The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"EF-hand
".
FunFam 1: Calmodulin 1
Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
There are 47 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).
|
1859 |
B4DJ51 (/IPI)
B4DJ51 (/IPI)
B4DJ51 (/IPI)
B4DJ51 (/IPI)
B4DJ51 (/IPI)
B4DJ51 (/IPI)
B4DJ51 (/IPI)
B4DJ51 (/IPI)
B4DJ51 (/IPI)
B4DJ51 (/IPI)
(1849 more) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
1678 |
P02599 (/IDA)
P04464 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(1668 more) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
900 |
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
(890 more) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
896 |
P04464 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
(886 more) |
Calcium channel inhibitor activity GO:0019855
Stops, prevents, or reduces the activity of a calcium channel.
|
716 |
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
(706 more) |
Disordered domain specific binding GO:0097718
Interacting selectively and non-covalently with a disordered domain of a protein.
|
716 |
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
(706 more) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
543 |
F4IEU4 (/TAS)
P0DP26 (/TAS)
P0DP26 (/TAS)
P0DP26 (/TAS)
P0DP26 (/TAS)
P0DP26 (/TAS)
P0DP26 (/TAS)
P0DP26 (/TAS)
P0DP26 (/TAS)
P0DP26 (/TAS)
(533 more) |
Protein kinase binding GO:0019901
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
|
538 |
P02599 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
(528 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.
|
537 |
P0DP33 (/IPI)
P0DP33 (/IPI)
P0DP33 (/IPI)
P0DP33 (/IPI)
P0DP33 (/IPI)
P0DP33 (/IPI)
P0DP33 (/IPI)
P0DP33 (/IPI)
P0DP33 (/IPI)
P0DP33 (/IPI)
(527 more) |
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Adenylate cyclase binding GO:0008179
Interacting selectively and non-covalently with the enzyme adenylate cyclase.
|
537 |
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(527 more) |
Adenylate cyclase binding GO:0008179
Interacting selectively and non-covalently with the enzyme adenylate cyclase.
|
537 |
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
(527 more) |
Adenylate cyclase binding GO:0008179
Interacting selectively and non-covalently with the enzyme adenylate cyclase.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Adenylate cyclase activator activity GO:0010856
Increases the activity of the enzyme that catalyzes the reaction: ATP = 3',5'-cyclic AMP + diphosphate.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 more) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Nitric-oxide synthase regulator activity GO:0030235
Modulates the activity of nitric oxide synthase.
|
537 |
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(527 more) |
Nitric-oxide synthase regulator activity GO:0030235
Modulates the activity of nitric oxide synthase.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Titin binding GO:0031432
Interacting selectively and non-covalently with titin, any of a family of giant proteins found in striated and smooth muscle. In striated muscle, single titin molecules span half the sarcomere, with their N- and C-termini in the Z-disc and M-line, respectively.
|
537 |
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
(527 more) |
Type 3 metabotropic glutamate receptor binding GO:0031800
Interacting selectively and non-covalently with a type 3 metabotropic glutamate receptor.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
N-terminal myristoylation domain binding GO:0031997
Interacting selectively and non-covalently with the N-terminus of a protein that has the potential to be, or has been, modified by N-terminal myristoylation. Binding affinity is typically altered by myristoylation; for example, N-terminal myristoylation of HIV Nef increases its affinity for calmodulin.
|
537 |
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
(527 more) |
Protein serine/threonine kinase activator activity GO:0043539
Binds to and increases the activity of a protein serine/threonine kinase.
|
537 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(527 more) |
Phosphatidylinositol 3-kinase binding GO:0043548
Interacting selectively and non-covalently with a phosphatidylinositol 3-kinase, any enzyme that catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Ion channel binding GO:0044325
Interacting selectively and non-covalently with one or more specific sites on an ion channel, a protein complex that spans a membrane and forms a water-filled channel across the phospholipid bilayer allowing selective ion transport down its electrochemical gradient.
|
537 |
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(527 more) |
Ion channel binding GO:0044325
Interacting selectively and non-covalently with one or more specific sites on an ion channel, a protein complex that spans a membrane and forms a water-filled channel across the phospholipid bilayer allowing selective ion transport down its electrochemical gradient.
|
537 |
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
P0DP23 (/IPI)
(527 more) |
Ion channel binding GO:0044325
Interacting selectively and non-covalently with one or more specific sites on an ion channel, a protein complex that spans a membrane and forms a water-filled channel across the phospholipid bilayer allowing selective ion transport down its electrochemical gradient.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 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.
