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 named:

"
TCP-1-like chaperonin intermediate domain
".

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.
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FunFam 1: 60 kDa chaperonin

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 55 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).
413 A0A0H3LCC3 (/IPI) A0A0H3LCC3 (/IPI) A0A0H3LCC3 (/IPI) A0A0H3LCC3 (/IPI) A0A0H3LCC3 (/IPI) A0A0H3LCC3 (/IPI) A0A0H3LCC3 (/IPI) A0A0H3LCC3 (/IPI) A0A0H3LCC3 (/IPI) A0A0H3LCC3 (/IPI)
(403 more)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
186 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(176 more)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
186 P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP)
(176 more)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
181 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(171 more)
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
178 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(168 more)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
178 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(168 more)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
178 P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI)
(168 more)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
178 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(168 more)
Single-stranded DNA binding GO:0003697
Interacting selectively and non-covalently with single-stranded DNA.
20 P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA)
(10 more)
Host cell surface binding GO:0046812
Interacting selectively and non-covalently with the surface of a host cell.
20 A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA)
(10 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.
16 Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS)
(6 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.
10 P10809 (/IPI) P10809 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI)
DNA replication origin binding GO:0003688
Interacting selectively and non-covalently with the DNA replication origin, a unique DNA sequence of a replicon at which DNA replication is initiated and proceeds bidirectionally or unidirectionally.
8 P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA)
Mannan binding GO:2001065
Interacting selectively and non-covalently with mannan.
6 P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA)
Lipopolysaccharide binding GO:0001530
Interacting selectively and non-covalently with lipopolysaccharide.
5 P10809 (/IDA) P10809 (/IDA) P63038 (/IDA) P63038 (/IDA) P63038 (/IDA)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
4 O02649 (/ISS) O02649 (/ISS) P10809 (/ISS) P10809 (/ISS)
Lipopolysaccharide binding GO:0001530
Interacting selectively and non-covalently with lipopolysaccharide.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
3 P63039 (/IPI) P63039 (/IPI) P63039 (/IPI)
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
P53 binding GO:0002039
Interacting selectively and non-covalently with one of the p53 family of proteins.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
3 P29197 (/IPI) P29197 (/IPI) Q8L7B5 (/IPI)
Double-stranded RNA binding GO:0003725
Interacting selectively and non-covalently with double-stranded RNA.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Copper ion binding GO:0005507
Interacting selectively and non-covalently with copper (Cu) ions.
3 P29197 (/IDA) P29197 (/IDA) Q8L7B5 (/IDA)
High-density lipoprotein particle binding GO:0008035
Interacting selectively and non-covalently with high-density lipoprotein particle, a lipoprotein particle with a high density (typically 1.063-1.21 g/ml) and a diameter of 5-10 nm that contains APOAs and may contain APOCs and APOE.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Apolipoprotein binding GO:0034185
Interacting selectively and non-covalently with an apolipoprotein, the protein component of a lipoprotein complex.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Apolipoprotein A-I binding GO:0034186
Interacting selectively and non-covalently with apolipoprotein A-I.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Insulin binding GO:0043559
Interacting selectively and non-covalently with insulin, a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
3 P63039 (/IPI) P63039 (/IPI) P63039 (/IPI)
Insulin binding GO:0043559
Interacting selectively and non-covalently with insulin, a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
3 P63039 (/IPI) P63039 (/IPI) P63039 (/IPI)
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
3 P63039 (/IPI) P63039 (/IPI) P63039 (/IPI)
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Modification-dependent protein binding GO:0140030
Interacting selectively and non-covalently with a protein upon post-translation modification of the target protein.
3 P63039 (/IPI) P63039 (/IPI) P63039 (/IPI)
Modification-dependent protein binding GO:0140030
Interacting selectively and non-covalently with a protein upon post-translation modification of the target protein.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
P53 binding GO:0002039
Interacting selectively and non-covalently with one of the p53 family of proteins.
2 P10809 (/IPI) P10809 (/IPI)
DNA replication origin binding GO:0003688
Interacting selectively and non-covalently with the DNA replication origin, a unique DNA sequence of a replicon at which DNA replication is initiated and proceeds bidirectionally or unidirectionally.
2 P10809 (/ISS) P10809 (/ISS)
Single-stranded DNA binding GO:0003697
Interacting selectively and non-covalently with single-stranded DNA.
2 P10809 (/ISS) P10809 (/ISS)
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
2 P10809 (/HDA) P10809 (/HDA)
Double-stranded RNA binding GO:0003725
Interacting selectively and non-covalently with double-stranded RNA.
2 P10809 (/IDA) P10809 (/IDA)
Structural constituent of ribosome GO:0003735
The action of a molecule that contributes to the structural integrity of the ribosome.
2 P29197 (/IDA) P29197 (/IDA)
High-density lipoprotein particle binding GO:0008035
Interacting selectively and non-covalently with high-density lipoprotein particle, a lipoprotein particle with a high density (typically 1.063-1.21 g/ml) and a diameter of 5-10 nm that contains APOAs and may contain APOCs and APOE.
