The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"Actin; Chain A, domain 4
".
FunFam 2: Heat shock 70 kDa
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 100 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).
|
171 |
C8Z3H3 (/IPI)
G3I8R9 (/IPI)
G3I8R9 (/IPI)
G3I8R9 (/IPI)
O59855 (/IPI)
O65719 (/IPI)
O65719 (/IPI)
P06761 (/IPI)
P07823 (/IPI)
P07823 (/IPI)
(161 more) |
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
|
94 |
G3I8R9 (/IDA)
G3I8R9 (/IDA)
G3I8R9 (/IDA)
P07823 (/IDA)
P07823 (/IDA)
P07823 (/IDA)
P09446 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
(84 more) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
78 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(68 more) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
77 |
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV9 (/IPI)
(67 more) |
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
|
70 |
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV9 (/IPI)
(60 more) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
64 |
B3VHV2 (/IDA)
B6EAX2 (/IDA)
P08106 (/IDA)
P08106 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
(54 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.
|
63 |
A0A1D5PFJ6 (/IPI)
A0PA16 (/IPI)
A0PA16 (/IPI)
A0PA16 (/IPI)
A0PA16 (/IPI)
A0PA16 (/IPI)
F1NWP3 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
(53 more) |
Cadherin binding GO:0045296
Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.
|
57 |
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P11021 (/HDA)
(47 more) |
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
|
52 |
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV9 (/HDA)
(42 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.
|
52 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(42 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.
|
52 |
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV9 (/IPI)
(42 more) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
37 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(27 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.
|
37 |
P11142 (/IPI)
P11142 (/IPI)
P11142 (/IPI)
P11142 (/IPI)
P11142 (/IPI)
P11142 (/IPI)
P11142 (/IPI)
P11142 (/IPI)
P11142 (/IPI)
P11142 (/IPI)
(27 more) |
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
|
35 |
P06761 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P10592 (/ISS)
P11021 (/ISS)
(25 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) |
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) |
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.
|
28 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(18 more) |
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.
|
22 |
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV9 (/IPI)
(12 more) |
G protein-coupled receptor binding GO:0001664
Interacting selectively and non-covalently with a G protein-coupled receptor.
|
18 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(8 more) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
18 |
G3I8R9 (/NAS)
G3I8R9 (/NAS)
G3I8R9 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
(8 more) |
Histone deacetylase binding GO:0042826
Interacting selectively and non-covalently with the enzyme histone deacetylase.
|
18 |
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV9 (/IPI)
(8 more) |
Protein folding chaperone GO:0044183
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) that contributes to the process of protein folding.
|
18 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(8 more) |
Protein N-terminus binding GO:0047485
Interacting selectively and non-covalently with a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
|
18 |
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV9 (/IPI)
(8 more) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
18 |
P0DMV8 (/NAS)
P0DMV8 (/NAS)
P0DMV8 (/NAS)
P0DMV8 (/NAS)
P0DMV8 (/NAS)
P0DMV8 (/NAS)
P0DMV8 (/NAS)
P0DMV8 (/NAS)
P0DMV8 (/NAS)
P0DMV9 (/NAS)
(8 more) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
17 |
P07823 (/IPI)
P07823 (/IPI)
P07823 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
P11021 (/IPI)
(7 more) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
17 |
O59855 (/ISO)
P16627 (/ISO)
P16627 (/ISO)
P17156 (/ISO)
P17156 (/ISO)
P17156 (/ISO)
P20029 (/ISO)
P20029 (/ISO)
P36604 (/ISO)
P63017 (/ISO)
(7 more) |
Misfolded protein binding GO:0051787
Interacting selectively and non-covalently with a misfolded protein.
|
17 |
P06761 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(7 more) |
Disordered domain specific binding GO:0097718
Interacting selectively and non-covalently with a disordered domain of a protein.
|
16 |
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P0DMV8 (/IPI)
P54652 (/IPI)
(6 more) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
14 |
O97125 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P09435 (/ISS)
P10592 (/ISS)
P11146 (/ISS)
(4 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.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
|
12 |
O59855 (/ISO)
P20029 (/ISO)
P20029 (/ISO)
P36604 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
Q10265 (/ISO)
Q10284 (/ISO)
(2 more) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
11 |
P17156 (/ISO)
P17156 (/ISO)
P17156 (/ISO)
P20029 (/ISO)
P20029 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
Q61696 (/ISO)
(1 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.
|
11 |
Q8IB24 (/IDA)
Q8IB24 (/IDA)
Q8IB24 (/IDA)
Q8IB24 (/IDA)
Q8IB24 (/IDA)
Q8IB24 (/IDA)
Q8IB24 (/IDA)
Q8IB24 (/IDA)
Q8IB24 (/IDA)
Q8IB24 (/IDA)
(1 more) |
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
|
10 | P16627 (/ISO) P16627 (/ISO) P20029 (/ISO) P20029 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
10 | P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) |
Transcription corepressor activity GO:0003714
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to repress the transcription of specific genes. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. A third class occludes DNA-binding transcription factor protein-protein interaction domains. A fourth class of corepressors prevents interactions of DNA bound DNA-binding transcription factor with coactivators.
|
9 | P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) |
Denatured protein binding GO:0031249
Interacting selectively and non-covalently with denatured proteins.
|
9 | P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
9 | P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P10592 (/IGI) P22202 (/IGI) |
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.
|
8 | P16627 (/ISO) P16627 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
Transcription corepressor activity GO:0003714
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to repress the transcription of specific genes. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. A third class occludes DNA-binding transcription factor protein-protein interaction domains. A fourth class of corepressors prevents interactions of DNA bound DNA-binding transcription factor with coactivators.
|
7 | P0DMW0 (/ISS) P0DMW0 (/ISS) P34930 (/ISS) Q27975 (/ISS) Q27975 (/ISS) Q61696 (/ISS) Q61696 (/ISS) |
Calmodulin binding GO:0005516
Interacting selectively and non-covalently with calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
|
7 | P11484 (/IDA) P11484 (/IDA) P11484 (/IDA) P11484 (/IDA) P11484 (/IDA) P11484 (/IDA) P11484 (/IDA) |
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
|
7 | P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) |
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.
|
7 | P17156 (/ISO) P17156 (/ISO) P17156 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) |
G protein-coupled receptor binding GO:0001664
Interacting selectively and non-covalently with a G protein-coupled receptor.
|
6 | P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
|
6 | O65719 (/IPI) O65719 (/IPI) P0DMW1 (/IPI) P0DMW1 (/IPI) P22953 (/IPI) P22953 (/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.
|
6 | P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
6 | P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/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.
|
6 | P41797 (/IDA) P46587 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) |
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.
|
6 | P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/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.
|
6 | P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
Progesterone receptor binding GO:0033142
Interacting selectively and non-covalently with a progesterone receptor.
|
5 | B3VHV2 (/IPI) B6EAX2 (/IPI) P08106 (/IPI) P08106 (/IPI) Q7SX63 (/IPI) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
5 | P06761 (/IPI) P63017 (/IPI) P63017 (/IPI) P63017 (/IPI) P63017 (/IPI) |
Disordered domain specific binding GO:0097718
Interacting selectively and non-covalently with a disordered domain of a protein.
|
5 | P17156 (/ISO) P17156 (/ISO) P17156 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
TRNA binding GO:0000049
Interacting selectively and non-covalently with transfer RNA.
|
4 | P10591 (/IDA) P10591 (/IDA) P10591 (/IDA) P10592 (/IDA) |
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) |
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) |
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) |
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 | 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) |
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) |
Tau protein binding GO:0048156
Interacting selectively and non-covalently with tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS.
|
3 | P14659 (/IPI) P14659 (/IPI) P14659 (/IPI) |
Tau protein binding GO:0048156
Interacting selectively and non-covalently with tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS.
|
3 | P17156 (/ISO) P17156 (/ISO) P17156 (/ISO) |
Glycolipid binding GO:0051861
Interacting selectively and non-covalently with a glycolipid, any compound containing one or more monosaccharide residues bound by a glycosidic linkage to a hydrophobic group such as an acylglycerol, a sphingoid, a ceramide (N-acylsphingoid) or a prenyl phosphate.
|
3 | P17156 (/IDA) P17156 (/IDA) P17156 (/IDA) |
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Transcription corepressor activity GO:0003714
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to repress the transcription of specific genes. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. A third class occludes DNA-binding transcription factor protein-protein interaction domains. A fourth class of corepressors prevents interactions of DNA bound DNA-binding transcription factor with coactivators.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Denatured protein binding GO:0031249
Interacting selectively and non-covalently with denatured proteins.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Histone deacetylase binding GO:0042826
Interacting selectively and non-covalently with the enzyme histone deacetylase.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Ribosome binding GO:0043022
Interacting selectively and non-covalently with any part of a ribosome.
|
2 | P20029 (/IDA) P20029 (/IDA) |
Protein folding chaperone GO:0044183
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) that contributes to the process of protein folding.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Protein N-terminus binding GO:0047485
Interacting selectively and non-covalently with a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
NF-kappaB binding GO:0051059
Interacting selectively and non-covalently with NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters.
|
2 | P0DMW1 (/IPI) P0DMW1 (/IPI) |
NF-kappaB binding GO:0051059
Interacting selectively and non-covalently with NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters.
|
2 | Q61696 (/ISO) Q61696 (/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.
|
2 | P11147 (/IDA) P11147 (/IDA) |
Misfolded protein binding GO:0051787
Interacting selectively and non-covalently with a misfolded protein.
|
2 | P20029 (/ISO) P20029 (/ISO) |
RNA polymerase II transcription factor binding GO:0001085
Interacting selectively and non-covalently with an RNA polymerase II transcription factor, any protein required to initiate or regulate transcription by RNA polymerase II.
|
1 | P20163 (/IPI) |
G protein-coupled receptor binding GO:0001664
Interacting selectively and non-covalently with a G protein-coupled receptor.
