ankyrin repeat and BTB (POZ) domain containing 1; May act as a mediator of the PTEN growth-suppressive signaling pathway. May play a role in developmental processes

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

deoxynucleotidyltransferase, terminal; Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5’-triphosphate to the 3’-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

deoxynucleotidyltransferase, terminal; Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5’-triphosphate to the 3’-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells

transcriptional regulating factor 1; Activates transcription of CYP11A1. Interaction with CREBBP and EP300 results in a synergistic transcriptional activation of CYP11A1

deoxynucleotidyltransferase, terminal; Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5’-triphosphate to the 3’-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells

ubiquitin C

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

ankyrin repeat and BTB (POZ) domain containing 1; May act as a mediator of the PTEN growth-suppressive signaling pathway. May play a role in developmental processes

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

deoxynucleotidyltransferase, terminal; Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5’-triphosphate to the 3’-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

ELM2 and Myb/SANT-like domain containing 1

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

histone deacetylase 1; Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST- mediated transcription in resting neurons. Upon calcium s [...]

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

histone deacetylase 2; Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed o [...]

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

homeobox and leucine zipper encoding; May function as a transcriptional regulator

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

SH3 domain containing ring finger 2; Inhibits PPP1CA phosphatase activity. May be a E3 ubiquitin-protein ligase (Potential). May play a role in cardiac function

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

transcriptional regulating factor 1; Activates transcription of CYP11A1. Interaction with CREBBP and EP300 results in a synergistic transcriptional activation of CYP11A1

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

ubiquitin C

ELM2 and Myb/SANT-like domain containing 1

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

ELM2 and Myb/SANT-like domain containing 1

histone deacetylase 1; Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST- mediated transcription in resting neurons. Upon calcium s [...]

ELM2 and Myb/SANT-like domain containing 1

histone deacetylase 2; Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed o [...]

ELM2 and Myb/SANT-like domain containing 1

ubiquitin C

histone deacetylase 1; Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST- mediated transcription in resting neurons. Upon calcium s [...]

deoxynucleotidyltransferase, terminal, interacting protein 1; Shown to enhance TdT activity, in vitro

histone deacetylase 1; Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST- mediated transcription in resting neurons. Upon calcium s [...]

ELM2 and Myb/SANT-like domain containing 1

histone deacetylase 1; Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST- mediated transcription in resting neurons. Upon calcium s [...]

histone deacetylase 2; Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed o [...]