Apoptosis in Cancer
Representative Targets Full List of Targets Tested Data-Supported Products
Apoptosis, or programmed cell death, plays a crucial role in cancer biology, influencing tumor development, progression, and response to therapy. Cancer cells often acquire mutations or dysregulate key components of the apoptotic machinery, allowing them to evade cell death and proliferate uncontrollably. Understanding the mechanisms underlying apoptosis dysregulation in cancer is essential for developing effective therapeutic strategies to target cancer cells selectively while sparing normal cells.
One of the hallmark features of cancer cells is their ability to evade apoptosis, allowing them to survive and proliferate despite genetic abnormalities or environmental stresses. This evasion can occur through various mechanisms, including the downregulation of pro-apoptotic factors, upregulation of anti-apoptotic factors, and alterations in apoptotic signaling pathways. For example, mutations or overexpression of anti-apoptotic Bcl-2 family proteins such as Bcl-2, Bcl-xL, and Mcl-1 can promote cell survival by inhibiting mitochondrial outer membrane permeabilization and preventing the release of pro-apoptotic factors like cytochrome c.
Additionally, cancer cells can acquire resistance to apoptosis-inducing signals, including chemotherapy and radiation therapy, leading to treatment failure and disease recurrence. This resistance can arise through multiple mechanisms, including mutations in apoptotic regulators, activation of survival signaling pathways such as PI3K/Akt and MAPK, and alterations in the tumor microenvironment that promote cell survival and proliferation. Overcoming apoptosis resistance is a significant challenge in cancer therapy, requiring the development of novel treatment strategies that target both cancer cell intrinsic factors and extrinsic signals from the tumor microenvironment.
Despite the challenges posed by apoptosis dysregulation in cancer, targeting apoptotic pathways remains a promising therapeutic approach for cancer treatment. Several strategies have been developed to induce apoptosis in cancer cells, including the use of small molecule inhibitors targeting anti-apoptotic proteins, gene therapy approaches to restore pro-apoptotic signaling, and immunotherapies that harness the immune system to target cancer cells for apoptosis. Combination therapies that target multiple components of the apoptotic machinery or synergize with conventional treatments like chemotherapy and radiation therapy are also being explored to overcome apoptosis resistance and improve patient outcomes.
Figure 1 Therapeutic approaches targeting apoptosis pathways in cancer cells. (Carneiro, 2020)
Representative Targets
CASP3
CASP3, or Caspase-3, is a critical executioner caspase in the process of apoptosis, the programmed cell death mechanism that is essential for development, maintenance of tissue homeostasis, and elimination of damaged or diseased cells. Caspase-3 is synthesized as an inactive proenzyme that is activated through proteolytic cleavage by initiator caspases such as Caspase-8 and Caspase-9, typically in response to pro-apoptotic signals including those from the intrinsic (mitochondrial) and extrinsic (death receptor) pathways. Once activated, Caspase-3 cleaves various cellular substrates, leading to the characteristic morphological and biochemical features of apoptosis. These substrates include structural proteins in the cytoskeleton, such as actin and lamin, as well as key proteins involved in DNA repair and cell cycle regulation. The enzymatic activity of Caspase-3 results in cellular changes such as DNA fragmentation, degradation of cytoskeletal and nuclear proteins, formation of apoptotic bodies, and eventually, the phagocytosis of cell debris by neighboring cells or immune cells. Dysregulation of Caspase-3 activity is implicated in numerous diseases. Insufficient Caspase-3 activation can contribute to cancer progression by allowing abnormal cells to escape programmed cell death, whereas excessive activation of Caspase-3 is associated with conditions characterized by excessive cell death, such as Alzheimer's disease, stroke, and myocardial infarction. In these diseases, unintended activation of apoptosis can lead to tissue damage and functional decline.
Recommended Mouse Anti-CASP3 mAb (CAT#: ZG-0016J)
Figure 2 Mouse Anti-CASP3 Recombinant Antibody (clone 5E1) in IHC. Immunohistochemical analysis of paraffin-embedded Rat-lung tissue. 1.Active Caspase-3 Monoclonal Antibody was diluted at 1:200 (4°C, overnight). 2, Sodium citrate pH 6.0 was used for Antibody retrieval(>98°C, 20min). 3, Secondary Antibody was diluted at 1:200 (room temperature, 30min). Negative control was used by secondary Antibody only.
Recommended Rabbit Anti-CASP3 mAb (CAT#: ZG-0012U)
Figure 3 Rabbit Anti-CASP3 Antibody (ZG-0012U) in IHC. IHC image of ZG-0012U diluted at 1:100 and staining in paraffin-embedded human breast cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit IgG polymer labeled by HRP and visualized using 0.05% DAB.
Recommended Rabbit Anti-CASP3 mAb (CAT#: ZG-0580J)
Figure 4 Rabbit Anti-CASP3 Antibody (ZG-0580J) in IF. Immunofluorescence staining of Hela Cells with ZG-0580J at 1:50, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeated by 0.2% TritonX-100, and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. Nuclear DNA was labeled in blue with DAPI. The secondary antibody was FITC-conjugated Goat Anti-Rabbit IgG (H+L).
CASP9
CASP9, or Caspase-9, is another initiator caspase in the intrinsic apoptosis pathway. Caspase-9 plays a pivotal role in the cascade of signaling events that lead to apoptosis, which is essential for removing damaged or diseased cells and maintaining tissue homeostasis. Caspase-9 is activated in response to pro-apoptotic signals that result in mitochondrial outer membrane permeabilization and the release of cytochrome c into the cytosol. Once released, cytochrome c forms a complex with Apaf-1 (apoptotic protease activating factor 1) and dATP, which then recruits pro-caspase-9. This complex, known as the apoptosome, facilitates the auto-cleavage and activation of Caspase-9. Activated Caspase-9 then cleaves and activates downstream effector caspases, such as Caspase-3 and Caspase-7, which carry out the execution phase of apoptosis, leading to cellular disassembly. Dysregulation of Caspase-9 activity is implicated in a range of diseases. Overactivation can contribute to excessive cell death, which is detrimental in diseases such as Alzheimer's, stroke, and myocardial infarction, where it can exacerbate tissue damage. Conversely, reduced activation of Caspase-9 can lead to impaired apoptosis, allowing the survival and proliferation of potentially cancerous cells, thus contributing to the development and progression of cancer.
Recommended Rabbit Anti-CASP9 mAb (CAT#: ZG-0581J)
Figure 5 Rabbit Anti-CASP9 Antibody (ZG-0581J) in IF. Immunofluorescence staining of HepG2 cells with ZG-0581J at 1:60, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated Goat Anti-Rabbit IgG (H+L).
