CATH Superfamily 3.30.30.30

FunFam 1: heat shock 70 kDa protein-like

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 90 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).	127	C8Z3H3 (/IPI) O59855 (/IPI) O65719 (/IPI) O65719 (/IPI) P08106 (/IPI) P08106 (/IPI) P09446 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) (117 more)
Unfolded protein binding GO:0051082 Interacting selectively and non-covalently with an unfolded protein.	70	P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV9 (/IDA) (60 more)
ATPase activity GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.	66	P09446 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) (56 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)
Enzyme binding GO:0019899 Interacting selectively and non-covalently with any enzyme.	63	P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV9 (/IPI) (53 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)
Ubiquitin protein ligase binding GO:0031625 Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.	56	P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV8 (/IPI) P0DMV9 (/IPI) (46 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)
Cadherin binding GO:0045296 Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.	43	P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P11142 (/HDA) (33 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)
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)
Unfolded protein binding GO:0051082 Interacting selectively and non-covalently with an unfolded protein.	23	P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV9 (/TAS) (13 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)
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)
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)
ATP binding GO:0005524 Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.	15	P59769 (/NAS) P59769 (/NAS) P59769 (/NAS) P59769 (/NAS) P59769 (/NAS) P59769 (/NAS) P59769 (/NAS) P59769 (/NAS) P59769 (/NAS) P59769 (/NAS) (5 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)
Unfolded protein binding GO:0051082 Interacting selectively and non-covalently with an unfolded protein.	13	O59855 (/ISO) P16627 (/ISO) P16627 (/ISO) P17156 (/ISO) P17156 (/ISO) P17156 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) (3 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)
ATPase activity GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.	10	P09435 (/ISS) P09435 (/ISS) P09435 (/ISS) P09435 (/ISS) P09435 (/ISS) P09435 (/ISS) P09435 (/ISS) P10592 (/ISS) P22202 (/ISS) Q7SX63 (/ISS)
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)
Enzyme binding GO:0019899 Interacting selectively and non-covalently with any enzyme.	9	P17156 (/ISO) P17156 (/ISO) P17156 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO)
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)
ATPase activity GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.	8	O59855 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q10265 (/ISO) Q61696 (/ISO) Q61696 (/ISO)
Heat shock protein binding GO:0031072 Interacting selectively and non-covalently with a heat shock protein, any protein synthesized or activated in response to heat shock.	8	P16627 (/ISO) P16627 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO)
Ubiquitin protein ligase binding GO:0031625 Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.	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)
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)
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)
Unfolded protein binding GO:0051082 Interacting selectively and non-covalently with an unfolded protein.	4	P63017 (/IPI) P63017 (/IPI) P63017 (/IPI) P63017 (/IPI)
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)
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)
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)
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	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 283 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.	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 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.	126	A0A024R6B5 (/ISS) A0A024R6B5 (/ISS) A0A024R6B5 (/ISS) A0A024R6B5 (/ISS) A0A024R6B5 (/ISS) A0A061I5U1 (/ISS) A0A087QQM7 (/ISS) A0A087QQM7 (/ISS) A0A087QQM7 (/ISS) A0A087V8L3 (/ISS) (116 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)
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)
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)
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)
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)
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.	22	A0A0R4IJ78 (/IDA) A8WFS0 (/IDA) B0S610 (/IDA) B0UXS6 (/IDA) B3VHV2 (/IDA) B6EAX2 (/IDA) B7ZV46 (/IDA) C1BEL8 (/IDA) P08106 (/IDA) P08106 (/IDA) (12 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.	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)
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.	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 apoptotic process GO:0043066 Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.	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 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.	16	O65719 (/IEP) O65719 (/IEP) P11145 (/IEP) P22953 (/IEP) P22953 (/IEP) P22954 (/IEP) P22954 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) (6 more)
Response to hypoxia GO:0001666 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.	15	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)
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)
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.	11	A8WFS0 (/IDA) B0S610 (/IDA) B7ZV46 (/IDA) C1BEL8 (/IDA) P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) (1 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.	11	A0A0R4IJ78 (/IEP) B0UXS6 (/IEP) O65719 (/IEP) O65719 (/IEP) P22953 (/IEP) P22953 (/IEP) P22954 (/IEP) P22954 (/IEP) Q9C7X7 (/IEP) Q9LHA8 (/IEP) (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)
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)
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)
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)
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 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)
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.	7	C1BEL8 (/IDA) P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA)
Clathrin coat disassembly GO:0072318 The disaggregation of a clathrin coat into its constituent components; results in stripping or removing the clathrin coat from clathrin-coated vesicles (CCV) before fusing with their targets. CVVs transport cargo from plasma membrane and trans-Golgi to the endosomal system.	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)
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.	7	C1BEL8 (/IDA) P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA)
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)
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.	6	P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP)
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)
Posttranslational protein targeting to membrane, translocation GO:0031204 The process in which a protein translocates through the ER membrane posttranslationally.	6	P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/IMP) P16474 (/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.	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)
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)
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)
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.	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.	4	P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Negative regulation of cardiac muscle cell apoptotic process GO:0010667 Any process that decreases the rate or extent of cardiac cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a cardiac muscle cell and result in its death.	4	P63018 (/IMP) P63018 (/IMP) P63018 (/IMP) P63018 (/IMP)
Negative regulation of cardiac muscle cell apoptotic process GO:0010667 Any process that decreases the rate or extent of cardiac cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a cardiac muscle cell and result in its death.	4	P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Response to activity GO:0014823 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an activity stimulus.	4	P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Synaptic vesicle uncoating GO:0016191 The removal of the protein coat on a synaptic vesicle following the pinching step at the end of budding from the presynaptic membrane.	4	P63018 (/IC) P63018 (/IC) P63018 (/IC) P63018 (/IC)
Cerebellum development GO:0021549 The process whose specific outcome is the progression of the cerebellum over time, from its formation to the mature structure. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. In mice, the cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.	4	P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Forebrain development GO:0030900 The process whose specific outcome is the progression of the forebrain over time, from its formation to the mature structure. The forebrain is the anterior of the three primary divisions of the developing chordate brain or the corresponding part of the adult brain (in vertebrates, includes especially the cerebral hemispheres, the thalamus, and the hypothalamus and especially in higher vertebrates is the main control center for sensory and associative information processing, visceral functions, and voluntary motor functions).	4	P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Regulation of protein stability GO:0031647 Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.	4	P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Response to estradiol GO:0032355 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of stimulus by estradiol, a C18 steroid hormone hydroxylated at C3 and C17 that acts as a potent estrogen.	4	P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
Response to progesterone GO:0032570 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a progesterone stimulus.	4	P63018 (/IEP) P63018 (/IEP) P63018 (/IEP) P63018 (/IEP)
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)
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.	4	A0A0R4IJ78 (/IMP) B0UXS6 (/IMP) Q6PH56 (/IMP) Q9IAC1 (/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)
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.	3	P10591 (/IMP) P10591 (/IMP) P10591 (/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 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)
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)
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)
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)
Synaptonemal complex disassembly GO:0070194 The controlled breakdown of a synaptonemal complex.	3	P17156 (/IMP) P17156 (/IMP) P17156 (/IMP)
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)
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)
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)
Protein folding GO:0006457 The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.	2	P11145 (/ISM) P20030 (/ISM)
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)
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	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 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.	2	P0DMW0 (/IEP) P0DMW0 (/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 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.	2	A0A0R4IJ78 (/IDA) B0UXS6 (/IDA)
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)
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)
Vesicle-mediated transport GO:0016192 A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane.	2	P11147 (/IMP) P11147 (/IMP)
RNA interference GO:0016246 The process in which double-stranded RNAs silence cognate genes. Involves posttranscriptional gene inactivation ('silencing') both of transgenes or dsRNA introduced into a germline, and of the host gene(s) homologous to the transgenes or dsRNA. This silencing is triggered by the introduction of transgenes or double-stranded RNA (dsRNA), and can occur through a specific decrease in the level of mRNA, or by negative regulation of translation, of both host genes and transgenes.	2	P11147 (/IMP) P11147 (/IMP)
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)
Neuron differentiation GO:0030182 The process in which a relatively unspecialized cell acquires specialized features of a neuron.	2	P0DMW0 (/IEP) P0DMW0 (/IEP)
Ovarian follicle cell development GO:0030707 The process that occurs during oogenesis involving the ovarian follicle cells, somatic cells which surround the germ cells of an ovary. An example of this is found in Drosophila melanogaster.	2	P11147 (/IMP) P11147 (/IMP)
Cellular response to topologically incorrect protein GO:0035967 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a protein that is not folded in its correct three-dimensional structure.	2	P11147 (/IMP) P11147 (/IMP)
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)
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)
Membrane organization GO:0061024 A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins.	2	P11147 (/IDA) P11147 (/IDA)
Heterochromatin organization involved in chromatin silencing GO:0070868 Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic heterochromatin and contributes to chromatin silencing.	2	P11147 (/IMP) P11147 (/IMP)
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)
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)
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)
Determination of adult lifespan GO:0008340 The control of viability and duration in the adult phase of the life-cycle.	1	P09446 (/IGI)
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)
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)
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)
TRNA import into nucleus GO:0035719 The directed movement of tRNA from the cytoplasm to the nucleus.	1	P10592 (/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 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)
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)
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)
Chaperone-mediated protein folding GO:0061077 The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.	1	O59855 (/NAS)
Cellular response to osmotic stress GO:0071470 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.	1	Q5B2V1 (/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)
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)

