The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
« Back to all FunFams

FunFam 3: heat shock cognate 71 kDa protein-like

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 51 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).
51 P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI)
(41 more)
Heat shock protein binding GO:0031072
Interacting selectively and non-covalently with a heat shock protein, any protein synthesized or activated in response to heat shock.
39 A0PA16 (/IPI) A0PA16 (/IPI) A0PA16 (/IPI) A0PA16 (/IPI) A0PA16 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI)
(29 more)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
38 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(28 more)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
38 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(28 more)
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
38 P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI)
(28 more)
G protein-coupled receptor binding GO:0001664
Interacting selectively and non-covalently with a G protein-coupled receptor.
34 P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI)
(24 more)
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
34 P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA)
(24 more)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
MHC class II protein complex binding GO:0023026
Interacting selectively and non-covalently with the class II major histocompatibility complex.
34 P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA)
(24 more)
Protein binding, bridging GO:0030674
The binding activity of a molecule that brings together two or more protein molecules, or a protein and another macromolecule or complex, through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.
34 P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI)
(24 more)
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
34 P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI)
(24 more)
ATPase activity, coupled GO:0042623
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction directly drives some other reaction, for example ion transport across a membrane.
34 P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS)
(24 more)
ATPase activity, coupled GO:0042623
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction directly drives some other reaction, for example ion transport across a membrane.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Cadherin binding GO:0045296
Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.
34 P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA)
(24 more)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
34 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(24 more)
Chaperone binding GO:0051087
Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
34 P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI)
(24 more)
C3HC4-type RING finger domain binding GO:0055131
Interacting selectively and non-covalently with a C3HC4-type zinc finger domain of a protein. The C3HC4-type zinc finger is a variant of RING finger, is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C, where X is any amino acid. Many proteins containing a C3HC4-type RING finger play a key role in the ubiquitination pathway.
34 P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI)
(24 more)
ATPase activity, coupled GO:0042623
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction directly drives some other reaction, for example ion transport across a membrane.
8 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
G protein-coupled receptor binding GO:0001664
Interacting selectively and non-covalently with a G protein-coupled receptor.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Phosphatidylserine binding GO:0001786
Interacting selectively and non-covalently with phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine.
4 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA)
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Signaling receptor binding GO:0005102
Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
4 P63018 (/IPI) P63018 (/IPI) P63018 (/IPI) P63018 (/IPI)
Signaling receptor binding GO:0005102
Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Transcription factor binding GO:0008134
Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.
4 P63018 (/IPI) P63018 (/IPI) P63018 (/IPI) P63018 (/IPI)
Transcription factor binding GO:0008134
Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Protein binding, bridging GO:0030674
The binding activity of a molecule that brings together two or more protein molecules, or a protein and another macromolecule or complex, through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Heat shock protein binding GO:0031072
Interacting selectively and non-covalently with a heat shock protein, any protein synthesized or activated in response to heat shock.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
A1 adenosine receptor binding GO:0031686
Interacting selectively and non-covalently with an A1 adenosine receptor.
4 P63018 (/IPI) P63018 (/IPI) P63018 (/IPI) P63018 (/IPI)
A1 adenosine receptor binding GO:0031686
Interacting selectively and non-covalently with an A1 adenosine receptor.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Peptide binding GO:0042277
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Peptide binding GO:0042277
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
ATPase activity, coupled GO:0042623
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction directly drives some other reaction, for example ion transport across a membrane.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
4 P63017 (/IPI) P63017 (/IPI) P63017 (/IPI) P63017 (/IPI)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Chaperone binding GO:0051087
Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
C3HC4-type RING finger domain binding GO:0055131
Interacting selectively and non-covalently with a C3HC4-type zinc finger domain of a protein. The C3HC4-type zinc finger is a variant of RING finger, is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C, where X is any amino acid. Many proteins containing a C3HC4-type RING finger play a key role in the ubiquitination pathway.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Prostaglandin binding GO:1904593
Interacting selectively and non-covalently with prostaglandin.
4 P63018 (/IPI) P63018 (/IPI) P63018 (/IPI) P63018 (/IPI)
Prostaglandin binding GO:1904593
Interacting selectively and non-covalently with prostaglandin.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Clathrin-uncoating ATPase activity GO:1990833
Catalysis of the reaction: ATP + H2O = ADP + phosphate. Catalysis of the removal of clathrin from vesicle membranes, coupled to the hydrolysis of ATP.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Clathrin-uncoating ATPase activity GO:1990833
Catalysis of the reaction: ATP + H2O = ADP + phosphate. Catalysis of the removal of clathrin from vesicle membranes, coupled to the hydrolysis of ATP.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
2 P11147 (/ISS) P11147 (/ISS)
Chaperone binding GO:0051087
Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
2 P11147 (/IDA) P11147 (/IDA)
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).