Recommended Rabbit Anti-CASP9 mAb (CAT#: VS3-FY197)
Figure 6 Recombinant Rabbit Anti-Casp9 Antibody (clone R04-8I4) in WB. Western blot analysis of Caspase9 in C6 lysates using Caspase9 Antibody.
Recommended Mouse Anti-CASP9 mAb (CAT#: ZG-0365F)
Figure 7 Mouse Anti-CASP9 Recombinant Antibody (ZG-0365F) in WB. Western blot detection of CHO-K1 cell lysate (B) and CHO K1 transfected with Caspase-9 (A) cell lysate was performed using Caspase-9 mouse mAb (1:1000 dilution). Predicted band size: 49/37KDa. Observed band size: 49/37KDa.
TNFRSF10B
TNFRSF10B, commonly known as Death Receptor 5 (DR5) or TRAIL receptor 2 (TRAIL-R2), is a member of the tumor necrosis factor receptor superfamily that plays a crucial role in mediating apoptosis through the extrinsic pathway. This receptor is specifically activated by its ligand TRAIL (TNF-related apoptosis-inducing ligand), a cytokine that selectively induces apoptosis in cancer cells while generally sparing normal cells, making it a valuable target for cancer therapy. Upon binding with TRAIL, TNFRSF10B undergoes trimerization, leading to the recruitment of the adaptor protein FADD (Fas-associated protein with death domain) and pro-caspase-8, forming the death-inducing signaling complex (DISC). This assembly triggers the activation of pro-caspase-8 to caspase-8, which then initiates a cascade of further caspase activations, ultimately leading to apoptosis. Caspase-8 can also cleave and activate other downstream effector caspases, such as caspase-3, enhancing the apoptotic process. TNFRSF10B is predominantly expressed in cancerous tissues and is minimally expressed in most normal tissues, which allows TRAIL-mediated therapy to target tumor cells preferentially. The role of TNFRSF10B in cancer apoptosis has spurred significant interest in developing TRAIL or DR5 agonists as anticancer therapeutics. These agents aim to exploit the natural tumor-selective killing mechanism of TRAIL, offering a strategy to induce cancer cell death with minimal side effects. However, resistance to TRAIL-induced apoptosis is a challenge in some cancer types, which has led to ongoing research efforts to understand the mechanisms of resistance and to develop combination therapies that sensitize tumor cells to TRAIL. In addition to cancer, the role of TNFRSF10B and TRAIL signaling is being investigated in other pathological conditions, such as immune disorders and inflammatory diseases, where modulating apoptosis can be beneficial.
Recommended Human Anti-TNFRSF10B mAb (CAT#: TAB-203)
Figure 8 Anti-Human DR5 Recombinant Antibody (TAB-203) in WB. Western blot analysis of TAB-203 was performed with DR5/TRAIL R2 Protein, Human, Recombinant (His Tag). TAB-203 incubation concentration: 2ng/μL. The secondary antibody: HRP-Anti-Human IgG (H+L). Lane 1: Reducing Antigen (0.1μg). Lane 2: Reducing Antigen (0.3μg). Lane 3: Reducing Antigen (0.6μg).
Recommended Mouse Anti-TNFRSF10B mAb (CAT#: ZG-0484F)
Figure 9 Mouse Anti-TNFRSF10B Recombinant Antibody (ZG-0484F) in WB. Western blot detection of DR5 in MCF-7 and T47D cell lysates was performed using DR5 mouse mAb (1:2000 dilution). Predicted band size: 40/48KDa. Observed band size: 40/48KDa.
Recommended Mouse Anti-TNFRSF10B mAb (CAT#: ZG-0485F)
Figure 10 Mouse Anti-TNFRSF10B Recombinant Antibody (ZG-0485F) in ICC. DR5 mouse mAb diluted 1:100 was used to perform immunocytochemistry on HeLa cells fixed with paraformaldehyde.
Full List of Targets
| Biomarker | Alternative Names | Gene ID | UniProt ID | Roles |
| ATR | ATR Serine/Threonine Kinase; Ataxia Telangiectasia And Rad3-Related Protein; EC 2.7.11.1; FRP1; MEC1; MEC1, Mitosis Entry Checkpoint 1, Homolog; Ataxia Telangiectasia And Rad3 Related; Mitosis Entry Checkpoint 1; Homolog (S. Cerevisiae); FRAP-Related Protein-1; FRAP-Related Protein 1; FCTCS; SCKL1; SCKL | 545 | Q13535 | The protein encoded by this gene belongs the PI3/PI4-kinase family, and is most closely related to ATM, a protein kinase encoded by the gene mutated in ataxia telangiectasia. This protein and ATM share similarity with Schizosaccharomyces pombe rad3, a cell cycle checkpoint gene required for cell cycle arrest and DNA damage repair in response to DNA damage. This kinase has been shown to phosphorylate checkpoint kinase CHK1, checkpoint proteins RAD17, and RAD9, as well as tumor suppressor protein BRCA1. Mutations of this gene are associated with Seckel syndrome. An alternatively spliced transcript variant of this gene has been reported, however, its full length nature is not known. Transcript variants utilizing alternative polyA sites exist. |
| BAG2 | BAG-2; dJ417I1.2 | 9532 | O95816 | BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. |
| BAG3 | BCL2 Associated Athanogene 3; Bcl-2-Binding Protein Bis; Docking Protein CAIR-1; BAG-3; BIS; BAG Family Molecular Chaperone Regulator 3 | 9531 | O95817 | BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. |
| BAK1 | BCL2 Antagonist/Killer 1; Apoptosis Regulator BAK; Bcl-2-Like Protein 7; Bcl2-L-7; BCL2L7; CDN1; BAK | 578 | Q16611 | The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein localizes to mitochondria, and functions to induce apoptosis. It interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, which leads to a loss in membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 after exposure to cell stress. |
| BAX | BCL2L4 | 581 | Q07812 | The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein forms a heterodimer with BCL2, and functions as an apoptotic activator. The association and the ratio of BAX to BCL2 also determines survival or death of a cell following an apoptotic stimulus. This protein is reported to interact with, and increase the opening of, the mitochondrial voltage-dependent anion channel (VDAC), which leads to the loss in membrane potential and the release of cytochrome c. The expression of this gene is regulated by the tumor suppressor P53 and has been shown to be involved in P53-mediated apoptosis. Multiple alternatively spliced transcript variants, which encode different isoforms, have been reported for this gene. |
| BCKDK | Branched Chain Ketoacid Dehydrogenase Kinase; BCKD-Kinase; EC 2.7.11.4; BCKDHKIN; [3-Methyl-2-Oxobutanoate Dehydrogenase [Lipoamide]] Kinase, Mitochondrial; 3-Methyl-2-Oxobutanoate Dehydrogenase [Lipoamide] Kinase, Mitochondrial | 29603 | Q00972 | The branched-chain alpha-ketoacid dehydrogenase complex (BCKD) is an important regulator of the valine, leucine, and isoleucine catabolic pathways. The protein encoded by this gene is found in the mitochondrion, where it phosphorylates and inactivates BCKD. Several transcript variants encoding different isoforms have been found for this gene. |
