| + |
RPP40 | form complex 
binding
|
Ribonuclease MRP complex |
0.747 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280680 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NEPRO | form complex
binding
|
Ribonuclease MRP complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280686 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ribonuclease MRP complex | up-regulates quantity 
chemical modification
|
ribosomal RNA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280690 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPP38 | form complex
binding
|
Ribonuclease MRP complex |
0.735 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280683 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POP7 | form complex
binding
|
Ribonuclease MRP complex |
0.678 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280679 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPP14 | form complex
binding
|
Ribonuclease MRP complex |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280681 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POP4 | form complex
binding
|
Ribonuclease MRP complex |
0.849 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280682 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPP30 | form complex
binding
|
Ribonuclease MRP complex |
0.845 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280684 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
C18orf21 | form complex
binding
|
Ribonuclease MRP complex |
0.427 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280685 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POP5 | form complex
binding
|
Ribonuclease MRP complex |
0.764 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280687 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POP1 | form complex
binding
|
Ribonuclease MRP complex |
0.62 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280688 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPP25 | form complex
binding
|
Ribonuclease MRP complex |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280689 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40413743 |
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities.Using a genome-wide forward genetic screening that leveraged the requirement of RNase MRP and RNase P for reporter translation, we identified two poorly characterized yet highly enriched human genes, c18orf21 and c3orf17, which we named ribonuclease MRP subunit P24 (RMP24) and RMP64, respectively. We demonstrate that these two genes are specifically required for the activity of human RNase MRP but not RNase P. The protein products of RMP24 and RMP64 associate extensively and exclusively with the only known human RNase MRP-specific component, MRP RNA, but not with the RNase P-specific H1 RNA. Our findings establish Rmp24 and Rmp64 as human protein components unique to RNase MRP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
Ribonuclease MRP complex
CPX-2876