|
537 |
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(527 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.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Calcium-dependent protein binding GO:0048306
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules), in the presence of calcium.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Nitric-oxide synthase binding GO:0050998
Interacting selectively and non-covalently with the enzyme nitric-oxide synthase.
|
537 |
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(527 more) |
Nitric-oxide synthase binding GO:0050998
Interacting selectively and non-covalently with the enzyme nitric-oxide synthase.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Protein phosphatase activator activity GO:0072542
Increases the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 more) |
Calcium channel inhibitor activity GO:0019855
Stops, prevents, or reduces the activity of a calcium channel.
|
358 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(348 more) |
Calcium channel regulator activity GO:0005246
Modulates the activity of a calcium channel.
|
179 |
P0DP29 (/NAS)
P0DP29 (/NAS)
P0DP29 (/NAS)
P0DP29 (/NAS)
P0DP29 (/NAS)
P0DP29 (/NAS)
P0DP29 (/NAS)
P0DP29 (/NAS)
P0DP29 (/NAS)
P0DP29 (/NAS)
(169 more) |
Protein C-terminus binding GO:0008022
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxyl function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
|
179 |
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
(169 more) |
Myosin binding GO:0017022
Interacting selectively and non-covalently with any part of a myosin complex; myosins are any of a superfamily of molecular motor proteins that bind to actin and use the energy of ATP hydrolysis to generate force and movement along actin filaments.
|
179 |
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
(169 more) |
Type 3 metabotropic glutamate receptor binding GO:0031800
Interacting selectively and non-covalently with a type 3 metabotropic glutamate receptor.
|
179 |
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
(169 more) |
Phosphatidylinositol 3-kinase binding GO:0043548
Interacting selectively and non-covalently with a phosphatidylinositol 3-kinase, any enzyme that catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring.
|
179 |
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
(169 more) |
Calcium-dependent protein binding GO:0048306
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules), in the presence of calcium.
|
179 |
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
P0DP29 (/IPI)
(169 more) |
CH domain binding GO:0051401
Interacting selectively and non-covalently with the calponin homology domain of a protein, a domain of 100 residues that occurs in signaling and cytoskeletal proteins.
|
179 |
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
P62149 (/IPI)
(169 more) |
Myosin VI head/neck binding GO:0070855
Interacting selectively and non-covalently with the head/neck region of a myosin VI heavy chain.
|
142 |
P49258 (/IPI)
P49258 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
(132 more) |
Myosin V binding GO:0031489
Interacting selectively and non-covalently with a class V myosin; myosin V is a dimeric molecule involved in intracellular transport.
|
140 |
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
(130 more) |
Myosin heavy chain binding GO:0032036
Interacting selectively and non-covalently with a heavy chain of a myosin complex.
|
140 |
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
(130 more) |
Myosin I binding GO:0017024
Interacting selectively and non-covalently with a class I myosin; myosin I heavy chains are single-headed, possess tails of various lengths, and do not self-associate into bipolar filaments.
|
1 | P02599 (/IDA) |
Kinase binding GO:0019900
Interacting selectively and non-covalently with a kinase, any enzyme that catalyzes the transfer of a phosphate group.
|
1 | P02599 (/IPI) |
Troponin I binding GO:0031013
Interacting selectively and non-covalently with troponin I, the inhibitory subunit of the troponin complex.
|
1 | P02599 (/IDA) |
Troponin I binding GO:0031013
Interacting selectively and non-covalently with troponin I, the inhibitory subunit of the troponin complex.
|
1 | Q09665 (/IPI) |
Cell adhesion molecule binding GO:0050839
Interacting selectively and non-covalently with a cell adhesion molecule.
|
1 | P02599 (/IPI) |
There are 90 GO terms relating to "biological process"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Negative regulation of ryanodine-sensitive calcium-release channel activity GO:0060315
Any process that decreases the activity of a ryanodine-sensitive calcium-release channel. The ryanodine-sensitive calcium-release channel catalyzes the transmembrane transfer of a calcium ion by a channel that opens when a ryanodine class ligand has been bound by the channel complex or one of its constituent parts.
|
895 |
P0DP25 (/ISS)
P0DP25 (/ISS)
P0DP25 (/ISS)
P0DP25 (/ISS)
P0DP25 (/ISS)
P0DP25 (/ISS)
P0DP25 (/ISS)
P0DP25 (/ISS)
P0DP25 (/ISS)
P0DP25 (/ISS)
(885 more) |
Regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum GO:0010880
Any process that modulates the rate, frequency or extent of release of sequestered calcium ion into cytosol by the sarcoplasmic reticulum, the process in which the release of sequestered calcium ion by sarcoplasmic reticulum into cytosol occurs via calcium release channels.
|
716 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(706 more) |
Regulation of ryanodine-sensitive calcium-release channel activity GO:0060314
Any process that modulates the activity of a ryanodine-sensitive calcium-release channel. The ryanodine-sensitive calcium-release channel catalyzes the transmembrane transfer of a calcium ion by a channel that opens when a ryanodine class ligand has been bound by the channel complex or one of its constituent parts.
|
716 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(706 more) |
Positive regulation of ryanodine-sensitive calcium-release channel activity GO:0060316
Any process that increases the activity of a ryanodine-sensitive calcium-release channel. The ryanodine-sensitive calcium-release channel catalyzes the transmembrane transfer of a calcium ion by a channel that opens when a ryanodine class ligand has been bound by the channel complex or one of its constituent parts.
|
716 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(706 more) |
Positive regulation of cyclic-nucleotide phosphodiesterase activity GO:0051343
Any process that activates or increases the frequency, rate or extent of cyclic nucleotide phosphodiesterase activity, the catalysis of the reaction: nucleotide 3',5'-cyclic phosphate + H2O = nucleotide 5'-phosphate.
|
538 |
P02599 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(528 more) |
G2/M transition of mitotic cell cycle GO:0000086
The mitotic cell cycle transition by which a cell in G2 commits to M phase. The process begins when the kinase activity of M cyclin/CDK complex reaches a threshold high enough for the cell cycle to proceed. This is accomplished by activating a positive feedback loop that results in the accumulation of unphosphorylated and active M cyclin/CDK complex.
|
537 |
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
(527 more) |
Response to amphetamine GO:0001975
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 amphetamine stimulus. Amphetamines consist of a group of compounds related to alpha-methylphenethylamine.
|
537 |
P0DP29 (/IEP)
P0DP29 (/IEP)
P0DP29 (/IEP)
P0DP29 (/IEP)
P0DP29 (/IEP)
P0DP29 (/IEP)
P0DP29 (/IEP)
P0DP29 (/IEP)
P0DP29 (/IEP)
P0DP29 (/IEP)
(527 more) |
Regulation of heart rate GO:0002027
Any process that modulates the frequency or rate of heart contraction.
|
537 |
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
(527 more) |
Detection of calcium ion GO:0005513
The series of events in which a calcium ion stimulus is received by a cell and converted into a molecular signal.
|
537 |
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
(527 more) |
G protein-coupled receptor signaling pathway GO:0007186
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription. The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
|
537 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(527 more) |
Activation of adenylate cyclase activity GO:0007190
Any process that initiates the activity of the inactive enzyme adenylate cyclase.
|
537 |
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(527 more) |
Positive regulation of peptidyl-threonine phosphorylation GO:0010800
Any process that increases the frequency, rate or extent of peptidyl-threonine phosphorylation. Peptidyl-threonine phosphorylation is the phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine.
|
537 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(527 more) |
Negative regulation of peptidyl-threonine phosphorylation GO:0010801
Any process that decreases the frequency, rate or extent of peptidyl-threonine phosphorylation. Peptidyl-threonine phosphorylation is the phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine.
|
537 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(527 more) |
Regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion GO:0010881
Any process that modulates the frequency, rate or extent of cardiac muscle contraction via the regulation of the release of sequestered calcium ion by sarcoplasmic reticulum into cytosol. The sarcoplasmic reticulum is the endoplasmic reticulum of striated muscle, specialised for the sequestration of calcium ions that are released upon receipt of a signal relayed by the T tubules from the neuromuscular junction.
|
537 |
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
(527 more) |
Calcium-mediated signaling GO:0019722
Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions.
|
537 |
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
(527 more) |
Substantia nigra development GO:0021762
The progression of the substantia nigra over time from its initial formation until its mature state. The substantia nigra is the layer of gray substance that separates the posterior parts of the cerebral peduncles (tegmentum mesencephali) from the anterior parts; it normally includes a posterior compact part with many pigmented cells (pars compacta) and an anterior reticular part whose cells contain little pigment (pars reticularis).
