
A 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 nerve growth factor stimulus.
|
1 | P06761 (/IEP) |
There are 70 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 |
---|---|---|
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).
|
38 |
B9RYP6 (/IDA)
P06761 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(28 more) |
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
17 |
G3I8R9 (/IDA)
G3I8R9 (/IDA)
G3I8R9 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(7 more) |
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.
|
17 |
P07823 (/IDA)
P07823 (/IDA)
P07823 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(7 more) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
16 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(6 more) |
Endoplasmic reticulum-Golgi intermediate compartment GO:0005793
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
|
16 |
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(6 more) |
Endoplasmic reticulum chaperone complex GO:0034663
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
|
16 |
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(6 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
15 |
P06761 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(5 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.
|
15 |
P06761 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(5 more) |
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).
|
15 |
P06761 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(5 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.
|
15 |
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(5 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.
|
14 |
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
(4 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.
|
14 |
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(4 more) |
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).
|
14 |
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(4 more) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
14 |
G3I8R9 (/IDA)
G3I8R9 (/IDA)
G3I8R9 (/IDA)
P20029 (/IDA)
P20029 (/IDA)
P36604 (/IDA)
Q6Z7B0 (/IDA)
Q6Z7B0 (/IDA)
Q6Z7B0 (/IDA)
Q6Z7B0 (/IDA)
(4 more) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
|
14 |
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
(4 more) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
14 |
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
(4 more) |
Midbody GO:0030496
A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis.
|
14 |
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(4 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.
|
14 |
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(4 more) |
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
|
14 |
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
(4 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.
|
12 |
G3I8R9 (/ISS)
G3I8R9 (/ISS)
G3I8R9 (/ISS)
P06761 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P20029 (/ISS)
P20029 (/ISS)
Q0VCX2 (/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.
|
11 |
G3I8R9 (/ISS)
G3I8R9 (/ISS)
G3I8R9 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P20029 (/ISS)
P20029 (/ISS)
Q0VCX2 (/ISS)
Q3S4T7 (/ISS)
(1 more) |
Plant-type vacuole membrane GO:0009705
The lipid bilayer surrounding a vacuole that retains the same shape regardless of cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this component is found in Arabidopsis thaliana.
|
8 | Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
6 | P07823 (/ISS) P07823 (/ISS) P07823 (/ISS) Q0VCX2 (/ISS) Q3S4T7 (/ISS) Q5R4P0 (/ISS) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
6 | P20029 (/IDA) P20029 (/IDA) Q39043 (/IDA) Q39043 (/IDA) Q5A397 (/IDA) Q9LKR3 (/IDA) |
Mediator complex GO:0016592
A protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The mediator complex is required for activation of transcription of most protein-coding genes, but can also act as a transcriptional corepressor. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins.
|
4 | Q39043 (/IDA) Q39043 (/IDA) Q8H1B3 (/IDA) Q9LKR3 (/IDA) |
Cell wall GO:0005618
The rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal, most prokaryotic cells and some protozoan parasites, maintaining their shape and protecting them from osmotic lysis. In plants it is made of cellulose and, often, lignin; in fungi it is composed largely of polysaccharides; in bacteria it is composed of peptidoglycan; in protozoan parasites such as Giardia species, it's made of carbohydrates and proteins.
|
3 | Q39043 (/IDA) Q39043 (/IDA) Q9LKR3 (/IDA) |
Vacuole GO:0005773
A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol.
|
3 | Q39043 (/IDA) Q39043 (/IDA) Q9LKR3 (/IDA) |
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
|
3 | Q39043 (/IDA) Q39043 (/IDA) Q9LKR3 (/IDA) |
Plasmodesma GO:0009506
A fine cytoplasmic channel, found in all higher plants, that connects the cytoplasm of one cell to that of an adjacent cell.
|
3 | Q39043 (/IDA) Q39043 (/IDA) Q9LKR3 (/IDA) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
3 | P20029 (/IDA) P20029 (/IDA) Q5A397 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
3 | P06761 (/IDA) Q39043 (/IDA) Q39043 (/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.
|
3 | Q0VCX2 (/ISS) Q3S4T7 (/ISS) Q5R4P0 (/ISS) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
3 | G3I8R9 (/IDA) G3I8R9 (/IDA) G3I8R9 (/IDA) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
2 | Q6P3L3 (/IDA) Q7SZD3 (/IDA) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
2 | P20029 (/TAS) P20029 (/TAS) |
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
|
2 | P29844 (/IDA) P29844 (/IDA) |
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 | Q39043 (/IDA) Q39043 (/IDA) |
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.