There are 186 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.	97	B3VHV2 (/IDA) B6EAX2 (/IDA) O65719 (/IDA) O65719 (/IDA) P08106 (/IDA) P08106 (/IDA) P09435 (/IDA) P09435 (/IDA) P09435 (/IDA) P09435 (/IDA) (87 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.	96	B3VHV2 (/IDA) B6EAX2 (/IDA) O59855 (/IDA) P08106 (/IDA) P08106 (/IDA) P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) P09446 (/IDA) P0DMV8 (/IDA) (86 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)
Cytoplasm GO:0005737 All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.	66	O59855 (/IDA) P08106 (/IDA) P08106 (/IDA) P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) P09446 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) (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)
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.	60	P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV9 (/HDA) (50 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.	54	P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV8 (/TAS) P0DMV9 (/TAS) (44 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)
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)
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.	52	P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV8 (/HDA) P0DMV9 (/HDA) (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.	42	P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) P11142 (/IDA) (32 more)
Membrane GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.	39	P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) P11142 (/HDA) (29 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)
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 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)
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)
Perinuclear region of cytoplasm GO:0048471 Cytoplasm situated near, or occurring around, the nucleus.	26	P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV9 (/IDA) (16 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.	24	P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV8 (/IDA) P0DMV9 (/IDA) (14 more)
Cytoplasm GO:0005737 All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.	23	A8WFS0 (/ISS) B0S610 (/ISS) B0UXR9 (/ISS) B0UXS6 (/ISS) B5B0I3 (/ISS) B5X4Z3 (/ISS) B6VAH2 (/ISS) B6VAH2 (/ISS) B6VD00 (/ISS) B6VD00 (/ISS) (13 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)
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)
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).	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)
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.	17	A0PA16 (/IDA) A0PA16 (/IDA) A0PA16 (/IDA) A0PA16 (/IDA) A0PA16 (/IDA) B3VHV2 (/IDA) B6EAX2 (/IDA) C1BEL8 (/IDA) P08106 (/IDA) P08106 (/IDA) (7 more)
Membrane GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.	14	P08108 (/IDA) P08108 (/IDA) P08108 (/IDA) P22953 (/IDA) P22953 (/IDA) P46587 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5DW63 (/IDA) Q5KT34 (/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).	12	P16474 (/IDA) P16474 (/IDA) P16474 (/IDA) P16474 (/IDA) P16474 (/IDA) P16474 (/IDA) Q2ULV1 (/IDA) Q2ULV1 (/IDA) Q2ULV1 (/IDA) Q2ULV1 (/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	O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA) P22954 (/IDA) P22954 (/IDA) P41797 (/IDA) P46587 (/IDA) Q9LHA8 (/IDA) Q9LHA8 (/IDA) (2 more)
Cell surface GO:0009986 The external part of the cell wall and/or plasma membrane.	12	A0A1D8PG96 (/IDA) A0A1D8PG96 (/IDA) G8BEU5 (/IDA) P17156 (/IDA) P17156 (/IDA) P17156 (/IDA) P41797 (/IDA) P46587 (/IDA) P63018 (/IDA) P63018 (/IDA) (2 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.	11	O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA) P22954 (/IDA) P22954 (/IDA) Q00043 (/IDA) Q9LHA8 (/IDA) Q9LHA8 (/IDA) Q9S9N1 (/IDA) (1 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.	11	O59855 (/HDA) P10591 (/HDA) P10591 (/HDA) P10591 (/HDA) P11147 (/HDA) P11147 (/HDA) P54652 (/HDA) P54652 (/HDA) P54652 (/HDA) P54652 (/HDA) (1 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.	11	P16627 (/ISO) P16627 (/ISO) P17156 (/ISO) P17156 (/ISO) P17156 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) (1 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.	10	A0A1D8PG96 (/IDA) A0A1D8PG96 (/IDA) Q2UBH7 (/IDA) Q2UBH7 (/IDA) Q2UBH7 (/IDA) Q2UBH7 (/IDA) Q2UBH7 (/IDA) Q2UBH7 (/IDA) Q2UBH7 (/IDA) Q5B2V1 (/IDA)
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)
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)
