The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"Cyclophilin-like
".
FunFam 1: Peptidyl-prolyl cis-trans isomerase
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 17 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 |
---|---|---|
Peptidyl-prolyl cis-trans isomerase activity GO:0003755
Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
|
85 |
A0A286XJS2 (/ISS)
A5YBL8 (/ISS)
D2GYR4 (/ISS)
F1PLV2 (/ISS)
F1PLV2 (/ISS)
F7BZB1 (/ISS)
F7DYN1 (/ISS)
F7HFK5 (/ISS)
F7HFK5 (/ISS)
F7HFK5 (/ISS)
(75 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).
|
83 |
A0A286XJS2 (/ISS)
A5YBL8 (/ISS)
D2GYR4 (/ISS)
F1PLV2 (/ISS)
F1PLV2 (/ISS)
F7BZB1 (/ISS)
F7DYN1 (/ISS)
F7HFK5 (/ISS)
F7HFK5 (/ISS)
F7HFK5 (/ISS)
(73 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).
|
24 |
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
(14 more) |
Peptidyl-prolyl cis-trans isomerase activity GO:0003755
Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
|
22 |
F4IX26 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
(12 more) |
Cyclosporin A binding GO:0016018
Interacting selectively and non-covalently with cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids.
|
14 |
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
(4 more) |
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
|
12 |
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
(2 more) |
Peptidyl-prolyl cis-trans isomerase activity GO:0003755
Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
|
12 |
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
(2 more) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
12 |
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
(2 more) |
RNA polymerase binding GO:0070063
Interacting selectively and non-covalently with an RNA polymerase molecule or complex.
|
12 |
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
P23284 (/IPI)
(2 more) |
Cyclosporin A binding GO:0016018
Interacting selectively and non-covalently with cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids.
|
11 |
P24367 (/ISS)
P24368 (/ISS)
P24369 (/ISS)
P24369 (/ISS)
P24369 (/ISS)
P30412 (/ISS)
P30412 (/ISS)
P80311 (/ISS)
P80311 (/ISS)
Q08E11 (/ISS)
(1 more) |
Peptidyl-prolyl cis-trans isomerase activity GO:0003755
Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
|
5 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) P30412 (/ISO) P30412 (/ISO) |
Cyclosporin A binding GO:0016018
Interacting selectively and non-covalently with cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids.
|
5 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) P30412 (/ISO) P30412 (/ISO) |
RNA polymerase binding GO:0070063
Interacting selectively and non-covalently with an RNA polymerase molecule or complex.
|
3 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) |
Peptidyl-prolyl cis-trans isomerase activity GO:0003755
Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
|
2 | Q9ASS6 (/IMP) Q9ASS6 (/IMP) |
Protein histidine kinase binding GO:0043424
Interacting selectively and non-covalently with protein histidine kinase.
|
2 | Q9ASS6 (/IPI) Q9ASS6 (/IPI) |
Peptidyl-prolyl cis-trans isomerase activity GO:0003755
Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
|
1 | Q57X93 (/ISM) |
Cyclosporin A binding GO:0016018
Interacting selectively and non-covalently with cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids.
|
1 | Q6AYQ9 (/TAS) |
There are 29 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 |
---|---|---|
Protein peptidyl-prolyl isomerization GO:0000413
The modification of a protein by cis-trans isomerization of a proline residue.
|
85 |
A0A286XJS2 (/ISS)
A5YBL8 (/ISS)
D2GYR4 (/ISS)
F1PLV2 (/ISS)
F1PLV2 (/ISS)
F7BZB1 (/ISS)
F7DYN1 (/ISS)
F7HFK5 (/ISS)
F7HFK5 (/ISS)
F7HFK5 (/ISS)
(75 more) |
Chaperone-mediated protein folding GO:0061077
The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
|
71 |
A0A286XJS2 (/ISS)
A5YBL8 (/ISS)
D2GYR4 (/ISS)
F1PLV2 (/ISS)
F1PLV2 (/ISS)
F7BZB1 (/ISS)
F7DYN1 (/ISS)
F7HFK5 (/ISS)
F7HFK5 (/ISS)
F7HFK5 (/ISS)
(61 more) |
Protein peptidyl-prolyl isomerization GO:0000413
The modification of a protein by cis-trans isomerization of a proline residue.
