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: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 1: Tropomyosin alpha-1 chain isoform 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 31 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 homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
244 A7UMC0 (/ISS) C5J049 (/ISS) O96764 (/ISS) P02561 (/ISS) P04268 (/ISS) P04268 (/ISS) P04268 (/ISS) P04268 (/ISS) P07951 (/ISS) P07951 (/ISS)
(234 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.
228 H8WHA8 (/ISS) H8WHA8 (/ISS) P02561 (/ISS) P04268 (/ISS) P04268 (/ISS) P04268 (/ISS) P04268 (/ISS) P07951 (/ISS) P07951 (/ISS) P07951 (/ISS)
(218 more)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
226 P02561 (/ISS) P04268 (/ISS) P04268 (/ISS) P04268 (/ISS) P04268 (/ISS) P07951 (/ISS) P07951 (/ISS) P07951 (/ISS) P07951 (/ISS) P07951 (/ISS)
(216 more)
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
226 P02561 (/ISS) P04268 (/ISS) P04268 (/ISS) P04268 (/ISS) P04268 (/ISS) P07951 (/ISS) P07951 (/ISS) P07951 (/ISS) P07951 (/ISS) P07951 (/ISS)
(216 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).
143 P04268 (/IPI) P04268 (/IPI) P04268 (/IPI) P04268 (/IPI) P06753 (/IPI) P06753 (/IPI) P06753 (/IPI) P06753 (/IPI) P06753 (/IPI) P06753 (/IPI)
(133 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.
81 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(71 more)
Structural constituent of cytoskeleton GO:0005200
The action of a molecule that contributes to the structural integrity of a cytoskeletal structure.
54 P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P58771 (/TAS) P58771 (/TAS) P58771 (/TAS) P58771 (/TAS) P58771 (/TAS)
(44 more)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
51 A2V735 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(41 more)
Structural constituent of muscle GO:0008307
The action of a molecule that contributes to the structural integrity of a muscle fiber.
50 P07951 (/TAS) P07951 (/TAS) P07951 (/TAS) P07951 (/TAS) P07951 (/TAS) P07951 (/TAS) P07951 (/TAS) P07951 (/TAS) P07951 (/TAS) P07951 (/TAS)
(40 more)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
50 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(40 more)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
50 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(40 more)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
50 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(40 more)
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
50 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(40 more)
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
50 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(40 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.
50 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(40 more)
Actin binding GO:0003779
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
40 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(30 more)
Actin binding GO:0003779
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
29 P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS)
(19 more)
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
27 P67936 (/NAS) P67936 (/NAS) P67936 (/NAS) P67936 (/NAS) P67936 (/NAS) P67936 (/NAS) P67936 (/NAS) P67936 (/NAS) P67936 (/NAS) P67936 (/NAS)
(17 more)
Disordered domain specific binding GO:0097718
Interacting selectively and non-covalently with a disordered domain of a protein.
26 P04692 (/IPI) P04692 (/IPI) P04692 (/IPI) P04692 (/IPI) P04692 (/IPI) P04692 (/IPI) P04692 (/IPI) P04692 (/IPI) P04692 (/IPI) P04692 (/IPI)
(16 more)
Actin binding GO:0003779
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
22 P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP)
(12 more)
Actin binding GO:0003779
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Troponin I binding GO:0031013
Interacting selectively and non-covalently with troponin I, the inhibitory subunit of the troponin complex.
22 P58772 (/IPI) P58772 (/IPI) P58772 (/IPI) P58772 (/IPI) P58772 (/IPI) P58772 (/IPI) P58772 (/IPI) P58772 (/IPI) P58772 (/IPI) P58772 (/IPI)
(12 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.
22 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(12 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.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 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.