1 O73885 (/IMP)

There are 136 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.
49 A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS)
(39 more)
Regulation of protein complex stability GO:0061635
Any process that affects the structure and integrity of a protein complex by altering the likelihood of its assembly or disassembly.
38 P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS)
(28 more)
Chaperone-mediated autophagy GO:0061684
The autophagy process which begins when chaperones and co-chaperones recognize a target motif and unfold the substrate protein. The proteins are then transported to the lysosome where they are degraded.
38 P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS)
(28 more)
Chaperone-mediated autophagy translocation complex disassembly GO:1904764
The disaggregation of a chaperone-mediated autophagy translocation complex into its constituent components.
38 P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS)
(28 more)
MRNA splicing, via spliceosome GO:0000398
The joining together of exons from one or more primary transcripts of messenger RNA (mRNA) and the excision of intron sequences, via a spliceosomal mechanism, so that mRNA consisting only of the joined exons is produced.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
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.
34 P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS)
(24 more)
Response to unfolded protein GO:0006986
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 unfolded protein stimulus.
34 P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS)
(24 more)
Neurotransmitter secretion GO:0007269
The regulated release of neurotransmitter from the presynapse into the synaptic cleft via calcium-regulated exocytosis during synaptic transmission.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Cellular response to starvation GO:0009267
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of nourishment.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Cytokine-mediated signaling pathway GO:0019221
A series of molecular signals initiated by the binding of a cytokine to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Regulation of protein stability GO:0031647
Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
34 P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP)
(24 more)
Protein refolding GO:0042026
The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
34 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(24 more)
Regulation of protein complex assembly GO:0043254
Any process that modulates the frequency, rate or extent of protein complex assembly.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Neutrophil degranulation GO:0043312
The regulated exocytosis of secretory granules containing preformed mediators such as proteases, lipases, and inflammatory mediators by a neutrophil.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Regulation of mRNA stability GO:0043488
Any process that modulates the propensity of mRNA molecules to degradation. Includes processes that both stabilize and destabilize mRNAs.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
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.
34 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(24 more)
ATP metabolic process GO:0046034
The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator.
34 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(24 more)
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.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Chaperone-mediated autophagy GO:0061684
The autophagy process which begins when chaperones and co-chaperones recognize a target motif and unfold the substrate protein. The proteins are then transported to the lysosome where they are degraded.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Protein targeting to lysosome involved in chaperone-mediated autophagy GO:0061740
The targeting of a protein to the lysosome process in which an input protein binds to a chaperone and subsequently to a lysosomal receptor.
34 P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP) P11142 (/IMP)
(24 more)
Protein targeting to lysosome involved in chaperone-mediated autophagy GO:0061740
The targeting of a protein to the lysosome process in which an input protein binds to a chaperone and subsequently to a lysosomal receptor.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Chaperone-mediated protein transport involved in chaperone-mediated autophagy GO:0061741
The chaperone-mediated protein transport process in which a protein that is bound to a chaperone and a lysosomal receptor is unfolded and transported into the lysosome as part of chaperone-mediated autophagy.
34 P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS) P11142 (/NAS)
(24 more)
Regulation of cellular response to heat GO:1900034
Any process that modulates the frequency, rate or extent of cellular response to heat.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Negative regulation of supramolecular fiber organization GO:1902904
Any process that stops, prevents or reduces the frequency, rate or extent of fibril organization.
34 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(24 more)
Regulation of protein import GO:1904589
Any process that modulates the frequency, rate or extent of protein import.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 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.
10 P11147 (/IDA) P11147 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Protein refolding GO:0042026
The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
8 P63017 (/ISS) P63017 (/ISS) P63017 (/ISS) P63017 (/ISS) P63018 (/ISS) P63018 (/ISS) P63018 (/ISS) P63018 (/ISS)
Response to heat GO:0009408
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 heat stimulus, a temperature stimulus above the optimal temperature for that organism.
6 P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA)
Response to cadmium ion GO:0046686
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cadmium (Cd) ion stimulus.
6 P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA)
Response to copper ion GO:0046688
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 copper ion stimulus.
6 P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA)
Late endosomal microautophagy GO:0061738
The autophagy process by which cytosolic proteins targeted for degradation are tagged with a chaperone and are directly transferred into and degraded in a late endosomal compartment.
6 P11147 (/IMP) P11147 (/IMP) P63017 (/IMP) P63017 (/IMP) P63017 (/IMP) P63017 (/IMP)
Response to arsenite ion GO:1903842
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 arsenite ion stimulus.
6 P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA)
Synaptic vesicle uncoating GO:0016191
The removal of the protein coat on a synaptic vesicle following the pinching step at the end of budding from the presynaptic membrane.
