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:

"
Immunoglobulins
".

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 421: LOW QUALITY PROTEIN: obscurin

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 27 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).
10 A0A0G2JUP3 (/IPI) A0A0G2JUP3 (/IPI) A0A0G2K3P4 (/IPI) A0A0G2K3P4 (/IPI) A0A0G2K8N1 (/IPI) A0A0G2K8N1 (/IPI) A2AAJ9 (/IPI) A2AAJ9 (/IPI) Q5VST9 (/IPI) Q5VST9 (/IPI)
Rho guanyl-nucleotide exchange factor activity GO:0005089
Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Rho family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase.
6 A0A0G2JUP3 (/NAS) A0A0G2JUP3 (/NAS) A0A0G2K3P4 (/NAS) A0A0G2K3P4 (/NAS) A0A0G2K8N1 (/NAS) A0A0G2K8N1 (/NAS)
Protein kinase activity GO:0004672
Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
2 A2AAJ9 (/IDA) A2AAJ9 (/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 Q5VST9 (/IDA) Q5VST9 (/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 A2AAJ9 (/ISO) A2AAJ9 (/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.
2 A2AAJ9 (/ISS) A2AAJ9 (/ISS)
Phosphatidylinositol-3,4,5-trisphosphate binding GO:0005547
Interacting selectively and non-covalently with phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions.
2 Q5VST9 (/IDA) Q5VST9 (/IDA)
Phosphatidylinositol-3,4,5-trisphosphate binding GO:0005547
Interacting selectively and non-covalently with phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
Phosphatidylinositol-3,4,5-trisphosphate binding GO:0005547
Interacting selectively and non-covalently with phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions.
2 A2AAJ9 (/ISS) A2AAJ9 (/ISS)
Structural constituent of muscle GO:0008307
The action of a molecule that contributes to the structural integrity of a muscle fiber.
2 Q5VST9 (/NAS) Q5VST9 (/NAS)
Phosphatidylinositol-5-phosphate binding GO:0010314
Interacting selectively and non-covalently with phosphatidylinositol-5-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 5' position.
2 Q5VST9 (/IDA) Q5VST9 (/IDA)
Phosphatidylinositol-5-phosphate binding GO:0010314
Interacting selectively and non-covalently with phosphatidylinositol-5-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 5' position.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
Phosphatidylinositol-5-phosphate binding GO:0010314
Interacting selectively and non-covalently with phosphatidylinositol-5-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 5' position.
2 A2AAJ9 (/ISS) A2AAJ9 (/ISS)
Ankyrin binding GO:0030506
Interacting selectively and non-covalently with ankyrin, a 200 kDa cytoskeletal protein that attaches other cytoskeletal proteins to integral membrane proteins.
2 Q5VST9 (/IPI) Q5VST9 (/IPI)
Ankyrin binding GO:0030506
Interacting selectively and non-covalently with ankyrin, a 200 kDa cytoskeletal protein that attaches other cytoskeletal proteins to integral membrane proteins.
2 A2AAJ9 (/ISO) A2AAJ9 (/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 Q5VST9 (/IPI) Q5VST9 (/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 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
Phosphatidylinositol-3-phosphate binding GO:0032266
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
2 Q5VST9 (/IDA) Q5VST9 (/IDA)
Phosphatidylinositol-3-phosphate binding GO:0032266
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
Phosphatidylinositol-3-phosphate binding GO:0032266
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
2 A2AAJ9 (/ISS) A2AAJ9 (/ISS)
Phosphatidylinositol-3,4-bisphosphate binding GO:0043325
Interacting selectively and non-covalently with phosphatidylinositol-3,4-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 4' positions.
2 Q5VST9 (/IDA) Q5VST9 (/IDA)
Phosphatidylinositol-3,4-bisphosphate binding GO:0043325
Interacting selectively and non-covalently with phosphatidylinositol-3,4-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 4' positions.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
Phosphatidylinositol-3,4-bisphosphate binding GO:0043325
Interacting selectively and non-covalently with phosphatidylinositol-3,4-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 4' positions.
2 A2AAJ9 (/ISS) A2AAJ9 (/ISS)
Cadherin binding GO:0045296
Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.
2 A2AAJ9 (/IPI) A2AAJ9 (/IPI)
Phosphatidylinositol-4-phosphate binding GO:0070273
Interacting selectively and non-covalently with phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position.
2 Q5VST9 (/IDA) Q5VST9 (/IDA)
Phosphatidylinositol-4-phosphate binding GO:0070273
Interacting selectively and non-covalently with phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
Phosphatidylinositol-4-phosphate binding GO:0070273
Interacting selectively and non-covalently with phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position.
2 A2AAJ9 (/ISS) A2AAJ9 (/ISS)