| BCL10 | B Cell CLL/Lymphoma 10; CED-3/ICH-1 Prodomain Homologous E10-Like Regulator; Mammalian CARD-Containing Adapter Molecule E10; CARD-Containing Molecule Enhancing NF-Kappa-B; Caspase-Recruiting Domain-Containing Protein; CARD-Containing Apoptotic Signaling Protein; CARD Containing Molecule Enhancing NF-KB; CARD-Containing Proapoptotic Protein; CARD-Like Apoptotic Protein; Cellular Homolog Of VCARMEN; B-Cell CLL/Lymphoma 10; Cellular-E10 | 8915 | O95999 | This gene was identified by its translocation in a case of mucosa-associated lymphoid tissue (MALT) lymphoma. The protein encoded by this gene contains a caspase recruitment domain (CARD), and has been shown to induce apoptosis and to activate NF-kappaB. This protein is reported to interact with other CARD domain containing proteins including CARD9, 10, 11 and 14, which are thought to function as upstream regulators in NF-kappaB signaling. This protein is found to form a complex with MALT1, a protein encoded by another gene known to be translocated in MALT lymphoma. MALT1 and this protein are thought to synergize in the activation of NF-kappaB, and the deregulation of either of them may contribute to the same pathogenetic process that leads to the malignancy. Alternative splicing results in multiple transcript variants. |
| BCL-2 | BCL2, Apoptosis Regulator; Protein Phosphatase 1, Regulatory Subunit 50; B-Cell CLL/Lymphoma 2; Apoptosis Regulator Bcl-2; PPP1R50; Bcl-2 | 596 | P10415 | This gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Alternative splicing results in multiple transcript variants. |
| BCL2A1 | BCL2 Related Protein A1; Hemopoietic-Specific Early Response Protein; Bcl-2-Like Protein 5; Protein BFL-1; Bcl2-L-5; BCL2L5; HBPA1; BFL1; GRS | 597 | Q16548 | This gene encodes a member of the BCL-2 protein family. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators that are involved in a wide variety of cellular activities such as embryonic development, homeostasis and tumorigenesis. The protein encoded by this gene is able to reduce the release of pro-apoptotic cytochrome c from mitochondria and block caspase activation. This gene is a direct transcription target of NF-kappa B in response to inflammatory mediators, and is up-regulated by different extracellular signals, such as granulocyte-macrophage colony-stimulating factor (GM-CSF), CD40, phorbol ester and inflammatory cytokine TNF and IL-1, which suggests a cytoprotective function that is essential for lymphocyte activation as well as cell survival. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. |
| BCL2L12 | BCL2-Like 12 (Proline Rich); Bcl-2-Related Proline-Rich Protein; Bcl2-L-12; BPR | 83596 | Q9HB09 | This gene encodes a member of a family of proteins containing a Bcl-2 homology domain 2 (BH2). The encoded protein is an anti-apoptotic factor that acts as an inhibitor of caspases 3 and 7 in the cytoplasm. In the nucleus, it binds to the p53 tumor suppressor protein, preventing its association with target genes. Overexpression of this gene has been detected in a number of different cancers. There is a pseudogene for this gene on chromosome 3. Alternative splicing results in multiple transcript variants. |
| BCL2L2 | BCLW; BCL-W; PPP1R51; BCL2-L-2 | 599 | Q92843 | This gene encodes a member of the BCL-2 protein family. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under cytotoxic conditions. Studies of the related gene in mice indicated a role in the survival of NGF- and BDNF-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult spermatogenesis. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring downstream PABPN1 (poly(A) binding protein, nuclear 1) gene. |
| Bcl-xL | Bcl-xL | |||
| BID | BH3 Interacting Domain Death Agonist; P22 BID; BH3-Interacting Domain Death Agonist; Human BID Coding Sequence; Apoptic Death Agonist; BID Isoform ES(1b) | 637 | P55957 | This gene encodes a death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. The encoded protein is a member of the BCL-2 family of cell death regulators. It is a mediator of mitochondrial damage induced by caspase-8 (CASP8); CASP8 cleaves this encoded protein, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. Multiple alternatively spliced transcript variants have been found, but the full-length nature of some variants has not been defined. |
| BIK | BIK; Human BIK | 638 | Q13323 | |
| BIRC3 | AIP1; API2; MIHC; CIAP2; HAIP1; HIAP1; IAP-1; MALT2; RNF49; c-IAP2 | 330 | Q13489 | This gene encodes a member of the IAP family of proteins that inhibit apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2, probably by interfering with activation of ICE-like proteases. The encoded protein inhibits apoptosis induced by serum deprivation but does not affect apoptosis resulting from exposure to menadione, a potent inducer of free radicals. It contains 3 baculovirus IAP repeats and a ring finger domain. Transcript variants encoding the same isoform have been identified. |
| BIRC7 | BIRC7; Human BIRC7 | 79444 | Q96CA5 | This gene encodes a member of the inhibitor of apoptosis protein (IAP) family, and contains a single copy of a baculovirus IAP repeat (BIR) as well as a RING-type zinc finger domain. The BIR domain is essential for inhibitory activity and interacts with caspases, while the RING finger domain sometimes enhances antiapoptotic activity but does not inhibit apoptosis alone. Elevated levels of the encoded protein may be associated with cancer progression and play a role in chemotherapy sensitivity. Alternative splicing results in multiple transcript variants |
| BNIP3 | BCL2 Interacting Protein 3; BCL2/Adenovirus E1B 19kDa Interacting Protein 3; NIP3; BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 3 | 664 | Q12983 | This gene is encodes a mitochondrial protein that contains a BH3 domain and acts as a pro-apoptotic factor. The encoded protein interacts with anti-apoptotic proteins, including the E1B 19 kDa protein and Bcl2. This gene is silenced in tumors by DNA methylation. |
| BNIP3L | BCL2 Interacting Protein 3 Like; BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 3A; BCL2/Adenovirus E1B 19kDa Interacting Protein 3 Like; NIP3-Like Protein X; BNIP3a; NIP3L; NIX | 665 | O60238 | This gene encodes a protein that belongs to the pro-apoptotic subfamily within the Bcl-2 family of proteins. The encoded protein binds to Bcl-2 and possesses the BH3 domain. The protein directly targets mitochondria and causes apoptotic changes, including loss of membrane potential and the release of cytochrome c. |
| Casp1 | Caspase 1; Caspase 1, Apoptosis-Related Cysteine Peptidase; Interleukin 1, Beta, Convertase; IL-1 Beta-Converting Enzyme; EC 3.4.22.36; Caspase-1; IL1BC; P45; ICE; Caspase 1, Apoptosis-Related Cysteine Peptidase (Interleukin 1, Beta, Convertase); Caspase 1, Apoptosis-Related Cysteine Protease (Interleukin 1, Beta, Convertase) | 12362 | P29452 | This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This gene was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. This gene has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing results in transcript variants encoding distinct isoforms. |