|
537 |
P0DP23 (/HEP)
P0DP23 (/HEP)
P0DP23 (/HEP)
P0DP23 (/HEP)
P0DP23 (/HEP)
P0DP23 (/HEP)
P0DP23 (/HEP)
P0DP23 (/HEP)
P0DP23 (/HEP)
P0DP23 (/HEP)
(527 more) |
Positive regulation of protein autophosphorylation GO:0031954
Any process that activates or increases the frequency, rate or extent of the phosphorylation by a protein of one or more of its own residues.
|
537 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(527 more) |
Regulation of cytokinesis GO:0032465
Any process that modulates the frequency, rate or extent of the division of the cytoplasm of a cell and its separation into two daughter cells.
|
537 |
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
(527 more) |
Positive regulation of phosphoprotein phosphatase activity GO:0032516
Any process that activates or increases the activity of a phosphoprotein phosphatase.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 more) |
Positive regulation of protein dephosphorylation GO:0035307
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a protein.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 more) |
Positive regulation of nitric-oxide synthase activity GO:0051000
Any process that activates or increases the activity of the enzyme nitric-oxide synthase.
|
537 |
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(527 more) |
Response to calcium ion GO:0051592
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 calcium ion stimulus.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 more) |
Regulation of cardiac muscle contraction GO:0055117
Any process that modulates the frequency, rate or extent of cardiac muscle contraction.
|
537 |
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
P0DP23 (/IMP)
(527 more) |
Negative regulation of ryanodine-sensitive calcium-release channel activity GO:0060315
Any process that decreases the activity of a ryanodine-sensitive calcium-release channel. The ryanodine-sensitive calcium-release channel catalyzes the transmembrane transfer of a calcium ion by a channel that opens when a ryanodine class ligand has been bound by the channel complex or one of its constituent parts.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 more) |
Positive regulation of protein serine/threonine kinase activity GO:0071902
Any process that increases the rate, frequency, or extent of protein serine/threonine kinase activity.
|
537 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(527 more) |
Positive regulation by host of symbiont cAMP-mediated signal transduction GO:0075206
Any process in which the host organism activates, maintains or increases the frequency, rate or extent of cAMP-mediated signal transduction in the symbiont organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 more) |
Establishment of protein localization to membrane GO:0090150
The directed movement of a protein to a specific location in a membrane.
|
537 |
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
(527 more) |
Establishment of protein localization to mitochondrial membrane GO:0090151
The directed movement of a protein to a specific location in the mitochondrial membrane.
|
537 |
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
(527 more) |
Regulation of synaptic vesicle endocytosis GO:1900242
Any process that modulates the frequency, rate or extent of synaptic vesicle endocytosis.
|
537 |
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
(527 more) |
Regulation of store-operated calcium channel activity GO:1901339
Any process that modulates the frequency, rate or extent of store-operated calcium channel activity.
|
537 |
P0DP29 (/IC)
P0DP29 (/IC)
P0DP29 (/IC)
P0DP29 (/IC)
P0DP29 (/IC)
P0DP29 (/IC)
P0DP29 (/IC)
P0DP29 (/IC)
P0DP29 (/IC)
P0DP29 (/IC)
(527 more) |
Regulation of high voltage-gated calcium channel activity GO:1901841
Any process that modulates the frequency, rate or extent of high voltage-gated calcium channel activity.
|
537 |
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
(527 more) |
Regulation of cell communication by electrical coupling involved in cardiac conduction GO:1901844
Any process that modulates the frequency, rate or extent of cell communication by electrical coupling involved in cardiac conduction.
|
537 |
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
P0DP23 (/IC)
(527 more) |
Regulation of synaptic vesicle exocytosis GO:2000300
Any process that modulates the frequency, rate or extent of synaptic vesicle exocytosis.
|
537 |
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
P0DP29 (/IMP)
(527 more) |
Regulation of ryanodine-sensitive calcium-release channel activity GO:0060314
Any process that modulates the activity of a ryanodine-sensitive calcium-release channel. The ryanodine-sensitive calcium-release channel catalyzes the transmembrane transfer of a calcium ion by a channel that opens when a ryanodine class ligand has been bound by the channel complex or one of its constituent parts.
|
358 |
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
(348 more) |
MAPK cascade GO:0000165
An intracellular protein kinase cascade containing at least a MAPK, a MAPKK and a MAP3K. The cascade can also contain an additional tiers: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinase in the downstream tier to transmit a signal within a cell.