22 P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP)
(12 more)
Disordered domain specific binding GO:0097718
Interacting selectively and non-covalently with a disordered domain of a protein.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Cytoskeletal protein binding GO:0008092
Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
14 F1NM23 (/IPI) F1NM23 (/IPI) F1NM23 (/IPI) F1NM23 (/IPI) P04268 (/IPI) P04268 (/IPI) P04268 (/IPI) P04268 (/IPI) P09493 (/IPI) P09493 (/IPI)
(4 more)
Microtubule binding GO:0008017
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
2 Q5ZLJ7 (/ISS) Q5ZLJ7 (/ISS)
Kinesin binding GO:0019894
Interacting selectively and non-covalently and stoichiometrically with kinesin, a member of a superfamily of microtubule-based motor proteins that perform force-generating tasks such as organelle transport and chromosome segregation.
1 P49455 (/IPI)
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.
1 P06754 (/IPI)
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 G3UPJ2 (/IPI)

There are 75 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
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.
124 P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS) P04692 (/TAS)
(114 more)
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.
74 P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS)
(64 more)
Regulation of ATPase activity GO:0043462
Any process that modulates the rate of ATP hydrolysis by an ATPase.
40 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(30 more)
Cardiac muscle contraction GO:0060048
Muscle contraction of cardiac muscle tissue.
33 F1QKG7 (/IMP) F1R412 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP)
(23 more)
Osteoblast differentiation GO:0001649
The process whereby a relatively unspecialized cell acquires the specialized features of an osteoblast, a mesodermal or neural crest cell that gives rise to bone.
27 P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA)
(17 more)
Ventricular cardiac muscle tissue morphogenesis GO:0055010
The process in which the anatomical structures of cardiac ventricle muscle is generated and organized.
27 P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP)
(17 more)
In utero embryonic development GO:0001701
The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus.
22 P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP)
(12 more)
Positive regulation of heart rate by epinephrine GO:0003065
The process in which the secretion of epinephrine into the bloodstream or released from nerve endings increases the rate of heart muscle contraction.
22 P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP) P58771 (/IMP)
(12 more)
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.
22 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(12 more)
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.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Negative regulation of cell migration GO:0030336
Any process that stops, prevents, or reduces the frequency, rate or extent of cell migration.
22 P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI)
(12 more)
Negative regulation of cell migration GO:0030336
Any process that stops, prevents, or reduces the frequency, rate or extent of cell migration.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Ruffle organization GO:0031529
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a ruffle, a projection at the leading edge of a crawling cell.
22 P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI)
(12 more)
Ruffle organization GO:0031529
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a ruffle, a projection at the leading edge of a crawling cell.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Positive regulation of ATPase activity GO:0032781
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
22 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(12 more)
Positive regulation of ATPase activity GO:0032781
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
22 P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP) P04692 (/IMP)
(12 more)
Positive regulation of ATPase activity GO:0032781
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Wound healing GO:0042060
The series of events that restore integrity to a damaged tissue, following an injury.
22 P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI)
(12 more)
Wound healing GO:0042060
The series of events that restore integrity to a damaged tissue, following an injury.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Regulation of ATPase activity GO:0043462
Any process that modulates the rate of ATP hydrolysis by an ATPase.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Positive regulation of cell adhesion GO:0045785
Any process that activates or increases the frequency, rate or extent of cell adhesion.
22 P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI)
(12 more)
Positive regulation of cell adhesion GO:0045785
Any process that activates or increases the frequency, rate or extent of cell adhesion.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Positive regulation of stress fiber assembly GO:0051496
Any process that activates or increases the frequency, rate or extent of the assembly of a stress fiber, a bundle of microfilaments and other proteins found in fibroblasts.
22 P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI) P04692 (/IGI)
(12 more)
Positive regulation of stress fiber assembly GO:0051496
Any process that activates or increases the frequency, rate or extent of the assembly of a stress fiber, a bundle of microfilaments and other proteins found in fibroblasts.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Actin filament capping GO:0051693
The binding of a protein or protein complex to the end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits.
22 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(12 more)
Actin filament capping GO:0051693
The binding of a protein or protein complex to the end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Cardiac muscle contraction GO:0060048
Muscle contraction of cardiac muscle tissue.