| CASP10 | Caspase 10; FAS-Associated Death Domain Protein Interleukin-1B-Converting Enzyme 2; Caspase 10, Apoptosis-Related Cysteine Protease; ICE-Like Apoptotic Protease 4; CASP-10; FLICE2; MCH4; Caspase 10, Apoptosis-Related Cysteine Peptidase; Caspase 10 Apoptosis-Related Cysteine Peptidase | 843 | Q92851 | This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 3 and 7, and the protein itself is processed by caspase 8. Mutations in this gene are associated with type IIA autoimmune lymphoproliferative syndrome, non-Hodgkin lymphoma and gastric cancer. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. |
| CASP14 | ARCI12 | 23581 | P31944 | This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This caspase has been shown to be processed and activated by caspase 8 and caspase 10 in vitro, and by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this caspase may be involved in keratinocyte terminal differentiation, which is important for the formation of the skin barrier. |
| CASP2 | ICH1; NEDD2; CASP-2; NEDD-2; PPP1R57 | 835 | P42575 | This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Caspases mediate cellular apoptosis through the proteolytic cleavage of specific protein substrates. The encoded protein may function in stress-induced cell death pathways, cell cycle maintenance, and the suppression of tumorigenesis. Increased expression of this gene may play a role in neurodegenerative disorders including Alzheimer's disease, Huntington's disease and temporal lobe epilepsy. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. |
| CASP3 | Caspase 3; Caspase 3, Apoptosis-Related Cysteine Peptidase; Caspase 3, Apoptosis-Related Cysteine Protease; SREBP Cleavage Activity 1; Cysteine Protease CPP32; Protein Yama; EC 3.4.22.56; Apopain; CASP-3 | 836 | P42574 | The protein encoded by this gene is a cysteine-aspartic acid protease that plays a central role in the execution-phase of cell apoptosis. The encoded protein cleaves and inactivates poly(ADP-ribose) polymerase while it cleaves and activates sterol regulatory element binding proteins as well as caspases 6, 7, and 9. This protein itself is processed by caspases 8, 9, and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. |
| Casp4 | CASP4; caspase 4, apoptosis-related cysteine peptidase; TX; ICH-2; Mih1/TX; ICEREL-II; ICE(rel)II; caspase-4; CASP-4; ICE(rel)-II; protease TX; protease ICH-2; apoptotic cysteine protease Mih1/TX; caspase 4, apoptosis-related cysteine protease; | 12363 | P70343 | This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain and a large and small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This caspase is able to cleave and activate its own precursor protein, as well as caspase 1 precursor. When overexpressed, this gene induces cell apoptosis. Alternative splicing results in transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2008] |
| CASP5 | ICH-3; ICEREL-III; ICE(rel)III | 838 | P51878 | This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. Overexpression of the active form of this enzyme induces apoptosis in fibroblasts. Max, a central component of the Myc/Max/Mad transcription regulation network important for cell growth, differentiation, and apoptosis, is cleaved by this protein; this process requires Fas-mediated dephosphorylation of Max. The expression of this gene is regulated by interferon-gamma and lipopolysaccharide. Alternatively spliced transcript variants have been identified for this gene. |
| CASP6 | MCH2; CSP-6; caspase-6 | 839 | P55212 | This gene encodes a member of the cysteine-aspartic acid protease (caspase) family of enzymes. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic acid residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Alternative splicing of this gene results in multiple transcript variants that encode different isoforms. |
| CASP7 | Caspase 7; Caspase 7, Apoptosis-Related Cysteine Peptidase; Caspase 7, Apoptosis-Related Cysteine Protease; ICE-Like Apoptotic Protease 3; ICE-LAP3; CASP-7; CMH-1; MCH3 | 840 | P55210 | This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. The precursor of the encoded protein is cleaved by caspase 3 and 10, is activated upon cell death stimuli and induces apoptosis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. |
| CASP8 | Caspase 8; Caspase 8, Apoptosis-Related Cysteine Peptidase; Caspase 8, Apoptosis-Related Cysteine Protease; MORT1-Associated Ced-3 Homolog; ICE-Like Apoptotic Protease 5; Apoptotic Cysteine Protease; Apoptotic Protease Mch-5; FADD-Like ICE; Casp-8; FLICE; CAP4 | 841 | Q14790 | This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined. |
| CASP9 | Caspase 9; Caspase 9, Apoptosis-Related Cysteine Peptidase; Protein Phosphatase 1, Regulatory Subunit 56; ICE-Like Apoptotic Protease 6; ICE-LAP6; APAF-3; MCH6; Caspase 9, Apoptosis-Related Cysteine Protease; Apoptotic Protease Activating Factor 3; | 842 | P55211 | This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein can undergo autoproteolytic processing and activation by the apoptosome, a protein complex of cytochrome c and the apoptotic peptidase activating factor 1; this step is thought to be one of the earliest in the caspase activation cascade. This protein is thought to play a central role in apoptosis and to be a tumor suppressor. Alternative splicing results in multiple transcript variants. |
| CLTC | Hc; CHC; CHC17; MRD56; CLH-17; CLTCL2 | 1213 | Q00610 | Clathrin is a major protein component of the cytoplasmic face of intracellular organelles, called coated vesicles and coated pits. These specialized organelles are involved in the intracellular trafficking of receptors and endocytosis of a variety of macromolecules. The basic subunit of the clathrin coat is composed of three heavy chains and three light chains. |
| CLTCL1 | Clathrin Heavy Chain Like 1; Clathrin Heavy Chain On Chromosome 22; Clathrin, Heavy Polypeptide-Like 1; CLH-22; CLTCL; CLH22; | 8218 | P53675 | This gene is a member of the clathrin heavy chain family and encodes a major protein of the polyhedral coat of coated pits and vesicles. Chromosomal aberrations involving this gene are associated with meningioma, DiGeorge syndrome, and velo-cardio-facial syndrome. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2009] |
