CATH Superfamily 1.20.58.60
The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was: waiting to be named.
FunFam 4: Actinin alpha 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 79 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 |
|---|---|---|
|
Vinculin binding GO:0017166
Interacting selectively and non-covalently with vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Alpha-actinin binding GO:0051393
Interacting selectively and non-covalently with alpha-actinin, one of a family of proteins that cross-link F-actin as antiparallel homodimers. Alpha-actinin has a molecular mass of 93-103 KDa; at the N-terminus there are two calponin homology domains, at the C-terminus there are two EF-hands. These two domains are connected by the rod domain. This domain is formed by triple-helical spectrin repeats.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
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).
|
39 |
B2R8Y4 (/IPI)
D3ZCV0 (/IPI)
D3ZCV0 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
(29 more) |
|
Actin filament binding GO:0051015
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
|
27 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(17 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.
|
22 |
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
(12 more) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
21 |
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
(11 more) |
|
Integrin binding GO:0005178
Interacting selectively and non-covalently with an integrin.
|
15 |
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
(5 more) |
|
Actin filament binding GO:0051015
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
|
14 |
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
(4 more) |
|
RNA polymerase II regulatory region sequence-specific DNA binding GO:0000977
Interacting selectively and non-covalently with a specific sequence of DNA that is part of a regulatory region that controls the transcription of a gene or cistron by RNA polymerase II.
|
13 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(3 more) |
|
Nucleoside binding GO:0001882
Interacting selectively and non-covalently with a nucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked either to ribose or deoxyribose.
|
13 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(3 more) |
|
Transcription coactivator activity GO:0003713
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators 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. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator.
|
13 |
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
(3 more) |
|
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
|
13 |
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
(3 more) |
|
Actin binding GO:0003779
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
|
13 |
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
(3 more) |
|
Nuclear receptor transcription coactivator activity GO:0030374
The function of a transcription cofactor that activates transcription in conjuction with a ligand-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
|
13 |
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
(3 more) |
|
Chromatin DNA binding GO:0031490
Interacting selectively and non-covalently with DNA that is assembled into chromatin.
|
13 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(3 more) |
|
Nuclear hormone receptor binding GO:0035257
Interacting selectively and non-covalently with a nuclear hormone receptor, a ligand-dependent receptor found in the nucleus of the cell.
|
13 |
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
(3 more) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
13 |
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
(3 more) |
|
Retinoic acid receptor binding GO:0042974
Interacting selectively and non-covalently with the retinoic acid receptor, a ligand-regulated transcription factor belonging to the nuclear receptor superfamily.
|
13 |
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
O43707 (/IPI)
(3 more) |
|
Vinculin binding GO:0017166
Interacting selectively and non-covalently with vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane.
|
7 | P05094 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) Q7TPR4 (/IDA) |
|
Nuclear receptor transcription coactivator activity GO:0030374
The function of a transcription cofactor that activates transcription in conjuction with a ligand-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
|
7 | P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) Q9JI91 (/IDA) Q9JI91 (/IDA) |
|
Nuclear receptor transcription coactivator activity GO:0030374
The function of a transcription cofactor that activates transcription in conjuction with a ligand-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
|
7 | A5D7D1 (/ISS) P57780 (/ISS) P57780 (/ISS) Q5RCS6 (/ISS) Q90734 (/ISS) Q9QXQ0 (/ISS) Q9QXQ0 (/ISS) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
7 | P05094 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) Q7TPR4 (/IDA) |
|
Integrin binding GO:0005178
Interacting selectively and non-covalently with an integrin.
|
6 | P12814 (/IPI) P12814 (/IPI) P12814 (/IPI) P12814 (/IPI) P12814 (/IPI) Q7TPR4 (/IPI) |
|
Double-stranded RNA binding GO:0003725
Interacting selectively and non-covalently with double-stranded RNA.
|
5 | P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) |
|
Integrin binding GO:0005178
Interacting selectively and non-covalently with an integrin.
|
5 | P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) |
|
Vinculin binding GO:0017166
Interacting selectively and non-covalently with vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane.
|
5 | P12814 (/IPI) P12814 (/IPI) P12814 (/IPI) P12814 (/IPI) P12814 (/IPI) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
5 | P57780 (/ISO) P57780 (/ISO) Q7TPR4 (/ISO) Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
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.
|
5 | P57780 (/ISO) P57780 (/ISO) Q7TPR4 (/ISO) Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Structural constituent of postsynapse GO:0099186
The action of a molecule that contributes to the structural integrity of a postsynapse.
|
5 | P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) |
|
Structural constituent of postsynapse GO:0099186
The action of a molecule that contributes to the structural integrity of a postsynapse.
|
5 | P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) |
|
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 | O88990 (/TAS) O88990 (/TAS) Q9JI91 (/TAS) Q9JI91 (/TAS) |
|
Actin filament binding GO:0051015
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
|
4 | O88990 (/TAS) O88990 (/TAS) Q9JI91 (/TAS) Q9JI91 (/TAS) |
|
Cytoskeletal protein binding GO:0008092
Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
|
3 | P35609 (/IDA) Q9JI91 (/IDA) Q9JI91 (/IDA) |
|
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
3 | Q7TPR4 (/ISO) Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
LIM domain binding GO:0030274
Interacting selectively and non-covalently with a LIM domain (for Lin-11 Isl-1 Mec-3) of a protein, a domain with seven conserved cysteine residues and a histidine, that binds two zinc ions and acts as an interface for protein-protein interactions.
|
3 | P05094 (/IPI) Q9JI91 (/IPI) Q9JI91 (/IPI) |
|
Nuclear receptor transcription coactivator activity GO:0030374
The function of a transcription cofactor that activates transcription in conjuction with a ligand-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
|
3 | P57780 (/ISO) P57780 (/ISO) Q7TPR4 (/ISO) |
|
Actin filament binding GO:0051015
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
|
3 | P57780 (/ISO) P57780 (/ISO) Q7TPR4 (/ISO) |
|
RNA polymerase II regulatory region sequence-specific DNA binding GO:0000977
Interacting selectively and non-covalently with a specific sequence of DNA that is part of a regulatory region that controls the transcription of a gene or cistron by RNA polymerase II.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Nucleoside binding GO:0001882
Interacting selectively and non-covalently with a nucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked either to ribose or deoxyribose.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Transcription coactivator activity GO:0003713
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators 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. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Tropomyosin binding GO:0005523
Interacting selectively and non-covalently with tropomyosin, a protein associated with actin filaments both in cytoplasm and, in association with troponin, in the thin filament of striated muscle.