|
18 |
F4IX26 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
(8 more) |
Chaperone-mediated protein folding GO:0061077
The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
|
13 |
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
(3 more) |
Positive regulation of multicellular organism growth GO:0040018
Any process that activates or increases the frequency, rate or extent of growth of an organism to reach its usual body size.
|
12 |
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
(2 more) |
Positive regulation by host of viral process GO:0044794
A process in which a host organism activates or increases the frequency, rate or extent of the release of a process being mediated by a virus with which it is infected.
|
12 |
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
(2 more) |
Positive regulation by host of viral genome replication GO:0044829
A process in which a host organism activates or increases the frequency, rate or extent of viral genome replication.
|
12 |
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
(2 more) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
12 |
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
(2 more) |
Bone development GO:0060348
The process whose specific outcome is the progression of bone over time, from its formation to the mature structure. Bone is the hard skeletal connective tissue consisting of both mineral and cellular components.
|
12 |
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
P23284 (/IMP)
(2 more) |
Protein peptidyl-prolyl isomerization GO:0000413
The modification of a protein by cis-trans isomerization of a proline residue.
|
5 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) P30412 (/ISO) P30412 (/ISO) |
Positive regulation of multicellular organism growth GO:0040018
Any process that activates or increases the frequency, rate or extent of growth of an organism to reach its usual body size.
|
3 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) |
Positive regulation by host of viral process GO:0044794
A process in which a host organism activates or increases the frequency, rate or extent of the release of a process being mediated by a virus with which it is infected.
|
3 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) |
Positive regulation by host of viral genome replication GO:0044829
A process in which a host organism activates or increases the frequency, rate or extent of viral genome replication.
|
3 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
3 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) |
Bone development GO:0060348
The process whose specific outcome is the progression of bone over time, from its formation to the mature structure. Bone is the hard skeletal connective tissue consisting of both mineral and cellular components.
|
3 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) |
NAD(P)H dehydrogenase complex assembly GO:0010275
The aggregation, arrangement and bonding together of a set of components to form NAD(P)H dehydrogenase complex, which is involved in electron transport from an unidentified electron donor, possibly NAD(P)H or ferredoxin(Fd) to the plastoquinone pool.
|
2 | Q9ASS6 (/IMP) Q9ASS6 (/IMP) |
Protein folding GO:0006457
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
|
1 | Q57X93 (/ISM) |
Response to oxidative stress GO:0006979
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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
|
1 | F4IX26 (/IMP) |
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.
|
1 | F4IX26 (/ISS) |
Response to light intensity GO:0009642
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 light intensity stimulus.
|
1 | F4IX26 (/IMP) |
Response to salt stress GO:0009651
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 an increase or decrease in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
|
1 | F4IX26 (/IMP) |
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.
|
1 | F4IX26 (/IDA) |
Response to abscisic acid GO:0009737
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 abscisic acid stimulus.
|
1 | F4IX26 (/IEP) |
Response to mannitol GO:0010555
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 mannitol stimulus.
|
1 | F4IX26 (/IMP) |
Cysteine biosynthetic process GO:0019344
The chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid.
|
1 | F4IX26 (/IMP) |
Multicellular organism reproduction GO:0032504
The biological process in which new individuals are produced by one or two multicellular organisms. The new individuals inherit some proportion of their genetic material from the parent or parents.
|
1 | Q9W227 (/HEP) |
Defense response to bacterium GO:0042742
Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.
|
1 | F4IX26 (/IEP) |
Nuclear transport GO:0051169
The directed movement of substances into, out of, or within the nucleus.
|
1 | P24368 (/TAS) |
Negative regulation of collagen fibril organization GO:1904027
Any process that stops, prevents or reduces the frequency, rate or extent of collagen fibril organization.
|
1 | P24367 (/IDA) |
There are 36 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 |
---|---|---|
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.
|
83 |
A0A286XJS2 (/ISS)
A5YBL8 (/ISS)
D2GYR4 (/ISS)
F1PLV2 (/ISS)
F1PLV2 (/ISS)
F7BZB1 (/ISS)
F7DYN1 (/ISS)
F7HFK5 (/ISS)
F7HFK5 (/ISS)
F7HFK5 (/ISS)
(73 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.