2 P10809 (/IDA) P10809 (/IDA)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
2 P10809 (/ISS) P10809 (/ISS)
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
2 P10809 (/IPI) P10809 (/IPI)
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
2 P10809 (/IPI) P10809 (/IPI)
Apolipoprotein binding GO:0034185
Interacting selectively and non-covalently with an apolipoprotein, the protein component of a lipoprotein complex.
2 P10809 (/IPI) P10809 (/IPI)
Apolipoprotein A-I binding GO:0034186
Interacting selectively and non-covalently with apolipoprotein A-I.
2 P10809 (/IPI) P10809 (/IPI)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
2 P10809 (/IC) P10809 (/IC)
ATPase binding GO:0051117
Interacting selectively and non-covalently with an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
2 P29185 (/IPI) P29185 (/IPI)
Integrin binding GO:0005178
Interacting selectively and non-covalently with an integrin.
1 P50142 (/IPI)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 Q09864 (/ISS)
Transcription factor binding GO:0008134
Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.
1 P50140 (/IPI)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
1 Q37683 (/ISA)

There are 141 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 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.
207 P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP)
(197 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.
178 P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP)
(168 more)
Response to radiation GO:0009314
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an electromagnetic radiation stimulus. Electromagnetic radiation is a propagating wave in space with electric and magnetic components. These components oscillate at right angles to each other and to the direction of propagation.
178 P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP)
(168 more)
Virion assembly GO:0019068
A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed.
178 P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP)
(168 more)
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.
178 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(168 more)
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.
91 A0A024R3X4 (/ISS) A0A024R3X4 (/ISS) A0A061IE32 (/ISS) A0A087RCJ8 (/ISS) A0A087VBS4 (/ISS) A0A088Q2J5 (/ISS) A0A088Q2J5 (/ISS) A0A088Q2J5 (/ISS) A0A091ET45 (/ISS) A0A091GL87 (/ISS)
(81 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 P10809 (/IDA) P10809 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA)
(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.
30 Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS)
(20 more)
Adhesion of symbiont to host GO:0044406
The attachment of a symbiont to its host via adhesion molecules, general stickiness etc., either directly or indirectly. The host is defined as the larger of the organisms involved in a symbiotic interaction.
24 A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA)
(14 more)
Positive regulation of transcription regulatory region DNA binding GO:2000679
Any process that activates or increases the frequency, rate or extent of transcription regulatory region DNA binding.
24 P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA)
(14 more)
Protein targeting to mitochondrion GO:0006626
The process of directing proteins towards and into the mitochondrion, usually mediated by mitochondrial proteins that recognize signals contained within the imported protein.
19 O02649 (/ISS) O02649 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS)
(9 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.
16 Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS) Q8IJN9 (/ISS)
(6 more)
Response to hypoxia GO:0001666
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
15 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP) P9WPE7 (/IEP) P9WPE7 (/IEP) P9WPE7 (/IEP) P9WPE7 (/IEP) P9WPE7 (/IEP) P9WPE7 (/IEP) P9WPE7 (/IEP)
(5 more)
DNA protection GO:0042262
Any process in which DNA is protected from damage by, for example, oxidative stress.
12 P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA)
(2 more)
Nucleoid organization GO:0090143
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleoid. The nucleoid is the region of a bacterial cell, virion, mitochondrion or chloroplast to which the DNA is confined.
12 P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA)
(2 more)
Positive regulation of interleukin-8 secretion GO:2000484
Any process that activates or increases the frequency, rate or extent of interleukin-8 secretion.
12 O68324 (/IGI) O68324 (/IGI) O68324 (/IGI) O68324 (/IGI) O68324 (/IGI) O68324 (/IGI) Q9AEP7 (/IGI) Q9AEP7 (/IGI) Q9KJ23 (/IGI) Q9KJ23 (/IGI)
(2 more)
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
10 P10809 (/IMP) P10809 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
'de novo' protein folding GO:0006458
The process of assisting in the folding of a nascent peptide chain into its correct tertiary structure.
8 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
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 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
Protein import into mitochondrial intermembrane space GO:0045041
The import of proteins into the space between the inner and outer mitochondrial membranes.
8 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
Chaperone-mediated protein complex assembly GO:0051131
The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
8 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
Protein maturation GO:0051604
Any process leading to the attainment of the full functional capacity of a protein.
8 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
'de novo' protein folding GO:0006458
The process of assisting in the folding of a nascent peptide chain into its correct tertiary structure.
5 O02649 (/ISS) O02649 (/ISS) P10809 (/ISS) P10809 (/ISS) Q9VMN5 (/ISS)
Positive regulation of interferon-alpha production GO:0032727
Any process that activates or increases the frequency, rate, or extent of interferon-alpha production.
5 P10809 (/IDA) P10809 (/IDA) P63038 (/IDA) P63038 (/IDA) P63038 (/IDA)
Positive regulation of interferon-gamma production GO:0032729
Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
5 P10809 (/IDA) P10809 (/IDA) P63038 (/IDA) P63038 (/IDA) P63038 (/IDA)
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.
