| + |
CyclinE/CDK2 | up-regulates 
phosphorylation
|
SF3B1 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216686 |
Thr244 |
GRAKGSEtPGATPGS |
Homo sapiens |
|
| pmid |
sentence |
| 12105215 |
To map the set of phosphorylation sites in sap155-(223-322) that determine its interaction with nipp1, we have identified phosphorylation sites of cyclin e-cdk2 by the sequencing of proteolytically derived phosphopeptide). Three phosphorylation sites were identified as thr244, thr248, and thr313 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216666 |
Thr248 |
GSETPGAtPGSKIWD |
Homo sapiens |
|
| pmid |
sentence |
| 12105215 |
To map the set of phosphorylation sites in sap155-(223-322) that determine its interaction with nipp1, we have identified phosphorylation sites of cyclin e-cdk2 by the sequencing of proteolytically derived phosphopeptides. Three phosphorylation sites were identified as thr244, thr248, and thr313 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK2 | up-regulates
phosphorylation
|
SF3B1 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90434 |
Thr244 |
GRAKGSEtPGATPGS |
Homo sapiens |
|
| pmid |
sentence |
| 12105215 |
To map the set of phosphorylation sites in sap155-(223-322) that determine its interaction with nipp1, we have identified phosphorylation sites of cyclin e-cdk2 by the sequencing of proteolytically derived phosphopeptide). Three phosphorylation sites were identified as thr244, thr248, and thr313 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90438 |
Thr248 |
GSETPGAtPGSKIWD |
Homo sapiens |
|
| pmid |
sentence |
| 12105215 |
To map the set of phosphorylation sites in sap155-(223-322) that determine its interaction with nipp1, we have identified phosphorylation sites of cyclin e-cdk2 by the sequencing of proteolytically derived phosphopeptides. Three phosphorylation sites were identified as thr244, thr248, and thr313 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CyclinE/CDK2 |
phosphorylation
|
SF3B1 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216717 |
Thr313 |
HGSGWAEtPRTDRGG |
Homo sapiens |
|
| pmid |
sentence |
| 12105215 |
We indeed found that sap155-(223_322) and sap155-(1_491) are excellent substrates for in vitrophosphorylation by cyclin e-cdk2 as well as cyclin b-cdk1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 |
phosphorylation
|
SF3B1 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90442 |
Thr313 |
HGSGWAEtPRTDRGG |
Homo sapiens |
|
| pmid |
sentence |
| 12105215 |
We indeed found that sap155-(223_322) and sap155-(1_491) are excellent substrates for in vitrophosphorylation by cyclin e-cdk2 as well as cyclin b-cdk1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A |
phosphorylation
|
SF3B1 |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144975 |
Thr434 |
PARKLTAtPTPLGGM |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16512921 |
The present data show that the splicing factor sf3b1 is a substrate of the protein kinase dyrk1a and suggest that dyrk1a may be involved in the regulation of pre mrna-splicing. by mass spectrometry and mutational analysis of sf3b1, thr434 was identified as the major phosphorylation site for dyrk1a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SF3B1 | up-regulates 
|
Proliferation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256003 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25428262 |
We have shown that SF3B1 knockdown in four myeloid cell lines resulted in inhibition of cell growth and disruption of the cell cycle.Taken together, these data show that SF3B1 knockdown results in inhibition of cell growth, induction of cell cycle arrest and impairment of erythroid differentiation in myeloid cell lines. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SF3B1 | form complex 
binding
|
SF3b |
0.937 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268403 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32140746 |
Characterization of the purified SF3b complex indicated that it consists of seven proteins with a molecular size ranging from 10 to 155 kDa [10–12] (Fig. 1a). Due to methodological differences in identifying SF3b components in human and yeast, a number of names have been designated for these proteins across different species. In this review, I will use SF3b1-7 for consistency and clarity (Fig. 1a). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SF3B1 | up-regulates
|
Differentiation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256004 |
|
|
Homo sapiens |
K-562 Cell, HEL Cell |
| pmid |
sentence |
| 25428262 |
Taken together, these data show that SF3B1 knockdown results in inhibition of cell growth, induction of cell cycle arrest and impairment of erythroid differentiation in myeloid cell lines.[…]SF3B1 knockdown compared with the scramble control, suggesting that normal SF3B1 function is required for erythroid differentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SF3B1 | form complex
binding
|
B-WICH complex |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268819 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21559432 |
The B-WICH complex is an extended form of WICH [26], and is involved in both RNA pol I and RNA pol III transcription [20], [21]. In addition to the three core proteins, WSTF, SNF2h, and nuclear myosin (NM1); the myb binding protein 1b, RNA helicase II/DXX21, and SAP155 all also associate via RNA species [21]. The subunit SNF2h is an ISWI ATPase, which slides nucleosomes in an ATP-dependent manner [27]. WSTF is a component of several complexes: two SNF2h complexes, B-WICH [21] and WICH [26], and one SWI/SNF type of chromatin remodelling complex, the WINAC complex, which is involved in vitamin D-mediated RNA pol II transcription |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SF3B1 | form complex
binding
|
U2 snRNP complex |
0.823 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270653 |
|
|
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 |
3.0
SF3B1
- 
- 