|
2 | Q3B7N2 (/IDA) Q3B7N2 (/IDA) |
|
Phosphatidylinositol-4,5-bisphosphate binding GO:0005546
Interacting selectively and non-covalently with phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Cytoskeletal protein binding GO:0008092
Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Structural constituent of muscle GO:0008307
The action of a molecule that contributes to the structural integrity of a muscle fiber.
|
2 | P35609 (/TAS) Q08043 (/TAS) |
|
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
2 | P35609 (/IPI) Q9Z1P2 (/IPI) |
|
Thyroid hormone receptor coactivator activity GO:0030375
The function of a transcription cofactor that activates transcription in conjunction with a thyroid hormone-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
|
2 | Q9JI91 (/IDA) Q9JI91 (/IDA) |
|
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.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Chromatin DNA binding GO:0031490
Interacting selectively and non-covalently with DNA that is assembled into chromatin.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Nuclear hormone receptor binding GO:0035257
Interacting selectively and non-covalently with a nuclear hormone receptor, a ligand-dependent receptor found in the nucleus of the cell.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Retinoic acid receptor binding GO:0042974
Interacting selectively and non-covalently with the retinoic acid receptor, a ligand-regulated transcription factor belonging to the nuclear receptor superfamily.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Protein membrane anchor GO:0043495
Interacting selectively and non-covalently with both a protein or protein complex and a membrane, in order to maintain the localization of the protein at a specific membrane location.
|
2 | Q3B7N2 (/NAS) Q3B7N2 (/NAS) |
|
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
2 | Q9QXQ0 (/IPI) Q9QXQ0 (/IPI) |
|
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Protein dimerization activity GO:0046983
The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
|
2 | Q9JI91 (/ISO) Q9JI91 (/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 | Q9QXQ0 (/IPI) Q9QXQ0 (/IPI) |
|
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 | P57780 (/ISO) P57780 (/ISO) |
|
FATZ binding GO:0051373
Interacting selectively and non-covalently with a member of the FATZ family of proteins, filamin-, actinin-, and telethonin-binding proteins of the Z-disc of striated muscle. FATZ proteins are located in the Z-disc of the sarcomere and are involved in a complex network of interactions with other Z-band components.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Titin Z domain binding GO:0070080
Interacting selectively and non-covalently with the titin Z domain, which recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Double-stranded RNA binding GO:0003725
Interacting selectively and non-covalently with double-stranded RNA.
|
1 | Q7TPR4 (/ISO) |
|
Actin binding GO:0003779
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
|
1 | P18091 (/IPI) |
|
Actin binding GO:0003779
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
|
1 | P18091 (/ISS) |
|
Integrin binding GO:0005178
Interacting selectively and non-covalently with an integrin.
|
1 | Q7TPR4 (/ISO) |
|
Phosphatidylinositol-4,5-bisphosphate binding GO:0005546
Interacting selectively and non-covalently with phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.
|
1 | P35609 (/IDA) |
|
Vinculin binding GO:0017166
Interacting selectively and non-covalently with vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane.
|
1 | P05094 (/IMP) |
|
Vinculin binding GO:0017166
Interacting selectively and non-covalently with vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane.
|
1 | Q7TPR4 (/ISO) |
|
IgE binding GO:0019863
Interacting selectively and non-covalently with an immunoglobulin of the IgE isotype.
|
1 | L7UZ85 (/IDA) |
|
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.
|
1 | P35609 (/IPI) |
|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | P35609 (/IPI) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
1 | P35609 (/IMP) |
|
Protein dimerization activity GO:0046983
The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
|
1 | P35609 (/IDA) |
|
Actin filament binding GO:0051015
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
|
1 | L7UZ85 (/ISS) |
|
Phosphoprotein binding GO:0051219
Interacting selectively and non-covalently with a phosphorylated protein.
|
1 | P05094 (/IPI) |
|
FATZ binding GO:0051373
Interacting selectively and non-covalently with a member of the FATZ family of proteins, filamin-, actinin-, and telethonin-binding proteins of the Z-disc of striated muscle. FATZ proteins are located in the Z-disc of the sarcomere and are involved in a complex network of interactions with other Z-band components.
|
1 | P35609 (/IDA) |
|
Alpha-actinin binding GO:0051393
Interacting selectively and non-covalently with alpha-actinin, one of a family of proteins that cross-link F-actin as antiparallel homodimers. Alpha-actinin has a molecular mass of 93-103 KDa; at the N-terminus there are two calponin homology domains, at the C-terminus there are two EF-hands. These two domains are connected by the rod domain. This domain is formed by triple-helical spectrin repeats.
|
1 | P05094 (/IDA) |
|
Titin Z domain binding GO:0070080
Interacting selectively and non-covalently with the titin Z domain, which recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34.
|
1 | P35609 (/IMP) |
|
Titin Z domain binding GO:0070080
Interacting selectively and non-covalently with the titin Z domain, which recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34.
|
1 | P35609 (/IPI) |
|
Structural constituent of postsynapse GO:0099186
The action of a molecule that contributes to the structural integrity of a postsynapse.
|
1 | Q7TPR4 (/ISO) |
There are 126 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 |
|---|---|---|
|
Sarcomere organization GO:0045214
The myofibril assembly process that results in the organization of muscle actomyosin into sarcomeres. The sarcomere is 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.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Skeletal muscle fiber development GO:0048741
The process whose specific outcome is the progression of the skeletal muscle fiber over time, from its formation to the mature structure. Muscle fibers are formed by the maturation of myotubes. They can be classed as slow, intermediate/fast or fast.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Regulation of apoptotic process GO:0042981
Any process that modulates the occurrence or rate of cell death by apoptotic process.
|
20 |
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
(10 more) |
|
Platelet degranulation GO:0002576
The regulated exocytosis of secretory granules containing preformed mediators such as histamine and serotonin by a platelet.
