The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"titin domain like
".
FunFam 1: Titin-cap (Telethonin)
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 16 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).
|
5 | A6HIS0 (/IPI) O15273 (/IPI) O15273 (/IPI) O70548 (/IPI) O70548 (/IPI) |
Structural constituent of muscle GO:0008307
The action of a molecule that contributes to the structural integrity of a muscle fiber.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Structural constituent of muscle GO:0008307
The action of a molecule that contributes to the structural integrity of a muscle fiber.
|
2 | O70548 (/ISO) O70548 (/ISO) |
Structural constituent of muscle GO:0008307
The action of a molecule that contributes to the structural integrity of a muscle fiber.
|
2 | O15273 (/TAS) O15273 (/TAS) |
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.
|
2 | O15273 (/IDA) O15273 (/IDA) |
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.
|
2 | O70548 (/ISO) O70548 (/ISO) |
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 | O15273 (/IPI) O15273 (/IPI) |
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 | O70548 (/ISO) O70548 (/ISO) |
BMP binding GO:0036122
Interacting selectively and non-covalently with a member of the bone morphogenetic protein (BMP) family.
|
2 | O15273 (/IPI) O15273 (/IPI) |
BMP binding GO:0036122
Interacting selectively and non-covalently with a member of the bone morphogenetic protein (BMP) family.
|
2 | O70548 (/ISO) O70548 (/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 | O15273 (/IPI) O15273 (/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.
|
2 | O70548 (/ISO) O70548 (/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 | O15273 (/IPI) O15273 (/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.
|
2 | O70548 (/ISO) O70548 (/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 | O15273 (/IPI) O15273 (/IPI) |
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 | O70548 (/ISO) O70548 (/ISO) |
There are 33 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 |
---|---|---|
Somitogenesis GO:0001756
The formation of mesodermal clusters that are arranged segmentally along the anterior posterior axis of an embryo.
|
2 | O70548 (/IEP) O70548 (/IEP) |
Skeletal muscle contraction GO:0003009
A process in which force is generated within skeletal 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. In the skeletal muscle, the muscle contraction takes advantage of an ordered sarcomeric structure and in most cases it is under voluntary control.
|
2 | O15273 (/IEP) O15273 (/IEP) |
Cardiac muscle hypertrophy GO:0003300
The enlargement or overgrowth of all or part of the heart muscle due to an increase in size of cardiac muscle cells without cell division.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Cardiac muscle hypertrophy GO:0003300
The enlargement or overgrowth of all or part of the heart muscle due to an increase in size of cardiac muscle cells without cell division.
|
2 | O70548 (/ISO) O70548 (/ISO) |
Adult heart development GO:0007512
The process whose specific outcome is the progression of the adult heart over time, from its formation to the mature structure.
|
2 | O70548 (/IEP) O70548 (/IEP) |
Adult heart development GO:0007512
The process whose specific outcome is the progression of the adult heart over time, from its formation to the mature structure.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Adult heart development GO:0007512
The process whose specific outcome is the progression of the adult heart over time, from its formation to the mature structure.
|
2 | O70548 (/ISO) O70548 (/ISO) |
Cardiac muscle hypertrophy in response to stress GO:0014898
The physiological enlargement or overgrowth of all or part of the heart muscle due to an increase in size (not length) of individual cardiac muscle fibers, without cell division, as a result of a disturbance in organismal or cellular homeostasis.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Cardiac muscle hypertrophy in response to stress GO:0014898
The physiological enlargement or overgrowth of all or part of the heart muscle due to an increase in size (not length) of individual cardiac muscle fibers, without cell division, as a result of a disturbance in organismal or cellular homeostasis.
|
2 | O70548 (/ISO) O70548 (/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 | O15273 (/TAS) O15273 (/TAS) |
Skeletal muscle thin filament assembly GO:0030240
The aggregation, arrangement and bonding together of proteins to form the actin-based thin filaments of myofibrils in skeletal muscle.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Skeletal muscle thin filament assembly GO:0030240
The aggregation, arrangement and bonding together of proteins to form the actin-based thin filaments of myofibrils in skeletal muscle.