5 O02649 (/IEP) O02649 (/IEP) P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
T cell activation GO:0042110
The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
5 P10809 (/IDA) P10809 (/IDA) P63038 (/IDA) P63038 (/IDA) P63038 (/IDA)
Negative regulation of apoptotic process GO:0043066
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
5 P10809 (/IMP) P10809 (/IMP) P63039 (/IMP) P63039 (/IMP) P63039 (/IMP)
Adhesion of symbiont to host cell GO:0044650
The attachment of a symbiont to a host cell via adhesion molecules, general stickiness etc., either directly or indirectly.
5 P50142 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q9KKF0 (/IDA)
Positive regulation of T cell activation GO:0050870
Any process that activates or increases the frequency, rate or extent of T cell activation.
5 P10809 (/IDA) P10809 (/IDA) P63038 (/IDA) P63038 (/IDA) P63038 (/IDA)
Regulation of entry of bacterium into host cell GO:2000535
Any process that modulates the frequency, rate or extent of entry of bacterium into host cell.
5 P31681 (/IDA) P31681 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA)
Protein folding GO:0006457
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
4 P21238 (/TAS) P21238 (/TAS) P29185 (/TAS) P29185 (/TAS)
Aggregation of unicellular organisms GO:0098630
The clustering together of unicellular organisms in suspension form aggregates.
4 Q9KJ23 (/IDA) Q9KJ23 (/IDA) Q9KJ23 (/IDA) Q9KJ23 (/IDA)
B cell cytokine production GO:0002368
Any process that contributes to cytokine production by a B cell.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
MyD88-dependent toll-like receptor signaling pathway GO:0002755
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the MyD88 adaptor molecule mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Positive regulation of T cell mediated immune response to tumor cell GO:0002842
Any process that activates or increases the frequency, rate, or extent of a T cell mediated immune response to tumor cell.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Response to ischemia GO:0002931
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a inadequate blood supply.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
'de novo' protein folding GO:0006458
The process of assisting in the folding of a nascent peptide chain into its correct tertiary structure.
3 P63039 (/IC) P63039 (/IC) P63039 (/IC)
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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Mitochondrion organization GO:0007005
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
3 O02649 (/IMP) O02649 (/IMP) P50140 (/IMP)
Apoptotic mitochondrial changes GO:0008637
The morphological and physiological alterations undergone by mitochondria during apoptosis.
3 P63039 (/IMP) P63039 (/IMP) P63039 (/IMP)
Apoptotic mitochondrial changes GO:0008637
The morphological and physiological alterations undergone by mitochondria during apoptosis.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Pathogenesis GO:0009405
The set of specific processes that generate the ability of an organism to induce an abnormal, generally detrimental state in another organism.
3 O66198 (/IMP) O66198 (/IMP) O66198 (/IMP)
Response to organic substance GO:0010033
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 organic substance stimulus.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
Response to organic cyclic compound GO:0014070
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 organic cyclic compound stimulus.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
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.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
Response to lipopolysaccharide GO:0032496
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
Positive regulation of interferon-alpha production GO:0032727
Any process that activates or increases the frequency, rate, or extent of interferon-alpha production.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Positive regulation of interferon-gamma production GO:0032729
Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
3 P63038 (/IGI) P63038 (/IGI) P63038 (/IGI)
Positive regulation of interferon-gamma production GO:0032729
Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Positive regulation of interleukin-10 production GO:0032733
Any process that activates or increases the frequency, rate, or extent of interleukin-10 production.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Positive regulation of interleukin-12 production GO:0032735
Any process that activates or increases the frequency, rate, or extent of interleukin-12 production.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Positive regulation of interleukin-6 production GO:0032755
Any process that activates or increases the frequency, rate, or extent of interleukin-6 production.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Response to ATP GO:0033198
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 ATP (adenosine 5'-triphosphate) stimulus.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
B cell proliferation GO:0042100
The expansion of a B cell population by cell division. Follows B cell activation.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
T cell activation GO:0042110
The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
3 P63038 (/IGI) P63038 (/IGI) P63038 (/IGI)
T cell activation GO:0042110
The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
B cell activation GO:0042113
The change in morphology and behavior of a mature or immature B cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Response to cocaine GO:0042220
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cocaine stimulus. Cocaine is a crystalline alkaloid obtained from the leaves of the coca plant.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
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.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
Response to hydrogen peroxide GO:0042542
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
Positive regulation of macrophage activation GO:0043032
Any process that stimulates, induces or increases the rate of macrophage activation.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Negative regulation of neuron apoptotic process GO:0043524
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process in neurons.
3 P63039 (/IMP) P63039 (/IMP) P63039 (/IMP)
Negative regulation of neuron apoptotic process GO:0043524
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process in neurons.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Response to estrogen GO:0043627
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 an estrogen, C18 steroid hormones that can stimulate the development of female sexual characteristics.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
Symbiont process GO:0044403
A process carried out by symbiont gene products that enables the interaction between two organisms living together in more or less intimate association. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
3 O66198 (/IMP) O66198 (/IMP) O66198 (/IMP)
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.