|
19 |
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
(9 more) |
|
Positive regulation of cellular component movement GO:0051272
Any process that activates or increases the frequency, rate or extent of the movement of a cellular component.
|
15 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(5 more) |
|
Positive regulation of cellular component movement GO:0051272
Any process that activates or increases the frequency, rate or extent of the movement of a cellular component.
|
15 |
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
(5 more) |
|
Vesicle transport along actin filament GO:0030050
Movement of a vesicle along an actin filament, mediated by motor proteins.
|
13 |
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
(3 more) |
|
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
13 |
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
(3 more) |
|
Positive regulation of sodium:proton antiporter activity GO:0032417
Any process that activates or increases the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
|
13 |
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
O43707 (/NAS)
(3 more) |
|
Tumor necrosis factor-mediated signaling pathway GO:0033209
A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
|
13 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(3 more) |
|
Peroxisome proliferator activated receptor signaling pathway GO:0035357
The series of molecular signals initiated by binding of a ligand to any of the peroxisome proliferator activated receptors (alpha, beta or gamma) in the nuclear membrane, and ending with the initiation or termination of the transcription of target genes.
|
13 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(3 more) |
|
Retinoic acid receptor signaling pathway GO:0048384
The series of molecular signals generated as a consequence of a retinoic acid receptor binding to one of its physiological ligands.
|
13 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(3 more) |
|
Negative regulation of substrate adhesion-dependent cell spreading GO:1900025
Any process that stops, prevents or reduces the frequency, rate or extent of substrate adhesion-dependent cell spreading.
|
13 |
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
(3 more) |
|
Positive regulation of NIK/NF-kappaB signaling GO:1901224
Any process that activates or increases the frequency, rate or extent of NIK/NF-kappaB signaling.
|
13 |
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
(3 more) |
|
Regulation of nucleic acid-templated transcription GO:1903506
Any process that modulates the frequency, rate or extent of nucleic acid-templated transcription.
|
13 |
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
O43707 (/IMP)
(3 more) |
|
Peroxisome proliferator activated receptor signaling pathway GO:0035357
The series of molecular signals initiated by binding of a ligand to any of the peroxisome proliferator activated receptors (alpha, beta or gamma) in the nuclear membrane, and ending with the initiation or termination of the transcription of target genes.
|
7 | A5D7D1 (/ISS) P57780 (/ISS) P57780 (/ISS) Q5RCS6 (/ISS) Q90734 (/ISS) Q9QXQ0 (/ISS) Q9QXQ0 (/ISS) |
|
Sarcomere organization GO:0045214
The myofibril assembly process that results in the organization of muscle actomyosin into sarcomeres. The sarcomere is 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.
|
7 | A0A2R8QBL5 (/IMP) D1GJ55 (/IMP) E9QFR8 (/IMP) P05094 (/IMP) P18091 (/IMP) P35609 (/IMP) Q2YDR5 (/IMP) |
|
Focal adhesion assembly GO:0048041
The aggregation and bonding together of a set of components to form a focal adhesion, a complex of intracellular signaling and structural proteins that provides a structural link between the internal actin cytoskeleton and the ECM, and also function as a locus of signal transduction activity.
|
7 | P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P35609 (/IMP) Q08043 (/IMP) |
|
Retinoic acid receptor signaling pathway GO:0048384
The series of molecular signals generated as a consequence of a retinoic acid receptor binding to one of its physiological ligands.
|
7 | A5D7D1 (/ISS) P57780 (/ISS) P57780 (/ISS) Q5RCS6 (/ISS) Q90734 (/ISS) Q9QXQ0 (/ISS) Q9QXQ0 (/ISS) |
|
Actin filament organization GO:0007015
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
|
5 | P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) |
|
Platelet formation GO:0030220
The process in which platelets bud from long processes extended by megakaryocytes.
|
5 | P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) |
|
Platelet morphogenesis GO:0036344
Generation and organization of a platelet, a non-nucleated disk-shaped cell formed by extrusion from megakaryocytes, found in the blood of all mammals, and mainly involved in blood coagulation.
|
5 | P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) |
|
Skeletal muscle fiber development GO:0048741
The process whose specific outcome is the progression of the skeletal muscle fiber over time, from its formation to the mature structure. Muscle fibers are formed by the maturation of myotubes. They can be classed as slow, intermediate/fast or fast.
|
5 | A0A2R8QBL5 (/IMP) D1GJ55 (/IMP) E9QFR8 (/IMP) P05094 (/IMP) Q2YDR5 (/IMP) |
|
Negative regulation of cellular component movement GO:0051271
Any process that stops, prevents, or reduces the frequency, rate or extent of the movement of a cellular component.
|
5 | P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) |
|
Actin filament network formation GO:0051639
The assembly of a network of actin filaments; actin filaments on different axes and with differing orientations are crosslinked together to form a mesh of filaments.
|
5 | P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) |
|
Eye development GO:0001654
The process whose specific outcome is the progression of the eye over time, from its formation to the mature structure. The eye is the organ of sight.
|
4 | A0A2R8QBL5 (/IMP) D1GJ55 (/IMP) E9QFR8 (/IMP) Q2YDR5 (/IMP) |
|
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.
|
4 | O88990 (/IDA) O88990 (/IDA) Q9JI91 (/IDA) Q9JI91 (/IDA) |
|
Heart development GO:0007507
The process whose specific outcome is the progression of the heart over time, from its formation to the mature structure. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood.
|
4 | A0A2R8QBL5 (/IMP) D1GJ55 (/IMP) E9QFR8 (/IMP) Q2YDR5 (/IMP) |
|
Myofibril assembly GO:0030239
Formation of myofibrils, the repeating units of striated muscle.
|
4 | A0A2R8QBL5 (/IMP) D1GJ55 (/IMP) E9QFR8 (/IMP) Q2YDR5 (/IMP) |
|
Microspike assembly GO:0030035
Formation of a microspike, a dynamic, actin-rich projection extending from the surface of a migrating animal cell.
|
3 | P20111 (/IDA) P20111 (/IDA) P35609 (/IDA) |
|
Focal adhesion assembly GO:0048041
The aggregation and bonding together of a set of components to form a focal adhesion, a complex of intracellular signaling and structural proteins that provides a structural link between the internal actin cytoskeleton and the ECM, and also function as a locus of signal transduction activity.