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2 | P20029 (/ISO) P20029 (/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.
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2 | Q39043 (/IDA) Q39043 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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2 | P20029 (/ISO) P20029 (/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.
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2 | P20029 (/ISO) P20029 (/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).
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2 | P20029 (/ISO) P20029 (/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).
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2 | P29844 (/NAS) P29844 (/NAS) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
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2 | P20029 (/IDA) P20029 (/IDA) |
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
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2 | P20029 (/ISO) P20029 (/ISO) |
Endoplasmic reticulum-Golgi intermediate compartment GO:0005793
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
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2 | P20029 (/ISO) P20029 (/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.
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2 | P20029 (/ISO) P20029 (/ISO) |
Endomembrane system GO:0012505
A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
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2 | P29844 (/HDA) P29844 (/HDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
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2 | P20029 (/ISO) P20029 (/ISO) |
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
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2 | P20029 (/ISO) P20029 (/ISO) |
Midbody GO:0030496
A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis.
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2 | P20029 (/ISO) P20029 (/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.
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2 | P20029 (/ISO) P20029 (/ISO) |
Endoplasmic reticulum chaperone complex GO:0034663
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
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2 | P20029 (/ISO) P20029 (/ISO) |
Endoplasmic reticulum chaperone complex GO:0034663
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
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2 | P20163 (/ISS) P27420 (/ISS) |
Myelin sheath GO:0043209
An electrically insulating fatty layer that surrounds the axons of many neurons. It is an outgrowth of glial cells: Schwann cells supply the myelin for peripheral neurons while oligodendrocytes supply it to those of the central nervous system.
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2 | P20029 (/HDA) P20029 (/HDA) |
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.
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2 | P20029 (/ISO) P20029 (/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).
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1 | P36604 (/HDA) |
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
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1 | P06761 (/IDA) |
Rough endoplasmic reticulum GO:0005791
The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae.
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1 | P20163 (/IDA) |
Golgi apparatus GO:0005794
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
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1 | Q9LKR3 (/IDA) |
Lipid droplet GO:0005811
An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.
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1 | Q8T869 (/HDA) |
Fungal-type cell wall GO:0009277
A rigid yet dynamic structure surrounding the plasma membrane that affords protection from stresses and contributes to cell morphogenesis, consisting of extensively cross-linked glycoproteins and carbohydrates. The glycoproteins may be modified with N- or O-linked carbohydrates, or glycosylphosphatidylinositol (GPI) anchors; the polysaccharides are primarily branched glucans, including beta-linked and alpha-linked glucans, and may also include chitin and other carbohydrate polymers, but not cellulose or pectin. Enzymes involved in cell wall biosynthesis are also found in the cell wall. Note that some forms of fungi develop a capsule outside of the cell wall under certain circumstances; this is considered a separate structure.
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1 | Q5A397 (/IDA) |
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
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1 | Q9LKR3 (/IDA) |
Yeast-form cell wall GO:0030445
The wall surrounding a cell of a dimorphic fungus growing in the single-cell budding yeast form, in contrast to the filamentous or hyphal form.
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1 | Q5A397 (/IDA) |
Nuclear membrane GO:0031965
Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
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1 | P36604 (/IDA) |
Phagocytic vesicle GO:0045335
A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
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1 | Q8T869 (/HDA) |
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
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1 | B5X397 (/IDA) |
Perinuclear endoplasmic reticulum lumen GO:0099020
The volume enclosed by the membranes of the perinuclear endoplasmic reticulum.
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1 | P36604 (/IDA) |
Cortical endoplasmic reticulum lumen GO:0099021
The volume enclosed by the membranes of the cortical endoplasmic reticulum.
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1 | P36604 (/IDA) |