| + |
CSNK2B |
phosphorylation
|
CDC34 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251057 |
Ser203 |
APAPDEGsDLFYDDY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11546811 |
CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. | Mutation of CDC34 at CK2-targeted residues, Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, abolishes the phosphorylation of CDC34 observed in vivo and markedly shifts nuclearly localized CDC34 to the cytoplasm. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251058 |
Ser222 |
EVEEEADsCFGDDED |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11546811 |
CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. | Mutation of CDC34 at CK2-targeted residues, Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, abolishes the phosphorylation of CDC34 observed in vivo and markedly shifts nuclearly localized CDC34 to the cytoplasm. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251059 |
Ser231 |
FGDDEDDsGTEES |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11546811 |
CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. | Mutation of CDC34 at CK2-targeted residues, Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, abolishes the phosphorylation of CDC34 observed in vivo and markedly shifts nuclearly localized CDC34 to the cytoplasm. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251060 |
Ser236 |
DDSGTEEs |
Homo sapiens |
|
| pmid |
sentence |
| 12037680 |
CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. | Mutation of CDC34 at CK2-targeted residues, Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, abolishes the phosphorylation of CDC34 observed in vivo and markedly shifts nuclearly localized CDC34 to the cytoplasm. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251061 |
Thr233 |
DDEDDSGtEES |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11546811 |
CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. | Mutation of CDC34 at CK2-targeted residues, Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, abolishes the phosphorylation of CDC34 observed in vivo and markedly shifts nuclearly localized CDC34 to the cytoplasm. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | down-regulates activity 
phosphorylation
|
CDC34 |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110383 |
Ser203 |
APAPDEGsDLFYDDY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11546811 |
The ubiquitin-conjugating enzyme, cdc34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(kip1), ikappabalpha, wee1, and myod. We show that mammalian cdc34 is a phosphoprotein that is phosphorylated in proliferating cells. Phosphorylation of cdc34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of cdc34 at ck2-targeted residues, ser-203, ser-222, ser-231, thr-233, and ser-236, abolishes the phosphorylation of cdc34 observed in vivo and markedly shifts nuclearly localized cdc34 to the cytoplasm. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110395 |
Ser222 |
EVEEEADsCFGDDED |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11546811 |
The ubiquitin-conjugating enzyme, cdc34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(kip1), ikappabalpha, wee1, and myod. We show that mammalian cdc34 is a phosphoprotein that is phosphorylated in proliferating cells. Phosphorylation of cdc34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of cdc34 at ck2-targeted residues, ser-203, ser-222, ser-231, thr-233, and ser-236, abolishes the phosphorylation of cdc34 observed in vivo and markedly shifts nuclearly localized cdc34 to the cytoplasm. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110399 |
Ser231 |
FGDDEDDsGTEES |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11546811 |
The ubiquitin-conjugating enzyme, cdc34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(kip1), ikappabalpha, wee1, and myod. We show that mammalian cdc34 is a phosphoprotein that is phosphorylated in proliferating cells. Phosphorylation of cdc34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of cdc34 at ck2-targeted residues, ser-203, ser-222, ser-231, thr-233, and ser-236, abolishes the phosphorylation of cdc34 observed in vivo and markedly shifts nuclearly localized cdc34 to the cytoplasm. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110403 |
Ser236 |
DDSGTEEs |
Homo sapiens |
|
| pmid |
sentence |
| 11546811 |
The ubiquitin-conjugating enzyme, cdc34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(kip1), ikappabalpha, wee1, and myod. We show that mammalian cdc34 is a phosphoprotein that is phosphorylated in proliferating cells. Phosphorylation of cdc34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of cdc34 at ck2-targeted residues, ser-203, ser-222, ser-231, thr-233, and ser-236, abolishes the phosphorylation of cdc34 observed in vivo and markedly shifts nuclearly localized cdc34 to the cytoplasm. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110407 |
Thr233 |
DDEDDSGtEES |
Homo sapiens |
|
| pmid |
sentence |
| 11546811 |