|
3 | Q7TPR4 (/ISO) Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Actin filament bundle assembly GO:0051017
The assembly of actin filament bundles; actin filaments are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
|
3 | P57780 (/IDA) P57780 (/IDA) Q7TPR4 (/IDA) |
|
Protein localization to plasma membrane GO:0072659
A process in which a protein is transported to, or maintained in, a specific location in the plasma membrane.
|
3 | P35609 (/IMP) Q9JI91 (/IMP) Q9JI91 (/IMP) |
|
Positive regulation of endocytic recycling GO:2001137
Any process that activates or increases the frequency, rate or extent of endocytic recycling.
|
3 | P35609 (/IMP) Q9JI91 (/IMP) Q9JI91 (/IMP) |
|
Positive regulation of cation channel activity GO:2001259
Any process that activates or increases the frequency, rate or extent of cation channel activity.
|
3 | P35609 (/IMP) Q9JI91 (/IMP) Q9JI91 (/IMP) |
|
Response to hypoxia GO:0001666
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
|
2 | Q9QXQ0 (/IEP) Q9QXQ0 (/IEP) |
|
Regulation of the force of skeletal muscle contraction GO:0014728
Any process that modulates the frequency, rate or extent of the force of skeletal muscle contraction. The force of skeletal muscle contraction is produced by acto-myosin interaction processes through the formation of cross bridges.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Skeletal muscle atrophy GO:0014732
A process, occurring in skeletal muscle, that is characterized by a decrease in protein content, fiber diameter, force production and fatigue resistance in response to different conditions such as starvation, aging and disuse.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Transition between fast and slow fiber GO:0014883
The process of conversion of fast-contracting muscle fibers to a slower character. This may involve slowing of contractile rate, slow myosin gene induction, increase in oxidative metabolic properties, altered electrophysiology and altered innervation. This process also regulates skeletal muscle adapatation.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Response to denervation involved in regulation of muscle adaptation GO:0014894
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 denervation stimulus. This process occurs as part of the regulation of muscle adaptation.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Microspike assembly GO:0030035
Formation of a microspike, a dynamic, actin-rich projection extending from the surface of a migrating animal cell.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Muscle filament sliding GO:0030049
The sliding of actin thin filaments and myosin thick filaments past each other in muscle contraction. This involves a process of interaction of myosin located on a thick filament with actin located on a thin filament. During this process ATP is split and forces are generated.
|
2 | P35609 (/TAS) Q08043 (/TAS) |
|
Vesicle transport along actin filament GO:0030050
Movement of a vesicle along an actin filament, mediated by motor proteins.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Positive regulation of fast-twitch skeletal muscle fiber contraction GO:0031448
Any process that activates or increases the frequency, rate or extent of fast-twitch skeletal muscle contraction.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Tumor necrosis factor-mediated signaling pathway GO:0033209
A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Peroxisome proliferator activated receptor signaling pathway GO:0035357
The series of molecular signals initiated by binding of a ligand to any of the peroxisome proliferator activated receptors (alpha, beta or gamma) in the nuclear membrane, and ending with the initiation or termination of the transcription of target genes.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Regulation of membrane potential GO:0042391
Any process that modulates the establishment or extent of a membrane potential, the electric potential existing across any membrane arising from charges in the membrane itself and from the charges present in the media on either side of the membrane.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Regulation of apoptotic process GO:0042981
Any process that modulates the occurrence or rate of cell death by apoptotic process.
|
2 | Q9QXQ0 (/IMP) Q9QXQ0 (/IMP) |
|
Regulation of apoptotic process GO:0042981
Any process that modulates the occurrence or rate of cell death by apoptotic process.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Negative regulation of potassium ion transport GO:0043267
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Positive regulation of potassium ion transport GO:0043268
Any process that activates or increases the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Regulation of ATPase activity GO:0043462
Any process that modulates the rate of ATP hydrolysis by an ATPase.
|
2 | Q3B7N2 (/IDA) Q3B7N2 (/IDA) |
|
Sarcomere organization GO:0045214
The myofibril assembly process that results in the organization of muscle actomyosin into sarcomeres. The sarcomere is 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.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Negative regulation of glycolytic process GO:0045820
Any process that stops, prevents, or reduces the frequency, rate or extent of glycolysis.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Regulation of neurotransmitter secretion GO:0046928
Any process that modulates the frequency, rate or extent of the regulated release of a neurotransmitter from a cell.
|
2 | Q3B7N2 (/NAS) Q3B7N2 (/NAS) |
|
Retinoic acid receptor signaling pathway GO:0048384
The series of molecular signals generated as a consequence of a retinoic acid receptor binding to one of its physiological ligands.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Positive regulation of pinocytosis GO:0048549
Any process that activates, maintains or increases the rate of pinocytosis. Pinocytosis is the process in which cells take in liquid material from their external environment; literally 'cell drinking'. Liquid is enclosed in vesicles, formed by invagination of the plasma membrane. These vesicles then move into the cell and pass their contents to endosomes.
|
2 | P57780 (/IMP) P57780 (/IMP) |
|
Positive regulation of skeletal muscle tissue growth GO:0048633
Any process that activates, maintains or increases the rate of skeletal muscle growth.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Positive regulation of skeletal muscle tissue growth GO:0048633
Any process that activates, maintains or increases the rate of skeletal muscle growth.
|
2 | Q08043 (/ISS) Q4VAM3 (/ISS) |
|
Positive regulation of skeletal muscle fiber development GO:0048743
Any process that activates, maintains or increases the rate of skeletal muscle fiber development. Muscle fibers are formed by the maturation of myotubes. They can be classed as slow, intermediate/fast or fast.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Establishment of localization GO:0051234
Any process that localizes a substance or cellular component. This may occur via movement, tethering or selective degradation.
|
2 | Q3B7N2 (/NAS) Q3B7N2 (/NAS) |
|
Negative regulation of cellular component movement GO:0051271
Any process that stops, prevents, or reduces the frequency, rate or extent of the movement of a cellular component.
|
2 | P57780 (/IDA) P57780 (/IDA) |
|
Positive regulation of cellular component movement GO:0051272
Any process that activates or increases the frequency, rate or extent of the movement of a cellular component.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Protein homotetramerization GO:0051289
The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Actin filament uncapping GO:0051695
The removal of capping protein from the end of actin filaments to free the ends for addition, exchange or removal of further actin subunits.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Cardiac muscle cell development GO:0055013
The process whose specific outcome is the progression of a cardiac muscle cell over time, from its formation to the mature state.