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Platelet degranulation GO:0002576
The regulated exocytosis of secretory granules containing preformed mediators such as histamine and serotonin by a platelet.
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Glycogen catabolic process GO:0005980
The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Muscle contraction GO:0006936
A process in which force is generated within muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis.
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Wnt signaling pathway, calcium modulating pathway GO:0007223
The series of molecular signals initiated by binding of a Wnt protein to a receptor on the surface of the target cell where activated receptors leads to an increase in intracellular calcium and activation of protein kinase C (PKC).
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Regulation of rhodopsin mediated signaling pathway GO:0022400
Any process that modulates the frequency, rate or extent of rhodopsin-mediated signaling.
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Fc-epsilon receptor signaling pathway GO:0038095
A series of molecular signals initiated by the binding of the Fc portion of immunoglobulin E (IgE) to an Fc-epsilon receptor on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region.
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Positive regulation of DNA binding GO:0043388
Any process that increases the frequency, rate or extent of DNA binding. DNA binding is any process in which a gene product interacts selectively with DNA (deoxyribonucleic acid).
|
179 |
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
(169 more) |
Inositol phosphate metabolic process GO:0043647
The chemical reactions and pathways involving inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with one or more phosphate groups attached.
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Regulation of nitric-oxide synthase activity GO:0050999
Any process that modulates the activity of the enzyme nitric-oxide synthase.
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Cofactor metabolic process GO:0051186
The chemical reactions and pathways involving a cofactor, a substance that is required for the activity of an enzyme or other protein. Cofactors may be inorganic, such as the metal atoms zinc, iron, and copper in certain forms, or organic, in which case they are referred to as coenzymes. Cofactors may either be bound tightly to active sites or bind loosely with the substrate.
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Response to corticosterone GO:0051412
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 corticosterone stimulus. Corticosterone is a 21 carbon steroid hormone of the corticosteroid type, produced in the cortex of the adrenal glands. In many species, corticosterone is the principal glucocorticoid, involved in regulation of fuel metabolism, immune reactions, and stress responses.
|
179 |
P0DP30 (/IEP)
P0DP30 (/IEP)
P0DP30 (/IEP)
P0DP30 (/IEP)
P0DP30 (/IEP)
P0DP30 (/IEP)
P0DP30 (/IEP)
P0DP30 (/IEP)
P0DP30 (/IEP)
P0DP30 (/IEP)
(169 more) |
Protein phosphorylation GO:0006468
The process of introducing a phosphate group on to a protein.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
Centriole replication GO:0007099
The cell cycle process in which a daughter centriole is formed perpendicular to an existing centriole. An immature centriole contains a ninefold radially symmetric array of single microtubules; mature centrioles consist of a radial array of nine microtubule triplets, doublets, or singlets depending upon the species and cell type. Duplicated centrioles also become the ciliary basal body in cells that form cilia during G0.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
Sensory perception of sound GO:0007605
The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
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.
|
140 |
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
(130 more) |
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.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
Rhodopsin mediated signaling pathway GO:0016056
The series of molecular signals generated as a consequence of excitation of rhodopsin by a photon and the events that convert the absorbed photons into a cellular response.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
Deactivation of rhodopsin mediated signaling GO:0016059
The process of restoring the photoreceptor cell to its unexcited state after termination of the stimulus (photon).
|
140 |
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
(130 more) |
Metarhodopsin inactivation GO:0016060
The process in which metarhodopsin is prevented from generating molecular signals. Activated rhodopsin (R*) is inactivated by a two-step process: first, R* is phosphorylated by rhodopsin kinase which lowers the activity of R*. Second, the protein arrestin binds to phosphorylated R* to de-activate it.
|
140 |
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
(130 more) |
Regulation of light-activated channel activity GO:0016061
Any process that modulates the frequency, rate or extent of light-activated channel activity.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
Adaptation of rhodopsin mediated signaling GO:0016062
The process in which a rhodopsin-mediated signaling pathway is adjusted to modulate the sensitivity and response of a visual system to light stimuli (that might vary over more than 6 magnitudes in intensity) without response saturation.
|
140 |
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
(130 more) |
Actin filament-based movement GO:0030048
Movement of organelles or other particles along actin filaments, or sliding of actin filaments past each other, mediated by motor proteins.