| CREBBP | CREBBP; CBP; CREB Binding Protein; KAT3A; RSTS; Rubinstein-Taybi Syndrome; CREB-Binding Protein | 1387 | Q92793 | This gene is ubiquitously expressed and is involved in the transcriptional coactivation of many different transcription factors. First isolated as a nuclear protein that binds to cAMP-response element binding protein (CREB), this gene is now known to play critical roles in embryonic development, growth control, and homeostasis by coupling chromatin remodeling to transcription factor recognition. The protein encoded by this gene has intrinsic histone acetyltransferase activity and also acts as a scaffold to stabilize additional protein interactions with the transcription complex. This protein acetylates both histone and non-histone proteins. This protein shares regions of very high sequence similarity with protein p300 in its bromodomain, cysteine-histidine-rich regions, and histone acetyltransferase domain. Mutations in this gene cause Rubinstein-Taybi syndrome (RTS). Chromosomal translocations involving this gene have been associated with acute myeloid leukemia. Alternative splicing results in multiple transcript variants encoding different isoforms. |
| DR5 | DR5; CD262; KILLER; TRICK2; TRICKB; ZTNFR9; TRAILR2; TRICK2A; TRICK2B; TRAIL-R2; KILLER/DR5 | 8795 | O14763 | The protein encoded by this gene is a member of the TNF-receptor superfamily, and contains an intracellular death domain. This receptor can be activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL/APO-2L), and transduces an apoptosis signal. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein. Two transcript variants encoding different isoforms and one non-coding transcript have been found for this gene. |
| DR6 | TNFRSF21; CD358; BM-018 | 27242 | O75509 | TNFRSF21 (death receptor-6, DR6) is an orphan TNF receptor superfamily member and belongs to a subgroup of receptors called death receptors. This type I transmembrane receptor possesses four extracellular cysteine-rich motifs and a cytoplasmic death domain. DR6 is an extensively posttranslationally modified transmembrane protein and that N-and O-glycosylations of amino acids in its extracellular part. DR6 interacts with the adaptor protein TRADD and mediates signal transduction through its death domain, and expression of DR6 in mammalian cells induces activation of both NF-kappaB and JNK and cell apoptosis. DR6 knockout mice have enhanced CD4+ T cell proliferation and Th2 cytokine production, suggested that DR6 serves as an important regulatory molecule in T-helper cell activation, and is involved in inflammation and immune regulation. DR6 is expressed ubiquitously with high expression in lymphoid organs, heart, brain and pancreas. Some tumor cells overexpress DR6, typically in conjunction with elevated anti-apoptosis molecules. DR6 may also be involved in tumor cell survival and immune evasion, which is subject to future investigations. |
| DYNLL1 | LC8; PIN; DLC1; DLC8; LC8a; DNCL1; hdlc1; DNCLC1 | 8655 | P63167 | Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized. |
| EDA2R | EDA2R; ectodysplasin A2 receptor; XEDAR; EDAA2R; EDA-A2R; TNFRSF27 | 60401 | Q9HAV5 | The protein encoded by this gene is a type III transmembrane protein of the TNFR (tumor necrosis factor receptor) superfamily, and contains cysteine-rich repeats and a single transmembrane domain. This protein binds to the EDA-A2 isoform of ectodysplasin, which plays an important role in maintenance of hair and teeth. Alternatively spliced transcript variants encodes distinct protein isoforms. |
| EIF5A | Eukaryotic Translation Initiation Factor 5A; Rev-Binding Factor; EIF-5A-1; EIF-5A1; EIF-5A; EIF-4D | 1984 | P63241 | Enables U6 snRNA binding activity and protein N-terminus binding activity. Involved in several processes, including cellular response to virus; positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; and tumor necrosis factor-mediated signaling pathway. Located in annulate lamellae; cytoplasm; and nucleus. Part of nuclear pore. |
| EP300 | E1A Binding Protein P300; EC 2.3.1.-; Protein Propionyltransferase P300; Histone Crotonyltransferase P300; Histone Butyryltransferase P300; Histone Acetyltransferase P300; E1A-Associated Protein P300 | 2033 | Q09472 | This gene encodes the adenovirus E1A-associated cellular p300 transcriptional co-activator protein. It functions as histone acetyltransferase that regulates transcription via chromatin remodeling and is important in the processes of cell proliferation and differentiation. It mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. This gene has also been identified as a co-activator of HIF1A (hypoxia-inducible factor 1 alpha), and thus plays a role in the stimulation of hypoxia-induced genes such as VEGF. Defects in this gene are a cause of Rubinstein-Taybi syndrome and may also play a role in epithelial cancer. |
| FAS | Fas Cell Surface Death Receptor; Tumor Necrosis Factor Receptor Superfamily, Member 6; Fas (TNF Receptor Superfamily, Member 6); Apoptosis-Mediating Surface Antigen FAS; TNF Receptor Superfamily Member 6; FASLG Receptor; CD95 Antigen; TNFRSF6; APT1; FAS1; Mutant Tumor Necrosis Receptor Superfamily Member 6 | 355 | P25445 | The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contains a death domain. It has been shown to play a central role in the physiological regulation of programmed cell death, and has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The interaction of this receptor with its ligand allows the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10. The autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, and leads to apoptosis. This receptor has been also shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is found to be involved in transducing the proliferating signals in normal diploid fibroblast and T cells. Several alternatively spliced transcript variants have been described, some of which are candidates for nonsense-mediated mRNA decay (NMD). The isoforms lacking the transmembrane domain may negatively regulate the apoptosis mediated by the full length isoform. [provided by RefSeq, Mar 2011] |
| Fasl | Fasl; Fas ligand (TNF superfamily, member 6); gld; CD178; CD95L; Fas-L; Faslg; CD95-L; Tnfsf6; Tnlg1a; APT1LG1 | 14103 | P41047 | This gene is a member of the tumor necrosis factor superfamily. The primary function of the encoded transmembrane protein is the induction of apoptosis triggered by binding to FAS. The FAS/FASLG signaling pathway is essential for immune system regulation, including activation-induced cell death (AICD) of T cells and cytotoxic T lymphocyte induced cell death. It has also been implicated in the progression of several cancers. Defects in this gene may be related to some cases of systemic lupus erythematosus (SLE). Alternatively spliced transcript variants have been described. |
| IFITM2 | IFITM2; Interferon-Inducible Protein 1-8D; Dispanin Subfamily A Member 2c; DSPA2c; 1-8D; Interferon-Induced Transmembrane Protein 2; Interferon Induced Transmembrane Protein 2 (1-8D) | 10581 | Q01629 | IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and vesicular stomatitis virus (VSV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV S protein-mediated viral entry and VSV G protein-mediated viral entry. Induces cell cycle arrest and mediates apoptosis by caspase activation and in p53-independent manner. |