There are 10 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
Protein phosphorylation GO:0006468
The process of introducing a phosphate group on to a protein.
2 A2AAJ9 (/IDA) A2AAJ9 (/IDA)
G protein-coupled receptor signaling pathway GO:0007186
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription. The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
2 Q5VST9 (/TAS) Q5VST9 (/TAS)
Myofibril assembly GO:0030239
Formation of myofibrils, the repeating units of striated muscle.
2 A0A140LFP6 (/IMP) A0A140LFP6 (/IMP)
Protein localization to M-band GO:0036309
Any process in which a protein is transported to, and/or maintained in, the M band. The M band is the midline of aligned thick filaments in a sarcomere.
2 Q5VST9 (/ISS) Q5VST9 (/ISS)
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
2 Q5VST9 (/TAS) Q5VST9 (/TAS)
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 Q5VST9 (/TAS) Q5VST9 (/TAS)
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
2 A2AAJ9 (/IDA) A2AAJ9 (/IDA)
Regulation of small GTPase mediated signal transduction GO:0051056
Any process that modulates the frequency, rate or extent of small GTPase mediated signal transduction.
2 Q5VST9 (/TAS) Q5VST9 (/TAS)
Striated muscle cell development GO:0055002
The process whose specific outcome is the progression of a striated muscle cell over time, from its formation to the mature structure. Striated muscle cells contain fibers that are divided by transverse bands into striations, and cardiac and skeletal muscle are types of striated muscle.
2 A0A140LFP6 (/IMP) A0A140LFP6 (/IMP)
Retina development in camera-type eye GO:0060041
The process whose specific outcome is the progression of the retina over time, from its formation to the mature structure. The retina is the innermost layer or coating at the back of the eyeball, which is sensitive to light and in which the optic nerve terminates.
2 A0A140LFP6 (/IMP) A0A140LFP6 (/IMP)

There are 20 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
M band GO:0031430
The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
10 A0A0G2JUP3 (/IDA) A0A0G2JUP3 (/IDA) A0A0G2K3P4 (/IDA) A0A0G2K3P4 (/IDA) A0A0G2K8N1 (/IDA) A0A0G2K8N1 (/IDA) A0A140LFP6 (/IDA) A0A140LFP6 (/IDA) A2AAJ9 (/IDA) A2AAJ9 (/IDA)
Z disc GO:0030018
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
8 A0A0G2JUP3 (/IDA) A0A0G2JUP3 (/IDA) A0A0G2K3P4 (/IDA) A0A0G2K3P4 (/IDA) A0A0G2K8N1 (/IDA) A0A0G2K8N1 (/IDA) A2AAJ9 (/IDA) A2AAJ9 (/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 A0A0G2JUP3 (/IDA) A0A0G2JUP3 (/IDA) A0A0G2K3P4 (/IDA) A0A0G2K3P4 (/IDA) A0A0G2K8N1 (/IDA) A0A0G2K8N1 (/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.
4 A6NGQ3 (/IDA) A6NGQ3 (/IDA) Q5VST9 (/IDA) Q5VST9 (/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 A6NGQ3 (/IDA) A6NGQ3 (/IDA) Q5VST9 (/IDA) Q5VST9 (/IDA)
Nuclear body GO:0016604
Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
4 A6NGQ3 (/IDA) A6NGQ3 (/IDA) Q5VST9 (/IDA) Q5VST9 (/IDA)
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
2 A2AAJ9 (/IDA) A2AAJ9 (/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 A2AAJ9 (/ISO) A2AAJ9 (/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 Q5VST9 (/TAS) Q5VST9 (/TAS)
Striated muscle myosin thick filament GO:0005863
Bipolar filaments formed of polymers of a muscle-specific myosin II isoform, found in the middle of sarcomeres in myofibrils.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
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.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
Intercalated disc GO:0014704
A complex cell-cell junction at which myofibrils terminate in cardiomyocytes; mediates mechanical and electrochemical integration between individual cardiomyocytes. The intercalated disc contains regions of tight mechanical attachment (fasciae adherentes and desmosomes) and electrical coupling (gap junctions) between adjacent cells.
2 A2AAJ9 (/IDA) A2AAJ9 (/IDA)
Nuclear body GO:0016604
Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
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.
2 Q5VST9 (/NAS) Q5VST9 (/NAS)
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.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
Z disc GO:0030018
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
Z disc GO:0030018
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
2 Q5VST9 (/ISS) Q5VST9 (/ISS)
M band GO:0031430
The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
2 A2AAJ9 (/ISO) A2AAJ9 (/ISO)
M band GO:0031430
The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
2 Q5VST9 (/ISS) Q5VST9 (/ISS)
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 A2AAJ9 (/IDA) A2AAJ9 (/IDA)
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