|
140 |
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
(130 more) |
Salivary gland cell autophagic cell death GO:0035071
The stage-specific programmed cell death of salivary gland cells during salivary gland histolysis.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
Rhabdomere development GO:0042052
The assembly and arrangement of a rhabdomere within a cell. The rhabdomere is the organelle on the apical surface of a photoreceptor cell that contains the visual pigments.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
Muscle cell cellular homeostasis GO:0046716
The cellular homeostatic process that preserves a muscle cell in a stable functional or structural state.
|
140 |
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
P62152 (/IGI)
(130 more) |
Kinetochore organization GO:0051383
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the kinetochore, a multisubunit complex that is located at the centromeric region of DNA and provides an attachment point for the spindle microtubules.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
Cellular response to ethanol GO:0071361
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 ethanol stimulus.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
Photoreceptor cell axon guidance GO:0072499
The chemotaxis process that directs the migration of a photoreceptor cell axon growth cone to its target in the optic lobe in response to a combination of attractive and repulsive cues.
|
140 |
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
P62152 (/IMP)
(130 more) |
Positive regulation of cation channel activity GO:2001259
Any process that activates or increases the frequency, rate or extent of cation channel activity.
|
140 |
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
(130 more) |
Regulation of cell cycle GO:0051726
Any process that modulates the rate or extent of progression through the cell cycle.
|
126 |
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
(116 more) |
Spore germination GO:0009847
The physiological and developmental changes that occur in a spore following release from dormancy up to the earliest signs of growth (e.g. emergence from a spore wall).
|
96 |
P60204 (/IMP)
P60204 (/IMP)
P60204 (/IMP)
P60204 (/IMP)
P60204 (/IMP)
P60204 (/IMP)
P60204 (/IMP)
P60204 (/IMP)
P60204 (/IMP)
P60204 (/IMP)
(86 more) |
Detection of calcium ion GO:0005513
The series of events in which a calcium ion stimulus is received by a cell and converted into a molecular signal.
|
95 |
F4K8M2 (/ISS)
O23320 (/ISS)
O23320 (/ISS)
P59220 (/ISS)
P59220 (/ISS)
P59220 (/ISS)
P59220 (/ISS)
P59220 (/ISS)
P59220 (/ISS)
P59220 (/ISS)
(85 more) |
Regulation of photomorphogenesis GO:0010099
Any process that modulates the rate or extent of photomorphogenesis.
|
92 |
P59220 (/IMP)
P59220 (/IMP)
P59220 (/IMP)
P59220 (/IMP)
P59220 (/IMP)
P59220 (/IMP)
P59220 (/IMP)
P59220 (/IMP)
P59220 (/IMP)
P59220 (/IMP)
(82 more) |
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.
|
30 |
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
(20 more) |
Cell migration GO:0016477
The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms.
|
30 |
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
(20 more) |
Regulation of protein localization GO:0032880
Any process that modulates the frequency, rate or extent of any process in which a protein is transported to, or maintained in, a specific location.
|
30 |
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
(20 more) |
Regulation of apoptotic process GO:0042981
Any process that modulates the occurrence or rate of cell death by apoptotic process.
|
30 |
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
(20 more) |
Apoptotic cell clearance GO:0043277
The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte.
|
30 |
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
(20 more) |
Establishment of meiotic spindle orientation GO:0051296
Any process that set the alignment of meiotic spindle relative to other cellular structures.
|
30 |
O16305 (/IGI)
O16305 (/IGI)
O16305 (/IGI)
O16305 (/IGI)
O16305 (/IGI)
O16305 (/IGI)
O16305 (/IGI)
O16305 (/IGI)
O16305 (/IGI)
O16305 (/IGI)
(20 more) |
Establishment of meiotic spindle orientation GO:0051296
Any process that set the alignment of meiotic spindle relative to other cellular structures.
|
30 |
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
O16305 (/IMP)
(20 more) |
Calcium-mediated signaling GO:0019722
Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions.
|
19 |
P0DH98 (/TAS)
P0DH98 (/TAS)
P0DH98 (/TAS)
P0DH98 (/TAS)
P0DH98 (/TAS)
P0DH98 (/TAS)
P0DH98 (/TAS)
P0DH98 (/TAS)
P0DH98 (/TAS)
P0DH98 (/TAS)
(9 more) |
Calcium-mediated signaling GO:0019722
Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions.
|
2 | O23320 (/IGI) O23320 (/IGI) |
Actin filament-based movement GO:0030048
Movement of organelles or other particles along actin filaments, or sliding of actin filaments past each other, mediated by motor proteins.
