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 52: Syntrophin beta 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 11 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
11 |
B5DFL0 (/IPI)
Q13424 (/IPI)
Q13425 (/IPI)
Q13425 (/IPI)
Q13425 (/IPI)
Q13884 (/IPI)
Q28626 (/IPI)
Q61234 (/IPI)
Q61235 (/IPI)
Q61235 (/IPI)
(1 more) |
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
|
3 | Q13425 (/HDA) Q13425 (/HDA) Q13425 (/HDA) |
Structural constituent of muscle GO:0008307
The action of a molecule that contributes to the structural integrity of a muscle fiber.
|
3 | M9PGE3 (/ISS) Q9VNY2 (/ISS) Q9VNY4 (/ISS) |
PDZ domain binding GO:0030165
Interacting selectively and non-covalently with a PDZ domain of a protein, a domain found in diverse signaling proteins.
|
2 | B5DFL0 (/IPI) D3ZWC6 (/IPI) |
PDZ domain binding GO:0030165
Interacting selectively and non-covalently with a PDZ domain of a protein, a domain found in diverse signaling proteins.
|
2 | Q61234 (/ISO) Q99L88 (/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.
|
2 | Q13424 (/IPI) Q61234 (/IPI) |
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.
|
1 | Q61234 (/ISO) |
Nitric-oxide synthase binding GO:0050998
Interacting selectively and non-covalently with the enzyme nitric-oxide synthase.
|
1 | Q13424 (/IPI) |
Nitric-oxide synthase binding GO:0050998
Interacting selectively and non-covalently with the enzyme nitric-oxide synthase.
|
1 | Q61234 (/ISO) |
ATPase binding GO:0051117
Interacting selectively and non-covalently with an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
|
1 | Q13424 (/IPI) |
ATPase binding GO:0051117
Interacting selectively and non-covalently with an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
|
1 | Q61234 (/ISO) |
There are 16 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 |
---|---|---|
Regulation of synaptic growth at neuromuscular junction GO:0008582
Any process that modulates the frequency, rate or extent of synaptic growth at neuromuscular junctions.
|
3 | M9PGE3 (/IGI) Q9VNY2 (/IGI) Q9VNY4 (/IGI) |
Locomotion GO:0040011
Self-propelled movement of a cell or organism from one location to another.
|
3 | M9PGE3 (/IMP) Q9VNY2 (/IMP) Q9VNY4 (/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.
|
2 | Q13424 (/TAS) Q13884 (/TAS) |
Regulation of heart rate GO:0002027
Any process that modulates the frequency or rate of heart contraction.
|
1 | Q13424 (/IMP) |
Regulation of heart rate GO:0002027
Any process that modulates the frequency or rate of heart contraction.
|
1 | Q61234 (/ISO) |
Regulation of vasoconstriction by circulating norepinephrine GO:0003117
Any process that modulates the frequency, rate or extent of reductions in the diameter of blood vessels as a result of secretion of norepinephrine into the bloodstream.
|
1 | Q61234 (/IMP) |
Neuromuscular junction development GO:0007528
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a neuromuscular junction.
|
1 | Q61234 (/IMP) |
Intracellular signal transduction GO:0035556
The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
|
1 | Q28626 (/IDA) |
Regulation of ventricular cardiac muscle cell membrane repolarization GO:0060307
Any process that modulates the establishment or extent of a membrane potential in the polarizing direction towards the resting potential in a ventricular cardiomyocyte.
|
1 | Q13424 (/IMP) |
Regulation of ventricular cardiac muscle cell membrane repolarization GO:0060307
Any process that modulates the establishment or extent of a membrane potential in the polarizing direction towards the resting potential in a ventricular cardiomyocyte.
|
1 | Q61234 (/ISO) |
Ventricular cardiac muscle cell action potential GO:0086005
An action potential that occurs in a ventricular cardiac muscle cell.
