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:
"I/LWEQ domain
".
FunFam 2: Huntingtin interacting protein 1
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 35 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).
|
5 | F1MUI0 (/IPI) O00291 (/IPI) O75146 (/IPI) Q8VD75 (/IPI) Q9JKY5 (/IPI) |
Clathrin binding GO:0030276
Interacting selectively and non-covalently with a clathrin heavy or light chain, the main components of the coat of coated vesicles and coated pits, and which also occurs in synaptic vesicles.
|
4 | G3V8Y8 (/IDA) O00291 (/IDA) O75146 (/IDA) Q9JKY5 (/IDA) |
Actin filament binding GO:0051015
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
|
4 | O00291 (/IDA) O75146 (/IDA) Q99PW9 (/IDA) Q9JKY5 (/IDA) |
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
3 | O00291 (/IDA) O75146 (/IDA) Q9JKY5 (/IDA) |
Clathrin binding GO:0030276
Interacting selectively and non-covalently with a clathrin heavy or light chain, the main components of the coat of coated vesicles and coated pits, and which also occurs in synaptic vesicles.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Clathrin light chain binding GO:0032051
Interacting selectively and non-covalently with a clathrin light chain.
|
2 | O00291 (/IPI) Q9JKY5 (/IPI) |
Phosphatidylinositol binding GO:0035091
Interacting selectively and non-covalently with any inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
|
2 | O00291 (/IDA) O75146 (/IDA) |
Phosphatidylinositol binding GO:0035091
Interacting selectively and non-covalently with any inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Phosphatidylinositol binding GO:0035091
Interacting selectively and non-covalently with any inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
|
2 | Q8VD75 (/ISS) Q9JKY5 (/ISS) |
Clathrin adaptor activity GO:0035615
Bringing together a cargo protein with clathrin, responsible for the formation of endocytic vesicles.
|
2 | O00291 (/IC) Q9JKY5 (/IC) |
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Phosphatidylinositol-3,4-bisphosphate binding GO:0043325
Interacting selectively and non-covalently with phosphatidylinositol-3,4-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 4' positions.
|
2 | O00291 (/IDA) O75146 (/IDA) |
Phosphatidylinositol-3,4-bisphosphate binding GO:0043325
Interacting selectively and non-covalently with phosphatidylinositol-3,4-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 4' positions.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
|
2 | O00291 (/IPI) Q9JKY5 (/IPI) |
Actin filament binding GO:0051015
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Phosphatidylinositol-3,5-bisphosphate binding GO:0080025
Interacting selectively and non-covalently with phosphatidylinositol-3,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 5' positions.
|
2 | O00291 (/IDA) O75146 (/IDA) |
Phosphatidylinositol-3,5-bisphosphate binding GO:0080025
Interacting selectively and non-covalently with phosphatidylinositol-3,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 5' positions.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Actin binding GO:0003779
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
|
1 | Q9JKY5 (/IDA) |
Epidermal growth factor receptor binding GO:0005154
Interacting selectively and non-covalently with the epidermal growth factor receptor.
|
1 | O00291 (/TAS) |
Structural constituent of cytoskeleton GO:0005200
The action of a molecule that contributes to the structural integrity of a cytoskeletal structure.
|
1 | O00291 (/TAS) |
Phosphatidylinositol-4,5-bisphosphate binding GO:0005546
Interacting selectively and non-covalently with phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.
|
1 | O75146 (/IDA) |
Phosphatidylinositol-4,5-bisphosphate binding GO:0005546
Interacting selectively and non-covalently with phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.
|
1 | Q9JKY5 (/ISO) |
Phosphatidylinositol-3,4,5-trisphosphate binding GO:0005547
Interacting selectively and non-covalently with phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions.
|
1 | O75146 (/IDA) |
Phosphatidylinositol-3,4,5-trisphosphate binding GO:0005547
Interacting selectively and non-covalently with phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions.