The ubiquitin-conjugating enzyme, cdc34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(kip1), ikappabalpha, wee1, and myod. We show that mammalian cdc34 is a phosphoprotein that is phosphorylated in proliferating cells. Phosphorylation of cdc34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of cdc34 at ck2-targeted residues, ser-203, ser-222, ser-231, thr-233, and ser-236, abolishes the phosphorylation of cdc34 observed in vivo and markedly shifts nuclearly localized cdc34 to the cytoplasm. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates quantity by destabilization
phosphorylation
|
CDC34 |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277330 |
Thr162 |
KGKDREYtDIIRKQV |
in vitro |
|
| pmid |
sentence |
| 27786305 |
RSK1 phosphorylated Thr162 on UBE2R1.RSK1 induced self-ubiquitination and destabilisation of UBE2R1 by phosphorylation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
RNF7 | down-regulates activity
polyubiquitination
|
CDC34 |
0.737 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271443 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10851089 |
SAG was found to be the second family member of Rbx (RING box protein) or ROC (Regulator of cullins) or Hrt that is a component of SCF E3 ubiquitin ligase. Indeed, like ROC1/Rbx1/Hrt1, SAG binds to Cul1 and SAG-Cul1 complex has ubiquitin ligase activity to promote poly-ubiquitination of E2/Cdc34. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC34 | up-regulates activity 
binding
|
SCF-betaTRCP |
0.766 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277331 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25425648 |
The ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase SCF are capable of building polyubiquitin chains onto protein substrates both rapidly and processively; this may be explained at least in part by the atypically fast rate of Cdc34 and SCF association.Here, we use protein cross-linking to demonstrate that the Cdc34-SCF interaction occurs in multiple conformations, where several residues from the Cdc34 acidic tail are capable of contacting a broad region of the SCF basic canyon. Similar patterns of cross-linking are also observed between Cdc34 and the Cul1 paralog Cul2, implicating the same mechanism for the Cdc34-SCF interaction in other members of the cullin-RING ubiquitin ligases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC34 | up-regulates activity
binding
|
SCF-FBW7 |
0.796 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277333 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25425648 |
The ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase SCF are capable of building polyubiquitin chains onto protein substrates both rapidly and processively; this may be explained at least in part by the atypically fast rate of Cdc34 and SCF association.Here, we use protein cross-linking to demonstrate that the Cdc34-SCF interaction occurs in multiple conformations, where several residues from the Cdc34 acidic tail are capable of contacting a broad region of the SCF basic canyon. Similar patterns of cross-linking are also observed between Cdc34 and the Cul1 paralog Cul2, implicating the same mechanism for the Cdc34-SCF interaction in other members of the cullin-RING ubiquitin ligases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC34 | up-regulates activity
binding
|
SCF-SKP2 |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277334 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25425648 |
The ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase SCF are capable of building polyubiquitin chains onto protein substrates both rapidly and processively; this may be explained at least in part by the atypically fast rate of Cdc34 and SCF association.Here, we use protein cross-linking to demonstrate that the Cdc34-SCF interaction occurs in multiple conformations, where several residues from the Cdc34 acidic tail are capable of contacting a broad region of the SCF basic canyon. Similar patterns of cross-linking are also observed between Cdc34 and the Cul1 paralog Cul2, implicating the same mechanism for the Cdc34-SCF interaction in other members of the cullin-RING ubiquitin ligases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC34 | up-regulates activity
binding
|
SCF-FBW2 |
0.707 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277332 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25425648 |
The ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase SCF are capable of building polyubiquitin chains onto protein substrates both rapidly and processively; this may be explained at least in part by the atypically fast rate of Cdc34 and SCF association.Here, we use protein cross-linking to demonstrate that the Cdc34-SCF interaction occurs in multiple conformations, where several residues from the Cdc34 acidic tail are capable of contacting a broad region of the SCF basic canyon. Similar patterns of cross-linking are also observed between Cdc34 and the Cul1 paralog Cul2, implicating the same mechanism for the Cdc34-SCF interaction in other members of the cullin-RING ubiquitin ligases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDC34
- 
- 