| IFITM3 | Interferon Induced Transmembrane Protein 3 | 10410 | Q01628 | The protein encoded by this gene is an interferon-induced membrane protein that helps confer immunity to influenza A H1N1 virus, West Nile virus, and dengue virus. Two transcript variants, only one of them protein-coding, have been found for this gene. Another variant encoding an N-terminally truncated isoform has been reported, but the full-length nature of this variant has not been determined. [provided by RefSeq, May 2012] |
| ING1 | Inhibitor Of Growth Family Member 1 | 3621 | Q9UK53 | This gene encodes a tumor suppressor protein that can induce cell growth arrest and apoptosis. The encoded protein is a nuclear protein that physically interacts with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. Reduced expression and rearrangement of this gene have been detected in various cancers. Multiple alternatively spliced transcript variants encoding distinct isoforms have been reported. |
| LRRC15 | LIB | 131578 | Q8TF66 | LRRC15 may play some role in innate immunity. LRRC15 is aberrantly expressed in cancer. It is highly expressed in CAFs within the stroma of numerous solid tumors and directly expressed in mesenchymal tumors such as glioblastoma, sarcomas, and melanoma. |
| MCL1 | MCL1, BCL2 Family Apoptosis Regulator; Myeloid Cell Leukemia Sequence 1 (BCL2-Related); Bcl-2-Related Protein EAT/Mcl1; Myeloid Cell Leukemia 1; Bcl-2-Like Protein 3; Bcl2-L-3; Mcl1/EAT; BCL2L3; Induced Myeloid Leukemia Cell Differentiation Protein Mcl-1 | 4170 | Q07820 | This gene encodes an anti-apoptotic protein, which is a member of the Bcl-2 family. Alternative splicing results in multiple transcript variants. The longest gene product (isoform 1) enhances cell survival by inhibiting apoptosis while the alternatively spliced shorter gene products (isoform 2 and isoform 3) promote apoptosis and are death-inducing. [provided by RefSeq, Oct 2010] |
| MDM2 | MDM2 Proto-Oncogene; MDM2 Proto-Oncogene, E3 Ubiquitin Protein Ligase; Oncoprotein Mdm2; Hdm2; Mdm2, Transformed 3T3 Cell Double Minute 2, P53 Binding Protein (Mouse); Mdm2, Transformed 3T3 Cell Double Minute 2, P53 Binding Protein; Mouse Double Minute 2, Human Homolog Of; P53-Binding Protein; Double Minute 2, Human Homolog Of; P53-Binding Protein; Mdm2, P53 E3 Ubiquitin Protein Ligase Homolog; MDM2 Oncogene, E3 Ubiquitin Protein Ligase | 4193 | A7UKX8 | This gene encodes a nuclear-localized E3 ubiquitin ligase. The encoded protein can promote tumor formation by targeting tumor suppressor proteins, such as p53, for proteasomal degradation. This gene is itself transcriptionally-regulated by p53. Overexpression or amplification of this locus is detected in a variety of different cancers. There is a pseudogene for this gene on chromosome 2. Alternative splicing results in a multitude of transcript variants, many of which may be expressed only in tumor cells. [provided by RefSeq, Jun 2013] |
| MOAP1 | MOAP1; Modulator Of Apoptosis 1; Paraneoplastic Ma Antigen Family Member 4; Paraneoplastic Antigen Ma4; Paraneoplastic Antigen Like 4; MAP1; MAP-1 | 64112 | Q96BY2 | The protein encoded by this gene was identified by its interaction with apoptosis regulator BAX protein. This protein contains a Bcl-2 homology 3 (BH3)-like motif, which is required for the association with BAX. When overexpressed, this gene has been shown to mediate caspase-dependent apoptosis. |
| NAIP | BIRC1; NLRB1; psiNAIP | 4671 | Q13075 | This gene is part of a 500 kb inverted duplication on chromosome 5q13. This duplicated region contains at least four genes and repetitive elements which make it prone to rearrangements and deletions. The repetitiveness and complexity of the sequence have also caused difficulty in determining the organization of this genomic region. This copy of the gene is full length; additional copies with truncations and internal deletions are also present in this region of chromosome 5q13. It is thought that this gene is a modifier of spinal muscular atrophy caused by mutations in a neighboring gene, SMN1. The protein encoded by this gene contains regions of homology to two baculovirus inhibitor of apoptosis proteins, and it is able to suppress apoptosis induced by various signals. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. |
| NPM1 | Nucleophosmin 1; Nucleophosmin (Nucleolar Phosphoprotein B23, Numatrin); Nucleophosmin/Nucleoplasmin Family, Member 1; Nucleolar Phosphoprotein B23; Nucleolar Protein NO38; Nucleophosmin | 4869 | P06748 | The protein encoded by this gene is involved in several cellular processes, including centrosome duplication, protein chaperoning, and cell proliferation. The encoded phosphoprotein shuttles between the nucleolus, nucleus, and cytoplasm, chaperoning ribosomal proteins and core histones from the nucleus to the cytoplasm. This protein is also known to sequester the tumor suppressor ARF in the nucleolus, protecting it from degradation until it is needed. Mutations in this gene are associated with acute myeloid leukemia. Dozens of pseudogenes of this gene have been identified. |
| NPM2 | Nucleophosmin/Nucleoplasmin 2; Nucleoplasmin-2 | 10361 | Q86SE8 | Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization. |
| NPM3 | Nucleophosmin/Nucleoplasmin 3; Nucleophosmin/Nucleoplasmin Family, Member 3; Nucleoplasmin-3; TMEM123; PORMIN | 10360 | O75607 | The protein encoded by this gene is related to the nuclear chaperone phosphoproteins, nucleoplasmin and nucleophosmin. This protein is strongly expressed in diverse cell types where it localizes primarily to the nucleus. Based on its similarity to nucleoplasmin and nucleophosmin, this protein likely functions as a molecular chaperone in the cell nucleus. [provided by RefSeq, Oct 2008] |
| NQO1 | NAD(P)H Quinone Dehydrogenase 1; Diaphorase (NADH/NADPH) (Cytochrome B-5 Reductase); NAD(P)H Dehydrogenase, Quinone 1; NAD(P)H:Quinone Oxidoreductase 1; Phylloquinone Reductase; Menadione Reductase; Quinone Reductase 1; DT-Diaphorase; Azoreductase; EC 1.6.5.2; NMOR1; DIA4 | 1728 | P15559 | This gene is a member of the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. This FAD-binding protein forms homodimers and reduces quinones to hydroquinones. This protein's enzymatic activity prevents the one electron reduction of quinones that results in the production of radical species. Mutations in this gene have been associated with tardive dyskinesia (TD), an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer. Altered expression of this protein has been seen in many tumors and is also associated with Alzheimer's disease (AD). Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008] |