|
2 | Q9JI91 (/IMP) Q9JI91 (/IMP) |
|
Bone morphogenesis GO:0060349
The process in which bones are generated and organized.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Bicellular tight junction assembly GO:0070830
The aggregation, arrangement and bonding together of a set of components to form a tight junction, an occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet.
|
2 | P57780 (/IMP) P57780 (/IMP) |
|
Negative regulation of calcineurin-NFAT signaling cascade GO:0070885
Any process that stops, prevents, or reduces the frequency, rate or extent of the calcineurin-NFAT signaling cascade.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Protein localization to plasma membrane GO:0072659
A process in which a protein is transported to, or maintained in, a specific location in the plasma membrane.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Phospholipase C-activating angiotensin-activated signaling pathway GO:0086097
An angiotensin-mediated signaling pathway where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Regulation of muscle system process GO:0090257
Any process that modulates the frequency, rate or extent of a muscle system process, a multicellular organismal process carried out by any of the organs or tissues in a muscle system.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Negative regulation of oxidative phosphorylation GO:0090324
Any process that decreases the frequency, rate or extent of the chemical reactions and pathways resulting in the phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Negative regulation of oxidative phosphorylation GO:0090324
Any process that decreases the frequency, rate or extent of the chemical reactions and pathways resulting in the phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.
|
2 | Q08043 (/ISS) Q4VAM3 (/ISS) |
|
Negative regulation of cold-induced thermogenesis GO:0120163
Any process that stops, prevents, or reduces the rate of cold-induced thermogenesis.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Negative regulation of cold-induced thermogenesis GO:0120163
Any process that stops, prevents, or reduces the rate of cold-induced thermogenesis.
|
2 | Q08043 (/ISS) Q8R4I6 (/ISS) |
|
Negative regulation of substrate adhesion-dependent cell spreading GO:1900025
Any process that stops, prevents or reduces the frequency, rate or extent of substrate adhesion-dependent cell spreading.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Positive regulation of bone mineralization involved in bone maturation GO:1900159
Any process that activates or increases the frequency, rate or extent of bone mineralization involved in bone maturation.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Negative regulation of potassium ion transmembrane transporter activity GO:1901017
Any process that stops, prevents or reduces the frequency, rate or extent of potassium ion transmembrane transporter activity.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Positive regulation of potassium ion transmembrane transporter activity GO:1901018
Any process that activates or increases the frequency, rate or extent of potassium ion transmembrane transporter activity.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Negative regulation of relaxation of muscle GO:1901078
Any process that stops, prevents or reduces the frequency, rate or extent of relaxation of muscle.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Positive regulation of NIK/NF-kappaB signaling GO:1901224
Any process that activates or increases the frequency, rate or extent of NIK/NF-kappaB signaling.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Protein localization to bicellular tight junction GO:1902396
A process in which a protein is transported to, or maintained in, a location within a bicellular tight junction.
|
2 | P57780 (/IMP) P57780 (/IMP) |
|
Regulation of nucleic acid-templated transcription GO:1903506
Any process that modulates the frequency, rate or extent of nucleic acid-templated transcription.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Regulation of aerobic respiration GO:1903715
Any process that modulates the frequency, rate or extent of aerobic respiration.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Positive regulation of glucose catabolic process to lactate via pyruvate GO:1904025
Any process that activates or increases the frequency, rate or extent of glucose catabolic process to lactate via pyruvate.
|
2 | O88990 (/IMP) O88990 (/IMP) |
|
Negative regulation of protein localization to cell surface GO:2000009
Any process that stops, prevents, or reduces the frequency, rate or extent of protein localization to the cell surface.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Positive regulation of endocytic recycling GO:2001137
Any process that activates or increases the frequency, rate or extent of endocytic recycling.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Positive regulation of cation channel activity GO:2001259
Any process that activates or increases the frequency, rate or extent of cation channel activity.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
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.
|
1 | P35609 (/TAS) |
|
Actin filament organization GO:0007015
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
|
1 | Q7TPR4 (/ISO) |
|
Cytoskeletal anchoring at plasma membrane GO:0007016
A cytoskeleton organization process that directly or indirectly links cytoskeletal filaments to the plasma membrane.
|
1 | P18091 (/ISS) |
|
Cell adhesion GO:0007155
The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules.
|
1 | P35609 (/TAS) |
|
Regulation of the force of skeletal muscle contraction GO:0014728
Any process that modulates the frequency, rate or extent of the force of skeletal muscle contraction. The force of skeletal muscle contraction is produced by acto-myosin interaction processes through the formation of cross bridges.
|
1 | Q08043 (/ISS) |
|
Skeletal muscle atrophy GO:0014732
A process, occurring in skeletal muscle, that is characterized by a decrease in protein content, fiber diameter, force production and fatigue resistance in response to different conditions such as starvation, aging and disuse.
|
1 | Q08043 (/ISS) |
|
Transition between fast and slow fiber GO:0014883
The process of conversion of fast-contracting muscle fibers to a slower character. This may involve slowing of contractile rate, slow myosin gene induction, increase in oxidative metabolic properties, altered electrophysiology and altered innervation. This process also regulates skeletal muscle adapatation.
|
1 | Q08043 (/ISS) |
|
Response to denervation involved in regulation of muscle adaptation GO:0014894
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 denervation stimulus. This process occurs as part of the regulation of muscle adaptation.
|
1 | Q08043 (/ISS) |
|
Platelet formation GO:0030220
The process in which platelets bud from long processes extended by megakaryocytes.
|
1 | Q7TPR4 (/ISO) |
|
Cortical cytoskeleton organization GO:0030865
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
|
1 | Q7TPR4 (/TAS) |
|
Positive regulation of fast-twitch skeletal muscle fiber contraction GO:0031448
Any process that activates or increases the frequency, rate or extent of fast-twitch skeletal muscle contraction.
|
1 | Q4VAM3 (/ISS) |
|
Actin cytoskeleton reorganization GO:0031532
A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of constituent parts of cytoskeletal structures comprising actin filaments and their associated proteins.