22 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(12 more)
Cardiac muscle contraction GO:0060048
Muscle contraction of cardiac muscle tissue.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Regulation of muscle contraction GO:0006937
Any process that modulates the frequency, rate or extent of muscle contraction.
18 A7UMC0 (/ISS) C5J049 (/ISS) O96764 (/ISS) P0DSM6 (/ISS) P0DSM7 (/ISS) Q3BJY7 (/ISS) Q3Y8M6 (/ISS) Q3Y8M6 (/ISS) Q3Y8M6 (/ISS) Q3Y8M6 (/ISS)
(8 more)
Cardiac myofibril assembly GO:0055003
The process whose specific outcome is the progression of the cardiac myofibril over time, from its formation to the mature structure. A cardiac myofibril is a myofibril specific to cardiac muscle cells.
6 F1QKG7 (/IMP) F1R412 (/IMP) Q1LXM1 (/IMP) Q1LXM2 (/IMP) Q5U3J6 (/IMP) Q7T3F0 (/IMP)
Heart contraction GO:0060047
The multicellular organismal process in which the heart decreases in volume in a characteristic way to propel blood through the body.
6 F1QKG7 (/IMP) F1R412 (/IMP) Q1LXM1 (/IMP) Q1LXM2 (/IMP) Q5U3J6 (/IMP) Q7T3F0 (/IMP)
Positive regulation of heart rate by epinephrine GO:0003065
The process in which the secretion of epinephrine into the bloodstream or released from nerve endings increases the rate of heart muscle contraction.
5 P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS)
Regulation of muscle contraction GO:0006937
Any process that modulates the frequency, rate or extent of muscle contraction.
5 P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P09493 (/TAS)
Cytoskeleton organization GO:0007010
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures.
5 P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P09493 (/TAS)
Regulation of heart contraction GO:0008016
Any process that modulates the frequency, rate or extent of heart contraction. Heart contraction is the process in which the heart decreases in volume in a characteristic way to propel blood through the body.
5 P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P09493 (/TAS)
Regulation of cell shape GO:0008360
Any process that modulates the surface configuration of a cell.
5 P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP)
Skeletal myofibril assembly GO:0014866
The process whose specific outcome is the progression of the skeletal myofibril over time, from its formation to the mature structure. A skeletal myofibril is a myofibril specific to skeletal muscle cells.
5 A0A2R8Q650 (/IMP) A0A2R8RR81 (/IMP) I3ISQ1 (/IMP) Q6P0W3 (/IMP) Q803M1 (/IMP)
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.
5 P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS)
Negative regulation of cell migration GO:0030336
Any process that stops, prevents, or reduces the frequency, rate or extent of cell migration.
5 P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS)
Ruffle organization GO:0031529
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a ruffle, a projection at the leading edge of a crawling cell.
5 P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS)
Positive regulation of ATPase activity GO:0032781
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
5 P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS)
Cellular response to reactive oxygen species GO:0034614
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
5 P09493 (/IEP) P09493 (/IEP) P09493 (/IEP) P09493 (/IEP) P09493 (/IEP)
Wound healing GO:0042060
The series of events that restore integrity to a damaged tissue, following an injury.
5 P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/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.
5 P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP)
Positive regulation of cell adhesion GO:0045785
Any process that activates or increases the frequency, rate or extent of cell adhesion.
5 P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS)
Positive regulation of stress fiber assembly GO:0051496
Any process that activates or increases the frequency, rate or extent of the assembly of a stress fiber, a bundle of microfilaments and other proteins found in fibroblasts.
5 P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS) P09493 (/ISS)
Negative regulation of vascular smooth muscle cell proliferation GO:1904706
Any process that stops, prevents or reduces the frequency, rate or extent of vascular smooth muscle cell proliferation.
5 P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP)
Negative regulation of vascular associated smooth muscle cell migration GO:1904753
Any process that stops, prevents or reduces the frequency, rate or extent of vascular associated smooth muscle cell migration.
5 P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP)
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.
