amyloid beta precursor protein (cytoplasmic tail) binding protein 2; May play a role in intracellular protein transport. May be involved in the translocation of APP along microtubules toward the cell surface

kinesin light chain 1

amyloid beta precursor protein (cytoplasmic tail) binding protein 2; May play a role in intracellular protein transport. May be involved in the translocation of APP along microtubules toward the cell surface

kinesin light chain 2; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

amyloid beta precursor protein (cytoplasmic tail) binding protein 2; May play a role in intracellular protein transport. May be involved in the translocation of APP along microtubules toward the cell surface

kinesin light chain 4; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

interferon-induced protein with tetratricopeptide repeats 1; Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single- stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-se [...]

interferon-induced protein with tetratricopeptide repeats 2; IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2’-O-methylation of the 5’ cap. The ribose 2’-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2’-O-methylase for their mRNAs or by stealing host cap containing the 2’-O- methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5’ triphosphorylat [...]

interferon-induced protein with tetratricopeptide repeats 1; Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single- stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-se [...]

interferon-induced protein with tetratricopeptide repeats 3; IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS- mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exihibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1 [...]

interferon-induced protein with tetratricopeptide repeats 2; IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2’-O-methylation of the 5’ cap. The ribose 2’-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2’-O-methylase for their mRNAs or by stealing host cap containing the 2’-O- methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5’ triphosphorylat [...]

interferon-induced protein with tetratricopeptide repeats 1; Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single- stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-se [...]

interferon-induced protein with tetratricopeptide repeats 2; IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2’-O-methylation of the 5’ cap. The ribose 2’-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2’-O-methylase for their mRNAs or by stealing host cap containing the 2’-O- methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5’ triphosphorylat [...]

interferon-induced protein with tetratricopeptide repeats 3; IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS- mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exihibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1 [...]

interferon-induced protein with tetratricopeptide repeats 3; IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS- mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exihibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1 [...]

interferon-induced protein with tetratricopeptide repeats 1; Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single- stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-se [...]

interferon-induced protein with tetratricopeptide repeats 3; IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS- mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exihibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1 [...]

interferon-induced protein with tetratricopeptide repeats 2; IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2’-O-methylation of the 5’ cap. The ribose 2’-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2’-O-methylase for their mRNAs or by stealing host cap containing the 2’-O- methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5’ triphosphorylat [...]

kinesin light chain 1

amyloid beta precursor protein (cytoplasmic tail) binding protein 2; May play a role in intracellular protein transport. May be involved in the translocation of APP along microtubules toward the cell surface

kinesin light chain 1

kinesin light chain 2; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

kinesin light chain 1

kinesin light chain 4; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

kinesin light chain 2; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

amyloid beta precursor protein (cytoplasmic tail) binding protein 2; May play a role in intracellular protein transport. May be involved in the translocation of APP along microtubules toward the cell surface

kinesin light chain 2; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

kinesin light chain 1

kinesin light chain 2; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

kinesin light chain 3; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport

kinesin light chain 2; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

kinesin light chain 4; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

kinesin light chain 3; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport

kinesin light chain 2; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

kinesin light chain 4; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

amyloid beta precursor protein (cytoplasmic tail) binding protein 2; May play a role in intracellular protein transport. May be involved in the translocation of APP along microtubules toward the cell surface

kinesin light chain 4; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

kinesin light chain 1

kinesin light chain 4; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)

kinesin light chain 2; Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)