|
1 | Q13424 (/IMP) |
Ventricular cardiac muscle cell action potential GO:0086005
An action potential that occurs in a ventricular cardiac muscle cell.
|
1 | Q61234 (/ISO) |
Negative regulation of peptidyl-cysteine S-nitrosylation GO:1902083
Any process that stops, prevents or reduces the frequency, rate or extent of peptidyl-cysteine S-nitrosylation.
|
1 | Q13424 (/IMP) |
Negative regulation of peptidyl-cysteine S-nitrosylation GO:1902083
Any process that stops, prevents or reduces the frequency, rate or extent of peptidyl-cysteine S-nitrosylation.
|
1 | Q61234 (/ISO) |
Regulation of sodium ion transmembrane transport GO:1902305
Any process that modulates the frequency, rate or extent of sodium ion transmembrane transport.
|
1 | Q13424 (/IMP) |
Regulation of sodium ion transmembrane transport GO:1902305
Any process that modulates the frequency, rate or extent of sodium ion transmembrane transport.
|
1 | Q61234 (/ISO) |
There are 15 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 |
---|---|---|
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.
|
5 | Q13424 (/IDA) Q13425 (/IDA) Q13425 (/IDA) Q13425 (/IDA) Q13884 (/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.
|
4 | Q13425 (/HDA) Q13425 (/HDA) Q13425 (/HDA) Q13884 (/HDA) |
Dystrophin-associated glycoprotein complex GO:0016010
A multiprotein complex that forms a strong mechanical link between the cytoskeleton and extracellular matrix; typical of, but not confined to, muscle cells. The complex is composed of transmembrane, cytoplasmic, and extracellular proteins, including dystrophin, sarcoglycans, dystroglycan, dystrobrevins, syntrophins, sarcospan, caveolin-3, and NO synthase.
|
4 | Q13425 (/TAS) Q13425 (/TAS) Q13425 (/TAS) Q13884 (/TAS) |
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.
|
4 | Q61234 (/ISO) Q61235 (/ISO) Q61235 (/ISO) Q99L88 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
3 | Q13425 (/IDA) Q13425 (/IDA) Q13425 (/IDA) |
Syntrophin complex GO:0016013
A protein complex that includes alpha-, beta1-, beta2-syntrophins and syntrophin-like proteins; the syntrophin complex binds to the second half of the carboxy-terminal domain of dystrophin; also associates with neuronal nitric oxide synthase.
|
3 | M9PGE3 (/ISS) Q9VNY2 (/ISS) Q9VNY4 (/ISS) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
3 | Q13425 (/TAS) Q13425 (/TAS) Q13425 (/TAS) |
Synapse GO:0045202
The junction between a nerve fiber of one neuron and another neuron, muscle fiber or glial cell. As the nerve fiber approaches the synapse it enlarges into a specialized structure, the presynaptic nerve ending, which contains mitochondria and synaptic vesicles. At the tip of the nerve ending is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic nerve ending secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
|
3 | Q61235 (/IDA) Q61235 (/IDA) Q99L88 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | Q61235 (/ISO) Q61235 (/ISO) |
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.
|
2 | B5DFL0 (/IDA) Q61234 (/IDA) |
Syntrophin complex GO:0016013
A protein complex that includes alpha-, beta1-, beta2-syntrophins and syntrophin-like proteins; the syntrophin complex binds to the second half of the carboxy-terminal domain of dystrophin; also associates with neuronal nitric oxide synthase.
|
1 | Q13424 (/TAS) |
Neuromuscular junction GO:0031594
The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential.
|
1 | B5DFL0 (/IDA) |
Neuromuscular junction GO:0031594
The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential.
|
1 | Q61234 (/ISO) |
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 | Q61234 (/ISO) |
Postsynaptic membrane GO:0045211
A specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters cross the synaptic cleft and transmit the signal to the postsynaptic membrane.
|
1 | Q61234 (/IDA) |