|
1 | P18091 (/IMP) |
|
Platelet morphogenesis GO:0036344
Generation and organization of a platelet, a non-nucleated disk-shaped cell formed by extrusion from megakaryocytes, found in the blood of all mammals, and mainly involved in blood coagulation.
|
1 | Q7TPR4 (/ISO) |
|
Regulation of membrane potential GO:0042391
Any process that modulates the establishment or extent of a membrane potential, the electric potential existing across any membrane arising from charges in the membrane itself and from the charges present in the media on either side of the membrane.
|
1 | P35609 (/IMP) |
|
Negative regulation of potassium ion transport GO:0043267
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
|
1 | P35609 (/IMP) |
|
Positive regulation of potassium ion transport GO:0043268
Any process that activates or increases the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
|
1 | P35609 (/IDA) |
|
Sarcomere organization GO:0045214
The myofibril assembly process that results in the organization of muscle actomyosin into sarcomeres. The sarcomere is 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.
|
1 | P18091 (/IDA) |
|
Negative regulation of glycolytic process GO:0045820
Any process that stops, prevents, or reduces the frequency, rate or extent of glycolysis.
|
1 | Q08043 (/ISS) |
|
Positive regulation of skeletal muscle fiber development GO:0048743
Any process that activates, maintains or increases the rate of skeletal muscle fiber development. Muscle fibers are formed by the maturation of myotubes. They can be classed as slow, intermediate/fast or fast.
|
1 | Q4VAM3 (/ISS) |
|
Actin filament bundle assembly GO:0051017
The assembly of actin filament bundles; actin filaments are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
|
1 | P18091 (/IMP) |
|
Actin filament bundle assembly GO:0051017
The assembly of actin filament bundles; actin filaments are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
|
1 | L7UZ85 (/ISS) |
|
Negative regulation of cellular component movement GO:0051271
Any process that stops, prevents, or reduces the frequency, rate or extent of the movement of a cellular component.
|
1 | Q7TPR4 (/ISO) |
|
Protein homotetramerization GO:0051289
The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
|
1 | P35609 (/IDA) |
|
Actin filament network formation GO:0051639
The assembly of a network of actin filaments; actin filaments on different axes and with differing orientations are crosslinked together to form a mesh of filaments.
|
1 | Q7TPR4 (/ISO) |
|
Actin filament uncapping GO:0051695
The removal of capping protein from the end of actin filaments to free the ends for addition, exchange or removal of further actin subunits.
|
1 | P35609 (/IMP) |
|
Negative regulation of calcineurin-NFAT signaling cascade GO:0070885
Any process that stops, prevents, or reduces the frequency, rate or extent of the calcineurin-NFAT signaling cascade.
|
1 | Q08043 (/ISS) |
|
Phospholipase C-activating angiotensin-activated signaling pathway GO:0086097
An angiotensin-mediated signaling pathway where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
|
1 | P35609 (/IMP) |
|
Regulation of muscle system process GO:0090257
Any process that modulates the frequency, rate or extent of a muscle system process, a multicellular organismal process carried out by any of the organs or tissues in a muscle system.
|
1 | Q4VAM3 (/ISS) |
|
Negative regulation of potassium ion transmembrane transporter activity GO:1901017
Any process that stops, prevents or reduces the frequency, rate or extent of potassium ion transmembrane transporter activity.
|
1 | P35609 (/IMP) |
|
Positive regulation of potassium ion transmembrane transporter activity GO:1901018
Any process that activates or increases the frequency, rate or extent of potassium ion transmembrane transporter activity.
|
1 | P35609 (/IDA) |
|
Negative regulation of relaxation of muscle GO:1901078
Any process that stops, prevents or reduces the frequency, rate or extent of relaxation of muscle.
|
1 | Q4VAM3 (/ISS) |
|
Regulation of nucleic acid-templated transcription GO:1903506
Any process that modulates the frequency, rate or extent of nucleic acid-templated transcription.
|
1 | Q90734 (/ISS) |
|
Regulation of aerobic respiration GO:1903715
Any process that modulates the frequency, rate or extent of aerobic respiration.
|
1 | Q08043 (/ISS) |
|
Positive regulation of glucose catabolic process to lactate via pyruvate GO:1904025
Any process that activates or increases the frequency, rate or extent of glucose catabolic process to lactate via pyruvate.
|
1 | Q08043 (/ISS) |
|
Negative regulation of protein localization to cell surface GO:2000009
Any process that stops, prevents, or reduces the frequency, rate or extent of protein localization to the cell surface.
|
1 | P35609 (/IMP) |
|
Regulation of NMDA receptor activity GO:2000310
Any process that modulates the frequency, rate or extent of N-methyl-D-aspartate selective glutamate receptor activity.
|
1 | P35609 (/TAS) |
There are 94 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 |
|---|---|---|
|
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.
|
205 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(195 more) |
|
Stress fiber GO:0001725
A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Zonula adherens GO:0005915
A cell-cell adherens junction which forms a continuous belt near the apex of epithelial cells.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Bicellular tight junction GO:0005923
An occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet; the outer leaflets of the two interacting plasma membranes are seen to be tightly apposed where sealing strands are present. Each sealing strand is composed of a long row of transmembrane adhesion proteins embedded in each of the two interacting plasma membranes.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Lateral plasma membrane GO:0016328
The portion of the plasma membrane at the lateral side of the cell. In epithelial cells, lateral plasma membranes are on the sides of cells which lie at the interface of adjacent cells.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Lamellipodium GO:0030027
A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Smooth muscle dense body GO:0030486
Electron-dense region associated with a smooth muscle contractile fiber.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Cell leading edge GO:0031252
The area of a motile cell closest to the direction of movement.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Sarcolemma GO:0042383
The outer membrane of a muscle cell, consisting of the plasma membrane, a covering basement membrane (about 100 nm thick and sometimes common to more than one fiber), and the associated loose network of collagen fibers.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Outer dense plaque of desmosome GO:0090636
The desmosomal part containing plakoglobins, plakophilins, the N-termini of desmoplakins, as well as the cytoplasmic tails of the desmosomal cadherins, which together attach the plaque to the plasma membrane.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Inner dense plaque of desmosome GO:0090637
The desmosomal part containing the C-termini of desmoplakins which interact with the keratin intermediate filaments, serving to tether the intermediate filaments to the plasma membrane.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Dense body GO:0097433
An electron dense body which may contain granules.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 more) |
|
Terminal web GO:1990357
An actin-rich cytoskeletal network located beneath the microvilli of the apical plasma membrane of polarized epithelial cells. In addition to actin filaments, the terminal web may contain actin-binding proteins, myosin motor proteins, and intermediate filaments. The terminal web can function as a contractile structure that influences the spatial distribution of microvilli as well as the development and morphogenesis of tissues containing polarized epithelial cells.