|
1 | Q9JKY5 (/ISO) |
SH3 domain binding GO:0017124
Interacting selectively and non-covalently with a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.
|
1 | Q9JKY5 (/IDA) |
Clathrin light chain binding GO:0032051
Interacting selectively and non-covalently with a clathrin light chain.
|
1 | Q8VD75 (/ISO) |
Phosphatidylinositol-3-phosphate binding GO:0032266
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
|
1 | O00291 (/IDA) |
Phosphatidylinositol-3-phosphate binding GO:0032266
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
|
1 | Q8VD75 (/ISO) |
Glutamate receptor binding GO:0035254
Interacting selectively and non-covalently with a glutamate receptor.
|
1 | O00291 (/TAS) |
AP-2 adaptor complex binding GO:0035612
Interacting selectively and non-covalently with the AP-2 adaptor complex. The AP-2 adaptor complex is a heterotetrameric AP-type membrane coat adaptor complex that consists of alpha, beta2, mu2 and sigma2 subunits and links clathrin to the membrane surface of a vesicle. In at least humans, the AP-2 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different alpha genes (alphaA and alphaC).
|
1 | O00291 (/IPI) |
AP-2 adaptor complex binding GO:0035612
Interacting selectively and non-covalently with the AP-2 adaptor complex. The AP-2 adaptor complex is a heterotetrameric AP-type membrane coat adaptor complex that consists of alpha, beta2, mu2 and sigma2 subunits and links clathrin to the membrane surface of a vesicle. In at least humans, the AP-2 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different alpha genes (alphaA and alphaC).
|
1 | Q8VD75 (/ISO) |
Clathrin adaptor activity GO:0035615
Bringing together a cargo protein with clathrin, responsible for the formation of endocytic vesicles.
|
1 | Q9JKY5 (/IDA) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | O75146 (/IPI) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | Q9JKY5 (/ISO) |
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
|
1 | Q8VD75 (/ISO) |
There are 52 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 |
---|---|---|
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.
|
5 | A0A2R8QB02 (/IDA) A0A2R8QJ16 (/IDA) C9K4U5 (/IDA) F1R6L2 (/IDA) X1WBM9 (/IDA) |
Chordate embryonic development GO:0043009
The process whose specific outcome is the progression of the embryo over time, from zygote formation through a stage including a notochord and neural tube until birth or egg hatching.
|
5 | A0A2R8QB02 (/IMP) A0A2R8QJ16 (/IMP) C9K4U5 (/IMP) F1R6L2 (/IMP) X1WBM9 (/IMP) |
Clathrin coat assembly GO:0048268
The process that results in the assembly of clathrin triskelia into the ordered structure known as a clathrin cage.
|
3 | G3V8Y8 (/IDA) O00291 (/IDA) Q9JKY5 (/IDA) |
Activation of cysteine-type endopeptidase activity involved in apoptotic process GO:0006919
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
|
2 | O00291 (/IDA) O75146 (/IDA) |
Activation of cysteine-type endopeptidase activity involved in apoptotic process GO:0006919
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Regulation of endocytosis GO:0030100
Any process that modulates the frequency, rate or extent of endocytosis.
|
2 | O00291 (/NAS) O75146 (/NAS) |
Positive regulation of epidermal growth factor receptor signaling pathway GO:0045742
Any process that activates or increases the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
|
2 | O00291 (/IMP) O75146 (/IMP) |
Positive regulation of epidermal growth factor receptor signaling pathway GO:0045742
Any process that activates or increases the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Positive regulation of receptor-mediated endocytosis GO:0048260
Any process that activates or increases the frequency, rate or extent of receptor mediated endocytosis, the uptake of external materials by cells, utilizing receptors to ensure specificity of transport.
|
2 | O00291 (/IMP) Q8VD75 (/IMP) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
2 | O00291 (/IDA) O75146 (/IDA) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Membrane organization GO:0061024
A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins.