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.	8	O97125 (/ISS) P11146 (/ISS) P11147 (/ISS) P11147 (/ISS) P17879 (/ISS) P29843 (/ISS) Q61696 (/ISS) Q61696 (/ISS)
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.	8	O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA) P22954 (/IDA) P22954 (/IDA) Q9LHA8 (/IDA) Q9LHA8 (/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.	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)
Chloroplast GO:0009507 A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.	7	O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA) Q9C7X7 (/IDA) Q9S9N1 (/IDA) Q9S9N1 (/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.	7	P17156 (/HDA) P17156 (/HDA) P17156 (/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.	6	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.	6	P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO)
Vacuolar membrane GO:0005774 The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.	6	O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA) Q9LHA8 (/IDA) Q9LHA8 (/IDA)
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)
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.	6	P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) Q61696 (/ISO) Q61696 (/ISO)
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)
Cytoplasm GO:0005737 All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.	5	P10591 (/HDA) P10591 (/HDA) P10591 (/HDA) P11147 (/HDA) P11147 (/HDA)
Mitochondrion GO:0005739 A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.	5	P10592 (/IDA) P17879 (/IDA) P55063 (/IDA) Q9LHA8 (/IDA) Q9LHA8 (/IDA)
Cytosol GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.	5	O59855 (/HDA) P10591 (/HDA) P10591 (/HDA) P10591 (/HDA) Q10265 (/HDA)
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)
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)
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.	4	P10591 (/IDA) P10591 (/IDA) P10591 (/IDA) P10592 (/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	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)
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.	4	P10591 (/HDA) P10591 (/HDA) P10591 (/HDA) P10592 (/HDA)
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)
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.	4	O65719 (/IDA) O65719 (/IDA) P22953 (/IDA) P22953 (/IDA)
Cell surface GO:0009986 The external part of the cell wall and/or plasma membrane.	4	P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
Postsynaptic density GO:0014069 An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.	4	P63018 (/IDA) P63018 (/IDA) P63018 (/IDA) P63018 (/IDA)
Postsynaptic density GO:0014069 An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.	4	P63017 (/ISO) P63017 (/ISO) P63017 (/ISO) P63017 (/ISO)
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)
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.	3	P36415 (/HDA) Q54BE0 (/HDA) Q557E0 (/HDA)
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)
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)
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)
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)
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.	2	P22953 (/IDA) P22953 (/IDA)
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.	2	O65719 (/IDA) O65719 (/IDA)
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)
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)
Hyphal cell wall GO:0030446 The cell wall surrounding a fungal hypha.	2	P41797 (/IDA) P46587 (/IDA)
Phagocytic vesicle GO:0045335 A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.	2	P36415 (/HDA) Q557E0 (/HDA)
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)
Nucleus GO:0005634 A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.	1	O73885 (/IMP)
Nucleoplasm GO:0005654 That part of the nuclear content other than the chromosomes or the nucleolus.	1	P20030 (/IDA)
Nucleoplasm GO:0005654 That part of the nuclear content other than the chromosomes or the nucleolus.	1	Q4Q7Y0 (/ISO)
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)
Cytosol GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.	1	Q7SX63 (/ISS)
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)
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)
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)

Functional Families

There are 90 GO terms relating to "molecular function"

There are 283 GO terms relating to "biological process"

There are 186 GO terms relating to "cellular component"