| + |
LUBAC | down-regulates quantity by destabilization 
ubiquitination
|
GLYR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272836 |
Lys338 |
VSDPKAAkDLVLGPS |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272838 |
Lys495 |
NILQGNFkPDFYLKY |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272839 |
Lys505 |
FYLKYIQkDLRLAIA |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272840 |
Lys535 |
NEVYKRAkALDQSDN |
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. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
SPOP | down-regulates quantity by destabilization
binding
|
GLYR1 |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272824 |
|
|
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. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
GLYR1
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