3 P29197 (/IEP) P29197 (/IEP) Q93ZM7 (/IEP)
Isotype switching to IgG isotypes GO:0048291
The switching of activated B cells from IgM biosynthesis to biosynthesis of an IgG isotype, accomplished through a recombination process involving an intrachromosomal deletion between switch regions that reside 5' of the IgM and one of the IgG constant region gene segments in the immunoglobulin heavy chain locus.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Positive regulation of inflammatory response GO:0050729
Any process that activates or increases the frequency, rate or extent of the inflammatory response.
3 P63039 (/IDA) P63039 (/IDA) P63039 (/IDA)
Positive regulation of inflammatory response GO:0050729
Any process that activates or increases the frequency, rate or extent of the inflammatory response.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Positive regulation of T cell activation GO:0050870
Any process that activates or increases the frequency, rate or extent of T cell activation.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Response to glucocorticoid GO:0051384
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 glucocorticoid stimulus. Glucocorticoids are hormonal C21 corticosteroids synthesized from cholesterol with the ability to bind with the cortisol receptor and trigger similar effects. Glucocorticoids act primarily on carbohydrate and protein metabolism, and have anti-inflammatory effects.
3 P63039 (/IEP) P63039 (/IEP) P63039 (/IEP)
Interaction with symbiont GO:0051702
An interaction between two organisms living together in more or less intimate association. The term symbiont is used for the smaller (macro) of the two members of a symbiosis; the various forms of symbiosis include parasitism, commensalism and mutualism.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Modification of morphology or physiology of other organism via secreted substance involved in symbiotic interaction GO:0052212
The process in which an organism effects a change in the structure or function of a second organism, mediated by a substance secreted by one of the organisms, where the two organisms are in a symbiotic interaction.
3 O66198 (/IMP) O66198 (/IMP) O66198 (/IMP)
Cellular response to temperature stimulus GO:0071502
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 temperature stimulus.
3 Q4X1P0 (/IEP) Q4X1P0 (/IEP) Q4X1P0 (/IEP)
Negative regulation of apoptotic process in bone marrow cell GO:0071866
Any process that stops, prevents, or reduces the frequency, rate or extent of the occurrence or rate of cell death by apoptotic process in the bone marrow.
3 P63039 (/IMP) P63039 (/IMP) P63039 (/IMP)
Negative regulation of apoptotic process in bone marrow cell GO:0071866
Any process that stops, prevents, or reduces the frequency, rate or extent of the occurrence or rate of cell death by apoptotic process in the bone marrow.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Cellular response to interleukin-7 GO:0098761
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-7 stimulus.
3 P63038 (/IDA) P63038 (/IDA) P63038 (/IDA)
Negative regulation of reactive oxygen species biosynthetic process GO:1903427
Any process that stops, prevents or reduces the frequency, rate or extent of reactive oxygen species biosynthetic process.
3 P63039 (/IMP) P63039 (/IMP) P63039 (/IMP)
Negative regulation of reactive oxygen species biosynthetic process GO:1903427
Any process that stops, prevents or reduces the frequency, rate or extent of reactive oxygen species biosynthetic process.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Positive regulation of tumor necrosis factor secretion GO:1904469
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
3 P63039 (/IMP) P63039 (/IMP) P63039 (/IMP)
Positive regulation of tumor necrosis factor secretion GO:1904469
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Positive regulation of interleukin-6 secretion GO:2000778
Any process that activates or increases the frequency, rate or extent of interleukin-6 secretion.
3 P63039 (/IMP) P63039 (/IMP) P63039 (/IMP)
Positive regulation of interleukin-6 secretion GO:2000778
Any process that activates or increases the frequency, rate or extent of interleukin-6 secretion.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Group II intron splicing GO:0000373
The splicing of Group II introns. This occurs by a ribozymic mechanism where the intron sequence forms a distinct 3D structure, characteristic of Group II introns and containing splice site consensus sequences, that is involved in catalyzing the splicing reactions, though protein factors are also required in vivo. Splicing occurs by a series of two transesterification reactions (mechanistically similar to those for splicing of nuclear mRNAs) initiated by a bulged adenosine residue within the intron sequence as the initiating nucleophile. The intron is excised as a lariat.
2 P29197 (/IPI) P29197 (/IPI)
B cell cytokine production GO:0002368
Any process that contributes to cytokine production by a B cell.
2 P10809 (/IDA) P10809 (/IDA)
MyD88-dependent toll-like receptor signaling pathway GO:0002755
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the MyD88 adaptor molecule mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
2 P10809 (/IDA) P10809 (/IDA)
Positive regulation of T cell mediated immune response to tumor cell GO:0002842
Any process that activates or increases the frequency, rate, or extent of a T cell mediated immune response to tumor cell.
2 P10809 (/IDA) P10809 (/IDA)
Regulation of transcription by RNA polymerase II GO:0006357
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
2 P10809 (/TAS) P10809 (/TAS)
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 P10809 (/IDA) P10809 (/IDA)
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.