|
2 | P49258 (/IC) P49258 (/IC) |
Mitotic cytokinesis GO:0000281
A cell cycle process that results in the division of the cytoplasm of a cell after mitosis, resulting in the separation of the original cell into two daughter cells.
|
1 | P02599 (/IMP) |
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.
|
1 | F4K8M2 (/IEP) |
Pollen germination GO:0009846
The physiological and developmental changes that occur in a heterosporous plant pollen grain, beginning with hydration and terminating with the emergence of the pollen tube through the aperture.
|
1 | F4IJ46 (/IMP) |
Protein catabolic process GO:0030163
The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
|
1 | F4IJ46 (/TAS) |
Regulation of sorocarp stalk cell differentiation GO:0031285
Any process that modulates the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
|
1 | P02599 (/IMP) |
Positive regulation of ATPase activity GO:0032781
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
|
1 | P02599 (/IDA) |
Regulation of kinase activity GO:0043549
Any process that modulates the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
|
1 | P02599 (/IDA) |
Negative regulation of proteolysis GO:0045861
Any process that stops, prevents, or reduces the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
|
1 | P02599 (/IDA) |
Positive regulation of sequestering of calcium ion GO:0051284
Any process that activates or increases the frequency, rate or extent of the binding or confining calcium ions such that they are separated from other components of a biological system.
|
1 | P02599 (/IMP) |
Positive regulation of positive chemotaxis to cAMP GO:0061122
Any process that increases the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP.
|
1 | P02599 (/IDA) |
Establishment of protein localization to vacuole GO:0072666
The directed movement of a protein to a specific location in a vacuole.
|
1 | P02599 (/IDA) |
Negative regulation of asexual reproduction GO:1903665
Any process that stops, prevents or reduces the frequency, rate or extent of asexual reproduction.
|
1 | P02599 (/IDA) |
There are 55 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 |
---|---|---|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1250 |
P02599 (/IDA)
P04464 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
(1240 more) |
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.
|
1074 |
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
P0DP26 (/IDA)
(1064 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.
|
895 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(885 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.
|
765 |
G1NK53 (/TAS)
G1NK53 (/TAS)
G1NK53 (/TAS)
G1NK53 (/TAS)
G1NK53 (/TAS)
G1NK53 (/TAS)
G1NK53 (/TAS)
G1NK53 (/TAS)
G1NK53 (/TAS)
G1NK53 (/TAS)
(755 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.
|
707 |
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
(697 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.
|
541 |
F4K8M2 (/IDA)
P02599 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(531 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.
|
539 |
F4IEU4 (/IDA)
F4IVN6 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(529 more) |
Spindle pole GO:0000922
Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 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.
|
537 |
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
(527 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.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
537 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(527 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
537 |
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
P0DP26 (/ISS)
(527 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
537 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(527 more) |
Spindle microtubule GO:0005876
Any microtubule that is part of a mitotic or meiotic spindle; anchored at one spindle pole.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 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.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 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.
|
537 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(527 more) |
Voltage-gated potassium channel complex GO:0008076
A protein complex that forms a transmembrane channel through which potassium ions may cross a cell membrane in response to changes in membrane potential.
|
537 |
P0DP26 (/IGI)
P0DP26 (/IGI)
P0DP26 (/IGI)
P0DP26 (/IGI)
P0DP26 (/IGI)
P0DP26 (/IGI)
P0DP26 (/IGI)
P0DP26 (/IGI)
P0DP26 (/IGI)
P0DP26 (/IGI)
(527 more) |
Sarcomere GO:0030017
The repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 more) |
Growth cone GO:0030426
The migrating motile tip of a growing neuron projection, where actin accumulates, and the actin cytoskeleton is the most dynamic.
|
537 |
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(527 more) |
Growth cone GO:0030426
The migrating motile tip of a growing neuron projection, where actin accumulates, and the actin cytoskeleton is the most dynamic.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Vesicle GO:0031982
Any small, fluid-filled, spherical organelle enclosed by membrane.
|
537 |
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
P0DP23 (/HDA)
(527 more) |
Calcium channel complex GO:0034704
An ion channel complex through which calcium ions pass.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 more) |
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
|
537 |
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
P0DP29 (/IDA)
(527 more) |
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
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.
|
537 |
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
P0DP26 (/ISO)
(527 more) |
Catalytic complex GO:1902494
A protein complex which is capable of catalytic activity.
|
537 |
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
P0DP23 (/IDA)
(527 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.