3 Q22866 (/IMP) Q22866 (/IMP) Q27249 (/IMP)
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.
3 P09491 (/IMP) P09491 (/IMP) P09491 (/IMP)
Regulation of actin filament polymerization GO:0030833
Any process that modulates the frequency, rate or extent of the assembly of actin filaments by the addition of actin monomers to a filament.
3 Q22866 (/IDA) Q22866 (/IDA) Q27249 (/IDA)
Negative regulation of actin filament depolymerization GO:0030835
Any process that stops, prevents, or reduces the frequency, rate or extent of actin depolymerization.
3 Q22866 (/IDA) Q22866 (/IDA) Q27249 (/IDA)
Spicule insertion GO:0034609
Insertion of the male copulatory spicules into the hermaphrodite. Spicule insertion behavior initiates when the male cloaca contacts the vulva. During most mating encounters, the spicule tips will prod the vulva continuously until they partially penetrate, which then causes the protractors to contract completely so that the spicules extend through the vulva.
3 Q22866 (/IMP) Q22866 (/IMP) Q27249 (/IMP)
Locomotion GO:0040011
Self-propelled movement of a cell or organism from one location to another.
3 Q22866 (/IMP) Q22866 (/IMP) Q27249 (/IMP)
Regulation of protein binding GO:0043393
Any process that modulates the frequency, rate or extent of protein binding.
3 Q22866 (/IDA) Q22866 (/IDA) Q27249 (/IDA)
Positive regulation of sarcomere organization GO:0060298
Any process that increases the rate, frequency or extent of myofibril assembly by 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.
3 P09491 (/IGI) P09491 (/IGI) P09491 (/IGI)
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.
2 P06754 (/NAS) P49455 (/NAS)
Regulation of muscle contraction GO:0006937
Any process that modulates the frequency, rate or extent of muscle contraction.
2 Q22866 (/IMP) Q22866 (/IMP)
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.
2 H8WHA8 (/ISS) H8WHA8 (/ISS)
Pole plasm assembly GO:0007315
Establishment of the specialized cytoplasm found at the poles of the egg. An example of this is found in Drosophila melanogaster.
2 P06754 (/NAS) P49455 (/NAS)
Regulation of lamellipodium assembly GO:0010591
Any process that modulates the rate, frequency or extent of the formation of a lamellipodium, a thin sheetlike extension of the surface of a migrating cell.
2 P06754 (/IMP) P49455 (/IMP)
Spicule insertion GO:0034609
Insertion of the male copulatory spicules into the hermaphrodite. Spicule insertion behavior initiates when the male cloaca contacts the vulva. During most mating encounters, the spicule tips will prod the vulva continuously until they partially penetrate, which then causes the protractors to contract completely so that the spicules extend through the vulva.
2 H8WHA8 (/ISS) H8WHA8 (/ISS)
Locomotion GO:0040011
Self-propelled movement of a cell or organism from one location to another.
2 H8WHA8 (/ISS) H8WHA8 (/ISS)
Pole plasm oskar mRNA localization GO:0045451
Any process in which oskar mRNA is transported to, or maintained in, the oocyte pole plasm.
2 P06754 (/IMP) P49455 (/IMP)
Pole plasm oskar mRNA localization GO:0045451
Any process in which oskar mRNA is transported to, or maintained in, the oocyte pole plasm.
2 P06754 (/TAS) P49455 (/TAS)
Oogenesis GO:0048477
The complete process of formation and maturation of an ovum or female gamete from a primordial female germ cell. Examples of this process are found in Mus musculus and Drosophila melanogaster.
2 P06754 (/TAS) P49455 (/TAS)
Dendrite morphogenesis GO:0048813
The process in which the anatomical structures of a dendrite are generated and organized.
2 P06754 (/IMP) P49455 (/IMP)
Dendrite morphogenesis GO:0048813
The process in which the anatomical structures of a dendrite are generated and organized.
2 P06754 (/TAS) P49455 (/TAS)
Response to hyperoxia GO:0055093
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 increased oxygen tension.