|
2 | O00291 (/TAS) O75146 (/TAS) |
Regulation of clathrin-dependent endocytosis GO:2000369
Any process that modulates the frequency, rate or extent of clathrin-mediated endocytosis.
|
2 | O75146 (/NAS) Q9JKY5 (/NAS) |
Positive regulation of platelet-derived growth factor receptor-beta signaling pathway GO:2000588
Any process that activates or increases the frequency, rate or extent of platelet-derived growth factor receptor-beta signaling pathway.
|
2 | O00291 (/IMP) O75146 (/IMP) |
Positive regulation of platelet-derived growth factor receptor-beta signaling pathway GO:2000588
Any process that activates or increases the frequency, rate or extent of platelet-derived growth factor receptor-beta signaling pathway.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Endocytosis GO:0006897
A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
|
1 | Q8VD75 (/IDA) |
Endocytosis GO:0006897
A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
|
1 | G3V8Y8 (/TAS) |
Receptor-mediated endocytosis GO:0006898
An endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles.
|
1 | Q9JKY5 (/IDA) |
Receptor-mediated endocytosis GO:0006898
An endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles.
|
1 | O75146 (/IMP) |
Receptor-mediated endocytosis GO:0006898
An endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles.
|
1 | Q9JKY5 (/ISO) |
Receptor-mediated endocytosis GO:0006898
An endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles.
|
1 | Q9JKY5 (/ISS) |
Apoptotic process GO:0006915
A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
|
1 | O00291 (/IDA) |
Apoptotic process GO:0006915
A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
|
1 | Q8VD75 (/ISO) |
Regulation of endocytosis GO:0030100
Any process that modulates the frequency, rate or extent of endocytosis.
|
1 | O75146 (/IMP) |
Regulation of endocytosis GO:0030100
Any process that modulates the frequency, rate or extent of endocytosis.
|
1 | Q9JKY5 (/ISO) |
Negative regulation of actin filament polymerization GO:0030837
Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
|
1 | Q9JKY5 (/IDA) |
Negative regulation of actin filament polymerization GO:0030837
Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
|
1 | O75146 (/IMP) |
Negative regulation of actin filament polymerization GO:0030837
Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
|
1 | Q9JKY5 (/ISO) |
Positive regulation of protein binding GO:0032092
Any process that activates or increases the frequency, rate or extent of protein binding.
|
1 | O75146 (/IDA) |
Positive regulation of protein binding GO:0032092
Any process that activates or increases the frequency, rate or extent of protein binding.
|
1 | Q9JKY5 (/ISO) |
Regulation of actin cytoskeleton organization GO:0032956
Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
|
1 | Q9JKY5 (/IGI) |
Regulation of actin cytoskeleton organization GO:0032956
Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
|
1 | O75146 (/IMP) |
Regulation of actin cytoskeleton organization GO:0032956
Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
|
1 | Q9JKY5 (/ISO) |
Negative regulation of Arp2/3 complex-mediated actin nucleation GO:0034316
Any process that stops, prevents, or reduces the frequency, rate or extent of actin nucleation mediated by the Arp2/3 complex and interacting proteins.
|
1 | Q9JKY5 (/IDA) |
Regulation of apoptotic process GO:0042981
Any process that modulates the occurrence or rate of cell death by apoptotic process.
|
1 | O00291 (/IDA) |
Regulation of apoptotic process GO:0042981
Any process that modulates the occurrence or rate of cell death by apoptotic process.
|
1 | Q8VD75 (/ISO) |
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
|
1 | O75146 (/IGI) |
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
|
1 | Q9JKY5 (/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.
|
1 | Q9JKY5 (/IMP) |
Positive regulation of receptor-mediated endocytosis GO:0048260
Any process that activates or increases the frequency, rate or extent of receptor mediated endocytosis, the uptake of external materials by cells, utilizing receptors to ensure specificity of transport.