5 P19120 (/EXP) P19120 (/EXP) P19120 (/EXP) P19120 (/EXP) P19120 (/EXP)
Synaptic vesicle uncoating GO:0016191
The removal of the protein coat on a synaptic vesicle following the pinching step at the end of budding from the presynaptic membrane.
5 P19120 (/IDA) P19120 (/IDA) P19120 (/IDA) P19120 (/IDA) P19120 (/IDA)
Positive regulation of flagellated sperm motility GO:1902093
Any process that activates or increases the frequency, rate or extent of flagellated sperm motility.
5 A0PA16 (/IDA) A0PA16 (/IDA) A0PA16 (/IDA) A0PA16 (/IDA) A0PA16 (/IDA)
G1/S transition of mitotic cell cycle GO:0000082
The mitotic cell cycle transition by which a cell in G1 commits to S phase. The process begins with the build up of G1 cyclin-dependent kinase (G1 CDK), resulting in the activation of transcription of G1 cyclins. The process ends with the positive feedback of the G1 cyclins on the G1 CDK which commits the cell to S phase, in which DNA replication is initiated.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Kidney development GO:0001822
The process whose specific outcome is the progression of the kidney over time, from its formation to the mature structure. The kidney is an organ that filters the blood and/or excretes the end products of body metabolism in the form of urine.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Positive regulation of T cell mediated cytotoxicity GO:0001916
Any process that activates or increases the frequency, rate or extent of T cell mediated cytotoxicity.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Positive regulation of T cell mediated cytotoxicity GO:0001916
Any process that activates or increases the frequency, rate or extent of T cell mediated cytotoxicity.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
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 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA)
Protein import into nucleus GO:0006606
The directed movement of a protein from the cytoplasm to the nucleus.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Protein import into nucleus GO:0006606
The directed movement of a protein from the cytoplasm to the nucleus.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
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.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
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).
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Sensory perception of smell GO:0007608
The series of events required for an organism to receive an olfactory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Olfaction involves the detection of chemical composition of an organism's ambient medium by chemoreceptors. This is a neurological process.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Axo-dendritic transport GO:0008088
The directed movement of organelles or molecules along microtubules in neuron projections.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Response to heat GO:0009408
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 heat stimulus, a temperature stimulus above the optimal temperature for that organism.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Response to nickel cation GO:0010045
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 nickel cation stimulus.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Positive regulation of gene expression GO:0010628
Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Positive regulation of gene expression GO:0010628
Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Negative regulation of cardiac muscle cell apoptotic process GO:0010667
Any process that decreases the rate or extent of cardiac cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a cardiac muscle cell and result in its death.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Negative regulation of cardiac muscle cell apoptotic process GO:0010667
Any process that decreases the rate or extent of cardiac cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a cardiac muscle cell and result in its death.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Response to activity GO:0014823
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 activity stimulus.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Synaptic vesicle uncoating GO:0016191
The removal of the protein coat on a synaptic vesicle following the pinching step at the end of budding from the presynaptic membrane.
4 P63018 (/IC) P63018 (/IC) P63018 (/IC) P63018 (/IC)
Cerebellum development GO:0021549
The process whose specific outcome is the progression of the cerebellum over time, from its formation to the mature structure. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. In mice, the cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Forebrain development GO:0030900
The process whose specific outcome is the progression of the forebrain over time, from its formation to the mature structure. The forebrain is the anterior of the three primary divisions of the developing chordate brain or the corresponding part of the adult brain (in vertebrates, includes especially the cerebral hemispheres, the thalamus, and the hypothalamus and especially in higher vertebrates is the main control center for sensory and associative information processing, visceral functions, and voluntary motor functions).
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Regulation of protein stability GO:0031647
Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/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.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Response to progesterone GO:0032570
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 progesterone stimulus.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Cellular response to heat GO:0034605
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 heat stimulus, a temperature stimulus above the optimal temperature for that organism.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Protein refolding GO:0042026
The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Response to drug GO:0042493
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 drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Response to starvation GO:0042594
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 starvation stimulus, deprivation of nourishment.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Positive regulation of catalytic activity GO:0043085
Any process that activates or increases the activity of an enzyme.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Positive regulation of catalytic activity GO:0043085
Any process that activates or increases the activity of an enzyme.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Cellular protein complex disassembly GO:0043624
The disaggregation of a protein complex into its constituent components, occurring at the level of an individual cell. Protein complexes may have other associated non-protein prosthetic groups, such as nucleic acids, metal ions or carbohydrate groups.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Cellular protein complex disassembly GO:0043624
The disaggregation of a protein complex into its constituent components, occurring at the level of an individual cell. Protein complexes may have other associated non-protein prosthetic groups, such as nucleic acids, metal ions or carbohydrate groups.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Protein transmembrane import into intracellular organelle GO:0044743
The directed movement of proteins into an intracellular organelle, across a membrane.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Modulation by host of viral process GO:0044788
A process in which a host organism modulates the frequency, rate or extent of any of a process being mediated by a virus with which it is infected.