|
13 |
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
(3 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.
|
12 |
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
(2 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.
|
12 |
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
(2 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).
|
12 |
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
(2 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).
|
12 |
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
(2 more) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
12 |
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
P23284 (/NAS)
(2 more) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
12 |
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
P23284 (/TAS)
(2 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.
|
12 |
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
(2 more) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
12 |
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
P23284 (/HDA)
(2 more) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
12 |
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
P23284 (/IDA)
(2 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.
|
3 | P24369 (/ISO) P24369 (/ISO) P24369 (/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).
|
3 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) |
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.
|
3 | P24369 (/ISO) P24369 (/ISO) P24369 (/ISO) |
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
|
3 | F4IX26 (/IDA) Q9ASS6 (/IDA) Q9ASS6 (/IDA) |
Chloroplast thylakoid membrane GO:0009535
The pigmented membrane of a chloroplast thylakoid. An example of this component is found in Arabidopsis thaliana.
|
3 | F4IX26 (/IDA) Q9ASS6 (/IDA) Q9ASS6 (/IDA) |
Thylakoid GO:0009579
A membranous cellular structure that bears the photosynthetic pigments in plants, algae, and cyanobacteria. In cyanobacteria thylakoids are of various shapes and are attached to, or continuous with, the plasma membrane. In eukaryotes they are flattened, membrane-bounded disk-like structures located in the chloroplasts; in the chloroplasts of higher plants the thylakoids form dense stacks called grana. Isolated thylakoid preparations can carry out photosynthetic electron transport and the associated phosphorylation.
|
3 | F4IX26 (/IDA) Q9ASS6 (/IDA) Q9ASS6 (/IDA) |
Thylakoid lumen GO:0031977
The volume enclosed by a thylakoid membrane.
|
3 | F4IX26 (/IDA) Q9ASS6 (/IDA) Q9ASS6 (/IDA) |
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.
|
3 | P24369 (/IDA) P24369 (/IDA) P24369 (/IDA) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
3 | P24369 (/ISO) P24369 (/ISO) P24369 (/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.
|
2 | E9PKY5 (/IDA) E9PKY5 (/IDA) |
Chloroplast stromal thylakoid GO:0009533
Unstacked thylakoids that connect the grana stacks through the stroma.
|
2 | Q9ASS6 (/IDA) Q9ASS6 (/IDA) |
Chloroplast thylakoid GO:0009534
Sac-like membranous structures (cisternae) in a chloroplast combined into stacks (grana) and present singly in the stroma (stroma thylakoids or frets) as interconnections between grana. An example of this component is found in Arabidopsis thaliana.
|
2 | Q9ASS6 (/IDA) Q9ASS6 (/IDA) |
Nuclear speck GO:0016607
A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
|
2 | E9PKY5 (/IDA) E9PKY5 (/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.
|
1 | Q9W227 (/HDA) |
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.
|
1 | Q9W227 (/HDA) |
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.
|
1 | Q9W227 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | P52013 (/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.
|
1 | P24368 (/IDA) |
Chloroplast stroma GO:0009570
The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis.
|
1 | F4IX26 (/IDA) |
Chloroplast envelope GO:0009941
The double lipid bilayer enclosing the chloroplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
|
1 | F4IX26 (/IDA) |
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.
|
1 | Q9W227 (/HDA) |
Glycosome GO:0020015
A membrane-bounded organelle found in organisms from the order Kinetoplastida that houses the enzymes of glycolysis.
|
1 | Q57X93 (/IDA) |
Cytosolic ribosome GO:0022626
A ribosome located in the cytosol.
|
1 | F4IX26 (/IDA) |
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
|
1 | P24367 (/IDA) |
Apoplast GO:0048046
The cell membranes and intracellular regions in a plant are connected through plasmodesmata, and plants may be described as having two major compartments: the living symplast and the non-living apoplast. The apoplast is external to the plasma membrane and includes cell walls, intercellular spaces and the lumen of dead structures such as xylem vessels. Water and solutes pass freely through it.
|
1 | F4IX26 (/IDA) |