2 P06754 (/IMP) P49455 (/IMP)
Brain development GO:0007420
The process whose specific outcome is the progression of the brain over time, from its formation to the mature structure. Brain development begins with patterning events in the neural tube and ends with the mature structure that is the center of thought and emotion. The brain is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.).
1 Q63610 (/IEP)
Embryo development ending in birth or egg hatching GO:0009792
The process whose specific outcome is the progression of an embryo over time, from zygote formation until the end of the embryonic life stage. The end of the embryonic life stage is organism-specific and may be somewhat arbitrary; for mammals it is usually considered to be birth, for insects the hatching of the first instar larva from the eggshell.
1 Q27249 (/IMP)
Response to lipopolysaccharide GO:0032496
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria.
1 A0A060W8G0 (/IDA)
Stress fiber assembly GO:0043149
The aggregation, arrangement and bonding together of a set of components to form a stress fiber. A stress fiber is a contractile actin filament bundle that consists of short actin filaments with alternating polarity.
1 P49455 (/IMP)
Myeloid cell development GO:0061515
The process whose specific outcome is the progression of a myeloid cell over time, from its formation to the mature structure.
1 P13104 (/IMP)
Positive regulation of actin-dependent ATPase activity GO:1904623
Any process that activates or increases the frequency, rate or extent of actin-dependent ATPase activity.
1 G3UPJ2 (/IDA)

There are 38 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
Actin cytoskeleton GO:0015629
The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
194 P02561 (/ISS) P04268 (/ISS) P04268 (/ISS) P04268 (/ISS) P04268 (/ISS) P07951 (/ISS) P07951 (/ISS) P07951 (/ISS) P07951 (/ISS) P07951 (/ISS)
(184 more)
Actin cytoskeleton GO:0015629
The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
154 A0A024R5W6 (/IDA) A0A024R5W6 (/IDA) A0A024R5W6 (/IDA) A0A0K0K1I0 (/IDA) A0A0K0K1I0 (/IDA) A0A0K0K1I0 (/IDA) A0A0S2Z4G4 (/IDA) A0A0S2Z4G4 (/IDA) A0A0S2Z4G4 (/IDA) A0A0S2Z4G4 (/IDA)
(144 more)
Muscle thin filament tropomyosin GO:0005862
A form of the tropomyosin dimer found associated with actin and the troponin complex in muscle thin filaments.
123 P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS)
(113 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.
104 A0A024R5W6 (/IDA) A0A024R5W6 (/IDA) A0A024R5W6 (/IDA) A0A0K0K1I0 (/IDA) A0A0K0K1I0 (/IDA) A0A0K0K1I0 (/IDA) A0A0S2Z4G4 (/IDA) A0A0S2Z4G4 (/IDA) A0A0S2Z4G4 (/IDA) A0A0S2Z4G4 (/IDA)
(94 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.
74 P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS)
(64 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.
56 P06753 (/IDA) P06753 (/IDA) P06753 (/IDA) P06753 (/IDA) P06753 (/IDA) P06753 (/IDA) P06753 (/IDA) P06753 (/IDA) P06753 (/IDA) P06753 (/IDA)
(46 more)
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.
56 P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS) P06753 (/TAS)
(46 more)
Actin cytoskeleton GO:0015629
The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
53 P21107 (/ISO) P21107 (/ISO) P21107 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(43 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.
51 P06753 (/HDA) P06753 (/HDA) P06753 (/HDA) P06753 (/HDA) P06753 (/HDA) P06753 (/HDA) P06753 (/HDA) P06753 (/HDA) P06753 (/HDA) P06753 (/HDA)
(41 more)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
29 P21107 (/IDA) P21107 (/IDA) P21107 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA)
(19 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.
27 P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA)
(17 more)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
27 P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA) P67936 (/HDA)
(17 more)
Myofibril GO:0030016
The contractile element of skeletal and cardiac muscle; a long, highly organized bundle of actin, myosin, and other proteins that contracts by a sliding filament mechanism.