4 P63017 (/IMP) P63017 (/IMP) P63017 (/IMP) P63017 (/IMP)
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.
4 P63017 (/IMP) P63017 (/IMP) P63017 (/IMP) P63017 (/IMP)
Estrous cycle GO:0044849
A type of ovulation cycle, which occurs in most mammalian therian females, where the endometrium is resorbed if pregnancy does not occur.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Response to ethanol GO:0045471
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 ethanol stimulus.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Positive regulation of proteolysis GO:0045862
Any process that activates or increases the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Positive regulation of proteolysis GO:0045862
Any process that activates or increases the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
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 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
ATP metabolic process GO:0046034
The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Positive regulation of mRNA splicing, via spliceosome GO:0048026
Any process that activates or increases the rate or extent of mRNA splicing via a spliceosomal mechanism.
4 P63017 (/IMP) P63017 (/IMP) P63017 (/IMP) P63017 (/IMP)
Positive regulation of phagocytosis GO:0050766
Any process that activates or increases the frequency, rate or extent of phagocytosis.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Positive regulation of phagocytosis GO:0050766
Any process that activates or increases the frequency, rate or extent of phagocytosis.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Chaperone cofactor-dependent protein refolding GO:0051085
The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.
4 P63017 (/IGI) P63017 (/IGI) P63017 (/IGI) P63017 (/IGI)
Regulation of cell cycle GO:0051726
Any process that modulates the rate or extent of progression through the cell cycle.
4 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA)
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.
4 P63017 (/IMP) P63017 (/IMP) P63017 (/IMP) P63017 (/IMP)
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.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Regulation of protein complex stability GO:0061635
Any process that affects the structure and integrity of a protein complex by altering the likelihood of its assembly or disassembly.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Regulation of protein complex stability GO:0061635
Any process that affects the structure and integrity of a protein complex by altering the likelihood of its assembly or disassembly.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Chaperone-mediated autophagy GO:0061684
The autophagy process which begins when chaperones and co-chaperones recognize a target motif and unfold the substrate protein. The proteins are then transported to the lysosome where they are degraded.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Chaperone-mediated autophagy GO:0061684
The autophagy process which begins when chaperones and co-chaperones recognize a target motif and unfold the substrate protein. The proteins are then transported to the lysosome where they are degraded.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Protein targeting to lysosome involved in chaperone-mediated autophagy GO:0061740
The targeting of a protein to the lysosome process in which an input protein binds to a chaperone and subsequently to a lysosomal receptor.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Chaperone-mediated protein transport involved in chaperone-mediated autophagy GO:0061741
The chaperone-mediated protein transport process in which a protein that is bound to a chaperone and a lysosomal receptor is unfolded and transported into the lysosome as part of chaperone-mediated autophagy.
4 P63018 (/IGI) P63018 (/IGI) P63018 (/IGI) P63018 (/IGI)
Chaperone-mediated protein transport involved in chaperone-mediated autophagy GO:0061741
The chaperone-mediated protein transport process in which a protein that is bound to a chaperone and a lysosomal receptor is unfolded and transported into the lysosome as part of chaperone-mediated autophagy.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Cellular response to cadmium ion GO:0071276
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 cadmium (Cd) ion stimulus.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Clathrin coat disassembly GO:0072318
The disaggregation of a clathrin coat into its constituent components; results in stripping or removing the clathrin coat from clathrin-coated vesicles (CCV) before fusing with their targets. CVVs transport cargo from plasma membrane and trans-Golgi to the endosomal system.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Clathrin coat disassembly GO:0072318
The disaggregation of a clathrin coat into its constituent components; results in stripping or removing the clathrin coat from clathrin-coated vesicles (CCV) before fusing with their targets. CVVs transport cargo from plasma membrane and trans-Golgi to the endosomal system.
4 P63017 (/IGI) P63017 (/IGI) P63017 (/IGI) P63017 (/IGI)
Clathrin coat disassembly GO:0072318
The disaggregation of a clathrin coat into its constituent components; results in stripping or removing the clathrin coat from clathrin-coated vesicles (CCV) before fusing with their targets. CVVs transport cargo from plasma membrane and trans-Golgi to the endosomal system.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Positive regulation of lysosomal membrane permeability GO:0097214
Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the lysosomal membrane.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Positive regulation of lysosomal membrane permeability GO:0097214
Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the lysosomal membrane.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Maintenance of postsynaptic specialization structure GO:0098880
A process which maintains the organization and the arrangement of proteins in the presynaptic specialization.