|
204 |
A0A091D150 (/ISS)
A0A091F494 (/ISS)
A0A091F494 (/ISS)
A0A091G7Q0 (/ISS)
A0A091GWQ5 (/ISS)
A0A091GWQ5 (/ISS)
A0A091HM09 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
A0A091ITT8 (/ISS)
(194 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.
|
26 |
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
(16 more) |
|
Nuclear body GO:0016604
Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
|
26 |
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
A0A0S2Z3G9 (/IDA)
(16 more) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
23 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(13 more) |
|
Pseudopodium GO:0031143
A temporary protrusion or retractile process of a cell, associated with flowing movements of the protoplasm, and serving for locomotion and feeding.
|
20 |
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
(10 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.
|
20 |
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
(10 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.
|
19 |
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
(9 more) |
|
Platelet alpha granule lumen GO:0031093
The volume enclosed by the membrane of the platelet alpha granule.
|
19 |
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
O43707 (/TAS)
(9 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.
|
18 |
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
(8 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.
|
18 |
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
(8 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.
|
16 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(6 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.
|
15 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(5 more) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
13 |
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
O43707 (/HDA)
(3 more) |
|
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
13 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(3 more) |
|
Ribonucleoprotein complex GO:1990904
A macromolecular complex containing both protein and RNA molecules.
|
13 |
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
O43707 (/IDA)
(3 more) |
|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
12 |
D3ZCV0 (/TAS)
D3ZCV0 (/TAS)
P12814 (/TAS)
P12814 (/TAS)
P12814 (/TAS)
P12814 (/TAS)
P12814 (/TAS)
P35609 (/TAS)
Q08043 (/TAS)
Q9QXQ0 (/TAS)
(2 more) |
|
Z disc GO:0030018
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
|
9 | O88990 (/IDA) O88990 (/IDA) P18091 (/IDA) P35609 (/IDA) P57780 (/IDA) P57780 (/IDA) Q7TPR4 (/IDA) Q9JI91 (/IDA) Q9JI91 (/IDA) |
|
Stress fiber GO:0001725
A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber.
|
8 | P05094 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P57780 (/IDA) P57780 (/IDA) |
|
Cell-cell junction GO:0005911
A cell junction that forms a connection between two or more cells in a multicellular organism; excludes direct cytoplasmic junctions such as ring canals.
|
7 | P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P57780 (/IDA) P57780 (/IDA) |
|
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
|
7 | P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P35609 (/IMP) Q08043 (/IMP) |
|
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
|
7 | D3ZCV0 (/IDA) D3ZCV0 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) |
|
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
|
6 | P05094 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) |
|
Ribonucleoprotein complex GO:1990904
A macromolecular complex containing both protein and RNA molecules.
|
6 | A5D7D1 (/ISS) P57780 (/ISS) P57780 (/ISS) Q5RCS6 (/ISS) Q9QXQ0 (/ISS) Q9QXQ0 (/ISS) |
|
Ruffle GO:0001726
Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork.
|
5 | P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) |
|
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.
|
5 | A5D7D1 (/ISS) P57780 (/ISS) P57780 (/ISS) Q5RCS6 (/ISS) Q90734 (/ISS) |
|
Brush border GO:0005903
The dense covering of microvilli on the apical surface of a epithelial cells in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell.
|
5 | O88990 (/IDA) O88990 (/IDA) Q3ULT2 (/IDA) Q3ULT2 (/IDA) Q7TPR4 (/IDA) |
|
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.
|
5 | O88990 (/IDA) O88990 (/IDA) Q7TPR4 (/IDA) Q9JI91 (/IDA) Q9JI91 (/IDA) |
|
Cell projection GO:0042995
A prolongation or process extending from a cell, e.g. a flagellum or axon.
|
5 | P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) P12814 (/IDA) |
|
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
|
5 | P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) P12814 (/IMP) |
|
Striated muscle thin filament GO:0005865
Filaments formed of actin and associated proteins; attached to Z discs at either end of sarcomeres in myofibrils.
|
4 | H2L2C8 (/IDA) H2L2C9 (/IDA) Q23158 (/IDA) Q9XVU8 (/IDA) |
|
Striated muscle thin filament GO:0005865
Filaments formed of actin and associated proteins; attached to Z discs at either end of sarcomeres in myofibrils.
|
4 | O88990 (/TAS) O88990 (/TAS) Q9JI91 (/TAS) Q9JI91 (/TAS) |
|
Striated muscle dense body GO:0055120
A vinculin-containing myofibril attachment structure of striated muscle that connects sarcomeres to the extracellular matrix. In nematode body wall muscle, the dense body performs the dual role of Z-disk and costamere.
|
4 | H2L2C8 (/IDA) H2L2C9 (/IDA) Q23158 (/IDA) Q9XVU8 (/IDA) |
|
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.
|
3 | P57780 (/ISO) P57780 (/ISO) Q7TPR4 (/ISO) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
3 | P57780 (/ISO) P57780 (/ISO) Q7TPR4 (/ISO) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
3 | A5D7D1 (/ISS) Q5RCS6 (/ISS) Q90734 (/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.
|
3 | Q7TPR4 (/ISO) Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Filopodium GO:0030175
Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
|
3 | P20111 (/IDA) P20111 (/IDA) P35609 (/IDA) |
|
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
|
3 | Q7TPR4 (/ISO) Q9JI91 (/ISO) Q9JI91 (/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.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Actin filament GO:0005884
A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
|
2 | P35609 (/TAS) Q08043 (/TAS) |
|
Vesicle membrane GO:0012506
The lipid bilayer surrounding any membrane-bounded vesicle in the cell.
