+ |
CSNK2A1 | up-regulates
phosphorylation
|
PRPF3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-158319 |
Thr494 |
TEAVQDPtKVEAHVR |
Homo sapiens |
|
pmid |
sentence |
17932117 |
Our findings provide new insights into the biology of hprp3p and suggest that the loss of hprp3p phosphorylation at thr494 is a key step for initiating thr494met aberrant interactions within u4/u6 snrnp complex and that these are likely linked to the rp18 phenotype. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
USP4 | down-regulates activity
deubiquitination
|
PRPF3 |
0.501 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271975 |
|
|
Homo sapiens |
|
pmid |
sentence |
20595234 |
Prp3 is deubiquitinated by Usp4 and its substrate targeting factor, the U4/U6 recycling protein Sart3, which likely facilitates ejection of U4 proteins from the spliceosome during maturation of its active site. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRPF19 | up-regulates activity
polyubiquitination
|
PRPF3 |
0.742 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271966 |
|
|
Homo sapiens |
|
pmid |
sentence |
20595234 |
Here, we report that the spliceosomal Prp19 complex modifies Prp3, a component of the U4 snRNP, with nonproteolytic K63-linked ubiquitin chains. The K63-linked chains increase the affinity of Prp3 for the U5 snRNP component Prp8, thereby allowing for the stabilization of the U4/U6.U5 snRNP. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MECP2 | up-regulates activity
binding
|
PRPF3 |
0.271 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277691 |
|
|
Mus musculus |
|
pmid |
sentence |
21070191 |
MeCP2 interacts directly with Prpf3 and Sdccag1|Notably, Mecp2308/Y mice, which produce a truncated form of MeCP2 and reproduce many of the classical features of RTT [43], have been shown to have multiple genes that are abnormally spliced in the brain [23]. This suggests the C-terminal portion of MeCP2, which we have identified as the putative Sdccag1 interaction domain, plays a critical role in regulating alternative splicing. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Brain |
+ |
PRPF3 | form complex
binding
|
U4/U6.U5 snRNP complex |
0.766 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271967 |
|
|
Homo sapiens |
|
pmid |
sentence |
30765414 |
The major spliceosomal building blocks are the U1, U2, U4/U6, and U5 small nuclear ribonucleoproteins (snRNPs). Each consists of a small nuclear RNA (snRNA) (or two, in the case of U4/U6), seven Sm proteins that form a ring (or seven Lsm proteins in the case of U6), and a variable number of snRNP-specific proteins (Fig. 1F) (Will and Lührmann 2011). Under splicing conditions, the U4/U6 and U5 snRNPs form a 25S U4/U6.U5 tri-snRNP, in which the U4 and U6 snRNAs are base-paired, forming a three-way junction. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |