SII-SWORD/CoKE huggingface dataset:
Tumour necrosis factor receptor 12 (TNFR_12)
Type: Family

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain - a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .

TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis . Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease .

TNF receptor 12, also known as TWEAK receptor (TWEAKR), fibroblast growth factor-inducible-14 (Fn14) or CD266, is expressed on a wide variety of different cell types and binds the ligand TWEAK (tumor necrosis factor-like weak inducer of apoptosis) to activate several signaling cascades through activation of NF-kappaB signaling mediated by adaptor TRAF proteins . The FN14/TWEAK pathway controls a range of cellular activities such as proliferation, differentiation, and apoptosis, and has diverse biological functions in pathological mechanisms like inflammation and fibrosis that are associated with cardiovascular diseases (CVDs) .

The Fn14 receptor is the smallest TNFR superfamily member described so far. It is initially synthesized as a 129-amino-acid type I transmembrane protein that is then proteolytically processed by signal peptidase. The mature form of TweakR has only 102 amino acids and six cysteine residues in its extracellular region .
Tumour necrosis factor receptor 13B (TNFR_13B)
Type: Family

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain -a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .

TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis . Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease .

TNF receptor 13B (also known as transmembrane activator and CAML interactor (TACI)) functions as a receptor for B-cell activating factor (BAFF) . Mutations in TNF receptor 13B cause common variable immunodeficiency (CVID) and IgA deficiency .
Tumour necrosis factor receptor 18 (TNFR_18)
Type: Family

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain -a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .

TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis . Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease .

TNF receptor 18 is also known as glucocorticoid-induced TNFR family-related gene (GITR) and activation-inducible TNFR family member (AITR). Expression of the receptor by T-lymphocytes has been shown to have an anti-apoptotic effect, indicating that it may play a role in the regulation of T-cell receptor-mediated cell death .
Tumour necrosis factor receptor 27 (TNFR_27)
Type: Family

TNF receptor 27 (also known as ectodysplasin A2 receptor (EDA2R) and ectodysplasin receptor, x-linked (XEDAR)) is highly expressed during embryogenesis , and has been implicated in the development of ectodermal appendages, such as hair follicles, teeth and sweat glands . Although it lacks a death domain, the receptor can nevertheless induce cell death via activation of caspase 8, and may play a role in the induction of apoptosis during embryonic development and adult life .

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain - a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .
Tumour necrosis factor receptor 17 (TNFR_17)
Type: Family

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain - a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .

TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis . Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease .

TNF receptor 17 acts as a receptor for both a proliferation-inducing ligand (APRIL) and B cell-activating factor (BAFF) . It is preferentially expressed by mature B-cells, suggesting a potential role for the receptor in the B-cell developmental process .
Insulin-like growth factor-binding protein family 1-6, chordata (IGFBP_1-6_chordata)
Type: Family

Insulin-like growth factors (IGFs)-I and -II are small secreted peptides that stimulate the survival, and promote the proliferation and differentiation, of many cell types . In biological fluids, these growth factors are usually bound to IGF-binding proteins (IGFBPs), which regulate their availability and activity by prolonging their half-life and modulating their receptor interactions.

To date, six IGFBP family members have been identified (termed IGFBP1-6) . They share a conserved gene (intron-exon) organisation and high IGF-binding affinity. Structurally, the proteins also share a common domain architecture, possessing a conserved N-terminal IGFBP domain, a highly variable mid-section, and a thyroglobulin type-1 (Tg1) domain in their C-terminal regions.
Insulin-like growth factor-binding protein 1 (IGFBP1)
Type: Family

Insulin-like growth factors (IGFs)-I and -II are small secreted peptides that stimulate the survival, and promote the proliferation and differentiation, of many cell types . In biological fluids, these growth factors are usually bound to IGF binding proteins (IGFBPs), which regulate their availability and activity by prolonging their half-life and modulating their receptor interactions.

To date, six IGFBP family members have been identified (termed IGFBP1-6) . They share a conserved gene (intron-exon) organisation and high IGF binding affinity. Structurally, the proteins also share a common domain architecture, possessing a conserved N-terminal IGFBP domain, a highly variable mid-section, and a thyroglobulin type-1 (Tg1) domain in their C-terminal regions.

In addition to their role in the regulation of IGF activity, there is evidence for the direct association of IGFBPs with a variety of extracellular and cell surface molecules , with consequent effects upon important biological processes. These include modulation of bone cell proliferation , and growth arrest of breast and prostate cancer cells .
Tumour necrosis factor receptor 11 (TNFR_11)
Type: Family

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain -a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .

TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis . Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease .

TNF receptors 11A and 11B mediate the effects of receptor activator for NF-kappa-B ligand (RANKL), an essential osteoclast regulatory factor. The receptors have opposing effects -activation of TNF receptor 11A by RANKL promotes osteoclast differentiation , while TNF receptor 11B acts as a soluble decoy receptor for the ligand, thus inhibiting differentiation .
Bacilysin exporter BacE, putative (Bacilysin_exporter_BacE_put)
Type: Family

The so-called putative bacilysin exporter, bacE, part of the bacilysin biosynthesis operon, has been shown to be involved in self-protection to bacilysin by permitting efflux of this antibiotic.
Tumour necrosis factor receptor 16 (TNFR_16)
Type: Family

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain -a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .

TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis . Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease .
Insulin-like growth factor-binding protein 6 (IGFBP-6)
Type: Family

Insulin-like growth factors (IGFs)-I and -II are small secreted peptides that stimulate the survival, and promote the proliferation and differentiation, of many cell types . In biological fluids, these growth factors are usually bound to IGF binding proteins (IGFBPs), which regulate their availability and activity by prolonging their half-life and modulating their receptor interactions.

To date, six IGFBP family members have been identified (termed IGFBP1-6) . They share a conserved gene (intron-exon) organisation and high IGF binding affinity. Structurally, the proteins also share a common domain architecture, possessing a conserved N-terminal IGFBP domain, a highly variable mid-section, and a thyroglobulin type-1 (Tg1) domain in their C-terminal regions.

In addition to their role in the regulation of IGF activity, there is evidence for the direct association of IGFBPs with a variety of extracellular and cell surface molecules , with consequent effects upon important biological processes. These include modulation of bone cell proliferation , and growth arrest of breast and prostate cancer cells .

IGFBP6 is a potent inducer of programmed cell death in lung cancer cells . The protein may therefore represent a potential target as a cancer therapeutic.
Insulin-like growth factor-binding protein 4 (IGFBP-4)
Type: Family

Insulin-like growth factors (IGFs)-I and -II are small secreted peptides that stimulate the survival, and promote the proliferation and differentiation, of many cell types . In biological fluids, these growth factors are usually bound to IGF binding proteins (IGFBPs), which regulate their availability and activity by prolonging their half-life and modulating their receptor interactions.

To date, six IGFBP family members have been identified (termed IGFBP1-6) . They share a conserved gene (intron-exon) organisation and high IGF binding affinity. Structurally, the proteins also share a common domain architecture, possessing a conserved N-terminal IGFBP domain, a highly variable mid-section, and a thyroglobulin type-1 (Tg1) domain in their C-terminal regions.

In addition to their role in the regulation of IGF activity, there is evidence for the direct association of IGFBPs with a variety of extracellular and cell surface molecules , with consequent effects upon important biological processes. These include modulation of bone cell proliferation , and growth arrest of breast and prostate cancer cells .

IGFBP4 is abundant in serum, and is expressed in many different tissues. The protein functions as a cardiogenic growth factor in mice -an effect that is IGF-independent, and mediated by inhibition on the canonical Wnt signalling pathway .
Tumour necrosis factor receptor 7 (TNFR_7)
Type: Family

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain -a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .

TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis . Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease .
Tumour necrosis factor receptor 25 (TNFR_25)
Type: Family

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain- a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .

TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis . Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease .
Tumour necrosis factor receptor 21 (TNFR_21)
Type: Family

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain -a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .

TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis . Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease .

TNF receptor 21, also termed death receptor 6 (DR6), is expressed ubiquitously, with high expression in lymphoid organs, heart, brain and pancreas. The receptor plays an important regulatory role in the generation of adaptive immunity and may be involved in tumour cell survival and immune evasion . It has also been implicated in the pathogenesis of Alzheimer's disease, as activation of the receptor by beta-amyloid precursor protein triggers neuronal death via a caspase-dependent pathway .
Neurogenic locus Notch 3 (Notch_3)
Type: Family

Notch cell surface receptors are large, single-pass type-1 transmembrane proteins found in a diverse range of metazoan species, from human to Caenorhabditis species. The fruit fly, Drosophila melanogaster, possesses only one Notch protein, whereas in C.elegans, two receptors have been found; by contrast, four Notch paralogues (designated N1-4) have been identified in mammals, playing both unique and redundant roles.

The hetero-oligomer Notch comprises a large extracellular domain (ECD), containing 10-36 tandem Epidermal Growth Factor (EFG)-like repeats, which are involved in ligand interactions; a negative regulatory region, including three cysteine-rich Lin12-Notch Repeats (LNR); a single trans-membrane domain (TM); a small intracellular domain (ICD), which includes a RAM (RBPjk-association module) domain; six ankyrin repeats (ANK), which are involved in protein-protein interactions; and a PEST domain. Drosophila Notch also contains an OPA domain .

Notch signalling is an evolutionarily conserved pathway involved in a wide variety of developmental processes, including adult homeostasis and stem cell maintenance, cell proliferation and apoptosis . Notch is activated by a range of ligands -the so-called DSL ligands (Delta/Seratte/LAG-2). Activation is also mediated by a sequence of proteolytic events: ligand binding leads to cleavage of Notch by ADAM proteases at site 2 (S2) and presenilin-1/g-secretase at sites 3 (S3)and 4 (S4) .The last cleavage releases the Notch intracellular part of the protein (NICD) from the membrane and, upon release, the NICD translocates to the nucleus where it associates with a CBF1/RBJk/Su(H)/Lag1 (CSL) family of DNA-binding proteins. The subsequent recruitment of a co-activator mastermind like (MAML1) protein promotes transcriptional activation of Notch target genes: well established Notch targets are the Hes and Hey gene families.

Notch3 displays a more restrictive distribution than the rest of the Notch subtypes, being expressed predominantly in vascular smooth muscle cells, the central nervous system, certain thymocytes subsets, and in regulatory T cells .
Tumour necrosis factor receptor 14 (TNFR_14)
Type: Family

The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain -a region that contains many cysteine residues arranged in a specific repetitive pattern . The cysteines allow formation of an extended rod-like structure, responsible for ligand binding .

Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences . Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved .

TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis . Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease .

TNF receptor 14 is also known as herpesvirus entry mediator (HVEM). It plays an important role in the entry of herpes simplex virus into cells, and hence pathogenesis of the virus .