|
1 | Q7SX63 (/ISS) |
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
|
1 | Q7SX63 (/ISS) |
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) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
1 | P36604 (/IC) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
1 | Q7SX63 (/ISS) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
1 | Q7SX63 (/ISS) |
MHC class II protein complex binding GO:0023026
Interacting selectively and non-covalently with the class II major histocompatibility complex.
|
1 | Q7SX63 (/ISS) |
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.
|
1 | Q7SX63 (/ISS) |
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
|
1 | Q7SX63 (/ISS) |
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.
|
1 | P46587 (/IMP) |
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.
|
1 | Q7SX63 (/ISS) |
There are 365 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.
|
128 |
A0A024R6B5 (/ISS)
A0A024R6B5 (/ISS)
A0A024R6B5 (/ISS)
A0A024R6B5 (/ISS)
A0A024R6B5 (/ISS)
A0A061I5U1 (/ISS)
A0A087QQM7 (/ISS)
A0A087QQM7 (/ISS)
A0A087QQM7 (/ISS)
A0A087V8L3 (/ISS)
(118 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.
|
127 |
A0A024R6B5 (/ISS)
A0A024R6B5 (/ISS)
A0A024R6B5 (/ISS)
A0A024R6B5 (/ISS)
A0A024R6B5 (/ISS)
A0A061I5U1 (/ISS)
A0A087QQM7 (/ISS)
A0A087QQM7 (/ISS)
A0A087QQM7 (/ISS)
A0A087V8L3 (/ISS)
(117 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.
|
78 |
A1CEK9 (/ISS)
A1DFN8 (/ISS)
A2QW80 (/ISS)
A2QW80 (/ISS)
A2QW80 (/ISS)
A2QW80 (/ISS)
A2QW80 (/ISS)
A2QW80 (/ISS)
A2QW80 (/ISS)
A2QW80 (/ISS)
(68 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.
|
64 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(54 more) |
Neutrophil degranulation GO:0043312
The regulated exocytosis of secretory granules containing preformed mediators such as proteases, lipases, and inflammatory mediators by a neutrophil.
|
54 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(44 more) |
Regulation of cellular response to heat GO:1900034
Any process that modulates the frequency, rate or extent of cellular response to heat.
|
54 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(44 more) |
ATP metabolic process GO:0046034
The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator.
|
52 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(42 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.
|
50 |
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
(40 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.
|
45 |
P02825 (/NAS)
P02825 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
(35 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.
|
43 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P11142 (/TAS)
(33 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.
|
39 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P59769 (/IDA)
(29 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) |
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.
|
36 |
A0A1D8PG96 (/NAS)
A0A1D8PG96 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
P11142 (/NAS)
(26 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.
|
36 |
P0DMW0 (/ISS)
P0DMW0 (/ISS)
P0DMW1 (/ISS)
P0DMW1 (/ISS)
P17879 (/ISS)
P34930 (/ISS)
P63017 (/ISS)
P63017 (/ISS)
P63017 (/ISS)
P63017 (/ISS)
(26 more) |
Negative regulation of apoptotic process GO:0043066
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
|
35 |
G3I8R9 (/IMP)
G3I8R9 (/IMP)
G3I8R9 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
(25 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) |
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) |
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) |
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) |
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) |
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) |
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.
|
32 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(22 more) |
Positive regulation of microtubule nucleation GO:0090063
Any process that increases the rate, frequency or extent of microtubule nucleation. Microtubule nucleation is the 'de novo' formation of a microtubule, in which tubulin heterodimers form metastable oligomeric aggregates, some of which go on to support formation of a complete microtubule. Microtubule nucleation usually occurs from a specific site within a cell.
|
27 |
P0DMW0 (/ISS)
P0DMW0 (/ISS)
P0DMW1 (/ISS)
P0DMW1 (/ISS)
P17879 (/ISS)
P34930 (/ISS)
Q27965 (/ISS)
Q27965 (/ISS)
Q27975 (/ISS)
Q27975 (/ISS)
(17 more) |
Negative regulation of protein homodimerization activity GO:0090074
Any process that decreases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.
|
27 |
P06761 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
(17 more) |
Regulation of mitotic spindle assembly GO:1901673
Any process that modulates the frequency, rate or extent of mitotic spindle assembly.
|
27 |
P0DMW0 (/ISS)
P0DMW0 (/ISS)
P0DMW1 (/ISS)
P0DMW1 (/ISS)
P17879 (/ISS)
P34930 (/ISS)
Q27965 (/ISS)
Q27965 (/ISS)
Q27975 (/ISS)
Q27975 (/ISS)
(17 more) |
Negative regulation of IRE1-mediated unfolded protein response GO:1903895
Any process that stops, prevents or reduces the frequency, rate or extent of the IRE1-mediated unfolded protein response.
|
27 |
P06761 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
P11021 (/ISS)
(17 more) |
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.
|
23 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(13 more) |
Negative regulation of inclusion body assembly GO:0090084
Any process that decreases the rate, frequency, or extent of inclusion body assembly. Inclusion body assembly is the aggregation, arrangement and bonding together of a set of components to form an inclusion body.
|
23 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(13 more) |
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.
|
22 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(12 more) |
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.
|
20 |
A8WFS0 (/IDA)
B0S610 (/IDA)
B0UXS6 (/IDA)
B3VHV2 (/IDA)
B6EAX2 (/IDA)
B7ZV46 (/IDA)
P08106 (/IDA)
P08106 (/IDA)
P08108 (/IDA)
P08108 (/IDA)
(10 more) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
20 |
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(10 more) |
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.
|
19 |
P02825 (/IMP)
P02825 (/IMP)
P22953 (/IMP)
P22953 (/IMP)
P82910 (/IMP)
P82910 (/IMP)
Q61696 (/IMP)
Q61696 (/IMP)
Q8INI8 (/IMP)
Q8INI8 (/IMP)
(9 more) |
MRNA catabolic process GO:0006402
The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes.
|
18 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(8 more) |
Negative regulation of cell population proliferation GO:0008285
Any process that stops, prevents or reduces the rate or extent of cell proliferation.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Negative regulation of cell growth GO:0030308
Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Regulation of protein ubiquitination GO:0031396
Any process that modulates the frequency, rate or extent of the addition of ubiquitin groups to a protein.
|
18 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(8 more) |
Negative regulation of protein ubiquitination GO:0031397
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein.
|
18 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(8 more) |
Positive regulation of interleukin-8 production GO:0032757
Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Cellular response to oxidative stress GO:0034599
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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
|
18 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(8 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.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Positive regulation of erythrocyte differentiation GO:0045648
Any process that activates or increases the frequency, rate or extent of erythrocyte differentiation.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
18 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(8 more) |
Positive regulation of NF-kappaB transcription factor activity GO:0051092
Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Negative regulation of cell death GO:0060548
Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Cellular heat acclimation GO:0070370
Any process that increases heat tolerance of a cell in response to high temperatures.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway GO:0070434
Any process that activates or increases the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing 2 (NOD2) pathway.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Positive regulation of microtubule nucleation GO:0090063
Any process that increases the rate, frequency or extent of microtubule nucleation. Microtubule nucleation is the 'de novo' formation of a microtubule, in which tubulin heterodimers form metastable oligomeric aggregates, some of which go on to support formation of a complete microtubule. Microtubule nucleation usually occurs from a specific site within a cell.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Regulation of mitotic spindle assembly GO:1901673
Any process that modulates the frequency, rate or extent of mitotic spindle assembly.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Positive regulation of tumor necrosis factor-mediated signaling pathway GO:1903265
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor-mediated signaling pathway.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
Negative regulation of extrinsic apoptotic signaling pathway in absence of ligand GO:2001240
Any process that stops, prevents or reduces the frequency, rate or extent of extrinsic apoptotic signaling pathway in absence of ligand.
|
18 |
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV8 (/IMP)
P0DMV9 (/IMP)
(8 more) |
SRP-dependent cotranslational protein targeting to membrane, translocation GO:0006616
The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
|
17 |
A0A1D8PG96 (/IMP)
A0A1D8PG96 (/IMP)
P09435 (/IMP)
P09435 (/IMP)
P09435 (/IMP)
P09435 (/IMP)
P09435 (/IMP)
P09435 (/IMP)
P09435 (/IMP)
P10592 (/IMP)
(7 more) |
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.
|
17 |
O45246 (/IEP)
O65719 (/IEP)
O65719 (/IEP)
P11145 (/IEP)
P22953 (/IEP)
P22953 (/IEP)
P22954 (/IEP)
P22954 (/IEP)
P63018 (/IEP)
P63018 (/IEP)
(7 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 |
P02825 (/IEP)
P02825 (/IEP)
P82910 (/IEP)
P82910 (/IEP)
Q8INI8 (/IEP)
Q8INI8 (/IEP)
Q8INI8 (/IEP)
Q9BIR7 (/IEP)
Q9BIR7 (/IEP)
Q9BIR7 (/IEP)
(5 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 |
P02825 (/IMP)
P02825 (/IMP)
P82910 (/IMP)
P82910 (/IMP)
Q8INI8 (/IMP)
Q8INI8 (/IMP)
Q8INI8 (/IMP)
Q9BIR7 (/IMP)
Q9BIR7 (/IMP)
Q9BIR7 (/IMP)
(5 more) |
Secretion by cell GO:0032940
The controlled release of a substance by a cell.
|
15 |
P83616 (/NAS)
P83616 (/NAS)
P83616 (/NAS)
P83616 (/NAS)
P83616 (/NAS)
P83616 (/NAS)
P83616 (/NAS)
P83616 (/NAS)
P83616 (/NAS)
P83616 (/NAS)
(5 more) |
Heat shock-mediated polytene chromosome puffing GO:0035080
The decondensing (loosening) and swelling of the chromosomal sites of heat shock genes on polytene chromosomes in response to a heat shock stimulus.