| p53 | 7157 | K7PPA8 | ||
| SIRT1 | Sirtuin 1; Regulatory Protein SIR2 Homolog 1; SIR2-Like Protein 1; SIR2L1; Sirtuin (Silent Mating Type Information Regulation 2, S. Cerevisiae, Homolog) 1; Sirtuin (Silent Mating Type Information Regulation 2 Homolog) 1 (S. Cerevisiae); NAD-Dependent Protein Deacetylase Sirtuin-1 | 23411 | Q96EB6 | This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2008] |
| STK11 | PJS; LKB1; hLKB1 | 6794 | Q15831 | The protein encoded by this gene is a serine/threonine kinase that regulates cell polarity and energy metabolism and functions as a tumor suppressor. Mutations in this gene have been associated with the autosomal dominant Peutz-Jeghers syndrome, as well as with skin, pancreatic, and testicular cancers. |
| Survivin | Survivin; baculoviral inhibitor of apoptosis repeat-containing 5; BIRC5 | 332 | O15392 | This gene is a member of the inhibitor of apoptosis (IAP) gene family, which encode negative regulatory proteins that prevent apoptotic cell death. IAP family members usually contain multiple baculovirus IAP repeat (BIR) domains, but this gene encodes proteins with only a single BIR domain. The encoded proteins also lack a C-terminus RING finger domain. Gene expression is high during fetal development and in most tumors, yet low in adult tissues. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. |
| TERF2 | Telomeric Repeat Binding Factor 2; TTAGGG Repeat-Binding Factor 2; Telomeric DNA-Binding Protein; TRBF2; TRF2; Telomeric Repeat Binding Protein 2; Telomeric Repeat-Binding Factor 2 | 7014 | Q15554 | This gene encodes a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. This protein is present at telomeres in metaphase of the cell cycle, is a second negative regulator of telomere length and plays a key role in the protective activity of telomeres. While having similar telomere binding activity and domain organization, TERF2 differs from TERF1 in that its N terminus is basic rather than acidic. |
| TFAP2C | ERF1; TFAP2G; hAP-2g; AP2-GAMMA | 7022 | Q92754 | The protein encoded by this gene is a sequence-specific DNA-binding transcription factor involved in the activation of several developmental genes. The encoded protein can act as either a homodimer or heterodimer with other family members and is induced during retinoic acid-mediated differentiation. |
| TIGAR | FR2BP; C12orf5 | 57103 | Q9NQ88 | This gene is regulated as part of the p53 tumor suppressor pathway and encodes a protein with sequence similarity to the bisphosphate domain of the glycolytic enzyme that degrades fructose-2,6-bisphosphate. The protein functions by blocking glycolysis and directing the pathway into the pentose phosphate shunt. Expression of this protein also protects cells from DNA damaging reactive oxygen species and provides some protection from DNA damage-induced apoptosis. The 12p13.32 region that includes this gene is paralogous to the 11q13.3 region. |
| TNF | Tnfa; RATTNF; TNF-alpha | 7124 | P01375 | Enables tumor necrosis factor receptor binding activity. Involved in several processes, including positive regulation of cell communication; positive regulation of macromolecule metabolic process; and positive regulation of neuron death. Located in several cellular components, including external side of plasma membrane; extracellular space; and neuronal cell body. Used to study several diseases, including cerebrovascular disease (multiple); liver disease (multiple); peptic esophagitis; perinatal necrotizing enterocolitis; and periventricular leukomalacia. Biomarker of several diseases, including brain disease (multiple); congestive heart failure (multiple); inflammatory bowel disease (multiple); lung disease (multiple); and non-alcoholic fatty liver disease (multiple). Human ortholog(s) of this gene implicated in several diseases, including artery disease (multiple); autoimmune disease (multiple); eye disease (multiple); lung disease (multiple); and skin disease (multiple). Orthologous to human TNF (tumor necrosis factor). |
| TNFRSF10B | TNFRSF10B; TRAILR2; TRAIL-R2; CD262; DR5; KILLER; TRICK2; ZTNFR9; TRICKB | 8795 | O14763 | The protein encoded by this gene is a member of the TNF-receptor superfamily, and contains an intracellular death domain. This receptor can be activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL/APO-2L), and transduces an apoptosis signal. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein. Two transcript variants encoding different isoforms and one non-coding transcript have been found for this gene. |
| TNFRSF1A | TNF Receptor Superfamily Member 1A; TNF-R1; TNF-RI; TNFR-I; TNFR1; TNFAR; P60; P55; Tumor Necrosis Factor Receptor Superfamily, Member 1A; Tumor Necrosis Factor Receptor Superfamily Member 1A; Tumor Necrosis Factor Receptor 1A Isoform Beta; Tumor Necrosis Factor Binding Protein 1; Tumor Necrosis Factor Receptor Type 1; Tumor Necrosis Factor Receptor Type I | 7132 | P19438 | This gene encodes a member of the TNF receptor superfamily of proteins. The encoded receptor is found in membrane-bound and soluble forms that interact with membrane-bound and soluble forms, respectively, of its ligand, tumor necrosis factor alpha. Binding of membrane-bound tumor necrosis factor alpha to the membrane-bound receptor induces receptor trimerization and activation, which plays a role in cell survival, apoptosis, and inflammation. Proteolytic processing of the encoded receptor results in release of the soluble form of the receptor, which can interact with free tumor necrosis factor alpha to inhibit inflammation. Mutations in this gene underlie tumor necrosis factor receptor-associated periodic syndrome (TRAPS), characterized by fever, abdominal pain and other features. Mutations in this gene may also be associated with multiple sclerosis in human patients. |
| TNFSF10 | TL2; APO2L; CD253; TANCR; TRAIL; Apo-2L; TNLG6A | 8743 | P50591 | The protein encoded by this gene is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues. This protein binds to several members of TNF receptor superfamily including TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4, and possibly also to TNFRSF11B/OPG. The activity of this protein may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4, and TNFRSF11B/OPG that cannot induce apoptosis. The binding of this protein to its receptors has been shown to trigger the activation of MAPK8/JNK, caspase 8, and caspase 3. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. |
| TNFSF15 | TL1; VEGI | 9966 | O95150 | The protein encoded by this gene is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of this protein is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. This cytokine is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. Two transcript variants encoding different isoforms have been found for this gene. |