|
2 | Q3B7N2 (/NAS) Q3B7N2 (/NAS) |
|
Nuclear body GO:0016604
Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Z disc GO:0030018
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Z disc GO:0030018
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
|
2 | P20111 (/ISS) P20111 (/ISS) |
|
Filopodium GO:0030175
Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Cortical cytoskeleton GO:0030863
The portion of the cytoskeleton that lies just beneath the plasma membrane.
|
2 | P57780 (/IDA) P57780 (/IDA) |
|
Pseudopodium GO:0031143
A temporary protrusion or retractile process of a cell, associated with flowing movements of the protoplasm, and serving for locomotion and feeding.
|
2 | P57780 (/IDA) P57780 (/IDA) |
|
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
|
2 | Q9QXQ0 (/IDA) Q9QXQ0 (/IDA) |
|
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Postsynaptic density membrane GO:0098839
The membrane component of the postsynaptic density. This is the region of the postsynaptic membrane in which the population of neurotransmitter receptors involved in synaptic transmission are concentrated.
|
2 | D3ZCV0 (/IDA) D3ZCV0 (/IDA) |
|
Postsynaptic density membrane GO:0098839
The membrane component of the postsynaptic density. This is the region of the postsynaptic membrane in which the population of neurotransmitter receptors involved in synaptic transmission are concentrated.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Postsynaptic density, intracellular component GO:0099092
A network of proteins adjacent to the postsynaptic membrane forming an electron dense disc. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize neurotransmitter receptors in the adjacent membrane, such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
|
2 | D3ZCV0 (/IDA) D3ZCV0 (/IDA) |
|
Postsynaptic density, intracellular component GO:0099092
A network of proteins adjacent to the postsynaptic membrane forming an electron dense disc. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize neurotransmitter receptors in the adjacent membrane, such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
|
2 | Q9JI91 (/ISO) Q9JI91 (/ISO) |
|
Ribonucleoprotein complex GO:1990904
A macromolecular complex containing both protein and RNA molecules.
|
2 | P57780 (/ISO) P57780 (/ISO) |
|
Stress fiber GO:0001725
A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber.
|
1 | Q7TPR4 (/ISO) |
|
Stress fiber GO:0001725
A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber.
|
1 | Q7TPR4 (/TAS) |
|
Ruffle GO:0001726
Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork.
|
1 | Q7TPR4 (/ISO) |
|
Cell GO:0005623
The basic structural and functional unit of all organisms. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope.
|
1 | P05094 (/IDA) |
|
Cytoskeleton GO:0005856
Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
|
1 | P35609 (/NAS) |
|
Cell-cell junction GO:0005911
A cell junction that forms a connection between two or more cells in a multicellular organism; excludes direct cytoplasmic junctions such as ring canals.
|
1 | Q7TPR4 (/ISO) |
|
Zonula adherens GO:0005915
A cell-cell adherens junction which forms a continuous belt near the apex of epithelial cells.
|
1 | P05094 (/IDA) |
|
Fascia adherens GO:0005916
A cell-cell adherens junction that contains the transmembrane protein N-cadherin, which interacts with identical molecules from neighboring cells to form a tight mechanical intercellular link; forms a large portion of the intercalated disc, the structure at which myofibrils terminate in cardiomyocytes.
|
1 | Q7TPR4 (/IDA) |
|
Bicellular tight junction GO:0005923
An occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet; the outer leaflets of the two interacting plasma membranes are seen to be tightly apposed where sealing strands are present. Each sealing strand is composed of a long row of transmembrane adhesion proteins embedded in each of the two interacting plasma membranes.
|
1 | P05094 (/IDA) |
|
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
|
1 | Q7TPR4 (/TAS) |
|
Lateral plasma membrane GO:0016328
The portion of the plasma membrane at the lateral side of the cell. In epithelial cells, lateral plasma membranes are on the sides of cells which lie at the interface of adjacent cells.
|
1 | P05094 (/IDA) |
|
Lamellipodium GO:0030027
A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.
|
1 | P05094 (/IDA) |
|
Secretory granule GO:0030141
A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
|
1 | Q7TPR4 (/NAS) |
|
Smooth muscle dense body GO:0030486
Electron-dense region associated with a smooth muscle contractile fiber.
|
1 | P05094 (/IDA) |
|
Cortical cytoskeleton GO:0030863
The portion of the cytoskeleton that lies just beneath the plasma membrane.
|
1 | Q7TPR4 (/TAS) |
|
Cell leading edge GO:0031252
The area of a motile cell closest to the direction of movement.
|
1 | P05094 (/IDA) |
|
Dense core granule membrane GO:0032127
The lipid bilayer surrounding a dense core granule.
|
1 | Q7TPR4 (/TAS) |
|
Sarcolemma GO:0042383
The outer membrane of a muscle cell, consisting of the plasma membrane, a covering basement membrane (about 100 nm thick and sometimes common to more than one fiber), and the associated loose network of collagen fibers.
|
1 | P05094 (/IMP) |
|
Cell projection GO:0042995
A prolongation or process extending from a cell, e.g. a flagellum or axon.
|
1 | Q7TPR4 (/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.
|
1 | Q9Z1P2 (/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.
|
1 | Q7TPR4 (/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.
|
1 | P35609 (/TAS) |
|
Outer dense plaque of desmosome GO:0090636
The desmosomal part containing plakoglobins, plakophilins, the N-termini of desmoplakins, as well as the cytoplasmic tails of the desmosomal cadherins, which together attach the plaque to the plasma membrane.
|
1 | P05094 (/IDA) |
|
Inner dense plaque of desmosome GO:0090637
The desmosomal part containing the C-termini of desmoplakins which interact with the keratin intermediate filaments, serving to tether the intermediate filaments to the plasma membrane.
|
1 | P05094 (/IDA) |
|
Dense body GO:0097433
An electron dense body which may contain granules.
|
1 | P05094 (/IDA) |
|
Terminal web GO:1990357
An actin-rich cytoskeletal network located beneath the microvilli of the apical plasma membrane of polarized epithelial cells. In addition to actin filaments, the terminal web may contain actin-binding proteins, myosin motor proteins, and intermediate filaments. The terminal web can function as a contractile structure that influences the spatial distribution of microvilli as well as the development and morphogenesis of tissues containing polarized epithelial cells.
|
1 | P05094 (/IDA) |
