CATH Superfamily 2.60.40.790
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: waiting to be named.
FunFam 11: Alpha-crystallin B chain
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 18 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 homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
41 |
P02510 (/ISS)
P02510 (/ISS)
P02510 (/ISS)
P02510 (/ISS)
P02512 (/ISS)
P05811 (/ISS)
P05811 (/ISS)
P05811 (/ISS)
P23927 (/ISS)
P23927 (/ISS)
(31 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).
|
16 |
P02510 (/IPI)
P02510 (/IPI)
P02510 (/IPI)
P02510 (/IPI)
P02511 (/IPI)
P02511 (/IPI)
P02511 (/IPI)
P02511 (/IPI)
P23927 (/IPI)
P23927 (/IPI)
(6 more) |
Amyloid-beta binding GO:0001540
Interacting selectively and non-covalently with amyloid-beta peptide/protein and/or its precursor.
|
4 | P02511 (/IPI) P02511 (/IPI) P02511 (/IPI) P02511 (/IPI) |
Structural constituent of eye lens GO:0005212
The action of a molecule that contributes to the structural integrity of the lens of an eye.
|
4 | P23927 (/TAS) P23927 (/TAS) P23928 (/TAS) P23928 (/TAS) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
4 | P02511 (/IPI) P02511 (/IPI) P02511 (/IPI) P02511 (/IPI) |
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
4 | P02511 (/IPI) P02511 (/IPI) P02511 (/IPI) P02511 (/IPI) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
4 | P02511 (/IPI) P02511 (/IPI) P02511 (/IPI) P02511 (/IPI) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
4 | P02511 (/IPI) P02511 (/IPI) P02511 (/IPI) P02511 (/IPI) |
Amyloid-beta binding GO:0001540
Interacting selectively and non-covalently with amyloid-beta peptide/protein and/or its precursor.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Microtubule binding GO:0008017
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
|
2 | P23928 (/IDA) P23928 (/IDA) |
Microtubule binding GO:0008017
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Cytoskeletal protein binding GO:0008092
Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
|
2 | P23928 (/IDA) P23928 (/IDA) |
Cytoskeletal protein binding GO:0008092
Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
|
2 | P23927 (/ISO) P23927 (/ISO) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
2 | A0A0R4IG31 (/IDA) Q6DG35 (/IDA) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
2 | P23927 (/ISO) P23927 (/ISO) |
There are 53 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 transcription, DNA-templated GO:0045892
Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
|
35 |
P02510 (/ISS)
P02510 (/ISS)
P02510 (/ISS)
P02510 (/ISS)
P05811 (/ISS)
P05811 (/ISS)
P05811 (/ISS)
P23927 (/ISS)
P23927 (/ISS)
P23928 (/ISS)
(25 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.
|
6 | P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P23928 (/IDA) P23928 (/IDA) |
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.
|
4 | P02511 (/NAS) P02511 (/NAS) P02511 (/NAS) P02511 (/NAS) |
Muscle contraction GO:0006936
A process in which force is generated within muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis.
|
4 | P02511 (/TAS) P02511 (/TAS) P02511 (/TAS) P02511 (/TAS) |
Regulation of cell death GO:0010941
Any process that modulates 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 | P02511 (/IMP) P02511 (/IMP) P02511 (/IMP) P02511 (/IMP) |
Negative regulation of intracellular transport GO:0032387
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances within cells.
|
4 | P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) |
Negative regulation of intracellular transport GO:0032387
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances within cells.
|
4 | P02510 (/ISS) P02510 (/ISS) P02510 (/ISS) P02510 (/ISS) |
Negative regulation of protein homooligomerization GO:0032463
Any process that stops, prevents, or reduces the frequency, rate or extent of protein homooligomerization.
|
4 | P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) |
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.
|
4 | P02510 (/ISS) P02510 (/ISS) P02510 (/ISS) P02510 (/ISS) |
Negative regulation of transcription, DNA-templated GO:0045892
Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
|
4 | P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
4 | P02511 (/IMP) P02511 (/IMP) P02511 (/IMP) P02511 (/IMP) |
Protein homooligomerization GO:0051260
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
|
4 | P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) |
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.