| TP53BP1 | Tumor Protein P53 Binding Protein 1; P53-Binding Protein 1; P53BP1; 53BP1; Tumor Suppressor P53-Binding Protein 1; Tumor Protein P53-Binding Protein, 1 | 7158 | Q12888 | This gene encodes a protein that functions in the DNA double-strand break repair pathway choice, promoting non-homologous end joining (NHEJ) pathways, and limiting homologous recombination. This protein plays multiple roles in the DNA damage response, including promoting checkpoint signaling following DNA damage, acting as a scaffold for recruitment of DNA damage response proteins to damaged chromatin, and promoting NHEJ pathways by limiting end resection following a double-strand break. These roles are also important during V(D)J recombination, class switch recombination and at unprotected telomeres. Alternative splicing results in multiple transcript variants encoding different isoforms. |
| UBE2A | Ubiquitin Conjugating Enzyme E2 A; E2 Ubiquitin-Conjugating Enzyme A; Ubiquitin-Conjugating Enzyme E2A; Ubiquitin Carrier Protein A; Ubiquitin-Protein Ligase A; RAD6 Homolog A; HHR6A; RAD6A; Ubiquitin-Conjugating Enzyme E2A (RAD6 Homolog) | 7319 | P49459 | The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, ubiquitin-conjugating enzymes, and ubiquitin-protein ligases. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is required for post-replicative DNA damage repair, and may play a role in transcriptional regulation. Mutations in this gene are associated with cognitive disability. Alternative splicing results in multiple transcript variants. |
| UBE2B | UBE2B; Ubiquitin-Conjugating Enzyme E2-17 KDa; RAD6B; E2-17kDa; Ubiquitin-Conjugating Enzyme E2B (RAD6 Homolog); RAD6 Homolog B; Ubiquitin Carrier Protein B; HR6B; EC 6.3.2.19; E2 Protein; HHR6B; Ubiquitin-Conjugating Enzyme E2 B; Ubiquitin-Conjugating En | 7320 | P63146 | The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is required for post-replicative DNA damage repair. Its protein sequence is 100% identical to the mouse, rat, and rabbit homologs, which indicates that this enzyme is highly conserved in eukaryotic evolution. |
| USP4 | USP4; Ubiquitin Thiolesterase 4; Ubiquitin Carboxyl-Terminal Esterase 4; Ubiquitin Carboxyl-Terminal Hydrolase 4; EC 3.4.19.12; Ubiquitin Thioesterase 4; Deubiquitinating Enzyme 4; Ubiquitin Specific Peptidase 4 (Proto-Oncogene); Ubiquitin Specific Protea | 7375 | Q13107 | Hydrolase that deubiquitinates target proteins such as the receptor ADORA2A, PDPK1 and TRIM21. Deubiquitination of ADORA2A increases the amount of functional receptor at the cell surface. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER. |
| USP7 | Ubiquitin Specific Peptidase 7; Ubiquitin Specific Peptidase 7 (Herpes Virus-Associated); Ubiquitin-Specific-Processing Protease 7; Deubiquitinating Enzyme 7; Ubiquitin Thioesterase 7; HAUSP; Ubiquitin Specific Protease 7 (Herpes Virus-Associated) | 7874 | B7ZAX6 | The protein encoded by this gene belongs to the peptidase C19 family, which includes ubiquitinyl hydrolases. This protein deubiquitinates target proteins such as p53 (a tumor suppressor protein) and WASH (essential for endosomal protein recycling), and regulates their activities by counteracting the opposing ubiquitin ligase activity of proteins such as HDM2 and TRIM27, involved in the respective process. Mutations in this gene have been implicated in a neurodevelopmental disorder. [provided by RefSeq, Mar 2016] |
| VRK1 | PCH1; PCH1A | 7443 | Q99986 | This gene encodes a member of the vaccinia-related kinase (VRK) family of serine/threonine protein kinases. This gene is widely expressed in human tissues and has increased expression in actively dividing cells, such as those in testis, thymus, fetal liver, and carcinomas. Its protein localizes to the nucleus and has been shown to promote the stability and nuclear accumulation of a transcriptionally active p53 molecule and, in vitro, to phosphorylate Thr18 of p53 and reduce p53 ubiquitination. This gene, therefore, may regulate cell proliferation. This protein also phosphorylates histone, casein, and the transcription factors ATF2 (activating transcription factor 2) and c-JUN. [provided by RefSeq, Jul 2008] |
| WISP1 | WISP1; WNT1 inducible signaling pathway protein 1; CCN4; WISP1c; WISP1i; WISP1tc | 8840 | O95388 | This gene encodes a member+AK267:AL268 of the WNT1 inducible signaling pathway (WISP) protein subfamily, which belongs to the connective tissue growth factor (CTGF) family. WNT1 is a member of a family of cysteine-rich, glycosylated signaling proteins that mediate diverse developmental processes. The CTGF family members are characterized by four conserved cysteine-rich domains: insulin-like growth factor-binding domain, von Willebrand factor type C module, thrombospondin domain and C-terminal cystine knot-like domain. This gene may be downstream in the WNT1 signaling pathway that is relevant to malignant transformation. It is expressed at a high level in fibroblast cells, and overexpressed in colon tumors. The encoded protein binds to decorin and biglycan, two members of a family of small leucine-rich proteoglycans present in the extracellular matrix of connective tissue, and possibly prevents the inhibitory activity of decorin and biglycan in tumor cell proliferation. It also attenuates p53-mediated apoptosis in response to DNA damage through activation of the Akt kinase. It is 83% identical to the mouse protein at the amino acid level. Multiple alternatively spliced transcript variants have been identified. |
| XIAP | API3; ILP1; MIHA; XLP2; BIRC4; IAP-3; hIAP3; hIAP-3 | 331 | P98170 | This gene encodes a protein that belongs to a family of apoptotic suppressor proteins. Members of this family share a conserved motif termed, baculovirus IAP repeat, which is necessary for their anti-apoptotic function. This protein functions through binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2 and inhibits apoptosis induced by menadione, a potent inducer of free radicals, and interleukin 1-beta converting enzyme. This protein also inhibits at least two members of the caspase family of cell-death proteases, caspase-3 and caspase-7. Mutations in this gene are the cause of X-linked lymphoproliferative syndrome. Alternate splicing results in multiple transcript variants. Pseudogenes of this gene are found on chromosomes 2 and 11.[provided by RefSeq, Feb 2011] |
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Reference
- Carneiro, Benedito A., and Wafik S. El-Deiry. "Targeting apoptosis in cancer therapy." Nature reviews Clinical oncology 17.7 (2020): 395-417.
For research use only. Not intended for any clinical use.
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