|
15 |
P02825 (/IMP)
P02825 (/IMP)
P82910 (/IMP)
P82910 (/IMP)
Q8INI8 (/IMP)
Q8INI8 (/IMP)
Q8INI8 (/IMP)
Q9BIR7 (/IMP)
Q9BIR7 (/IMP)
Q9BIR7 (/IMP)
(5 more) |
Lysosomal transport GO:0007041
The directed movement of substances into, out of or within a lysosome.
|
14 |
P0DMV8 (/ISS)
P0DMV8 (/ISS)
P0DMV8 (/ISS)
P0DMV8 (/ISS)
P0DMV8 (/ISS)
P0DMV8 (/ISS)
P0DMV8 (/ISS)
P0DMV8 (/ISS)
P0DMV8 (/ISS)
P0DMW0 (/ISS)
(4 more) |
Substantia nigra development GO:0021762
The progression of the substantia nigra over time from its initial formation until its mature state. The substantia nigra is the layer of gray substance that separates the posterior parts of the cerebral peduncles (tegmentum mesencephali) from the anterior parts; it normally includes a posterior compact part with many pigmented cells (pars compacta) and an anterior reticular part whose cells contain little pigment (pars reticularis).
|
14 |
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
P11021 (/HEP)
(4 more) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
14 |
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(4 more) |
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Protein folding in endoplasmic reticulum GO:0034975
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Maintenance of protein localization in endoplasmic reticulum GO:0035437
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
|
14 |
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(4 more) |
IRE1-mediated unfolded protein response GO:0036498
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
PERK-mediated unfolded protein response GO:0036499
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
ATF6-mediated unfolded protein response GO:0036500
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Cellular response to glucose starvation GO:0042149
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 glucose.
|
14 |
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(4 more) |
Regulation of protein folding in endoplasmic reticulum GO:0060904
Any process that modulates the rate, frequency or extent of the protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Negative regulation of protein homodimerization activity GO:0090074
Any process that decreases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Regulation of ATF6-mediated unfolded protein response GO:1903891
Any process that modulates the frequency, rate or extent of the ATF6-mediated unfolded protein response.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Regulation of IRE1-mediated unfolded protein response GO:1903894
Any process that modulates the frequency, rate or extent of the IRE1-mediated unfolded protein response.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Regulation of PERK-mediated unfolded protein response GO:1903897
Any process that modulates the frequency, rate or extent of the PERK-mediated unfolded protein response.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress GO:1990440
Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of an endoplasmic reticulum stress.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
12 |
G3I8R9 (/ISS)
G3I8R9 (/ISS)
G3I8R9 (/ISS)
P06761 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P20029 (/ISS)
P20029 (/ISS)
Q0VCX2 (/ISS)
(2 more) |
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.
|
12 |
B0UXS6 (/IEP)
O65719 (/IEP)
O65719 (/IEP)
P22953 (/IEP)
P22953 (/IEP)
P22954 (/IEP)
P22954 (/IEP)
Q39043 (/IEP)
Q39043 (/IEP)
Q9C7X7 (/IEP)
(2 more) |
Cytoplasmic translation GO:0002181
The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein.
|
11 |
P10591 (/IMP)
P10591 (/IMP)
P10591 (/IMP)
P11484 (/IMP)
P11484 (/IMP)
P11484 (/IMP)
P11484 (/IMP)
P11484 (/IMP)
P11484 (/IMP)
P11484 (/IMP)
(1 more) |
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.
|
11 |
P02825 (/NAS)
P02825 (/NAS)
Q8INI8 (/NAS)
Q8INI8 (/NAS)
Q8INI8 (/NAS)
Q9BIR7 (/NAS)
Q9BIR7 (/NAS)
Q9BIR7 (/NAS)
Q9BIS2 (/NAS)
Q9BIS2 (/NAS)
(1 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.
|
11 |
O59855 (/ISO)
P16627 (/ISO)
P16627 (/ISO)
P17156 (/ISO)
P17156 (/ISO)
P17156 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
(1 more) |
Negative regulation of cell death GO:0060548
Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.
|
11 |
P0DMV9 (/IDA)
P0DMV9 (/IDA)
P0DMV9 (/IDA)
P0DMV9 (/IDA)
P0DMV9 (/IDA)
P0DMV9 (/IDA)
P0DMV9 (/IDA)
P0DMV9 (/IDA)
P0DMV9 (/IDA)
P0DMW0 (/IDA)
(1 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.
|
10 | P0DMW0 (/IMP) P0DMW0 (/IMP) P0DMW1 (/IMP) P0DMW1 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) |
Spermatogenesis GO:0007283
The process of formation of spermatozoa, including spermatocytogenesis and spermiogenesis.
|
10 | P14659 (/ISS) P14659 (/ISS) P14659 (/ISS) P34933 (/ISS) P54652 (/ISS) P54652 (/ISS) P54652 (/ISS) P54652 (/ISS) P54652 (/ISS) Q9TUG3 (/ISS) |
Response to virus GO:0009615
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a virus.
|
10 | O65719 (/IEP) O65719 (/IEP) P22953 (/IEP) P22953 (/IEP) P22954 (/IEP) P22954 (/IEP) Q9LHA8 (/IEP) Q9LHA8 (/IEP) Q9S9N1 (/IEP) Q9S9N1 (/IEP) |
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.
|
10 | A8WFS0 (/IDA) B0S610 (/IDA) B7ZV46 (/IDA) P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q8UUJ8 (/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.
|
10 | P11147 (/IDA) P11147 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/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.
|
9 | P17066 (/TAS) P17066 (/TAS) P34931 (/TAS) P34931 (/TAS) P54652 (/TAS) P54652 (/TAS) P54652 (/TAS) P54652 (/TAS) P54652 (/TAS) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
9 | P06761 (/ISS) P07823 (/ISS) P07823 (/ISS) P07823 (/ISS) P20029 (/ISS) P20029 (/ISS) Q0VCX2 (/ISS) Q3S4T7 (/ISS) Q5R4P0 (/ISS) |
Negative regulation of transforming growth factor beta receptor signaling pathway GO:0030512
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
|
9 | P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) |
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process GO:0032436
Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
|
9 | P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) |
Positive regulation of RNA splicing GO:0033120
Any process that activates or increases the frequency, rate or extent of RNA splicing.
|
9 | P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) |
Cellular response to unfolded protein GO:0034620
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 unfolded protein stimulus.
|
9 | P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) P0DMV8 (/IMP) |
Maintenance of protein localization in endoplasmic reticulum GO:0035437
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
|
9 | P06761 (/ISS) P07823 (/ISS) P07823 (/ISS) P07823 (/ISS) P20029 (/ISS) P20029 (/ISS) Q0VCX2 (/ISS) Q3S4T7 (/ISS) Q5R4P0 (/ISS) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
9 | P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) |
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.
|
9 | P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) |
Negative regulation of transcription from RNA polymerase II promoter in response to stress GO:0097201
Any process that decreases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).
|
9 | P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) |
Negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway GO:1901029
Any process that stops, prevents or reduces the frequency, rate or extent of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway.
|
9 | P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) |
Negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway GO:1902236
Any process that stops, prevents or reduces the frequency, rate or extent of an endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway.
|
9 | P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) |
Positive regulation of endoribonuclease activity GO:1902380
Any process that activates or increases the frequency, rate or extent of endoribonuclease activity.
|
9 | P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) |
Ribosomal subunit export from nucleus GO:0000054
The directed movement of a ribosomal subunit from the nucleus into the cytoplasm.
|
8 | P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P40150 (/IGI) |
Cytoplasmic translation GO:0002181
The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein.
|
8 | P11484 (/IPI) P11484 (/IPI) P11484 (/IPI) P11484 (/IPI) P11484 (/IPI) P11484 (/IPI) P11484 (/IPI) P40150 (/IPI) |
RRNA processing GO:0006364
Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules.
|
8 | P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P40150 (/IGI) |
Regulation of translational fidelity GO:0006450
Any process that modulates the ability of the translational apparatus to interpret the genetic code.
|
8 | P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P40150 (/IMP) |
Translational frameshifting GO:0006452
A mechanism whereby different proteins may result from a single mRNA molecule, due to a change in the parsing of three nucleotides per codon relative to an initiating AUG codon.
|
8 | P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P40150 (/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.
|
8 | P10591 (/IDA) P10591 (/IDA) P10591 (/IDA) P10592 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/IDA) P63017 (/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.
|
8 | P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P09435 (/IGI) P22202 (/IGI) |
Protein folding in endoplasmic reticulum GO:0034975
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
|
8 | Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) Q6Z7B0 (/IMP) |
Cellular response to glucose starvation GO:0042149
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 glucose.
|
8 | P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P11484 (/IGI) P40150 (/IGI) |
'de novo' cotranslational protein folding GO:0051083
The process of assisting in the correct noncovalent assembly of the ribosome-bound nascent chains of a multidomain protein whilst other parts of the protein are still being translated.
|
8 | P11484 (/IDA) P11484 (/IDA) P11484 (/IDA) P11484 (/IDA) P11484 (/IDA) P11484 (/IDA) P11484 (/IDA) P40150 (/IDA) |
Translational termination GO:0006415
The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code).
|
7 | P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) P11484 (/IMP) |
Protein quality control for misfolded or incompletely synthesized proteins GO:0006515
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
|
7 | P09435 (/IMP) P09435 (/IMP) P09435 (/IMP) P09435 (/IMP) P09435 (/IMP) P09435 (/IMP) P09435 (/IMP) |
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
|
7 | P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) Q9LKR3 (/IMP) |
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.
|
7 | P10591 (/IDA) P10591 (/IDA) P10591 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) |
Negative regulation of transcription from RNA polymerase II promoter in response to stress GO:0097201
Any process that decreases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).