4 P63018 (/EXP) P63018 (/EXP) P63018 (/EXP) P63018 (/EXP)
Maintenance of postsynaptic specialization structure GO:0098880
A process which maintains the organization and the arrangement of proteins in the presynaptic specialization.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Maintenance of postsynaptic specialization structure GO:0098880
A process which maintains the organization and the arrangement of proteins in the presynaptic specialization.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Maintenance of postsynaptic specialization structure GO:0098880
A process which maintains the organization and the arrangement of proteins in the presynaptic specialization.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Regulation of postsynapse organization GO:0099175
Any process that modulates the physical form of a postsynapse.
4 P63017 (/EXP) P63017 (/EXP) P63017 (/EXP) P63017 (/EXP)
Regulation of postsynapse organization GO:0099175
Any process that modulates the physical form of a postsynapse.
4 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA)
Negative regulation of supramolecular fiber organization GO:1902904
Any process that stops, prevents or reduces the frequency, rate or extent of fibril organization.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Negative regulation of hydrogen peroxide-induced cell death GO:1903206
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen peroxide-induced cell death.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Positive regulation of protein refolding GO:1904592
Any process that activates or increases the frequency, rate or extent of protein refolding.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Positive regulation of protein refolding GO:1904592
Any process that activates or increases the frequency, rate or extent of protein refolding.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Chaperone-mediated autophagy translocation complex disassembly GO:1904764
The disaggregation of a chaperone-mediated autophagy translocation complex into its constituent components.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Chaperone-mediated autophagy translocation complex disassembly GO:1904764
The disaggregation of a chaperone-mediated autophagy translocation complex into its constituent components.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Slow axonal transport GO:1990832
The directed slow movement of non-membranous molecules in nerve cell axons. It is comprised of a \slow component a\ (SCa) and a \slow component b\ (SCb) which differ in transport rates and protein composition.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Response to odorant GO:1990834
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 odorant stimulus. An odorant is any substance capable of stimulating the sense of smell.
4 P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
MRNA splicing, via spliceosome GO:0000398
The joining together of exons from one or more primary transcripts of messenger RNA (mRNA) and the excision of intron sequences, via a spliceosomal mechanism, so that mRNA consisting only of the joined exons is produced.
2 P11147 (/IC) P11147 (/IC)
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 P11147 (/ISS) P11147 (/ISS)
Neurotransmitter secretion GO:0007269
The regulated release of neurotransmitter from the presynapse into the synaptic cleft via calcium-regulated exocytosis during synaptic transmission.
2 P11147 (/IGI) P11147 (/IGI)
Neurotransmitter secretion GO:0007269
The regulated release of neurotransmitter from the presynapse into the synaptic cleft via calcium-regulated exocytosis during synaptic transmission.
2 P11147 (/IMP) P11147 (/IMP)
Neurotransmitter secretion GO:0007269
The regulated release of neurotransmitter from the presynapse into the synaptic cleft via calcium-regulated exocytosis during synaptic transmission.
2 P11147 (/IPI) P11147 (/IPI)
Nervous system development GO:0007399
The process whose specific outcome is the progression of nervous tissue over time, from its formation to its mature state.
2 P11147 (/IMP) P11147 (/IMP)
Axon guidance GO:0007411
The chemotaxis process that directs the migration of an axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
2 P11147 (/IMP) P11147 (/IMP)
Axonal fasciculation GO:0007413
The collection of axons into a bundle of rods, known as a fascicle.
2 P11147 (/IMP) P11147 (/IMP)
Vesicle-mediated transport GO:0016192
A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane.
2 P11147 (/IMP) P11147 (/IMP)
RNA interference GO:0016246
The process in which double-stranded RNAs silence cognate genes. Involves posttranscriptional gene inactivation ('silencing') both of transgenes or dsRNA introduced into a germline, and of the host gene(s) homologous to the transgenes or dsRNA. This silencing is triggered by the introduction of transgenes or double-stranded RNA (dsRNA), and can occur through a specific decrease in the level of mRNA, or by negative regulation of translation, of both host genes and transgenes.
2 P11147 (/IMP) P11147 (/IMP)
Ovarian follicle cell development GO:0030707
The process that occurs during oogenesis involving the ovarian follicle cells, somatic cells which surround the germ cells of an ovary. An example of this is found in Drosophila melanogaster.
2 P11147 (/IMP) P11147 (/IMP)
Cellular response to topologically incorrect protein GO:0035967
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 protein that is not folded in its correct three-dimensional structure.
2 P11147 (/IMP) P11147 (/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.
2 P11147 (/IDA) P11147 (/IDA)
Heterochromatin organization involved in chromatin silencing GO:0070868
Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic heterochromatin and contributes to chromatin silencing.