|
4 | P02511 (/IMP) P02511 (/IMP) P02511 (/IMP) P02511 (/IMP) |
Regulation of cellular response to heat GO:1900034
Any process that modulates the frequency, rate or extent of cellular response to heat.
|
4 | P02511 (/TAS) P02511 (/TAS) P02511 (/TAS) P02511 (/TAS) |
Negative regulation of amyloid fibril formation GO:1905907
Any process that stops, prevents or reduces the frequency, rate or extent of amyloid fibril formation.
|
4 | P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) |
Negative regulation of amyloid fibril formation GO:1905907
Any process that stops, prevents or reduces the frequency, rate or extent of amyloid fibril formation.
|
4 | P02511 (/TAS) P02511 (/TAS) P02511 (/TAS) P02511 (/TAS) |
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 | P23927 (/IMP) P23927 (/IMP) |
Lens development in camera-type eye GO:0002088
The process whose specific outcome is the progression of the lens over time, from its formation to the mature structure. The lens is a transparent structure in the eye through which light is focused onto the retina. An example of this process is found in Mus musculus.
|
2 | P23927 (/IGI) P23927 (/IGI) |
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.
|
2 | P23928 (/IDA) P23928 (/IDA) |
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.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Tubulin complex assembly GO:0007021
The aggregation and bonding together of alpha- and beta-tubulin to form a tubulin heterodimer.
|
2 | P23927 (/IMP) P23927 (/IMP) |
Muscle organ development GO:0007517
The process whose specific outcome is the progression of the muscle over time, from its formation to the mature structure. The muscle is an organ consisting of a tissue made up of various elongated cells that are specialized to contract and thus to produce movement and mechanical work.
|
2 | P23927 (/IGI) P23927 (/IGI) |
Skeletal muscle tissue development GO:0007519
The developmental sequence of events leading to the formation of adult skeletal muscle tissue. The main events are: the fusion of myoblasts to form myotubes that increase in size by further fusion to them of myoblasts, the formation of myofibrils within their cytoplasm and the establishment of functional neuromuscular junctions with motor neurons. At this stage they can be regarded as mature muscle fibers.
|
2 | A0A0R4IG31 (/IMP) Q6DG35 (/IMP) |
Aging GO:0007568
A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
|
2 | P23928 (/IEP) P23928 (/IEP) |
Locomotory behavior GO:0007626
The specific movement from place to place of an organism in response to external or internal stimuli. Locomotion of a whole organism in a manner dependent upon some combination of that organism's internal state and external conditions.
|
2 | A0A0R4IG31 (/IMP) Q6DG35 (/IMP) |
Multicellular organism aging GO:0010259
An aging process that has as participant a whole multicellular organism. Multicellular organism aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Multicellular organisms aging includes processes like cellular senescence and organ senescence, but is more inclusive. May precede death (GO:0016265) of an organism and may succeed developmental maturation (GO:0021700).
|
2 | P23928 (/IEP) P23928 (/IEP) |
Negative regulation of gene expression GO:0010629
Any process that decreases 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.
|
2 | P23927 (/IMP) P23927 (/IMP) |
Regulation of cell death GO:0010941
Any process that modulates 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.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Myofibril assembly GO:0030239
Formation of myofibrils, the repeating units of striated muscle.
|
2 | A0A0R4IG31 (/IMP) Q6DG35 (/IMP) |
Negative regulation of cell growth GO:0030308
Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
|
2 | P23928 (/IDA) P23928 (/IDA) |
Negative regulation of cell growth GO:0030308
Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Microtubule polymerization or depolymerization GO:0031109
Assembly or disassembly of microtubules by the addition or removal of tubulin heterodimers from a microtubule.
|
2 | P23928 (/IMP) P23928 (/IMP) |
Microtubule polymerization or depolymerization GO:0031109
Assembly or disassembly of microtubules by the addition or removal of tubulin heterodimers from a microtubule.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Response to estradiol GO:0032355
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 stimulus by estradiol, a C18 steroid hormone hydroxylated at C3 and C17 that acts as a potent estrogen.
|
2 | P23928 (/IEP) P23928 (/IEP) |
Negative regulation of intracellular transport GO:0032387
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances within cells.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Negative regulation of protein homooligomerization GO:0032463
Any process that stops, prevents, or reduces the frequency, rate or extent of protein homooligomerization.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Response to hydrogen peroxide GO:0042542
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 hydrogen peroxide (H2O2) stimulus.
|
2 | P23928 (/IEP) P23928 (/IEP) |
Response to hydrogen peroxide GO:0042542
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 hydrogen peroxide (H2O2) stimulus.
|
2 | P23927 (/IMP) P23927 (/IMP) |
Camera-type eye development GO:0043010
The process whose specific outcome is the progression of the camera-type eye over time, from its formation to the mature structure. The camera-type eye is an organ of sight that receives light through an aperture and focuses it through a lens, projecting it on a photoreceptor field.
|
2 | P23927 (/IGI) P23927 (/IGI) |
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 | P23927 (/IMP) P23927 (/IMP) |
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 | P23927 (/ISO) P23927 (/ISO) |
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.
|
2 | P23927 (/IGI) P23927 (/IGI) |
Negative regulation of transcription, DNA-templated GO:0045892
Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Protein homooligomerization GO:0051260
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Stress-activated MAPK cascade GO:0051403
A series of molecular signals in which a stress-activated MAP kinase cascade relays one or more of the signals; MAP kinase cascades involve at least three protein kinase activities and culminate in the phosphorylation and activation of a MAP kinase.
|
2 | P23928 (/IMP) P23928 (/IMP) |
Stress-activated MAPK cascade GO:0051403
A series of molecular signals in which a stress-activated MAP kinase cascade relays one or more of the signals; MAP kinase cascades involve at least three protein kinase activities and culminate in the phosphorylation and activation of a MAP kinase.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Heart contraction GO:0060047
The multicellular organismal process in which the heart decreases in volume in a characteristic way to propel blood through the body.
|
2 | A0A0R4IG31 (/IMP) Q6DG35 (/IMP) |
Apoptotic process involved in morphogenesis GO:0060561
Any apoptotic process that contributes to the shaping of an anatomical structure.
|
2 | P23927 (/IGI) P23927 (/IGI) |
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.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Negative regulation of amyloid fibril formation GO:1905907
Any process that stops, prevents or reduces the frequency, rate or extent of amyloid fibril formation.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Negative regulation of reactive oxygen species metabolic process GO:2000378
Any process that stops, prevents or reduces the frequency, rate or extent of reactive oxygen species metabolic process.
|
2 | P23928 (/IDA) P23928 (/IDA) |
Negative regulation of reactive oxygen species metabolic process GO:2000378
Any process that stops, prevents or reduces the frequency, rate or extent of reactive oxygen species metabolic process.
|
2 | P23927 (/ISO) P23927 (/ISO) |
There are 43 GO terms relating to "cellular component"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
|
35 |
P02510 (/ISS)
P02510 (/ISS)
P02510 (/ISS)
P02510 (/ISS)
P05811 (/ISS)
P05811 (/ISS)
P05811 (/ISS)
P23927 (/ISS)
P23927 (/ISS)
P23928 (/ISS)
(25 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.
|
35 |
P02510 (/ISS)
P02510 (/ISS)
P02510 (/ISS)
P02510 (/ISS)
P05811 (/ISS)
P05811 (/ISS)
P05811 (/ISS)
P23927 (/ISS)
P23927 (/ISS)
P23928 (/ISS)
(25 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
31 |
P02510 (/ISS)
P02510 (/ISS)
P02510 (/ISS)
P02510 (/ISS)
P05811 (/ISS)
P05811 (/ISS)
P05811 (/ISS)
P41316 (/ISS)
Q5ENY9 (/ISS)
Q5R9K0 (/ISS)
(21 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.
|
6 | P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P23928 (/IDA) P23928 (/IDA) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
4 | P02511 (/TAS) P02511 (/TAS) P02511 (/TAS) P02511 (/TAS) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
4 | P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P02511 (/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 | P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) P02511 (/IDA) |
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.
|
4 | P02511 (/HDA) P02511 (/HDA) P02511 (/HDA) P02511 (/HDA) |
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 | P23927 (/ISO) P23927 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
2 | P23927 (/IDA) P23927 (/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.