|
7 | P0DMW0 (/ISS) P0DMW0 (/ISS) P34930 (/ISS) Q27975 (/ISS) Q27975 (/ISS) Q61696 (/ISS) Q61696 (/ISS) |
Karyogamy involved in conjugation with cellular fusion GO:0000742
During sexual reproduction, the creation of a single nucleus from multiple nuclei as a result of fusing the lipid bilayers that surround each nuclei. This occurs after cytogamy.
|
6 | P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) |
MRNA catabolic process GO:0006402
The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes.
|
6 | P0DMW0 (/ISS) P0DMW0 (/ISS) P0DMW1 (/ISS) P0DMW1 (/ISS) Q61696 (/ISS) Q61696 (/ISS) |
Negative regulation of cell population proliferation GO:0008285
Any process that stops, prevents or reduces the rate or extent of cell proliferation.
|
6 | P0DMW0 (/ISS) P0DMW0 (/ISS) P0DMW1 (/ISS) P0DMW1 (/ISS) Q61696 (/ISS) Q61696 (/ISS) |
Negative regulation of cell growth GO:0030308
Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
|
6 | P0DMW0 (/ISS) P0DMW0 (/ISS) P0DMW1 (/ISS) P0DMW1 (/ISS) Q61696 (/ISS) Q61696 (/ISS) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
6 | P16474 (/IDA) P16474 (/IDA) P16474 (/IDA) P16474 (/IDA) P16474 (/IDA) P16474 (/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.
|
6 | P22202 (/IEP) P41797 (/IEP) 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.
|
6 | P0DMW0 (/IEP) P0DMW0 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) |
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) |
Fungal-type cell wall beta-glucan biosynthetic process GO:0070880
The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of fungal cells.
|
6 | P16474 (/IGI) P16474 (/IGI) P16474 (/IGI) P16474 (/IGI) P16474 (/IGI) P16474 (/IGI) |
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) |
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.
|
5 | O97125 (/ISS) P11146 (/ISS) P11147 (/ISS) P11147 (/ISS) P29843 (/ISS) |
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.
|
5 | Q26733 (/TAS) Q384Q5 (/TAS) Q384Q5 (/TAS) Q384Q5 (/TAS) Q384Q5 (/TAS) |
SRP-dependent cotranslational protein targeting to membrane GO:0006614
The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.
|
5 | Q26733 (/TAS) Q384Q5 (/TAS) Q384Q5 (/TAS) Q384Q5 (/TAS) Q384Q5 (/TAS) |
Male meiotic nuclear division GO:0007140
A cell cycle process by which the cell nucleus divides as part of a meiotic cell cycle in the male germline.
|
5 | P54652 (/TAS) P54652 (/TAS) P54652 (/TAS) P54652 (/TAS) P54652 (/TAS) |
Spermatid development GO:0007286
The process whose specific outcome is the progression of a spermatid over time, from its formation to the mature structure.
|
5 | P54652 (/TAS) P54652 (/TAS) P54652 (/TAS) P54652 (/TAS) P54652 (/TAS) |
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.
|
5 | B3VHV2 (/IDA) B6EAX2 (/IDA) P08106 (/IDA) P08106 (/IDA) Q7SX63 (/IDA) |
Response to organonitrogen compound GO:0010243
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 organonitrogen stimulus. An organonitrogen compound is formally a compound containing at least one carbon-nitrogen bond.
|
5 | B3VHV2 (/IDA) B6EAX2 (/IDA) P08106 (/IDA) P08106 (/IDA) Q7SX63 (/IDA) |
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.
|
5 | B3VHV2 (/IDA) B6EAX2 (/IDA) P08106 (/IDA) P08106 (/IDA) Q7SX63 (/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) |
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.
|
5 | B3VHV2 (/IDA) B6EAX2 (/IDA) P08106 (/IDA) P08106 (/IDA) Q7SX63 (/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) |
Blood vessel development GO:0001568
The process whose specific outcome is the progression of a blood vessel over time, from its formation to the mature structure. The blood vessel is the vasculature carrying blood.
|
4 | A8WFS0 (/IMP) B0S610 (/IMP) B7ZV46 (/IMP) Q8UUJ8 (/IMP) |
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 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.
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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 bacterium GO:0009617
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a bacterium.
|
4 | P22954 (/IEP) P22954 (/IEP) Q9LHA8 (/IEP) Q9LHA8 (/IEP) |
Response to metal ion GO:0010038
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 metal ion stimulus.
|
4 | A8WFS0 (/IDA) B0S610 (/IDA) B7ZV46 (/IDA) Q8UUJ8 (/IDA) |
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.
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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) |
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.
|
4 | P11147 (/IMP) P11147 (/IMP) P29844 (/IMP) P29844 (/IMP) |
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) |
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) |
Proteasome-mediated ubiquitin-dependent protein catabolic process GO:0043161
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
|
4 | P10591 (/IGI) P10591 (/IGI) P10591 (/IGI) P10592 (/IGI) |
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) |
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) |
Definitive hemopoiesis GO:0060216
A second wave of blood cell production that, in vertebrates, generates long-term hemopoietic stem cells that continously provide erythroid, myeloid and lymphoid lineages throughout adulthood.
|
4 | A8WFS0 (/IGI) B0S610 (/IGI) B7ZV46 (/IGI) Q8UUJ8 (/IGI) |
Definitive hemopoiesis GO:0060216
A second wave of blood cell production that, in vertebrates, generates long-term hemopoietic stem cells that continously provide erythroid, myeloid and lymphoid lineages throughout adulthood.
|
4 | A8WFS0 (/IMP) B0S610 (/IMP) B7ZV46 (/IMP) Q8UUJ8 (/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 (/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 | 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) |
Negative regulation of cell aging GO:0090344
Any process that decreases the rate, frequency, or extent of cell aging. Cell aging is the progression of the cell from its inception to the end of its lifespan.
|
4 | P10591 (/IMP) P10591 (/IMP) P10591 (/IMP) P10592 (/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 | 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) |
Protein polyubiquitination GO:0000209
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
|
3 | P10591 (/IDA) P10591 (/IDA) P10591 (/IDA) |
Positive regulation of protein phosphorylation GO:0001934
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein.
|
3 | P17156 (/IMP) P17156 (/IMP) P17156 (/IMP) |
Protein import into nucleus GO:0006606
The directed movement of a protein from the cytoplasm to the nucleus.
|
3 | P10591 (/IDA) P10591 (/IDA) P10591 (/IDA) |
Protein import into nucleus GO:0006606
The directed movement of a protein from the cytoplasm to the nucleus.
|
3 | P10591 (/IGI) P10591 (/IGI) P10591 (/IGI) |
SRP-dependent cotranslational protein targeting to membrane, translocation GO:0006616
The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
|
3 | P10591 (/IDA) P10591 (/IDA) P10591 (/IDA) |
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.
|
3 | P10591 (/IMP) P10591 (/IMP) P10591 (/IMP) |
Male meiotic nuclear division GO:0007140
A cell cycle process by which the cell nucleus divides as part of a meiotic cell cycle in the male germline.
|
3 | P17156 (/IMP) P17156 (/IMP) P17156 (/IMP) |
Male meiosis I GO:0007141
A cell cycle process comprising the steps by which a cell progresses through male meiosis I, the first meiotic division in the male germline.
|
3 | P17156 (/IMP) P17156 (/IMP) P17156 (/IMP) |
Spermatogenesis GO:0007283
The process of formation of spermatozoa, including spermatocytogenesis and spermiogenesis.
|
3 | P17156 (/IMP) P17156 (/IMP) P17156 (/IMP) |
Spermatid development GO:0007286
The process whose specific outcome is the progression of a spermatid over time, from its formation to the mature structure.
|
3 | P17156 (/IMP) P17156 (/IMP) P17156 (/IMP) |
Binding of sperm to zona pellucida GO:0007339
The process in which the sperm binds to the zona pellucida glycoprotein layer of the egg. The process begins with the attachment of the sperm plasma membrane to the zona pellucida and includes attachment of the acrosome inner membrane to the zona pellucida after the acrosomal reaction takes place.
|
3 | P16627 (/IDA) P16627 (/IDA) P17879 (/IDA) |
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.
|
3 | A0A1D5PFJ6 (/IEP) F1NWP3 (/IEP) O73885 (/IEP) |
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.
|
3 | P06761 (/IEP) P0DMW0 (/IEP) P0DMW0 (/IEP) |
Response to toxic substance GO:0009636
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 toxic stimulus.
|
3 | Q9BIR7 (/IEP) Q9BIR7 (/IEP) Q9BIR7 (/IEP) |
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.
|
3 | A0A1D5PFJ6 (/IEP) F1NWP3 (/IEP) O73885 (/IEP) |
Positive regulation of G2/M transition of mitotic cell cycle GO:0010971
Any signalling pathway that activates or increases the activity of a cell cycle cyclin-dependent protein kinase to modulate the switch from G2 phase to M phase of the mitotic cell cycle.
|
3 | P17156 (/IMP) P17156 (/IMP) P17156 (/IMP) |
Neuron differentiation GO:0030182
The process in which a relatively unspecialized cell acquires specialized features of a neuron.
|
3 | P06761 (/IEP) P0DMW0 (/IEP) P0DMW0 (/IEP) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
3 | O45246 (/HEP) P20163 (/HEP) P27420 (/HEP) |
Positive regulation of ATPase activity GO:0032781
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
|
3 | P17156 (/IMP) P17156 (/IMP) P17156 (/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.
|
3 | P17066 (/IMP) P17066 (/IMP) P41797 (/IMP) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
3 | P06761 (/IEP) Q39043 (/IEP) Q39043 (/IEP) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
3 | P20029 (/ISO) P20029 (/ISO) Q10284 (/ISO) |
Stress granule disassembly GO:0035617
The disaggregation of a stress granule into its constituent protein and RNA parts.
|
3 | P10591 (/IDA) P10591 (/IDA) P10591 (/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.