|
1 | Q8VD75 (/ISO) |
Clathrin coat assembly GO:0048268
The process that results in the assembly of clathrin triskelia into the ordered structure known as a clathrin cage.
|
1 | Q8VD75 (/ISO) |
Positive regulation of protein kinase B signaling GO:0051897
Any process that activates or increases the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
|
1 | O00291 (/IC) |
Digestive system development GO:0055123
The process whose specific outcome is the progression of the digestive system over time, from its formation to the mature structure. The digestive system is the entire structure in which digestion takes place. Digestion is all of the physical, chemical, and biochemical processes carried out by multicellular organisms to break down ingested nutrients into components that may be easily absorbed and directed into metabolism.
|
1 | Q9JKY5 (/IMP) |
Regulation of gastric acid secretion GO:0060453
Any process that modulates the rate frequency or extent of gastric secretion. Gastric secretion is the regulated release of gastric acid (hydrochloric acid) by parietal or oxyntic cells during digestion.
|
1 | Q9JKY5 (/IMP) |
Membrane organization GO:0061024
A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins.
|
1 | Q9JKY5 (/IMP) |
Apoptotic signaling pathway GO:0097190
A series of molecular signals which triggers the apoptotic death of a cell. The pathway starts with reception of a signal, and ends when the execution phase of apoptosis is triggered.
|
1 | O00291 (/IDA) |
Apoptotic signaling pathway GO:0097190
A series of molecular signals which triggers the apoptotic death of a cell. The pathway starts with reception of a signal, and ends when the execution phase of apoptosis is triggered.
|
1 | Q8VD75 (/ISO) |
Neurotransmitter receptor transport GO:0099637
The directed movement of neurotransmitter receptors.
|
1 | O00291 (/TAS) |
Positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway GO:1901030
Any process that activates or increases the frequency, rate or extent of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway.
|
1 | O75146 (/IGI) |
Positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway GO:1901030
Any process that activates or increases the frequency, rate or extent of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway.
|
1 | Q9JKY5 (/ISO) |
Positive regulation of clathrin coat assembly GO:1905445
Any process that activates or increases the frequency, rate or extent of clathrin coat assembly.
|
1 | Q9JKY5 (/IDA) |
Positive regulation of clathrin-dependent endocytosis GO:2000370
Any process that activates or increases the frequency, rate or extent of clathrin-mediated endocytosis.
|
1 | Q9JKY5 (/IC) |
There are 53 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 |
---|---|---|
Clathrin-coated vesicle GO:0030136
A vesicle with a coat formed of clathrin connected to the membrane via one of the clathrin adaptor complexes.
|
4 | G3V8Y8 (/IDA) O00291 (/IDA) O75146 (/IDA) Q9JKY5 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
3 | B5DFK5 (/IDA) F1LML7 (/IDA) Q99PW9 (/IDA) |
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 | O00291 (/TAS) O75146 (/TAS) |
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 | O75146 (/ISS) Q9JKY5 (/ISS) |
Clathrin-coated vesicle GO:0030136
A vesicle with a coat formed of clathrin connected to the membrane via one of the clathrin adaptor complexes.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/ISO) |
Dendrite cytoplasm GO:0032839
All of the contents of a dendrite, excluding the surrounding plasma membrane.
|
2 | O75146 (/ISS) Q9JKY5 (/ISS) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
2 | O75146 (/ISS) Q9JKY5 (/ISS) |
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.
|
2 | O75146 (/ISS) Q9JKY5 (/ISS) |
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.
|
2 | O00291 (/IDA) O75146 (/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.
|
2 | Q8VD75 (/ISO) Q9JKY5 (/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.
|
2 | O75146 (/ISS) Q9JKY5 (/ISS) |
Presynapse GO:0098793
The part of a synapse that is part of the presynaptic cell.
|
2 | G3V8Y8 (/IDA) O00291 (/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.
|
1 | O00291 (/TAS) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | O00291 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q8VD75 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | O00291 (/TAS) |
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.
