| + |
GEMIN6 | form complex 
binding
|
SMN complex |
0.833 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253120 |
|
|
|
|
| pmid |
sentence |
| 12065586 |
SMN is part of a large macromolecular complex that also contains Gemin2, Gemin3, Gemin4, Gemin5, and Gemin6. The SMN complex functions in the assembly of spliceosomal small nuclear ribonucleoproteins and probably other ribonucleoprotein particles. We have identified a novel protein component of the SMN complex termed Gemin7 using native purified SMN complexes and peptide sequencing by mass spectrometry. |
|
| Publications: |
1 |
| + |
GEMIN7 | form complex
binding
|
SMN complex |
0.819 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253121 |
|
|
|
|
| pmid |
sentence |
| 12065586 |
SMN is part of a large macromolecular complex that also contains Gemin2, Gemin3, Gemin4, Gemin5, and Gemin6. The SMN complex functions in the assembly of spliceosomal small nuclear ribonucleoproteins and probably other ribonucleoprotein particles. We have identified a novel protein component of the SMN complex termed Gemin7 using native purified SMN complexes and peptide sequencing by mass spectrometry. |
|
| Publications: |
1 |
| + |
GEMIN5 | form complex
binding
|
SMN complex |
0.746 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253119 |
|
|
|
|
| pmid |
sentence |
| 12065586 |
SMN is part of a large macromolecular complex that also contains Gemin2, Gemin3, Gemin4, Gemin5, and Gemin6. The SMN complex functions in the assembly of spliceosomal small nuclear ribonucleoproteins and probably other ribonucleoprotein particles. We have identified a novel protein component of the SMN complex termed Gemin7 using native purified SMN complexes and peptide sequencing by mass spectrometry. |
|
| Publications: |
1 |
| + |
GEMIN2 | form complex
binding
|
SMN complex |
0.872 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253116 |
|
|
|
|
| pmid |
sentence |
| 12065586 |
SMN is part of a large macromolecular complex that also contains Gemin2, Gemin3, Gemin4, Gemin5, and Gemin6. The SMN complex functions in the assembly of spliceosomal small nuclear ribonucleoproteins and probably other ribonucleoprotein particles. We have identified a novel protein component of the SMN complex termed Gemin7 using native purified SMN complexes and peptide sequencing by mass spectrometry. |
|
| Publications: |
1 |
| + |
DDX20 | form complex
binding
|
SMN complex |
0.857 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253117 |
|
|
|
|
| pmid |
sentence |
| 12065586 |
SMN is part of a large macromolecular complex that also contains Gemin2, Gemin3, Gemin4, Gemin5, and Gemin6. The SMN complex functions in the assembly of spliceosomal small nuclear ribonucleoproteins and probably other ribonucleoprotein particles. We have identified a novel protein component of the SMN complex termed Gemin7 using native purified SMN complexes and peptide sequencing by mass spectrometry. |
|
| Publications: |
1 |
| + |
SMN1 | form complex
binding
|
SMN complex |
0.736 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253115 |
|
|
|
|
| pmid |
sentence |
| 12065586 |
SMN is part of a large macromolecular complex that also contains Gemin2, Gemin3, Gemin4, Gemin5, and Gemin6. The SMN complex functions in the assembly of spliceosomal small nuclear ribonucleoproteins and probably other ribonucleoprotein particles. We have identified a novel protein component of the SMN complex termed Gemin7 using native purified SMN complexes and peptide sequencing by mass spectrometry. |
|
| Publications: |
1 |
| + |
PKA | up-regulates quantity by stabilization 
phosphorylation
|
SMN complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253122 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19103745 |
PKA increases SMN complex formation and SMN stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMN complex | up-regulates 
|
Spliceosomal_snRNP_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253123 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9323129 |
These findings suggest a role for SMN and SIP1 in spliceosomal snRNP biogenesis and function and provide a likely molecular mechanism for the cause of SMA |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GEMIN4 | form complex
binding
|
SMN complex |
0.808 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253118 |
|
|
|
|
| pmid |
sentence |
| 12065586 |
SMN is part of a large macromolecular complex that also contains Gemin2, Gemin3, Gemin4, Gemin5, and Gemin6. The SMN complex functions in the assembly of spliceosomal small nuclear ribonucleoproteins and probably other ribonucleoprotein particles. We have identified a novel protein component of the SMN complex termed Gemin7 using native purified SMN complexes and peptide sequencing by mass spectrometry. |
|
| Publications: |
1 |
3.0
SMN complex
CPX-6031