Actin-related protein 2; ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (By similarity). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (By similarity). Seems to contact the pointed end of the daughter actin filament (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and r [...]

Actin-related protein 3; ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (By similarity). Seems to contact the pointed end of the daughter actin filament (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged [...]

Actin-related protein 3; ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (By similarity). Seems to contact the pointed end of the daughter actin filament (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged [...]

Actin-related protein 2; ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (By similarity). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (By similarity). Seems to contact the pointed end of the daughter actin filament (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and r [...]

Uncharacterized protein.

Poly [ADP-ribose] polymerase.

Uncharacterized protein.

Uncharacterized protein.

Uncharacterized protein.

DNA polymerase lambda.

Cyclic GMP-AMP synthase.

Deoxynucleoside triphosphate triphosphohydrolase SAMHD1; Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks. Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells. Functions during S phase at stalled DNA replication forks to promote the resection [...]

Poly [ADP-ribose] polymerase.

Uncharacterized protein.

Poly [ADP-ribose] polymerase.

Uncharacterized protein.

Uncharacterized protein.

Uncharacterized protein.

Uncharacterized protein.

Poly [ADP-ribose] polymerase.

Uncharacterized protein.

DNA polymerase lambda.

DNA polymerase lambda.

Uncharacterized protein.

DNA polymerase lambda.

Uncharacterized protein.

Telomere-associated protein RIF1; Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs. In response to DNA damage, interacts with ATM- phosphorylated TP53BP1, allowing recruitment to DNA DSBs (By similarity). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs. In the same time, RIF1 and TP53BP1 specifically counteract DSBs resection via homologous recombination (HR) during G1 phase (By similarity).

E3 ubiquitin-protein ligase RNF168; E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and ubiquitinates histone H2A and H2AX, leading to amplify the RNF8-dependent H2A ubiquitination and promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recrui [...]

Telomere-associated protein RIF1; Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs. In response to DNA damage, interacts with ATM- phosphorylated TP53BP1, allowing recruitment to DNA DSBs (By similarity). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs. In the same time, RIF1 and TP53BP1 specifically counteract DSBs resection via homologous recombination (HR) during G1 phase (By similarity).

Shieldin complex subunit 1.

Telomere-associated protein RIF1; Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs. In response to DNA damage, interacts with ATM- phosphorylated TP53BP1, allowing recruitment to DNA DSBs (By similarity). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs. In the same time, RIF1 and TP53BP1 specifically counteract DSBs resection via homologous recombination (HR) during G1 phase (By similarity).

Shieldin complex subunit 2.

Telomere-associated protein RIF1; Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs. In response to DNA damage, interacts with ATM- phosphorylated TP53BP1, allowing recruitment to DNA DSBs (By similarity). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs. In the same time, RIF1 and TP53BP1 specifically counteract DSBs resection via homologous recombination (HR) during G1 phase (By similarity).

Shieldin complex subunit 3.

Telomere-associated protein RIF1; Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs. In response to DNA damage, interacts with ATM- phosphorylated TP53BP1, allowing recruitment to DNA DSBs (By similarity). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs. In the same time, RIF1 and TP53BP1 specifically counteract DSBs resection via homologous recombination (HR) during G1 phase (By similarity).

Tumor protein p53 binding protein 1.

E3 ubiquitin-protein ligase RNF168; E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and ubiquitinates histone H2A and H2AX, leading to amplify the RNF8-dependent H2A ubiquitination and promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recrui [...]

Telomere-associated protein RIF1; Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs. In response to DNA damage, interacts with ATM- phosphorylated TP53BP1, allowing recruitment to DNA DSBs (By similarity). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs. In the same time, RIF1 and TP53BP1 specifically counteract DSBs resection via homologous recombination (HR) during G1 phase (By similarity).

E3 ubiquitin-protein ligase RNF168; E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and ubiquitinates histone H2A and H2AX, leading to amplify the RNF8-dependent H2A ubiquitination and promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recrui [...]

Ring finger protein 169.