2 P10809 (/IDA) P10809 (/IDA)
Mitochondrion organization GO:0007005
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
2 P29197 (/TAS) P29197 (/TAS)
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.
2 P50142 (/IMP) Q9KKF0 (/IMP)
Chloroplast organization GO:0009658
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the chloroplast.
2 P21238 (/IMP) P21238 (/IMP)
Embryo development ending in seed dormancy GO:0009793
The process whose specific outcome is the progression of the embryo over time, from zygote formation to the end of seed dormancy. An example of this process is found in Arabidopsis thaliana.
2 P21238 (/IMP) P21238 (/IMP)
Positive regulation of interferon-gamma production GO:0032729
Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
2 P10809 (/ISS) P10809 (/ISS)
Positive regulation of interleukin-10 production GO:0032733
Any process that activates or increases the frequency, rate, or extent of interleukin-10 production.
2 P10809 (/IDA) P10809 (/IDA)
Positive regulation of interleukin-12 production GO:0032735
Any process that activates or increases the frequency, rate, or extent of interleukin-12 production.
2 P10809 (/IDA) P10809 (/IDA)
Positive regulation of interleukin-6 production GO:0032755
Any process that activates or increases the frequency, rate, or extent of interleukin-6 production.
2 P10809 (/IDA) P10809 (/IDA)
B cell proliferation GO:0042100
The expansion of a B cell population by cell division. Follows B cell activation.
2 P10809 (/IDA) P10809 (/IDA)
B cell activation GO:0042113
The change in morphology and behavior of a mature or immature B cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
2 P10809 (/IDA) P10809 (/IDA)
Positive regulation of macrophage activation GO:0043032
Any process that stimulates, induces or increases the rate of macrophage activation.
2 P10809 (/IDA) P10809 (/IDA)
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
2 P10809 (/IMP) P10809 (/IMP)
Isotype switching to IgG isotypes GO:0048291
The switching of activated B cells from IgM biosynthesis to biosynthesis of an IgG isotype, accomplished through a recombination process involving an intrachromosomal deletion between switch regions that reside 5' of the IgM and one of the IgG constant region gene segments in the immunoglobulin heavy chain locus.
2 P10809 (/IDA) P10809 (/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 P10809 (/ISS) P10809 (/ISS)
Positive regulation of T cell activation GO:0050870
Any process that activates or increases the frequency, rate or extent of T cell activation.
2 P10809 (/ISS) P10809 (/ISS)
Chaperone-mediated protein complex assembly GO:0051131
The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
2 P10809 (/ISS) P10809 (/ISS)
Protein maturation GO:0051604
Any process leading to the attainment of the full functional capacity of a protein.
2 P10809 (/ISS) P10809 (/ISS)
Interaction with symbiont GO:0051702
An interaction between two organisms living together in more or less intimate association. The term symbiont is used for the smaller (macro) of the two members of a symbiosis; the various forms of symbiosis include parasitism, commensalism and mutualism.
2 P10809 (/IMP) P10809 (/IMP)
Positive regulation of NIK/NF-kappaB signaling GO:1901224
Any process that activates or increases the frequency, rate or extent of NIK/NF-kappaB signaling.
2 P31681 (/IDA) P31681 (/IDA)
Nematode larval development GO:0002119
The process whose specific outcome is the progression of the nematode larva over time, from its formation to the mature structure. Nematode larval development begins with the newly hatched first-stage larva (L1) and ends with the end of the last larval stage (for example the fourth larval stage (L4) in C. elegans). Each stage of nematode larval development is characterized by proliferation of specific cell lineages and an increase in body size without alteration of the basic body plan. Nematode larval stages are separated by molts in which each stage-specific exoskeleton, or cuticle, is shed and replaced anew.
1 P50140 (/IMP)
Protein folding GO:0006457
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
1 Q37683 (/ISA)
Spermatogenesis GO:0007283
The process of formation of spermatozoa, including spermatocytogenesis and spermiogenesis.
1 Q9VMN5 (/IMP)
Female germline ring canal formation GO:0007301
Assembly of the intercellular bridges that connect the germ-line cells of a female cyst.
1 Q9VMN5 (/IMP)
Open tracheal system development GO:0007424
The process whose specific outcome is the progression of an open tracheal system over time, from its formation to the mature structure. An open tracheal system is a respiratory system, a branched network of epithelial tubes that supplies oxygen to target tissues via spiracles. An example of this is found in Drosophila melanogaster.
1 Q9VMN5 (/IMP)
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 Q5ZL72 (/IDA)
Response to cytokinin GO:0009735
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cytokinin stimulus.
1 Q8L7B5 (/IDA)
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 P50140 (/IMP)
Response to acidic pH GO:0010447
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 pH stimulus with pH < 7. pH is a measure of the acidity or basicity of an aqueous solution.
1 Q9KKF0 (/IMP)
Asexual reproduction GO:0019954
The biological process in which new individuals are produced by either a single cell or a group of cells, in the absence of any sexual process.