|
2 | P23928 (/IDA) P23928 (/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.
|
2 | P23927 (/ISO) P23927 (/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 | P23927 (/IDA) P23927 (/IDA) |
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.
|
2 | P23927 (/IDA) P23927 (/IDA) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
2 | P23928 (/IDA) P23928 (/IDA) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Postsynaptic density GO:0014069
An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
|
2 | P23928 (/IDA) P23928 (/IDA) |
Postsynaptic density GO:0014069
An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Microtubule cytoskeleton GO:0015630
The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins.
|
2 | P23928 (/IDA) P23928 (/IDA) |
Microtubule cytoskeleton GO:0015630
The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins.
|
2 | P23927 (/ISO) P23927 (/ISO) |
Z disc GO:0030018
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
|
2 | P23927 (/IDA) P23927 (/IDA) |
Axon GO:0030424
The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter.
|
2 | P23928 (/IDA) P23928 (/IDA) |
Axon GO:0030424
The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter.
|
2 | P23927 (/ISO) P23927 (/ISO) |
M band GO:0031430
The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
|
2 | P23928 (/IDA) P23928 (/IDA) |
M band GO:0031430
The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
|
2 | P23927 (/ISO) P23927 (/ISO) |
I band GO:0031674
A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end.
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2 | P23928 (/IDA) P23928 (/IDA) |
I band GO:0031674
A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end.
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2 | P23927 (/ISO) P23927 (/ISO) |
Actin filament bundle GO:0032432
An assembly of actin filaments that are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
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2 | P23928 (/IDA) P23928 (/IDA) |
Actin filament bundle GO:0032432
An assembly of actin filaments that are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
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2 | P23927 (/ISO) P23927 (/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 | P23927 (/ISO) P23927 (/ISO) |
Dendritic spine GO:0043197
A small, membranous protrusion from a dendrite that forms a postsynaptic compartment - typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable including \thin\, \stubby\, \mushroom\, and \branched\, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity.
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2 | P23928 (/IDA) P23928 (/IDA) |
Dendritic spine GO:0043197
A small, membranous protrusion from a dendrite that forms a postsynaptic compartment - typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable including \thin\, \stubby\, \mushroom\, and \branched\, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity.
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2 | P23927 (/ISO) P23927 (/ISO) |
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
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2 | P23928 (/IDA) P23928 (/IDA) |
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
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2 | P23927 (/ISO) P23927 (/ISO) |
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 | P23927 (/HDA) P23927 (/HDA) |
Contractile fiber GO:0043292
Fibers, composed of actin, myosin, and associated proteins, found in cells of smooth or striated muscle.
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2 | P23927 (/IDA) P23927 (/IDA) |
Synapse GO:0045202
The junction between a nerve fiber of one neuron and another neuron, muscle fiber or glial cell. As the nerve fiber approaches the synapse it enlarges into a specialized structure, the presynaptic nerve ending, which contains mitochondria and synaptic vesicles. At the tip of the nerve ending is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic nerve ending secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
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2 | P23928 (/IDA) P23928 (/IDA) |
Synapse GO:0045202
The junction between a nerve fiber of one neuron and another neuron, muscle fiber or glial cell. As the nerve fiber approaches the synapse it enlarges into a specialized structure, the presynaptic nerve ending, which contains mitochondria and synaptic vesicles. At the tip of the nerve ending is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic nerve ending secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
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2 | P23927 (/ISO) P23927 (/ISO) |
Synaptic membrane GO:0097060
A specialized area of membrane on either the presynaptic or the postsynaptic side of a synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell.
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2 | P23928 (/IDA) P23928 (/IDA) |
Synaptic membrane GO:0097060
A specialized area of membrane on either the presynaptic or the postsynaptic side of a synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell.
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2 | P23927 (/ISO) P23927 (/ISO) |
Cardiac myofibril GO:0097512
A cardiac myofibril is a myofibril specific to cardiac muscle cells.
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2 | P23928 (/IDA) P23928 (/IDA) |
Cardiac myofibril GO:0097512
A cardiac myofibril is a myofibril specific to cardiac muscle cells.
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2 | P23927 (/ISO) P23927 (/ISO) |