|
179 |
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
P0DP23 (/TAS)
(169 more) |
Mitotic spindle GO:0072686
A spindle that forms as part of mitosis. Mitotic and meiotic spindles contain distinctive complements of proteins associated with microtubules.
|
170 |
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
(160 more) |
Myosin VI complex GO:0031476
A myosin complex containing one or more class VI myosin heavy chains and associated light chains. Myosin VI has a single IQ motif in the neck and a tail region with a coiled coil domain followed by a unique globular domain; a unique insertion that enables myosin VI to move towards the pointed or minus end of actin filaments.
|
142 |
P49258 (/IPI)
P49258 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
(132 more) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
140 |
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
(130 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.
|
140 |
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
(130 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.
|
140 |
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
(130 more) |
Spindle GO:0005819
The array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during mitosis or meiosis and serves to move the duplicated chromosomes apart.
|
140 |
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
(130 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.
|
140 |
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
P62152 (/HDA)
(130 more) |
Rhabdomere GO:0016028
The specialized microvilli-containing organelle on the apical surfaces of a photoreceptor cell containing the visual pigment rhodopsin and most of the proteins involved in phototransduction.
|
140 |
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
(130 more) |
Rhabdomere GO:0016028
The specialized microvilli-containing organelle on the apical surfaces of a photoreceptor cell containing the visual pigment rhodopsin and most of the proteins involved in phototransduction.
|
140 |
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
P62152 (/TAS)
(130 more) |
Midbody GO:0030496
A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis.
|
140 |
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
(130 more) |
Myosin V complex GO:0031475
A myosin complex containing a dimer of class V myosin heavy chains and associated light chains; involved in intracellular transport. Myosin V is a dimeric molecule consisting of conserved motor domains followed by 6 IQ motifs which bind specific light chains and calmodulin. The tail domain is important for cellular localization and cargo binding and can be divided into an alpha-helical coiled coil region and a C-terminal globular region.
|
140 |
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
P62152 (/IPI)
(130 more) |
Mitotic spindle pole GO:0097431
Either of the ends of a mitotic spindle, a spindle that forms as part of mitosis, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.
|
140 |
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
P62152 (/IDA)
(130 more) |
Hyphal tip GO:0001411
The end, or tip, of a fungal hypha, where polarized growth occurs during hyphal elongation.
|
96 |
P60204 (/IDA)
P60204 (/IDA)
P60204 (/IDA)
P60204 (/IDA)
P60204 (/IDA)
P60204 (/IDA)
P60204 (/IDA)
P60204 (/IDA)
P60204 (/IDA)
P60204 (/IDA)
(86 more) |
Nuclear membrane GO:0031965
Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
|
30 |
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
(20 more) |
Cell periphery GO:0071944
The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures.
|
30 |
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
O16305 (/IDA)
(20 more) |
Contractile vacuole GO:0000331
A specialized vacuole of eukaryotic cells, especially Protozoa, that fills with water from the cytoplasm and then discharges this externally by the opening of contractile vacuole pores. Its function is probably osmoregulatory.
|
21 |
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
(11 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.
|
21 |
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
Q4QHT2 (/ISO)
(11 more) |
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.
|
16 |
P0DH98 (/IDA)
P0DH98 (/IDA)
P0DH98 (/IDA)
P0DH98 (/IDA)
P0DH98 (/IDA)
P0DH98 (/IDA)
P0DH98 (/IDA)
P0DH98 (/IDA)
P0DH98 (/IDA)
P0DH98 (/IDA)
(6 more) |
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.
|
16 |
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
P0DH97 (/IDA)
(6 more) |
Cilium GO:0005929
A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
|
8 | P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) |
Axoneme GO:0005930
The bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements.
|
8 | P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) P69097 (/IDA) P69097 (/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.
|
4 | P27482 (/HDA) P27482 (/HDA) P27482 (/HDA) P27482 (/HDA) |
Investment cone GO:0070865
A cytoskeletal part that consists of a microfilament-rich cone that forms round each nucleus in a spermatogenic cyst and translocates the length of the cyst during sperm individualization.
|
2 | P49258 (/IDA) P49258 (/IDA) |
Contractile vacuole GO:0000331
A specialized vacuole of eukaryotic cells, especially Protozoa, that fills with water from the cytoplasm and then discharges this externally by the opening of contractile vacuole pores. Its function is probably osmoregulatory.
|
1 | P02599 (/IDA) |
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
|
1 | P02599 (/IDA) |
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
|
1 | F4IVN6 (/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 | P02599 (/IDA) |