1 Q54J97 (/IMP)
Protein import into mitochondrial matrix GO:0030150
The import of proteins across the outer and inner mitochondrial membranes into the matrix. Unfolded proteins enter the mitochondrial matrix with a chaperone protein; the information required to target the precursor protein from the cytosol to the mitochondrial matrix is contained within its N-terminal matrix-targeting sequence. Translocation of precursors to the matrix occurs at the rare sites where the outer and inner membranes are close together.
1 Q37683 (/ISA)
Protein import into mitochondrial matrix GO:0030150
The import of proteins across the outer and inner mitochondrial membranes into the matrix. Unfolded proteins enter the mitochondrial matrix with a chaperone protein; the information required to target the precursor protein from the cytosol to the mitochondrial matrix is contained within its N-terminal matrix-targeting sequence. Translocation of precursors to the matrix occurs at the rare sites where the outer and inner membranes are close together.
1 Q09864 (/ISO)
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.
1 Q9VMN5 (/IMP)
Fin regeneration GO:0031101
The regrowth of fin tissue following its loss or destruction.
1 Q803B0 (/IMP)
Sorocarp morphogenesis GO:0031288
The process in which the sorocarp is generated and organized. An example of this process is found in Dictyostelium discoideum.
1 Q54J97 (/IMP)
Mitochondrial unfolded protein response GO:0034514
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the mitochondrial matrix; results in transcriptional upregulation of nuclear genes encoding mitochondrial stress proteins.
1 P50140 (/IEP)
Mitochondrial unfolded protein response GO:0034514
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the mitochondrial matrix; results in transcriptional upregulation of nuclear genes encoding mitochondrial stress proteins.
1 P50140 (/IMP)
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.
1 O74261 (/IMP)
Tissue regeneration GO:0042246
The regrowth of lost or destroyed tissues.
1 Q803B0 (/IMP)
Hyperosmotic salinity response GO:0042538
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 detection of, or exposure to, an increase in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
1 Q9KKF0 (/IMP)
Positive phototaxis GO:0046956
The directed movement of a cell or organism towards a source of light.
1 Q54J97 (/IMP)
Oogenesis GO:0048477
The complete process of formation and maturation of an ovum or female gamete from a primordial female germ cell. Examples of this process are found in Mus musculus and Drosophila melanogaster.
1 Q9VMN5 (/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.
1 Q09864 (/NAS)
Cellular response to osmotic stress GO:0071470
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 stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
1 Q5B041 (/IEP)
Positive regulation of cellular response to heat GO:1900036
Any process that activates or increases the frequency, rate or extent of cellular response to heat.
1 P50142 (/IDA)
Response to iron ion starvation GO:1990641
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 iron ion.
1 Q9KKF0 (/IMP)

There are 89 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
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
191 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(181 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.
190 P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA)
(180 more)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
180 P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA)
(170 more)
GroEL-GroES complex GO:1990220
Bacterial chaperonin complex consisting of a heptameric 10kDa chaperonin subunit GroES and a tetradecameric (2x7) 60kDa chaperonin subunit GroEL. The 60kDa subunit possesses ATPase activity while the holo-enzyme is responsible for the correct folding of proteins.
178 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(168 more)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
45 A0A024R3X4 (/IDA) A0A024R3X4 (/IDA) O02649 (/IDA) O02649 (/IDA) P10809 (/IDA) P10809 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA)
(35 more)
Cell wall GO:0005618
The rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal, most prokaryotic cells and some protozoan parasites, maintaining their shape and protecting them from osmotic lysis. In plants it is made of cellulose and, often, lignin; in fungi it is composed largely of polysaccharides; in bacteria it is composed of peptidoglycan; in protozoan parasites such as Giardia species, it's made of carbohydrates and proteins.
24 P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA)
(14 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.
24 P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA) P9WPE7 (/HDA)
(14 more)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
21 P10809 (/IDA) P10809 (/IDA) P31681 (/IDA) P31681 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA)
(11 more)
Cell wall GO:0005618
The rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal, most prokaryotic cells and some protozoan parasites, maintaining their shape and protecting them from osmotic lysis. In plants it is made of cellulose and, often, lignin; in fungi it is composed largely of polysaccharides; in bacteria it is composed of peptidoglycan; in protozoan parasites such as Giardia species, it's made of carbohydrates and proteins.
14 P50142 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA)
(4 more)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
14 O02649 (/HDA) O02649 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA)
(4 more)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
13 P10809 (/IDA) P10809 (/IDA) P50142 (/IDA) P63038 (/IDA) P63038 (/IDA) P63038 (/IDA) P63039 (/IDA) P63039 (/IDA) P63039 (/IDA) Q37683 (/IDA)
(3 more)
Capsule GO:0042603
A protective structure surrounding some fungi and bacteria, attached externally to the cell wall and composed primarily of polysaccharides. Capsules are highly organized structures that adhere strongly to cells and cannot be easily removed. Capsules play important roles in pathogenicity, preventing phagocytosis by other cells, adherance, and resistance to dessication.
12 P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA) P9WPE7 (/IDA)
(2 more)
Bacterial nucleoid GO:0043590
The region of a bacterial cell to which the DNA is confined.
12 P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA) P9WPE9 (/IDA)
(2 more)
Host cell surface GO:0044228
The external part of the host cell wall and/or host plasma membrane.
12 A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA) A0A0H3LCC3 (/IDA)
(2 more)
Mitochondrial matrix GO:0005759
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
10 P10809 (/TAS) P10809 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS)
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.
9 P18687 (/ISS) P31081 (/ISS) P63038 (/ISS) P63038 (/ISS) P63038 (/ISS) P63039 (/ISS) P63039 (/ISS) P63039 (/ISS) Q5NVM5 (/ISS)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
8 P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS)
Mitochondrial intermembrane space GO:0005758
The region between the inner and outer lipid bilayers of the mitochondrial envelope.
8 P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS)
Mitochondrial matrix GO:0005759
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
8 P10809 (/IDA) P10809 (/IDA) P29185 (/IDA) P29185 (/IDA) P29197 (/IDA) P29197 (/IDA) Q09864 (/IDA) Q803B0 (/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.
8 P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS)
Mitochondrial nucleoid GO:0042645
The region of a mitochondrion to which the DNA is confined.
8 P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
7 P10809 (/IDA) P10809 (/IDA) P63038 (/IDA) P63038 (/IDA) P63038 (/IDA) Q8L7B5 (/IDA) Q9KKF0 (/IDA)
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.
6 P10809 (/IDA) P10809 (/IDA) P63039 (/IDA) P63039 (/IDA) P63039 (/IDA) Q9KKF0 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
6 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO) Q4Q1M0 (/ISO) Q4Q1M1 (/ISO) Q4Q594 (/ISO)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
6 P0C923 (/IDA) P0C923 (/IDA) P0C923 (/IDA) P0C923 (/IDA) P21238 (/IDA) P21238 (/IDA)
Secretory granule GO:0030141
A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
6 P63038 (/IDA) P63038 (/IDA) P63038 (/IDA) P63039 (/IDA) P63039 (/IDA) P63039 (/IDA)
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.
5 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO) Q4Q1M0 (/ISO) Q4Q1M1 (/ISO)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
5 O02649 (/IDA) O02649 (/IDA) P63039 (/IDA) P63039 (/IDA) P63039 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
4 P18687 (/ISS) P31081 (/ISS) Q5NVM5 (/ISS) Q5ZL72 (/ISS)
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
4 P29197 (/IDA) P29197 (/IDA) Q8L7B5 (/IDA) Q93ZM7 (/IDA)
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
4 P21238 (/IDA) P21238 (/IDA) Q56XV8 (/IDA) Q8L7B5 (/IDA)
Cytosolic ribosome GO:0022626
A ribosome located in the cytosol.
4 P21238 (/IDA) P21238 (/IDA) P29197 (/IDA) P29197 (/IDA)
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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
3 Q37683 (/RCA) Q381T1 (/RCA) Q381T1 (/RCA)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
3 P63038 (/HDA) P63038 (/HDA) P63038 (/HDA)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Mitochondrial matrix GO:0005759
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Mitochondrial matrix GO:0005759
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
3 O02649 (/ISS) O02649 (/ISS) Q9VMN5 (/ISS)
Early endosome GO:0005769
A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Peroxisomal matrix GO:0005782
The volume contained within the membranes of a peroxisome; in many cells the matrix contains a crystalloid core largely composed of urate oxidase.
3 P63039 (/IDA) P63039 (/IDA) P63039 (/IDA)
Peroxisomal matrix GO:0005782
The volume contained within the membranes of a peroxisome; in many cells the matrix contains a crystalloid core largely composed of urate oxidase.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Rough endoplasmic reticulum GO:0005791
The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae.
3 P63039 (/IDA) P63039 (/IDA) P63039 (/IDA)
Rough endoplasmic reticulum GO:0005791
The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
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.
3 P63039 (/IDA) P63039 (/IDA) P63039 (/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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Chloroplast stroma GO:0009570
The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis.
3 P21238 (/IDA) P21238 (/IDA) Q8L7B5 (/IDA)
Chloroplast envelope GO:0009941
The double lipid bilayer enclosing the chloroplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
3 P21238 (/IDA) P21238 (/IDA) Q8L7B5 (/IDA)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
3 P63038 (/IMP) P63038 (/IMP) P63038 (/IMP)
Mitochondrial crista GO:0030061
Any of the inward folds of the mitochondrial inner membrane. Their number, extent, and shape differ in mitochondria from different tissues and organisms. They appear to be devices for increasing the surface area of the mitochondrial inner membrane, where the enzymes of electron transport and oxidative phosphorylation are found. Their shape can vary with the respiratory state of the mitochondria.
3 P63039 (/IDA) P63039 (/IDA) P63039 (/IDA)
Mitochondrial crista GO:0030061
Any of the inward folds of the mitochondrial inner membrane. Their number, extent, and shape differ in mitochondria from different tissues and organisms. They appear to be devices for increasing the surface area of the mitochondrial inner membrane, where the enzymes of electron transport and oxidative phosphorylation are found. Their shape can vary with the respiratory state of the mitochondria.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Coated vesicle GO:0030135
Small membrane-bounded organelle formed by pinching off of a coated region of membrane. Some coats are made of clathrin, whereas others are made from other proteins.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Secretory granule GO:0030141
A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Zymogen granule GO:0042588
A membrane-bounded, cytoplasmic secretory granule found in enzyme-secreting cells and visible by light microscopy. Contain zymogen, an inactive enzyme precursor, often of a digestive enzyme.
3 P63039 (/IDA) P63039 (/IDA) P63039 (/IDA)
Zymogen granule GO:0042588
A membrane-bounded, cytoplasmic secretory granule found in enzyme-secreting cells and visible by light microscopy. Contain zymogen, an inactive enzyme precursor, often of a digestive enzyme.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/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.
3 P63038 (/HDA) P63038 (/HDA) P63038 (/HDA)
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
3 P63038 (/IDA) P63038 (/IDA) P63038 (/IDA)
Host cell endosome membrane GO:0044175
The lipid bilayer surrounding a host cell endosome.
3 Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/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.
3 P63039 (/IDA) P63039 (/IDA) P63039 (/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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Lipopolysaccharide receptor complex GO:0046696
A multiprotein complex that consists of at least three proteins, CD14, TLR4, and MD-2, each of which is glycosylated and which functions as a lipopolysaccharide (LPS) receptor that primes the innate immune response against bacterial pathogens.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/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.
3 P63038 (/ISO) P63038 (/ISO) P63038 (/ISO)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
2 Q381T1 (/ISA) Q381T1 (/ISA)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
2 P10809 (/ISS) P10809 (/ISS)
Early endosome GO:0005769
A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways.
2 P10809 (/IDA) P10809 (/IDA)
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.
2 P10809 (/IDA) P10809 (/IDA)
Cilium GO:0005929
A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
2 Q4Q1M0 (/ISO) Q4Q1M1 (/ISO)
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
2 P21238 (/ISS) P21238 (/ISS)
Thylakoid GO:0009579
A membranous cellular structure that bears the photosynthetic pigments in plants, algae, and cyanobacteria. In cyanobacteria thylakoids are of various shapes and are attached to, or continuous with, the plasma membrane. In eukaryotes they are flattened, membrane-bounded disk-like structures located in the chloroplasts; in the chloroplasts of higher plants the thylakoids form dense stacks called grana. Isolated thylakoid preparations can carry out photosynthetic electron transport and the associated phosphorylation.
2 P21238 (/IDA) P21238 (/IDA)
Symbiont-containing vacuole GO:0020003
Membrane-bounded vacuole within a host cell in which a symbiont organism resides. The vacuole membrane is derived from both the host and symbiont.
2 P31681 (/IDA) P31681 (/IDA)
Coated vesicle GO:0030135
Small membrane-bounded organelle formed by pinching off of a coated region of membrane. Some coats are made of clathrin, whereas others are made from other proteins.
2 P10809 (/IDA) P10809 (/IDA)
Secretory granule GO:0030141
A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
2 P10809 (/ISS) P10809 (/ISS)
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.
2 P10809 (/IDA) P10809 (/IDA)
Polysomal ribosome GO:0042788
A ribosome bound to mRNA that forms part of a polysome.
2 P29197 (/IDA) P29197 (/IDA)
Lipopolysaccharide receptor complex GO:0046696
A multiprotein complex that consists of at least three proteins, CD14, TLR4, and MD-2, each of which is glycosylated and which functions as a lipopolysaccharide (LPS) receptor that primes the innate immune response against bacterial pathogens.
2 P10809 (/IDA) P10809 (/IDA)
Apoplast GO:0048046
The cell membranes and intracellular regions in a plant are connected through plasmodesmata, and plants may be described as having two major compartments: the living symplast and the non-living apoplast. The apoplast is external to the plasma membrane and includes cell walls, intercellular spaces and the lumen of dead structures such as xylem vessels. Water and solutes pass freely through it.
2 P21238 (/IDA) P21238 (/IDA)
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
2 P10809 (/HDA) P10809 (/HDA)
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
2 P10809 (/IDA) P10809 (/IDA)
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.
1 Q37683 (/ISM)
Mitochondrial intermembrane space GO:0005758
The region between the inner and outer lipid bilayers of the mitochondrial envelope.
1 Q09864 (/IDA)
Cilium GO:0005929
A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
1 Q37683 (/IDA)
Mitochondrial membrane GO:0031966
Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
1 Q09864 (/IDA)
Mitochondrial nucleoid GO:0042645
The region of a mitochondrion to which the DNA is confined.
1 Q09864 (/ISO)
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
1 Q5ZL72 (/IDA)
Post-mRNA release spliceosomal complex GO:0071014
A spliceosomal complex that is formed following the release of the spliced product from the post-spliceosomal complex and contains the excised intron and three snRNPs, including U5.
1 Q09864 (/IDA)
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