|
1 | O00291 (/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.
|
1 | Q8VD75 (/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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1 | O75146 (/IDA) |
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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1 | Q9JKY5 (/ISO) |
Cytoskeleton GO:0005856
Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
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1 | Q9JKY5 (/IDA) |
Cytoskeleton GO:0005856
Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
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1 | O00291 (/TAS) |
Clathrin-coated pit GO:0005905
A part of the endomembrane system in the form of an invagination of a membrane upon which a clathrin coat forms, and that can be converted by vesicle budding into a clathrin-coated vesicle. Coated pits form on the plasma membrane, where they are involved in receptor-mediated selective transport of many proteins and other macromolecules across the cell membrane, in the trans-Golgi network, and on some endosomes.
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1 | Q9JKY5 (/IDA) |
Cell cortex GO:0005938
The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
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1 | Q9JKY5 (/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.
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1 | Q99PW9 (/IDA) |
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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1 | Q9JKY5 (/ISO) |
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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1 | O00291 (/TAS) |
Integral component of membrane GO:0016021
The component of a 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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1 | G3V8Y8 (/TAS) |
Apical plasma membrane GO:0016324
The region of the plasma membrane located at the apical end of the cell.
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1 | Q9JKY5 (/IDA) |
Clathrin-coated vesicle GO:0030136
A vesicle with a coat formed of clathrin connected to the membrane via one of the clathrin adaptor complexes.
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1 | Q9JKY5 (/ISS) |
Dendrite GO:0030425
A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
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1 | Q99PW9 (/IDA) |
Extrinsic component of cytoplasmic side of plasma membrane GO:0031234
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
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1 | G3V8Y8 (/IDA) |
Extrinsic component of cytoplasmic side of plasma membrane GO:0031234
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
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1 | Q8VD75 (/ISO) |
Ruffle membrane GO:0032587
The portion of the plasma membrane surrounding a ruffle.
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1 | O75146 (/IDA) |
Ruffle membrane GO:0032587
The portion of the plasma membrane surrounding a ruffle.
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1 | Q9JKY5 (/ISO) |
Dendrite cytoplasm GO:0032839
All of the contents of a dendrite, excluding the surrounding plasma membrane.
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1 | Q99PW9 (/IDA) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
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1 | Q99PW9 (/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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1 | Q99PW9 (/IDA) |
Postsynaptic membrane GO:0045211
A specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters cross the synaptic cleft and transmit the signal to the postsynaptic membrane.
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1 | G3V8Y8 (/IDA) |
Postsynaptic membrane GO:0045211
A specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters cross the synaptic cleft and transmit the signal to the postsynaptic membrane.
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1 | Q8VD75 (/ISO) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
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1 | Q9JKY5 (/IDA) |
Endocytic patch GO:0061645
The part of the cell cortex consisting of an aggregation of proteins that will give rise to an endocytic vesicle.
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1 | F1MUI0 (/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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1 | Q99PW9 (/IDA) |
Presynapse GO:0098793
The part of a synapse that is part of the presynaptic cell.
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1 | Q8VD75 (/ISO) |
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
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1 | G3V8Y8 (/IDA) |
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
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1 | Q8VD75 (/ISO) |
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
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1 | O00291 (/TAS) |
Extrinsic component of presynaptic membrane GO:0098888
The component of the presynaptic membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
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1 | G3V8Y8 (/IDA) |
Extrinsic component of presynaptic membrane GO:0098888
The component of the presynaptic membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
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1 | Q8VD75 (/ISO) |
Extrinsic component of postsynaptic membrane GO:0098890
The component of the postsynaptic membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
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1 | G3V8Y8 (/IDA) |
Extrinsic component of postsynaptic membrane GO:0098890
The component of the postsynaptic membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
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1 | Q8VD75 (/ISO) |
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
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1 | G3V8Y8 (/IDA) |
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
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1 | Q8VD75 (/ISO) |