| + |
Cullin 3-RBX1-Skp1 | down-regulates quantity by destabilization 
ubiquitination
|
DEK |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272831 |
Lys137 |
FSGFPFEkGSVQYKK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. This result aligns well with the observation that multiple ubiquitylated DEK lysine residues were detected in the initial proteome analysis (fig. S2E). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272830 |
Lys284 |
VKSANVKkADSSTTK |
Homo sapiens |
|
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. This result aligns well with the observation that multiple ubiquitylated DEK lysine residues were detected in the initial proteome analysis (fig. S2E). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272832 |
Lys331 |
ELKETIKkLLASANL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. This result aligns well with the observation that multiple ubiquitylated DEK lysine residues were detected in the initial proteome analysis (fig. S2E). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272833 |
Lys344 |
NLEEVTMkQICKKVY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. This result aligns well with the observation that multiple ubiquitylated DEK lysine residues were detected in the initial proteome analysis (fig. S2E). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272834 |
Lys349 |
TMKQICKkVYENYPT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. This result aligns well with the observation that multiple ubiquitylated DEK lysine residues were detected in the initial proteome analysis (fig. S2E). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272835 |
Lys371 |
DFIKTTVkELIS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. This result aligns well with the observation that multiple ubiquitylated DEK lysine residues were detected in the initial proteome analysis (fig. S2E). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272828 |
Lys57 |
KSLIVEGkREKKKVE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. This result aligns well with the observation that multiple ubiquitylated DEK lysine residues were detected in the initial proteome analysis (fig. S2E). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272829 |
Lys84 |
PFTIAQGkGQKLCEI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. This result aligns well with the observation that multiple ubiquitylated DEK lysine residues were detected in the initial proteome analysis (fig. S2E). |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | up-regulates 
phosphorylation
|
DEK |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125912 |
Ser32 |
MPGPREEsEEEEDED |
Homo sapiens |
|
| pmid |
sentence |
| 15199154 |
Dek is phosphorylated by the protein kinase ck2 in vitro and in vivo on ser32 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147365 |
Ser32 |
MPGPREEsEEEEDED |
Homo sapiens |
|
| pmid |
sentence |
| 16809543 |
Dek phosphorylated at serines 19 and 32. Dek and its phosphorylation are required for intron removal |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates quantity by destabilization
phosphorylation
|
DEK |
0.437 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276303 |
Thr67 |
KKKVERLtMQVSSLQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21282377 |
These data suggest that the E3 ligase SCFFbxw7-α degrades p-DEK in a GSK-3β–dependent manner.Therefore, the phosphorylation of DEK by GSK-3β is a crucial step to mediate Tpm RNA splicing. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
polyubiquitination
|
DEK |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276304 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21282377 |
These data suggest that the E3 ligase SCFFbxw7-α degrades p-DEK in a GSK-3β–dependent manner.Therefore, the phosphorylation of DEK by GSK-3β is a crucial step to mediate Tpm RNA splicing. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DEK | form complex 
binding
|
B-WICH complex |
0.449 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268823 |
|
|
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 |
| + |
DEK | down-regulates quantity by repression 
transcriptional regulation
|
PRDX5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254125 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19229864 |
We further demonstrated by ChIP analysis that knock-down of DEK caused hyperacetylation of histones around Prx VI promoter which is upregulated in our profile. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SPOP | down-regulates quantity by destabilization
binding
|
DEK |
0.438 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272826 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. This result aligns well with the observation that multiple ubiquitylated DEK lysine residues were detected in the initial proteome analysis (fig. S2E). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
DEK
- 
- 