| + |
PRKCZ | down-regulates activity 
phosphorylation
|
HABP4 |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249251 |
Thr354 |
RKPANDItSQLEINF |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249257 |
Thr375 |
GRGARGGtRGGRGRI |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCG | down-regulates activity
phosphorylation
|
HABP4 |
0.295 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249249 |
Thr354 |
RKPANDItSQLEINF |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249255 |
Thr375 |
GRGARGGtRGGRGRI |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates activity
phosphorylation
|
HABP4 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249246 |
Thr354 |
RKPANDItSQLEINF |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249252 |
Thr375 |
GRGARGGtRGGRGRI |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCD | down-regulates activity
phosphorylation
|
HABP4 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249248 |
Thr354 |
RKPANDItSQLEINF |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249254 |
Thr375 |
GRGARGGtRGGRGRI |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCB | down-regulates activity
phosphorylation
|
HABP4 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249247 |
Thr354 |
RKPANDItSQLEINF |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249253 |
Thr375 |
GRGARGGtRGGRGRI |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | down-regulates activity
phosphorylation
|
HABP4 |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249250 |
Thr354 |
RKPANDItSQLEINF |
Homo sapiens |
|
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249256 |
Thr375 |
GRGARGGtRGGRGRI |
Homo sapiens |
|
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
HABP4 | down-regulates activity
binding
|
MEF2C |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238283 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 15862299 |
MEF2C DNA-binding activity is inhibited through its interaction with the regulatory protein Ki-1/57. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
3.0
HABP4
- 
- 