centromere protein F, 350/400kDa (mitosin); Required for kinetochore function and chromosome segregation in mitosis. Required for kinetochore localization of dynein, LIS1, NDE1 and NDEL1. Regulates recycling of the plasma membrane by acting as a link between recycling vesicles and the microtubule network though its association with STX4 and SNAP25. Acts as a potential inhibitor of pocket protein-mediated cellular processes during development by regulating the activity of RB proteins during cell division and proliferation. May play a regulatory or permissive role in the normal embryonic [...]

farnesyltransferase, CAAX box, alpha; Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity)

centromere protein F, 350/400kDa (mitosin); Required for kinetochore function and chromosome segregation in mitosis. Required for kinetochore localization of dynein, LIS1, NDE1 and NDEL1. Regulates recycling of the plasma membrane by acting as a link between recycling vesicles and the microtubule network though its association with STX4 and SNAP25. Acts as a potential inhibitor of pocket protein-mediated cellular processes during development by regulating the activity of RB proteins during cell division and proliferation. May play a regulatory or permissive role in the normal embryonic [...]

farnesyltransferase, CAAX box, beta; Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding

dehydrodolichyl diphosphate synthase

Uncharacterized protein

dehydrodolichyl diphosphate synthase

farnesyl-diphosphate farnesyltransferase 1

dehydrodolichyl diphosphate synthase

farnesyltransferase, CAAX box, beta; Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding

dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1A; May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates such as CRY2, FOXO1 and SIRT1

family with sequence similarity 53, member C

dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1A; May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates such as CRY2, FOXO1 and SIRT1

farnesyltransferase, CAAX box, alpha; Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity)

dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1A; May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates such as CRY2, FOXO1 and SIRT1

farnesyltransferase, CAAX box, beta; Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding

dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1A; May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates such as CRY2, FOXO1 and SIRT1

related RAS viral (r-ras) oncogene homolog 2; It is a plasma membrane-associated GTP-binding protein with GTPase activity. Might transduce growth inhibitory signals across the cell membrane, exerting its effect through an effector shared with the Ras proteins but in an antagonistic fashion

CHURC1-FNTB readthrough

Uncharacterized protein

CHURC1-FNTB readthrough

farnesyltransferase, CAAX box, alpha; Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity)

CHURC1-FNTB readthrough

farnesyltransferase, CAAX box, beta; Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding

CHURC1-FNTB readthrough

GDP dissociation inhibitor 1; Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them

CHURC1-FNTB readthrough

GDP dissociation inhibitor 2; Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them

CHURC1-FNTB readthrough

v-Ha-ras Harvey rat sarcoma viral oncogene homolog; Ras proteins bind GDP/GTP and possess intrinsic GTPase activity

CHURC1-FNTB readthrough

v-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog; Ras proteins bind GDP/GTP and possess intrinsic GTPase activity

CHURC1-FNTB readthrough

Rab geranylgeranyltransferase, alpha subunit; Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A and RAB5A respectively

CHURC1-FNTB readthrough

RAP2A, member of RAS oncogene family; Small GTP-binding protein which cycles between a GDP- bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading

CHURC1-FNTB readthrough

related RAS viral (r-ras) oncogene homolog 2; It is a plasma membrane-associated GTP-binding protein with GTPase activity. Might transduce growth inhibitory signals across the cell membrane, exerting its effect through an effector shared with the Ras proteins but in an antagonistic fashion

CHURC1-FNTB readthrough

zinc metallopeptidase STE24 homolog (S. cerevisiae); Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C