|
2 | O70548 (/ISO) O70548 (/ISO) |
Skeletal muscle myosin thick filament assembly GO:0030241
The aggregation, arrangement and bonding together of proteins to form the myosin-based thick filaments of myofibrils in skeletal muscle.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Skeletal muscle myosin thick filament assembly GO:0030241
The aggregation, arrangement and bonding together of proteins to form the myosin-based thick filaments of myofibrils in skeletal muscle.
|
2 | O70548 (/ISO) O70548 (/ISO) |
Otic vesicle formation GO:0030916
The process resulting in the transition of the otic placode into the otic vesicle, a transient embryonic structure formed during development of the vertebrate inner ear.
|
2 | O70548 (/IEP) O70548 (/IEP) |
Response to muscle stretch GO:0035994
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 myofibril being extended beyond its slack length.
|
2 | O15273 (/TAS) O15273 (/TAS) |
Detection of muscle stretch GO:0035995
The series of events by which a muscle stretch stimulus is received by a cell and converted into a molecular signal.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Detection of muscle stretch GO:0035995
The series of events by which a muscle stretch stimulus is received by a cell and converted into a molecular signal.
|
2 | O70548 (/ISO) O70548 (/ISO) |
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 | O15273 (/IMP) O15273 (/IMP) |
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 | O70548 (/ISO) O70548 (/ISO) |
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 | O15273 (/TAS) O15273 (/TAS) |
Cardiac muscle fiber development GO:0048739
The process whose specific outcome is the progression of cardiac muscle fiber over time, from its formation to the mature structure.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Cardiac muscle fiber development GO:0048739
The process whose specific outcome is the progression of cardiac muscle fiber over time, from its formation to the mature structure.
|
2 | O70548 (/ISO) O70548 (/ISO) |
Sarcomerogenesis GO:0048769
The process in which sarcomeres are added in series within a fiber.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Sarcomerogenesis GO:0048769
The process in which sarcomeres are added in series within a fiber.
|
2 | O70548 (/ISO) O70548 (/ISO) |
Detection of mechanical stimulus GO:0050982
The series of events by which a mechanical stimulus is received and converted into a molecular signal.
|
2 | O15273 (/TAS) O15273 (/TAS) |
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.
|
2 | O15273 (/IMP) O15273 (/IMP) |
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.
|
2 | O70548 (/ISO) O70548 (/ISO) |
Cardiac muscle tissue morphogenesis GO:0055008
The process in which the anatomical structures of cardiac muscle tissue are generated and organized.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Cardiac muscle tissue morphogenesis GO:0055008
The process in which the anatomical structures of cardiac muscle tissue are generated and organized.
|
2 | O70548 (/ISO) O70548 (/ISO) |
Cardiac muscle contraction GO:0060048
Muscle contraction of cardiac muscle tissue.
|
2 | O15273 (/IMP) O15273 (/IMP) |
Cardiac muscle contraction GO:0060048
Muscle contraction of cardiac muscle tissue.
|
2 | O70548 (/ISO) O70548 (/ISO) |
Protein-containing complex assembly GO:0065003
The aggregation, arrangement and bonding together of a set of macromolecules to form a protein-containing complex.
|
2 | O15273 (/TAS) O15273 (/TAS) |
There are 5 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 |
---|---|---|
Z disc GO:0030018
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
|
4 | O15273 (/IDA) O15273 (/IDA) O70548 (/IDA) O70548 (/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.
|
2 | O15273 (/TAS) O15273 (/TAS) |
Z disc GO:0030018
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
|
2 | O70548 (/ISO) O70548 (/ISO) |
I band GO:0031674
A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end.
|
2 | O70548 (/IDA) O70548 (/IDA) |
I band GO:0031674
A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end.
|
2 | O15273 (/ISS) O15273 (/ISS) |