|
3 | P0DMW1 (/IDA) P0DMW1 (/IDA) P17879 (/IDA) |
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process GO:0043154
Any process that stops, prevents, or reduces the frequency, rate or extent of a cysteine-type endopeptidase activity involved in the apoptotic process.
|
3 | P0DMW1 (/IDA) P0DMW1 (/IDA) P17879 (/IDA) |
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process GO:0043154
Any process that stops, prevents, or reduces the frequency, rate or extent of a cysteine-type endopeptidase activity involved in the apoptotic process.
|
3 | G3I8R9 (/IMP) G3I8R9 (/IMP) G3I8R9 (/IMP) |
Proteasome-mediated ubiquitin-dependent protein catabolic process GO:0043161
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
|
3 | P10591 (/IMP) P10591 (/IMP) P10591 (/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.
|
3 | A0A1D5PFJ6 (/IEP) F1NWP3 (/IEP) O73885 (/IEP) |
Camera-type eye morphogenesis GO:0048593
The process in which the anatomical structures of the eye are generated and organized. The camera-type eye is an organ of sight that receives light through an aperture and focuses it through a lens, projecting it on a photoreceptor field.
|
3 | B0UXS6 (/IMP) Q6PH56 (/IMP) Q9IAC1 (/IMP) |
Synaptonemal complex disassembly GO:0070194
The controlled breakdown of a synaptonemal complex.
|
3 | P17156 (/IMP) P17156 (/IMP) P17156 (/IMP) |
Negative regulation of protein homodimerization activity GO:0090074
Any process that decreases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.
|
3 | G3I8R9 (/IDA) G3I8R9 (/IDA) G3I8R9 (/IDA) |
Negative regulation of inclusion body assembly GO:0090084
Any process that decreases the rate, frequency, or extent of inclusion body assembly. Inclusion body assembly is the aggregation, arrangement and bonding together of a set of components to form an inclusion body.
|
3 | P17156 (/ISO) P17156 (/ISO) P17156 (/ISO) |
Positive regulation of ATPase-coupled calcium transmembrane transporter activity GO:1901896
Any process that activates or increases the frequency, rate or extent of an ATPase-coupled calcium transmembrane transporter activity.
|
3 | P17156 (/IMP) P17156 (/IMP) P17156 (/IMP) |
Negative regulation of IRE1-mediated unfolded protein response GO:1903895
Any process that stops, prevents or reduces the frequency, rate or extent of the IRE1-mediated unfolded protein response.
|
3 | G3I8R9 (/IDA) G3I8R9 (/IDA) G3I8R9 (/IDA) |
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) |
Telomere maintenance GO:0000723
Any process that contributes to the maintenance of proper telomeric length and structure by affecting and monitoring the activity of telomeric proteins, the length of telomeric DNA and the replication and repair of the DNA. These processes includes those that shorten, lengthen, replicate and repair the telomeric DNA sequences.
|
2 | Q61696 (/IMP) Q61696 (/IMP) |
Response to hypoxia GO:0001666
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
|
2 | Q6P3L3 (/IDA) Q7SZD3 (/IDA) |
Response to yeast GO:0001878
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a yeast species.
|
2 | Q6P3L3 (/IDA) Q7SZD3 (/IDA) |
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.
|
2 | P0DMW1 (/IDA) P0DMW1 (/IDA) |
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.
|
2 | P0DMW0 (/IEP) P0DMW0 (/IEP) |
DNA repair GO:0006281
The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
|
2 | Q61696 (/IMP) Q61696 (/IMP) |
SRP-dependent cotranslational protein targeting to membrane, translocation GO:0006616
The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
|
2 | A0A1D8PG96 (/IGI) A0A1D8PG96 (/IGI) |
Defense response GO:0006952
Reactions, triggered in response to the presence of a foreign body or the occurrence of an injury, which result in restriction of damage to the organism attacked or prevention/recovery from the infection caused by the attack.
|
2 | P0DMW1 (/IDA) P0DMW1 (/IDA) |
ER overload response GO:0006983
The series of molecular signals generated by the accumulation of normal or misfolded proteins in the endoplasmic reticulum and leading to activation of transcription by NF-kappaB.
|
2 | P20029 (/IDA) P20029 (/IDA) |
Lysosomal transport GO:0007041
The directed movement of substances into, out of or within a lysosome.
|
2 | Q61696 (/IMP) Q61696 (/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 (/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) |
Determination of adult lifespan GO:0008340
The control of viability and duration in the adult phase of the life-cycle.
|
2 | O45246 (/IGI) P09446 (/IGI) |
Determination of adult lifespan GO:0008340
The control of viability and duration in the adult phase of the life-cycle.
|
2 | O97125 (/IMP) P09446 (/IMP) |
Response to temperature stimulus GO:0009266
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 temperature stimulus.
|
2 | Q9LHA8 (/IEP) Q9LHA8 (/IEP) |
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.
|
2 | P22953 (/IEP) P22953 (/IEP) |
Response to mechanical stimulus GO:0009612
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 mechanical stimulus.
|
2 | P0DMW0 (/IEP) P0DMW0 (/IEP) |
Response to toxic substance GO:0009636
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 toxic stimulus.
|
2 | P41797 (/IMP) P46587 (/IMP) |
Response to high light intensity GO:0009644
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 high light intensity stimulus.
|
2 | Q9LHA8 (/IEP) Q9LHA8 (/IEP) |
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.
|
2 | Q39043 (/IDA) Q39043 (/IDA) |
Negative regulation of seed germination GO:0010187
Any process that stops, prevents, or reduces the frequency, rate or extent of seed germination.
|
2 | P22953 (/IMP) P22953 (/IMP) |
Positive regulation of neuron projection development GO:0010976
Any process that increases the rate, frequency or extent of neuron projection development. Neuron projection development is the process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
|
2 | P20029 (/ISO) P20029 (/ISO) |
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) |
Protein ubiquitination GO:0016567
The process in which one or more ubiquitin groups are added to a protein.
|
2 | Q9LHA8 (/IMP) Q9LHA8 (/IMP) |
Antimicrobial humoral response GO:0019730
An immune response against microbes mediated through a body fluid. Examples of this process are seen in the antimicrobial humoral response of Drosophila melanogaster and Mus musculus.
|
2 | P41797 (/TAS) P46587 (/TAS) |
Cerebellum structural organization GO:0021589
The process that contributes to the act of creating the structural organization of the cerebellum. This process pertains to the physical shaping of a rudimentary structure. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. The cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
|
2 | P20029 (/IMP) P20029 (/IMP) |
Cerebellar Purkinje cell layer development GO:0021680
The process whose specific outcome is the progression of the cerebellar Purkinje cell layer over time, from its formation to the mature structure. The Purkinje cell layer lies just underneath the molecular layer of the cerebellar cortex. It contains the neuronal cell bodies of the Purkinje cells that are arranged side by side in a single layer. Candelabrum interneurons are vertically oriented between the Purkinje cells. Purkinje neurons are inhibitory and provide the output of the cerebellar cortex through axons that project into the white matter. Extensive dendritic trees from the Purkinje cells extend upward in a single plane into the molecular layer where they synapse with parallel fibers of granule cells.
|
2 | P20029 (/IMP) P20029 (/IMP) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Sleep GO:0030431
Any process in which an organism enters and maintains a periodic, readily reversible state of reduced awareness and metabolic activity. Usually accompanied by physical relaxation, the onset of sleep in humans and other mammals is marked by a change in the electrical activity of the brain.
|
2 | P29844 (/TAS) P29844 (/TAS) |
Negative regulation of transforming growth factor beta receptor signaling pathway GO:0030512
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
|
2 | P20029 (/IGI) P20029 (/IGI) |
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) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
2 | P20163 (/IEP) P27420 (/IEP) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
2 | P20029 (/IMP) P20029 (/IMP) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Positive regulation of protein ubiquitination GO:0031398
Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein.
|
2 | P20029 (/IMP) P20029 (/IMP) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
2 | P29844 (/IMP) P29844 (/IMP) |
Maintenance of protein localization in endoplasmic reticulum GO:0035437
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
|
2 | P20029 (/ISO) P20029 (/ISO) |
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) |
Intestinal stem cell homeostasis GO:0036335
Any biological process involved in the maintenance of the steady-state number of intestinal stem cells within a population of cells.
|
2 | P29844 (/IMP) P29844 (/IMP) |
Positive regulation of embryonic development GO:0040019
Any process that activates or increases the frequency, rate or extent of embryonic development.
|
2 | P20029 (/TAS) P20029 (/TAS) |
Cellular response to glucose starvation GO:0042149
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 glucose.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Response to hydrogen peroxide GO:0042542
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.
|
2 | Q9LHA8 (/IEP) Q9LHA8 (/IEP) |
Defense response to bacterium GO:0042742
Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.
|
2 | P22953 (/IMP) P22953 (/IMP) |
Negative regulation of apoptotic process GO:0043066
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Positive regulation of neuron differentiation GO:0045666
Any process that activates or increases the frequency, rate or extent of neuron differentiation.
|
2 | P0DMW0 (/IMP) P0DMW0 (/IMP) |
Negative regulation of vasoconstriction GO:0045906
Any process that stops, prevents, or reduces the frequency, rate or extent of vasoconstriction.
|
2 | P0DMW1 (/IMP) P0DMW1 (/IMP) |
Defense response to fungus GO:0050832
Reactions triggered in response to the presence of a fungus that act to protect the cell or organism.
|
2 | P22953 (/IMP) P22953 (/IMP) |
Proteolysis involved in cellular protein catabolic process GO:0051603
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
|
2 | P20029 (/IDA) P20029 (/IDA) |
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) |
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.
|
2 | O59855 (/NAS) Q10284 (/NAS) |
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) |
Cellular response to interleukin-4 GO:0071353
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-4 stimulus.
|
2 | P20029 (/IDA) P20029 (/IDA) |
Response to karrikin GO:0080167
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 karrikin stimulus. Karrikins are signaling molecules in smoke from burning vegetation that trigger seed germination for many angiosperms (flowering plants).
