cysteinyl-tRNA synthetase

mitochondrial rRNA methyltransferase 1 homolog (S. cerevisiae); Probably methylates the ribose of guanosine G-2270 in the peptidyl transferase center of the mitochondrial large ribosomal RNA (21S) (By similarity)

cysteinyl-tRNA synthetase

mitochondrial ribosomal protein L1

cysteinyl-tRNA synthetase

RNA methyltransferase like 1; Probable RNA methyltransferase (By similarity)

cysteinyl-tRNA synthetase

ribosomal protein L10a

cysteinyl-tRNA synthetase

SEC24 family, member D (S. cerevisiae); Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex

cysteinyl-tRNA synthetase

TAR (HIV-1) RNA binding protein 1; Probable S-adenosyl-L-methionine-dependent methyltransferase which methylates RNA molecules such as tRNAs. In case of infection by HIV-1, it binds to the loop region of TAR RNA, a region also bound by RNA polymerase II. Binding of TARBP1 and RNA polymerase II to HIV-1 TAR RNA is mutually exclusive, suggesting that TARBP1 may function alone or in conjunction with HIV-1 Tat to disengage RNA polymerase II from HIV-1 TAR RNA. May act by methylating HIV-1 TAR RNA

cysteinyl-tRNA synthetase

THUMP domain containing 3

cysteinyl-tRNA synthetase

exportin 7; Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate ano [...]

DIS3 mitotic control homolog (S. cerevisiae)

DIS3 mitotic control homolog (S. cerevisiae)-like; Putative cytoplasm-specific catalytic component of the RNA exosome complex which has 3’->5’ exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3’ untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA

DIS3 mitotic control homolog (S. cerevisiae)

mitochondrial rRNA methyltransferase 1 homolog (S. cerevisiae); Probably methylates the ribose of guanosine G-2270 in the peptidyl transferase center of the mitochondrial large ribosomal RNA (21S) (By similarity)

DIS3 mitotic control homolog (S. cerevisiae)

RNA methyltransferase like 1; Probable RNA methyltransferase (By similarity)

DIS3 mitotic control homolog (S. cerevisiae)

TAR (HIV-1) RNA binding protein 1; Probable S-adenosyl-L-methionine-dependent methyltransferase which methylates RNA molecules such as tRNAs. In case of infection by HIV-1, it binds to the loop region of TAR RNA, a region also bound by RNA polymerase II. Binding of TARBP1 and RNA polymerase II to HIV-1 TAR RNA is mutually exclusive, suggesting that TARBP1 may function alone or in conjunction with HIV-1 Tat to disengage RNA polymerase II from HIV-1 TAR RNA. May act by methylating HIV-1 TAR RNA

DIS3 mitotic control homolog (S. cerevisiae)-like; Putative cytoplasm-specific catalytic component of the RNA exosome complex which has 3’->5’ exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3’ untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA

DIS3 mitotic control homolog (S. cerevisiae)

DIS3 mitotic control homolog (S. cerevisiae)-like; Putative cytoplasm-specific catalytic component of the RNA exosome complex which has 3’->5’ exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3’ untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA

mitochondrial rRNA methyltransferase 1 homolog (S. cerevisiae); Probably methylates the ribose of guanosine G-2270 in the peptidyl transferase center of the mitochondrial large ribosomal RNA (21S) (By similarity)

DIS3 mitotic control homolog (S. cerevisiae)-like; Putative cytoplasm-specific catalytic component of the RNA exosome complex which has 3’->5’ exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3’ untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA

RNA methyltransferase like 1; Probable RNA methyltransferase (By similarity)

DIS3 mitotic control homolog (S. cerevisiae)-like; Putative cytoplasm-specific catalytic component of the RNA exosome complex which has 3’->5’ exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3’ untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA

TAR (HIV-1) RNA binding protein 1; Probable S-adenosyl-L-methionine-dependent methyltransferase which methylates RNA molecules such as tRNAs. In case of infection by HIV-1, it binds to the loop region of TAR RNA, a region also bound by RNA polymerase II. Binding of TARBP1 and RNA polymerase II to HIV-1 TAR RNA is mutually exclusive, suggesting that TARBP1 may function alone or in conjunction with HIV-1 Tat to disengage RNA polymerase II from HIV-1 TAR RNA. May act by methylating HIV-1 TAR RNA

DIS3 mitotic control homolog (S. cerevisiae)-like 2; Ribonuclease that plays a critical role in RNA metabolism. It is essential for correct mitosis, and negatively regulates cell proliferation

mitochondrial rRNA methyltransferase 1 homolog (S. cerevisiae); Probably methylates the ribose of guanosine G-2270 in the peptidyl transferase center of the mitochondrial large ribosomal RNA (21S) (By similarity)

DIS3 mitotic control homolog (S. cerevisiae)-like 2; Ribonuclease that plays a critical role in RNA metabolism. It is essential for correct mitosis, and negatively regulates cell proliferation

RNA methyltransferase like 1; Probable RNA methyltransferase (By similarity)

DIS3 mitotic control homolog (S. cerevisiae)-like 2; Ribonuclease that plays a critical role in RNA metabolism. It is essential for correct mitosis, and negatively regulates cell proliferation

TAR (HIV-1) RNA binding protein 1; Probable S-adenosyl-L-methionine-dependent methyltransferase which methylates RNA molecules such as tRNAs. In case of infection by HIV-1, it binds to the loop region of TAR RNA, a region also bound by RNA polymerase II. Binding of TARBP1 and RNA polymerase II to HIV-1 TAR RNA is mutually exclusive, suggesting that TARBP1 may function alone or in conjunction with HIV-1 Tat to disengage RNA polymerase II from HIV-1 TAR RNA. May act by methylating HIV-1 TAR RNA

family with sequence similarity 114, member A1; May play a role in neuronal cell development (By similarity)

SEC24 family, member D (S. cerevisiae); Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex