| + |
SRP54 | up-regulates activity 
binding
|
SRPRB |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261165 |
|
|
in vitro |
|
| pmid |
sentence |
| 30649417 |
The multi-domain SRP GTPase SRP54 recognizes the signal with its M domain and establishes the targeting complex consisting of its NG domain bound to the homologous NG domain of the SRP receptor SRα at a proximal ribosome binding site. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SRP54 | up-regulates activity
binding
|
SRPRA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261163 |
|
|
in vitro |
|
| pmid |
sentence |
| 30649417 |
The multi-domain SRP GTPase SRP54 recognizes the signal with its M domain and establishes the targeting complex consisting of its NG domain bound to the homologous NG domain of the SRP receptor SRα at a proximal ribosome binding site. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SRP54 | up-regulates activity
binding
|
U2AF1/U2AF2 |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261162 |
|
|
in vitro |
|
| pmid |
sentence |
| 8816452 |
We have now demonstrated that p54 interacts not only with SC35 and ASF/SF2 but also with U2AF. Pairwise interactions between p54 and other RS domain-containing spliceosomal proteins in comparison with SC35 and ASF/SF2 as detected by the yeast two-hybrid interaction assay. . It is conceivable that p54 can mediate 59 and 39 splice site interaction by interacting directly with U2AF65 associated with the 39 splice site and at the same time interact with other SR proteins, such as ASF/SF2 and SC35, which in turn interact with U1-70K. In this scenario, p54 is different from SC35 or ASF/SF2 in that it cannot directly interact with the 59 component (U1-70K) but can interact with the protein associated with the 39 splice site (U2AF65). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SRP54 | up-regulates activity
binding
|
SRSF2 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261160 |
|
|
in vitro |
|
| pmid |
sentence |
| 8816452 |
We have now demonstrated that p54 interacts not only with SC35 and ASF/SF2 but also with U2AF. Pairwise interactions between p54 and other RS domain-containing spliceosomal proteins in comparison with SC35 and ASF/SF2 as detected by the yeast two-hybrid interaction assay. . It is conceivable that p54 can mediate 59 and 39 splice site interaction by interacting directly with U2AF65 associated with the 39 splice site and at the same time interact with other SR proteins, such as ASF/SF2 and SC35, which in turn interact with U1-70K. In this scenario, p54 is different from SC35 or ASF/SF2 in that it cannot directly interact with the 59 component (U1-70K) but can interact with the protein associated with the 39 splice site (U2AF65). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SRP19 | up-regulates activity
binding
|
SRP54 |
0.962 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261168 |
|
|
in vitro |
|
| pmid |
sentence |
| 30649418 |
Mammalian SRP comprises the highly base-paired SRP RNA (also referred to as 7SL RNA) of ∼300 nt and six proteins (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) (Figure (Figure1A).1A). The hierarchy of protein addition always starts with the scaffolding protein SRP19 (together with SRP9/14 for the entire SRP) followed by SRP68/72 and finally by SRP54. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SRP54 | up-regulates activity
binding
|
SRSF1 |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261161 |
|
|
in vitro |
|
| pmid |
sentence |
| 8816452 |
We have now demonstrated that p54 interacts not only with SC35 and ASF/SF2 but also with U2AF. Pairwise interactions between p54 and other RS domain-containing spliceosomal proteins in comparison with SC35 and ASF/SF2 as detected by the yeast two-hybrid interaction assay. . It is conceivable that p54 can mediate 59 and 39 splice site interaction by interacting directly with U2AF65 associated with the 39 splice site and at the same time interact with other SR proteins, such as ASF/SF2 and SC35, which in turn interact with U1-70K. In this scenario, p54 is different from SC35 or ASF/SF2 in that it cannot directly interact with the 59 component (U1-70K) but can interact with the protein associated with the 39 splice site (U2AF65). |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
SRP54
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