|
2 | O65719 (/IEP) O65719 (/IEP) |
Stomatal closure GO:0090332
The process of closing of stomata, pores in the epidermis of leaves and stems bordered by two guard cells and serving in gas exchange.
|
2 | P22953 (/IMP) P22953 (/IMP) |
Defense response to other organism GO:0098542
Reactions triggered in response to the presence of another organism that act to protect the cell or organism from damage caused by that organism.
|
2 | P22953 (/IMP) P22953 (/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) |
Toxin transport GO:1901998
The directed movement of a toxin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
|
2 | P20029 (/IMP) P20029 (/IMP) |
Positive regulation of protein targeting to mitochondrion GO:1903955
Any process that activates or increases the frequency, rate or extent of protein targeting to mitochondrion.
|
2 | P34931 (/IMP) P34931 (/IMP) |
Positive regulation of protein targeting to mitochondrion GO:1903955
Any process that activates or increases the frequency, rate or extent of protein targeting to mitochondrion.
|
2 | P16627 (/ISO) P16627 (/ISO) |
Luteolysis GO:0001554
The lysis or structural demise of the corpus luteum. During normal luteolysis, two closely related events occur. First, there is loss of the capacity to synthesize and secrete progesterone (functional luteolysis) followed by loss of the cells that comprise the corpus luteum (structural luteolysis). Preventing luteolysis is crucial to maintain pregnancy.
|
1 | P06761 (/IEP) |
Cytoplasmic translation GO:0002181
The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein.
|
1 | Q10265 (/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.
|
1 | P10592 (/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 | P11145 (/ISM) |
Response to xenobiotic stimulus GO:0009410
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 xenobiotic compound stimulus. Xenobiotic compounds are compounds foreign to living organisms.
|
1 | B0UXS6 (/IDA) |
Response to bacterium GO:0009617
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a bacterium.
|
1 | Q557E0 (/HEP) |
Pollen tube growth GO:0009860
Growth of pollen via tip extension of the intine wall.
|
1 | Q8H1B3 (/IEP) |
Positive regulation of neuron projection development GO:0010976
Any process that increases the rate, frequency or extent of neuron projection development. Neuron projection development is the process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
|
1 | P06761 (/IMP) |
Peptide transport GO:0015833
The directed movement of peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
|
1 | P46587 (/IMP) |
Entry into host cell GO:0030260
The invasion by an organism of a cell of its host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
|
1 | P41797 (/IMP) |
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
|
1 | P36604 (/ISO) |
Fin regeneration GO:0031101
The regrowth of fin tissue following its loss or destruction.
|
1 | Q90473 (/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.
|
1 | Q7SX63 (/ISS) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
1 | P06761 (/IDA) |
Cellular response to drug GO:0035690
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 drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
|
1 | P06761 (/IEP) |
TRNA import into nucleus GO:0035719
The directed movement of tRNA from the cytoplasm to the nucleus.
|
1 | P10592 (/IMP) |
IRE1-mediated unfolded protein response GO:0036498
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
|
1 | P36604 (/IMP) |
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) |
Retrograde transport, endosome to Golgi GO:0042147
The directed movement of membrane-bounded vesicles from endosomes back to the trans-Golgi network where they are recycled for further rounds of transport.
|
1 | P09446 (/IMP) |
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.
|
1 | P06761 (/IEP) |
Ribosome biogenesis GO:0042254
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of ribosome subunits; includes transport to the sites of protein synthesis.
|
1 | Q10284 (/ISO) |
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.
|
1 | O97125 (/IMP) |
Induction by symbiont of host defense response GO:0044416
The activation by an organism of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
|
1 | P41797 (/IDA) |
ATP metabolic process GO:0046034
The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator.
|
1 | Q7SX63 (/ISS) |
Response to mercury ion GO:0046689
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 mercury ion stimulus.
|
1 | Q8T869 (/IDA) |
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) |
'de novo' cotranslational protein folding GO:0051083
The process of assisting in the correct noncovalent assembly of the ribosome-bound nascent chains of a multidomain protein whilst other parts of the protein are still being translated.
|
1 | Q10284 (/ISO) |
Neuron apoptotic process GO:0051402
Any apoptotic process in a neuron, the basic cellular unit of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the nervous system.
|
1 | P06761 (/IEP) |
Interaction with host GO:0051701
An interaction between two organisms living together in more or less intimate association. The term host is used for the larger (macro) of the two members of a symbiosis; the various forms of symbiosis include parasitism, commensalism and mutualism.
|
1 | P41797 (/IDA) |
Cellular response to antibiotic GO:0071236
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 antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
|
1 | P06761 (/IEP) |
Cellular response to calcium ion GO:0071277
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 calcium ion stimulus.
|
1 | P06761 (/IEP) |
Cellular response to manganese ion GO:0071287
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 manganese ion stimulus.
|
1 | P06761 (/IEP) |
Cellular response to cAMP GO:0071320
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 cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus.
|
1 | P06761 (/IEP) |
Cellular response to interferon-gamma GO:0071346
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 interferon-gamma stimulus. Interferon gamma is the only member of the type II interferon found so far.
|
1 | B5X397 (/IMP) |
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 | Q5B2V1 (/IEP) |
Cellular response to gamma radiation GO:0071480
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gamma radiation stimulus. Gamma radiation is a form of electromagnetic radiation (EMR) or light emission of a specific frequency produced from sub-atomic particle interaction, such as electron-positron annihilation and radioactive decay. Gamma rays are generally characterized as EMR having the highest frequency and energy, and also the shortest wavelength, within the electromagnetic radiation spectrum.
|
1 | P06761 (/IEP) |
Cellular response to farnesol GO:0097308
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 farnesol stimulus.
|
1 | Q5B2V1 (/IEP) |
Stress response to metal ion GO:0097501
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 disturbance in organismal or cellular homeostasis caused by a metal ion stimulus.
|
1 | P06761 (/IEP) |
Negative regulation of cellular response to heat GO:1900035
Any process that stops, prevents or reduces the frequency, rate or extent of cellular response to heat.
|
1 | O59855 (/IMP) |
Negative regulation of supramolecular fiber organization GO:1902904
Any process that stops, prevents or reduces the frequency, rate or extent of fibril organization.
|
1 | Q7SX63 (/ISS) |
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) |
Response to methamphetamine hydrochloride GO:1904313
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 methamphetamine hydrochloride stimulus.
|
1 | P06761 (/IEP) |
Cellular response to nerve growth factor stimulus GO:1990090
A 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 nerve growth factor stimulus.
|
1 | P06761 (/IEP) |
There are 219 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.
|
114 |
B3VHV2 (/IDA)
B6EAX2 (/IDA)
O65719 (/IDA)
O65719 (/IDA)
P08106 (/IDA)
P08106 (/IDA)
P09435 (/IDA)
P09435 (/IDA)
P09435 (/IDA)
P09435 (/IDA)
(104 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.
|
97 |
B3VHV2 (/IDA)
B6EAX2 (/IDA)
O59855 (/IDA)
P08106 (/IDA)
P08106 (/IDA)
P08108 (/IDA)
P08108 (/IDA)
P08108 (/IDA)
P09446 (/IDA)
P0DMV8 (/IDA)
(87 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
88 |
O59855 (/IDA)
P06761 (/IDA)
P08106 (/IDA)
P08106 (/IDA)
P08108 (/IDA)
P08108 (/IDA)
P08108 (/IDA)
P09446 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
(78 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.
|
74 |
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV9 (/HDA)
(64 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.
|
73 |
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
(63 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.
|
66 |
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV9 (/HDA)
(56 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.
|
61 |
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV9 (/HDA)
(51 more) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
57 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(47 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.
|
56 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(46 more) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
55 |
B9RYP6 (/IDA)
P06761 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(45 more) |
Ficolin-1-rich granule lumen GO:1904813
Any membrane-enclosed lumen that is part of a ficolin-1-rich granule.
|
54 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(44 more) |
Ribonucleoprotein complex GO:1990904
A macromolecular complex containing both protein and RNA molecules.
|
54 |
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
(44 more) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
53 |
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
(43 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.
|
52 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(42 more) |
Ribonucleoprotein complex GO:1990904
A macromolecular complex containing both protein and RNA molecules.
|
52 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(42 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.
|
50 |
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
A2Q0Z1 (/ISS)
(40 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.
|
43 |
B5X397 (/IDA)
P11142 (/IDA)
P11142 (/IDA)
P11142 (/IDA)
P11142 (/IDA)
P11142 (/IDA)
P11142 (/IDA)
P11142 (/IDA)
P11142 (/IDA)
P11142 (/IDA)
(33 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) |
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.
|
38 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(28 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.
|
36 |
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
(26 more) |
Secretory granule lumen GO:0034774
The volume enclosed by the membrane of a secretory granule.
|
36 |
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
P11142 (/TAS)
(26 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 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) |
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) |
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) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
33 |
P06761 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
(23 more) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
30 |
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
P59769 (/NAS)
(20 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
29 |
A8WFS0 (/ISS)
B0S610 (/ISS)
B0UXR9 (/ISS)
B0UXS6 (/ISS)
B5B0I3 (/ISS)
B5X4Z3 (/ISS)
B6VAH2 (/ISS)
B6VAH2 (/ISS)
B6VD00 (/ISS)
B6VD00 (/ISS)
(19 more) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
29 |
G3I8R9 (/IDA)
G3I8R9 (/IDA)
G3I8R9 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
(19 more) |
Centrosome GO:0005813
A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
|
27 |
P0DMW0 (/ISS)
P0DMW0 (/ISS)
P0DMW1 (/ISS)
P0DMW1 (/ISS)
P17879 (/ISS)
P34930 (/ISS)
Q27965 (/ISS)
Q27965 (/ISS)
Q27975 (/ISS)
Q27975 (/ISS)
(17 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.
|
25 |
O59855 (/HDA)
P10591 (/HDA)
P10591 (/HDA)
P10591 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
P11021 (/HDA)
(15 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.
|
20 |
P06761 (/IDA)
P10592 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(10 more) |
Centriole GO:0005814
A cellular organelle, found close to the nucleus in many eukaryotic cells, consisting of a small cylinder with microtubular walls, 300-500 nm long and 150-250 nm in diameter. It contains nine short, parallel, peripheral microtubular fibrils, each fibril consisting of one complete microtubule fused to two incomplete microtubules. Cells usually have two centrioles, lying at right angles to each other. At division, each pair of centrioles generates another pair and the twin pairs form the pole of the mitotic spindle.
|
20 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(10 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.
|
19 |
G3I8R9 (/ISS)
G3I8R9 (/ISS)
G3I8R9 (/ISS)
O97125 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P11146 (/ISS)
P11147 (/ISS)
P11147 (/ISS)
(9 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
18 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(8 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.
|
18 |
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV8 (/TAS)
P0DMV9 (/TAS)
(8 more) |
Centrosome GO:0005813
A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
|
18 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(8 more) |
Inclusion body GO:0016234
A discrete intracellular part formed of aggregated molecules such as proteins or other biopolymers.
|
18 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(8 more) |
Aggresome GO:0016235
An inclusion body formed by dynein-dependent retrograde transport of an aggregated protein on microtubules.
|
18 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(8 more) |
Nuclear speck GO:0016607
A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
|
18 |
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV8 (/IDA)
P0DMV9 (/IDA)
(8 more) |
Vesicle GO:0031982
Any small, fluid-filled, spherical organelle enclosed by membrane.
|
18 |
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV8 (/HDA)
P0DMV9 (/HDA)
(8 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.
|
17 |
O65719 (/IDA)
O65719 (/IDA)
P20029 (/IDA)
P20029 (/IDA)
P22953 (/IDA)
P22953 (/IDA)
P22954 (/IDA)
P22954 (/IDA)
P41797 (/IDA)
P46587 (/IDA)
(7 more) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
17 |
P06761 (/IDA)
P08108 (/IDA)
P08108 (/IDA)
P08108 (/IDA)
P22953 (/IDA)
P22953 (/IDA)
P46587 (/IDA)
Q39043 (/IDA)
Q39043 (/IDA)
Q5DW63 (/IDA)
(7 more) |
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
17 |
G3I8R9 (/IDA)
G3I8R9 (/IDA)
G3I8R9 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(7 more) |
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.
|
17 |
P07823 (/IDA)
P07823 (/IDA)
P07823 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(7 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.
|
16 |
A0PA16 (/IDA)
A0PA16 (/IDA)
A0PA16 (/IDA)
A0PA16 (/IDA)
A0PA16 (/IDA)
B3VHV2 (/IDA)
B6EAX2 (/IDA)
P08106 (/IDA)
P08106 (/IDA)
P08108 (/IDA)
(6 more) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
16 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(6 more) |
Endoplasmic reticulum-Golgi intermediate compartment GO:0005793
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
|
16 |
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(6 more) |
Endoplasmic reticulum chaperone complex GO:0034663
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
|
16 |
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(6 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.
|
15 |
O73885 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(5 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 |
O65719 (/IDA)
O65719 (/IDA)
P22953 (/IDA)
P22953 (/IDA)
P22954 (/IDA)
P22954 (/IDA)
Q00043 (/IDA)
Q39043 (/IDA)
Q39043 (/IDA)
Q9LHA8 (/IDA)
(4 more) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
14 |
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
P11021 (/IMP)
(4 more) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
14 |
G3I8R9 (/IDA)
G3I8R9 (/IDA)
G3I8R9 (/IDA)
P20029 (/IDA)
P20029 (/IDA)
P36604 (/IDA)
Q6Z7B0 (/IDA)
Q6Z7B0 (/IDA)
Q6Z7B0 (/IDA)
Q6Z7B0 (/IDA)
(4 more) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
14 |
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
P11021 (/TAS)
(4 more) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
14 |
A0A1D8PG96 (/IDA)
A0A1D8PG96 (/IDA)
G8BEU5 (/IDA)
P17156 (/IDA)
P17156 (/IDA)
P17156 (/IDA)
P20029 (/IDA)
P20029 (/IDA)
P41797 (/IDA)
P46587 (/IDA)
(4 more) |
Midbody GO:0030496
A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis.
|
14 |
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
P11021 (/IDA)
(4 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.
|
13 |
P16627 (/ISO)
P16627 (/ISO)
P17156 (/ISO)
P17156 (/ISO)
P17156 (/ISO)
P20029 (/ISO)
P20029 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
P63017 (/ISO)
(3 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.
|
13 |
G3I8R9 (/ISS)
G3I8R9 (/ISS)
G3I8R9 (/ISS)
P06761 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P07823 (/ISS)
P20029 (/ISS)
P20029 (/ISS)
Q0VCX2 (/ISS)
(3 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.
|
12 |
A0A1D8PG96 (/IDA)
A0A1D8PG96 (/IDA)
Q2UBH7 (/IDA)
Q2UBH7 (/IDA)
Q2UBH7 (/IDA)
Q2UBH7 (/IDA)
Q2UBH7 (/IDA)
Q2UBH7 (/IDA)
Q2UBH7 (/IDA)
Q5B2V1 (/IDA)
(2 more) |
Polysome GO:0005844
A multiribosomal structure representing a linear array of ribosomes held together by messenger RNA. They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro.
|
12 |
P10591 (/IDA)
P10591 (/IDA)
P10591 (/IDA)
P10592 (/IDA)
P11484 (/IDA)
P11484 (/IDA)
P11484 (/IDA)
P11484 (/IDA)
P11484 (/IDA)
P11484 (/IDA)
(2 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.
|
12 |
P10591 (/HDA)
P10591 (/HDA)
P10591 (/HDA)
P10592 (/HDA)
P11484 (/HDA)
P11484 (/HDA)
P11484 (/HDA)
P11484 (/HDA)
P11484 (/HDA)
P11484 (/HDA)
(2 more) |
CatSper complex GO:0036128
A sperm-specific voltage-gated calcium channel that controls the intracellular calcium ion concentration and, thereby, the swimming behavior of sperm. Consists of a heteromeric tetramer surrounding a calcium ion- selective pore. May also contain additional auxiliary subunits.
|
10 | P14659 (/ISS) P14659 (/ISS) P14659 (/ISS) P34933 (/ISS) P54652 (/ISS) P54652 (/ISS) P54652 (/ISS) P54652 (/ISS) P54652 (/ISS) Q9TUG3 (/ISS) |
Meiotic spindle GO:0072687
A spindle that forms as part of meiosis. Several proteins, such as budding yeast Spo21p, fission yeast Spo2 and Spo13, and C. elegans mei-1, localize specifically to the meiotic spindle and are absent from the mitotic spindle.
|
10 | P14659 (/ISS) P14659 (/ISS) P14659 (/ISS) P34933 (/ISS) P54652 (/ISS) P54652 (/ISS) P54652 (/ISS) P54652 (/ISS) P54652 (/ISS) Q9TUG3 (/ISS) |
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
|
9 | O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA) Q39043 (/IDA) Q39043 (/IDA) Q9LHA8 (/IDA) Q9LHA8 (/IDA) Q9LKR3 (/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.
|
9 | O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA) P22954 (/IDA) P22954 (/IDA) Q9LHA8 (/IDA) Q9LHA8 (/IDA) Q9LKR3 (/IDA) |
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
|
9 | B3VHV2 (/IDA) B6EAX2 (/IDA) P08106 (/IDA) P08106 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) Q7SX63 (/IDA) |
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.
|
9 | P17156 (/HDA) P17156 (/HDA) P17156 (/HDA) P20029 (/HDA) P20029 (/HDA) P63017 (/HDA) P63017 (/HDA) P63017 (/HDA) P63017 (/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.
|
8 | P20029 (/ISO) P20029 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
8 | P20029 (/ISO) P20029 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
|
8 | O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA) Q9C7X7 (/IDA) Q9LKR3 (/IDA) Q9S9N1 (/IDA) Q9S9N1 (/IDA) |
Plant-type vacuole membrane GO:0009705
The lipid bilayer surrounding a vacuole that retains the same shape regardless of cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this component is found in Arabidopsis thaliana.
|
8 | Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/IDA) Q6Z7B0 (/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.
|
8 | P20029 (/ISO) P20029 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/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.
|
8 | P0DMW0 (/IDA) P0DMW0 (/IDA) P0DMW1 (/IDA) P0DMW1 (/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) |
Plasmodesma GO:0009506
A fine cytoplasmic channel, found in all higher plants, that connects the cytoplasm of one cell to that of an adjacent cell.
|
7 | O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA) Q39043 (/IDA) Q39043 (/IDA) Q9LKR3 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
6 | P10591 (/HDA) P10591 (/HDA) P10591 (/HDA) P11147 (/HDA) P11147 (/HDA) P40150 (/HDA) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
6 | O59855 (/HDA) P10591 (/HDA) P10591 (/HDA) P10591 (/HDA) Q10265 (/HDA) Q10284 (/HDA) |
Fungal-type cell wall GO:0009277
A rigid yet dynamic structure surrounding the plasma membrane that affords protection from stresses and contributes to cell morphogenesis, consisting of extensively cross-linked glycoproteins and carbohydrates. The glycoproteins may be modified with N- or O-linked carbohydrates, or glycosylphosphatidylinositol (GPI) anchors; the polysaccharides are primarily branched glucans, including beta-linked and alpha-linked glucans, and may also include chitin and other carbohydrate polymers, but not cellulose or pectin. Enzymes involved in cell wall biosynthesis are also found in the cell wall. Note that some forms of fungi develop a capsule outside of the cell wall under certain circumstances; this is considered a separate structure.
|
6 | P10591 (/IDA) P10591 (/IDA) P10591 (/IDA) P10592 (/IDA) P41797 (/IDA) P46587 (/IDA) |
Nuclear speck GO:0016607
A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
|
6 | P0DMW0 (/ISS) P0DMW0 (/ISS) P0DMW1 (/ISS) P0DMW1 (/ISS) Q61696 (/ISS) Q61696 (/ISS) |
Luminal surveillance complex GO:0034099
A multiprotein complex that recognizes ERAD-luminal misfolded substrates and brings them to the ubiquitination/extraction machinery. In yeast, this complex consists of Yos9p, Kar2p and Hrd3p proteins.
|
6 | P16474 (/IDA) P16474 (/IDA) P16474 (/IDA) P16474 (/IDA) P16474 (/IDA) P16474 (/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.
|
6 | P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
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.
|
6 | O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA) Q9LHA8 (/IDA) Q9LHA8 (/IDA) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
6 | P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
6 | P0DMW0 (/ISS) P0DMW0 (/ISS) P0DMW1 (/ISS) P0DMW1 (/ISS) Q61696 (/ISS) Q61696 (/ISS) |
Ribonucleoprotein complex GO:1990904
A macromolecular complex containing both protein and RNA molecules.
|
6 | P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO) |
Vacuole GO:0005773
A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol.
|
5 | O65719 (/IDA) O65719 (/IDA) Q39043 (/IDA) Q39043 (/IDA) Q9LKR3 (/IDA) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
5 | Q26733 (/EXP) Q384Q5 (/EXP) Q384Q5 (/EXP) Q384Q5 (/EXP) Q384Q5 (/EXP) |
Receptor complex GO:0043235
Any protein complex that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
|
5 | B3VHV2 (/IDA) B6EAX2 (/IDA) P08106 (/IDA) P08106 (/IDA) Q7SX63 (/IDA) |
Fungal-type vacuole membrane GO:0000329
The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae.
|
4 | P10591 (/IDA) P10591 (/IDA) P10591 (/IDA) P10592 (/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) |
Nucleolus GO:0005730
A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
|
4 | P22953 (/IDA) P22953 (/IDA) Q39043 (/IDA) Q39043 (/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.
|
4 | P10592 (/HDA) P17156 (/HDA) P17156 (/HDA) P17156 (/HDA) |
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) |
Lipid droplet GO:0005811
An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.
|
4 | P36415 (/HDA) Q54BE0 (/HDA) Q557E0 (/HDA) Q8T869 (/HDA) |
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 | 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) |
Mediator complex GO:0016592
A protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The mediator complex is required for activation of transcription of most protein-coding genes, but can also act as a transcriptional corepressor. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins.
|
4 | Q39043 (/IDA) Q39043 (/IDA) Q8H1B3 (/IDA) Q9LKR3 (/IDA) |
Cytosolic ribosome GO:0022626
A ribosome located in the cytosol.
|
4 | O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/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 | 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) |
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 | P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) |
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) |
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) |
Synaptonemal complex GO:0000795
A proteinaceous scaffold found between homologous chromosomes during meiosis. It consists of 2 lateral elements and a central element, all running parallel to each other. Transverse filaments connect the lateral elements to the central element.
|
3 | P17156 (/IDA) P17156 (/IDA) P17156 (/IDA) |
Male germ cell nucleus GO:0001673
The nucleus of a male germ cell, a reproductive cell in males.
|
3 | P17156 (/IDA) P17156 (/IDA) P17156 (/IDA) |
Zona pellucida receptor complex GO:0002199
A multisubunit complex comprising the chaperonin-containing T-complex and several other components involved in mediating sperm-oocyte Interaction.
|
3 | P16627 (/IDA) P16627 (/IDA) P17879 (/IDA) |
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) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
3 | P20029 (/ISO) P20029 (/ISO) Q4Q8E6 (/ISO) |
CatSper complex GO:0036128
A sperm-specific voltage-gated calcium channel that controls the intracellular calcium ion concentration and, thereby, the swimming behavior of sperm. Consists of a heteromeric tetramer surrounding a calcium ion- selective pore. May also contain additional auxiliary subunits.
|
3 | P17156 (/IDA) P17156 (/IDA) P17156 (/IDA) |
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
3 | Q0VCX2 (/ISS) Q3S4T7 (/ISS) Q5R4P0 (/ISS) |
Cell body GO:0044297
The portion of a cell bearing surface projections such as axons, dendrites, cilia, or flagella that includes the nucleus, but excludes all cell projections.
|
3 | P16627 (/IDA) P16627 (/IDA) P17879 (/IDA) |
Phagocytic vesicle GO:0045335
A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
|
3 | P36415 (/HDA) Q557E0 (/HDA) Q8T869 (/HDA) |
Meiotic spindle GO:0072687
A spindle that forms as part of meiosis. Several proteins, such as budding yeast Spo21p, fission yeast Spo2 and Spo13, and C. elegans mei-1, localize specifically to the meiotic spindle and are absent from the mitotic spindle.
|
3 | P17156 (/IDA) P17156 (/IDA) P17156 (/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.
|
2 | P29844 (/IDA) P29844 (/IDA) |
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) |
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 | P20029 (/ISO) P20029 (/ISO) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
2 | P29844 (/NAS) P29844 (/NAS) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
2 | P20029 (/IDA) P20029 (/IDA) |
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Endoplasmic reticulum-Golgi intermediate compartment GO:0005793
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Centrosome GO:0005813
A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Centriole GO:0005814
A cellular organelle, found close to the nucleus in many eukaryotic cells, consisting of a small cylinder with microtubular walls, 300-500 nm long and 150-250 nm in diameter. It contains nine short, parallel, peripheral microtubular fibrils, each fibril consisting of one complete microtubule fused to two incomplete microtubules. Cells usually have two centrioles, lying at right angles to each other. At division, each pair of centrioles generates another pair and the twin pairs form the pole of the mitotic spindle.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Endomembrane system GO:0012505
A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
|
2 | P29844 (/HDA) P29844 (/HDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Inclusion body GO:0016234
A discrete intracellular part formed of aggregated molecules such as proteins or other biopolymers.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Aggresome GO:0016235
An inclusion body formed by dynein-dependent retrograde transport of an aggregated protein on microtubules.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Basolateral plasma membrane GO:0016323
The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis.
|
2 | P0DMW1 (/IDA) P0DMW1 (/IDA) |
Basolateral plasma membrane GO:0016323
The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Apical plasma membrane GO:0016324
The region of the plasma membrane located at the apical end of the cell.
|
2 | P0DMW1 (/IDA) P0DMW1 (/IDA) |
Apical plasma membrane GO:0016324
The region of the plasma membrane located at the apical end of the cell.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Nuclear matrix GO:0016363
The dense fibrillar network lying on the inner side of the nuclear membrane.
|
2 | O65719 (/IDA) O65719 (/IDA) |
Nuclear speck GO:0016607
A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
|
2 | Q61696 (/ISO) Q61696 (/ISO) |
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Hyphal cell wall GO:0030446
The cell wall surrounding a fungal hypha.
|
2 | P41797 (/IDA) P46587 (/IDA) |
Midbody GO:0030496
A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Endoplasmic reticulum chaperone complex GO:0034663
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Endoplasmic reticulum chaperone complex GO:0034663
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
|
2 | P20163 (/ISS) P27420 (/ISS) |
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
2 | P20029 (/ISO) P20029 (/ISO) |
Fungal biofilm matrix GO:0062040
An extracellular matrix lying external to fungal cells. The fungal biofilm matrix consists of polysaccharides, proteins, lipids, and nucleic acids. Fungal biofilms mediate adherence to host tissues, and provide protection from host immune defenses.
|
2 | P41797 (/IDA) P46587 (/IDA) |
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) |
Ubiquitin ligase complex GO:0000151
A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex.
|
1 | Q7SX63 (/ISS) |
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
|
1 | Q7SX63 (/ISS) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | O73885 (/IMP) |
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.
|
1 | P55063 (/IDA) |
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.
|
1 | P17879 (/ISO) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
1 | P36604 (/HDA) |
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
|
1 | P06761 (/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.
|
1 | P20163 (/IDA) |
Chaperonin-containing T-complex GO:0005832
A multisubunit ring-shaped complex that mediates protein folding in the cytosol without a cofactor.
|
1 | O45246 (/IDA) |
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.
|
1 | Q7SX63 (/ISS) |
Chloroplast envelope GO:0009941
The double lipid bilayer enclosing the chloroplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
|
1 | Q9C7X7 (/IDA) |
Cytoplasmic stress granule GO:0010494
A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress.
|
1 | P40150 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | Q7SX63 (/ISS) |
Glycosome GO:0020015
A membrane-bounded organelle found in organisms from the order Kinetoplastida that houses the enzymes of glycolysis.
|
1 | P11145 (/IDA) |
Yeast-form cell wall GO:0030445
The wall surrounding a cell of a dimorphic fungus growing in the single-cell budding yeast form, in contrast to the filamentous or hyphal form.
|
1 | P41797 (/IDA) |
Extracellular matrix GO:0031012
A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
|
1 | P36415 (/HDA) |
Nuclear membrane GO:0031965
Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
|
1 | P36604 (/IDA) |
Vesicle GO:0031982
Any small, fluid-filled, spherical organelle enclosed by membrane.
|
1 | P36415 (/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.
|
1 | Q7SX63 (/ISS) |
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 | O59855 (/IDA) |
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.
|
1 | Q7SX63 (/ISS) |
Perinuclear endoplasmic reticulum lumen GO:0099020
The volume enclosed by the membranes of the perinuclear endoplasmic reticulum.
|
1 | P36604 (/IDA) |
Cortical endoplasmic reticulum lumen GO:0099021
The volume enclosed by the membranes of the cortical endoplasmic reticulum.
|
1 | P36604 (/IDA) |