2 P11147 (/IMP) P11147 (/IMP)
Positive regulation of small RNA loading onto RISC GO:0106161
Any process that activates or increases the frequency, rate or extent of small RNA loading onto RISC.
2 P11147 (/IGI) P11147 (/IGI)
Gastrulation GO:0007369
A complex and coordinated series of cellular movements that occurs at the end of cleavage during embryonic development of most animals. The details of gastrulation vary from species to species, but usually result in the formation of the three primary germ layers, ectoderm, mesoderm and endoderm.
1 O73885 (/IEP)
Response to heat GO:0009408
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 heat stimulus, a temperature stimulus above the optimal temperature for that organism.
1 G1SBT8 (/ISS)
Response to cold GO:0009409
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 cold stimulus, a temperature stimulus below the optimal temperature for that organism.
1 G1SBT8 (/ISS)
Embryo development ending in birth or egg hatching GO:0009792
The process whose specific outcome is the progression of an embryo over time, from zygote formation until the end of the embryonic life stage. The end of the embryonic life stage is organism-specific and may be somewhat arbitrary; for mammals it is usually considered to be birth, for insects the hatching of the first instar larva from the eggshell.
1 O73885 (/IEP)
Fin regeneration GO:0031101
The regrowth of fin tissue following its loss or destruction.
1 Q90473 (/IEP)
Regulation of fibroblast growth factor receptor signaling pathway GO:0040036
Any process that modulates the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
1 Q90473 (/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 Q90473 (/IMP)
Embryonic organ development GO:0048568
Development, taking place during the embryonic phase, of a tissue or tissues that work together to perform a specific function or functions. Development pertains to the process whose specific outcome is the progression of a structure over time, from its formation to the mature structure. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions.
1 O73885 (/IEP)
Protein localization to early endosome GO:1902946
A process in which a protein is transported to, or maintained in, a location within an early endosome.
1 Q90473 (/IMP)

There are 112 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
Ribonucleoprotein complex GO:1990904
A macromolecular complex containing both protein and RNA molecules.
50 A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS)
(40 more)
Prp19 complex GO:0000974
A protein complex consisting of Prp19 and associated proteins that is involved in the transition from the precatalytic spliceosome to the activated form that catalyzes step 1 of splicing, and which remains associated with the spliceosome through the second catalytic step. It is widely conserved, found in both yeast and mammals, though the exact composition varies. In S. cerevisiae, it contains Prp19p, Ntc20p, Snt309p, Isy1p, Syf2p, Cwc2p, Prp46p, Clf1p, Cef1p, and Syf1p.
49 A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS)
(39 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.
49 A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS) A2Q0Z1 (/ISS)
(39 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.
46 P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(36 more)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
42 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(32 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.
42 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(32 more)
Lysosomal membrane GO:0005765
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
38 P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS) P11142 (/ISS)
(28 more)
Prp19 complex GO:0000974
A protein complex consisting of Prp19 and associated proteins that is involved in the transition from the precatalytic spliceosome to the activated form that catalyzes step 1 of splicing, and which remains associated with the spliceosome through the second catalytic step. It is widely conserved, found in both yeast and mammals, though the exact composition varies. In S. cerevisiae, it contains Prp19p, Ntc20p, Snt309p, Isy1p, Syf2p, Cwc2p, Prp46p, Clf1p, Cef1p, and Syf1p.
34 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(24 more)
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.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
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.
34 P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA)
(24 more)
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
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.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 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.
34 P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA)
(24 more)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
34 P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA)
(24 more)
Secretory granule lumen GO:0034774
The volume enclosed by the membrane of a secretory granule.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Lysosomal lumen GO:0043202
The volume enclosed within the lysosomal membrane.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane GO:0061202
The lipid bilayer surrounding a clathrin-sculpted gamma-aminobutyric acid transport vesicle.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 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.
34 P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA)
(24 more)
Blood microparticle GO:0072562
A phospholipid microvesicle that is derived from any of several cell types, such as platelets, blood cells, endothelial cells, or others, and contains membrane receptors as well as other proteins characteristic of the parental cell. Microparticles are heterogeneous in size, and are characterized as microvesicles free of nucleic acids.
34 P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA)
(24 more)
Lumenal side of lysosomal membrane GO:0098575
The side (leaflet) of the lysosomal membrane that faces the lumen.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Chaperone complex GO:0101031
A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins.
34 P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI) P11142 (/IPI)
(24 more)
Ficolin-1-rich granule lumen GO:1904813
Any membrane-enclosed lumen that is part of a ficolin-1-rich granule.
34 P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS) P11142 (/TAS)
(24 more)
Ribonucleoprotein complex GO:1990904
A macromolecular complex containing both protein and RNA molecules.
