| + |
TEX10 | form complex 
binding
|
Rix1 complex |
0.874 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265472 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22190735 |
LAS1L was first described as a nucleolar protein required for maturation of the 60S preribosomal subunit. In this paper, we demonstrate that LAS1L interacts with PELP1, TEX10, and WDR18, the mammalian homologues of the budding yeast Rix1 complex, along with NOL9 and SENP3, to form a novel nucleolar complex that cofractionates with the 60S preribosomal subunit. our data identify a novel mammalian complex required for 60S ribosomal subunit synthesis, providing further insight into the intricate, yet poorly described, process of ribosome biogenesis in higher eukaryotes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WDR18 | form complex
binding
|
Rix1 complex |
0.867 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265471 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22190735 |
LAS1L was first described as a nucleolar protein required for maturation of the 60S preribosomal subunit. In this paper, we demonstrate that LAS1L interacts with PELP1, TEX10, and WDR18, the mammalian homologues of the budding yeast Rix1 complex, along with NOL9 and SENP3, to form a novel nucleolar complex that cofractionates with the 60S preribosomal subunit. our data identify a novel mammalian complex required for 60S ribosomal subunit synthesis, providing further insight into the intricate, yet poorly described, process of ribosome biogenesis in higher eukaryotes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SENP3 | form complex
binding
|
Rix1 complex |
0.797 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265468 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22190735 |
LAS1L was first described as a nucleolar protein required for maturation of the 60S preribosomal subunit. In this paper, we demonstrate that LAS1L interacts with PELP1, TEX10, and WDR18, the mammalian homologues of the budding yeast Rix1 complex, along with NOL9 and SENP3, to form a novel nucleolar complex that cofractionates with the 60S preribosomal subunit. our data identify a novel mammalian complex required for 60S ribosomal subunit synthesis, providing further insight into the intricate, yet poorly described, process of ribosome biogenesis in higher eukaryotes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LAS1L | up-regulates activity 
binding
|
Rix1 complex |
0.844 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265467 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22190735 |
LAS1L was first described as a nucleolar protein required for maturation of the 60S preribosomal subunit. In this paper, we demonstrate that LAS1L interacts with PELP1, TEX10, and WDR18, the mammalian homologues of the budding yeast Rix1 complex, along with NOL9 and SENP3, to form a novel nucleolar complex that cofractionates with the 60S preribosomal subunit. our data identify a novel mammalian complex required for 60S ribosomal subunit synthesis, providing further insight into the intricate, yet poorly described, process of ribosome biogenesis in higher eukaryotes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOL9 | form complex
binding
|
Rix1 complex |
0.79 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265470 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22190735 |
LAS1L was first described as a nucleolar protein required for maturation of the 60S preribosomal subunit. In this paper, we demonstrate that LAS1L interacts with PELP1, TEX10, and WDR18, the mammalian homologues of the budding yeast Rix1 complex, along with NOL9 and SENP3, to form a novel nucleolar complex that cofractionates with the 60S preribosomal subunit. our data identify a novel mammalian complex required for 60S ribosomal subunit synthesis, providing further insight into the intricate, yet poorly described, process of ribosome biogenesis in higher eukaryotes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PELP1 | form complex
binding
|
Rix1 complex |
0.794 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265469 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22190735 |
LAS1L was first described as a nucleolar protein required for maturation of the 60S preribosomal subunit. In this paper, we demonstrate that LAS1L interacts with PELP1, TEX10, and WDR18, the mammalian homologues of the budding yeast Rix1 complex, along with NOL9 and SENP3, to form a novel nucleolar complex that cofractionates with the 60S preribosomal subunit. our data identify a novel mammalian complex required for 60S ribosomal subunit synthesis, providing further insight into the intricate, yet poorly described, process of ribosome biogenesis in higher eukaryotes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Rix1 complex | up-regulates 
|
Ribosome biogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265473 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22190736 |
In this study, we show that LAS1L forms a protein complex with PELP1, TEX10, NOL9, SENP3, and WDR18. Our data demonstrate that all the components of the LAS1L complex cosediment with the pre-60S ribosomal particle and are required for proper processing of the 32S rRNA intermediate.These findings demonstrate that the LAS1L complex is critical for ribosome biogenesis and cell proliferation and provide additional evidence that multiple protein complexes have distinct functions in the synthesis of eukaryotic ribosomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Rix1 complex