26 P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA) P58771 (/IDA)
(16 more)
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.
24 P06753 (/NAS) P06753 (/NAS) P06753 (/NAS) P06753 (/NAS) P06753 (/NAS) P06753 (/NAS) P06753 (/NAS) P06753 (/NAS) P06753 (/NAS) P06753 (/NAS)
(14 more)
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.
22 P58772 (/IMP) P58772 (/IMP) P58772 (/IMP) P58772 (/IMP) P58772 (/IMP) P58772 (/IMP) P58772 (/IMP) P58772 (/IMP) P58772 (/IMP) P58772 (/IMP)
(12 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.
22 P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA) P04692 (/IDA)
(12 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.
22 P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO) P58771 (/ISO)
(12 more)
Striated muscle thin filament GO:0005865
Filaments formed of actin and associated proteins; attached to Z discs at either end of sarcomeres in myofibrils.
8 A0A0R4IAL5 (/IDA) A0A0R4IM99 (/IDA) A0A0R4IMN8 (/IDA) A0A0R4INL7 (/IDA) Q22866 (/IDA) Q22866 (/IDA) Q27249 (/IDA) Q6IQD7 (/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.
6 P06754 (/IDA) P49455 (/IDA) Q5KR49 (/IDA) Q5KR49 (/IDA) Q5KR49 (/IDA) Q5KR49 (/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 P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P09493 (/TAS) P09493 (/TAS)
Bleb GO:0032059
A cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Blebs are formed during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses.
5 P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP) P09493 (/IMP)
Ruffle membrane GO:0032587
The portion of the plasma membrane surrounding a ruffle.
5 P09493 (/IDA) P09493 (/IDA) P09493 (/IDA) P09493 (/IDA) P09493 (/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.
4 P21107 (/ISO) P21107 (/ISO) P21107 (/ISO) Q6IRU2 (/ISO)
Podosome GO:0002102
An actin-rich adhesion structure characterized by formation upon cell substrate contact and localization at the substrate-attached part of the cell, contain an F-actin-rich core surrounded by a ring structure containing proteins such as vinculin and talin, and have a diameter of 0.5 mm.
4 P21107 (/IDA) P21107 (/IDA) P21107 (/IDA) Q6IRU2 (/IDA)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
4 P04268 (/IDA) P04268 (/IDA) P04268 (/IDA) P04268 (/IDA)
Cortical cytoskeleton GO:0030863
The portion of the cytoskeleton that lies just beneath the plasma membrane.
4 P21107 (/IDA) P21107 (/IDA) P21107 (/IDA) Q6IRU2 (/IDA)
Cardiac myofibril GO:0097512
A cardiac myofibril is a myofibril specific to cardiac muscle cells.
4 Q5KR49 (/IDA) Q5KR49 (/IDA) Q5KR49 (/IDA) Q5KR49 (/IDA)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
3 P21107 (/ISO) P21107 (/ISO) P21107 (/ISO)
Growth cone GO:0030426
The migrating motile tip of a growing neuron projection, where actin accumulates, and the actin cytoskeleton is the most dynamic.
3 P21107 (/IDA) P21107 (/IDA) P21107 (/IDA)
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
3 P21107 (/IDA) P21107 (/IDA) P21107 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
2 H8WHA8 (/ISS) H8WHA8 (/ISS)
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 P06754 (/HDA) P49455 (/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 P06754 (/IDA) P49455 (/IDA)
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.
1 G3UPJ2 (/IDA)
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.
1 Q63610 (/IDA)
Myofilament GO:0036379
Any of the smallest contractile units of a myofibril (striated muscle fiber).
1 A0A060W8G0 (/IDA)
P granule GO:0043186
A small cytoplasmic, non-membranous RNA/protein complex aggregates in the primordial germ cells of many higher eukaryotes.
1 P49455 (/IDA)
Contractile fiber GO:0043292
Fibers, composed of actin, myosin, and associated proteins, found in cells of smooth or striated muscle.
1 Q3BJY7 (/IDA)