34 P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA)
(24 more)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
16 P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) P11147 (/IDA) P11147 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63018 (/IDA)
(6 more)
Cell GO:0005623
The basic structural and functional unit of all organisms. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope.
11 A0PA16 (/IDA) A0PA16 (/IDA) A0PA16 (/IDA) A0PA16 (/IDA) A0PA16 (/IDA) P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA)
(1 more)
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
8 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Glycinergic synapse GO:0098690
A synapse that uses glycine as a neurotransmitter.
8 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Presynapse GO:0098793
The part of a synapse that is part of the presynaptic cell.
8 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
8 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
6 P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA)
Prp19 complex GO:0000974
A protein complex consisting of Prp19 and associated proteins that is involved in the transition from the precatalytic spliceosome to the activated form that catalyzes step 1 of splicing, and which remains associated with the spliceosome through the second catalytic step. It is widely conserved, found in both yeast and mammals, though the exact composition varies. In S. cerevisiae, it contains Prp19p, Ntc20p, Snt309p, Isy1p, Syf2p, Cwc2p, Prp46p, Clf1p, Cef1p, and Syf1p.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Photoreceptor inner segment GO:0001917
The inner segment of a vertebrate photoreceptor containing mitochondria, ribosomes and membranes where opsin molecules are assembled and passed to be part of the outer segment discs.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Photoreceptor inner segment GO:0001917
The inner segment of a vertebrate photoreceptor containing mitochondria, ribosomes and membranes where opsin molecules are assembled and passed to be part of the outer segment discs.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
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.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Lysosome GO:0005764
A small lytic vacuole that has cell cycle-independent morphology and is found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Lysosome GO:0005764
A small lytic vacuole that has cell cycle-independent morphology and is found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Lysosomal membrane GO:0005765
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Lysosomal membrane GO:0005765
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Late endosome GO:0005770
A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center.
4 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA)
Autophagosome GO:0005776
A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the lytic vacuole/lysosome for degradation as part of macroautophagy.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Autophagosome GO:0005776
A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the lytic vacuole/lysosome for degradation as part of macroautophagy.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Microtubule GO:0005874
Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Microtubule GO:0005874
Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Intermediate filament GO:0005882
A cytoskeletal structure that forms a distinct elongated structure, characteristically 10 nm in diameter, that occurs in the cytoplasm of eukaryotic cells. Intermediate filaments form a fibrous system, composed of chemically heterogeneous subunits and involved in mechanically integrating the various components of the cytoplasmic space. Intermediate filaments may be divided into five chemically distinct classes: Type I, acidic keratins; Type II, basic keratins; Type III, including desmin, vimentin and others; Type IV, neurofilaments and related filaments; and Type V, lamins.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Intermediate filament GO:0005882
A cytoskeletal structure that forms a distinct elongated structure, characteristically 10 nm in diameter, that occurs in the cytoplasm of eukaryotic cells. Intermediate filaments form a fibrous system, composed of chemically heterogeneous subunits and involved in mechanically integrating the various components of the cytoplasmic space. Intermediate filaments may be divided into five chemically distinct classes: Type I, acidic keratins; Type II, basic keratins; Type III, including desmin, vimentin and others; Type IV, neurofilaments and related filaments; and Type V, lamins.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Synaptic vesicle GO:0008021
A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Synaptic vesicle GO:0008021
A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/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.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/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.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
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.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/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.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
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.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
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.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Asymmetric synapse GO:0032279
A type of synapse occurring between an axon and a dendritic spine or dendritic shaft. Asymmetric synapses, the most abundant synapse type in the central nervous system, involve axons that contain predominantly spherical vesicles and contain a thickened postsynaptic density. Most or all synapses of this type are excitatory.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Asymmetric synapse GO:0032279
A type of synapse occurring between an axon and a dendritic spine or dendritic shaft. Asymmetric synapses, the most abundant synapse type in the central nervous system, involve axons that contain predominantly spherical vesicles and contain a thickened postsynaptic density. Most or all synapses of this type are excitatory.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/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 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Terminal bouton GO:0043195
Terminal inflated portion of the axon, containing the specialized apparatus necessary to release neurotransmitters. The axon terminus is considered to be the whole region of thickening and the terminal bouton is a specialized region of it.
4 P63018 (/HDA) P63018 (/HDA) P63018 (/HDA) P63018 (/HDA)
Terminal bouton GO:0043195
Terminal inflated portion of the axon, containing the specialized apparatus necessary to release neurotransmitters. The axon terminus is considered to be the whole region of thickening and the terminal bouton is a specialized region of it.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Terminal bouton GO:0043195
Terminal inflated portion of the axon, containing the specialized apparatus necessary to release neurotransmitters. The axon terminus is considered to be the whole region of thickening and the terminal bouton is a specialized region of it.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/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.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/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.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Dendritic shaft GO:0043198
Cylindric portion of the dendrite, directly stemming from the perikaryon, and carrying the dendritic spines.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Dendritic shaft GO:0043198
Cylindric portion of the dendrite, directly stemming from the perikaryon, and carrying the dendritic spines.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/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.
4 P63017 (/HDA) P63017 (/HDA) P63017 (/HDA) P63017 (/HDA)
Neuron spine GO:0044309
A small membranous protrusion, often ending in a bulbous head and attached to the neuron by a narrow stalk or neck.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Neuron spine GO:0044309
A small membranous protrusion, often ending in a bulbous head and attached to the neuron by a narrow stalk or neck.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
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 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Photoreceptor ribbon synapse GO:0098684
A ribbon synapse between a retinal photoreceptor cell (rod or cone) and a retinal bipolar cell. These contain a plate-like synaptic ribbon.
4 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA)
Glycinergic synapse GO:0098690
A synapse that uses glycine as a neurotransmitter.
4 P63018 (/EXP) P63018 (/EXP) P63018 (/EXP) P63018 (/EXP)
Glycinergic synapse GO:0098690
A synapse that uses glycine as a neurotransmitter.
4 P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Glycinergic synapse GO:0098690
A synapse that uses glycine as a neurotransmitter.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Presynapse GO:0098793
The part of a synapse that is part of the presynaptic cell.
4 P63017 (/IMP) P63017 (/IMP) P63017 (/IMP) P63017 (/IMP)
Presynapse GO:0098793
The part of a synapse that is part of the presynaptic cell.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
4 P63017 (/EXP) P63017 (/EXP) P63017 (/EXP) P63017 (/EXP)
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Presynaptic cytosol GO:0099523
The region of the cytosol consisting of all cytosol that is part of the presynapse.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Presynaptic cytosol GO:0099523
The region of the cytosol consisting of all cytosol that is part of the presynapse.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Postsynaptic cytosol GO:0099524
The region of the cytosol consisting of all cytosol that is part of the postsynapse.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Postsynaptic cytosol GO:0099524
The region of the cytosol consisting of all cytosol that is part of the postsynapse.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Postsynaptic specialization membrane GO:0099634
The membrane component of the postsynaptic specialization. This is the region of the postsynaptic membrane in which the population of neurotransmitter receptors involved in synaptic transmission are concentrated.
4 P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA)
Chaperone complex GO:0101031
A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Messenger ribonucleoprotein complex GO:1990124
A ribonucleoprotein complex containing both protein and messenger RNA (mRNA) molecules.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Messenger ribonucleoprotein complex GO:1990124
A ribonucleoprotein complex containing both protein and messenger RNA (mRNA) molecules.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Lysosomal matrix GO:1990836
A matrix composed of supramolecular assemblies of lysosomal enzymes and lipids which forms at a pH of 5.0 within the lysosome.
4 P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Lysosomal matrix GO:1990836
A matrix composed of supramolecular assemblies of lysosomal enzymes and lipids which forms at a pH of 5.0 within the lysosome.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Ribonucleoprotein complex GO:1990904
A macromolecular complex containing both protein and RNA molecules.
4 P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Cell GO:0005623
The basic structural and functional unit of all organisms. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope.
3 B5DFX7 (/ISS) B5DFX7 (/ISS) B5DFX7 (/ISS)
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 P11147 (/HDA) P11147 (/HDA)
Perichromatin fibrils GO:0005726
Structures of variable diameter visible in the nucleoplasm by electron microscopy, mainly observed near the border of condensed chromatin. The fibrils are enriched in RNA, and are believed to be sites of pre-mRNA splicing and polyadenylylation representing the in situ form of nascent transcripts.
2 P11147 (/IDA) P11147 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
2 P11147 (/HDA) P11147 (/HDA)
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 P11147 (/ISS) P11147 (/ISS)
Precatalytic spliceosome GO:0071011
A spliceosomal complex that is formed by the recruitment of a preassembled U5-containing tri-snRNP to the prespliceosome. Although all 5 snRNPs are present, the precatalytic spliceosome is catalytically inactive. The precatalytic spliceosome includes many proteins in addition to those found in the associated snRNPs.
2 P11147 (/HDA) P11147 (/HDA)
Catalytic step 2 spliceosome GO:0071013
A spliceosomal complex that contains three snRNPs, including U5, bound to a splicing intermediate in which the first catalytic cleavage of the 5' splice site has occurred. The precise subunit composition differs significantly from that of the catalytic step 1, or activated, spliceosome, and includes many proteins in addition to those found in the associated snRNPs.
2 P11147 (/HDA) P11147 (/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.
1 O73885 (/IMP)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 O73885 (/IMP)
CATH-Gene3D is a Global Biodata Core Resource Learn more...