+ |
VCP | down-regulates quantity by destabilization
ubiquitination
|
DDX58 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261000 |
Lys181 |
ALEKERNkFSELWIV |
Homo sapiens |
|
pmid |
sentence |
26471729 |
Here, we report a new role for p97 with Npl4-Ufd1 as its cofactor in reducing antiviral innate immune responses by facilitating proteasomal degradation of RIG-I. The p97 complex is able to directly bind both non-ubiquitinated RIG-I and the E3 ligase RNF125, promoting K48-linked ubiquitination of RIG-I at residue K181. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
METTL21C | up-regulates activity
methylation
|
VCP |
0.314 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255918 |
Lys315 |
AIAPKREkTHGEVER |
Mus musculus |
Skeletal Muscle Fiber |
pmid |
sentence |
29719249 |
We reveal that METTL21C trimethylates p97 on the Lys315 residue and found that loss of this modification reduced p97 hexamer formation and ATPase activity in vivo. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
AKT | up-regulates
phosphorylation
|
VCP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145284 |
Ser352 |
AATNRPNsIDPALRR |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
16551632 |
Site-directed mutagenesis identified ser-351, ser-745, and ser-747 as akt phosphorylation sites on vcp. however, our study also suggests that other known biological activities of vcp, such as those related to intracellular trafficking, ubiquitin-mediated proteolysis, and activation of transcription (28), might be regulated by akt through the activation of vcp. I |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145288 |
Ser746 |
AMRFARRsVSDNDIR |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
16551632 |
Site-directed mutagenesis identified ser-351, ser-745, and ser-747 as akt phosphorylation sites on vcp. however, our study also suggests that other known biological activities of vcp, such as those related to intracellular trafficking, ubiquitin-mediated proteolysis, and activation of transcription (28), might be regulated by akt through the activation of vcp. I |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145292 |
Ser748 |
RFARRSVsDNDIRKY |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
16551632 |
Site-directed mutagenesis identified ser-351, ser-745, and ser-747 as akt phosphorylation sites on vcp. however, our study also suggests that other known biological activities of vcp, such as those related to intracellular trafficking, ubiquitin-mediated proteolysis, and activation of transcription (28), might be regulated by akt through the activation of vcp. I |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
AKT1 | up-regulates
phosphorylation
|
VCP |
0.523 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252491 |
Ser352 |
AATNRPNsIDPALRR |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
16551632 |
Site-directed mutagenesis identified ser-351, ser-745, and ser-747 as akt phosphorylation sites on vcp. however, our study also suggests that other known biological activities of vcp, such as those related to intracellular trafficking, ubiquitin-mediated proteolysis, and activation of transcription (28), might be regulated by akt through the activation of vcp. I |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252492 |
Ser746 |
AMRFARRsVSDNDIR |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
16551632 |
Site-directed mutagenesis identified ser-351, ser-745, and ser-747 as akt phosphorylation sites on vcp. however, our study also suggests that other known biological activities of vcp, such as those related to intracellular trafficking, ubiquitin-mediated proteolysis, and activation of transcription (28), might be regulated by akt through the activation of vcp. I |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252493 |
Ser748 |
RFARRSVsDNDIRKY |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
16551632 |
Site-directed mutagenesis identified ser-351, ser-745, and ser-747 as akt phosphorylation sites on vcp. however, our study also suggests that other known biological activities of vcp, such as those related to intracellular trafficking, ubiquitin-mediated proteolysis, and activation of transcription (28), might be regulated by akt through the activation of vcp. I |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PTPN3 | down-regulates activity
dephosphorylation
|
VCP |
0.491 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248460 |
Tyr796 |
GGTGGSVyTEDNDDD |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10364224 |
Identification of VCP as a substrate of PTPH1in vivo.|The tyrosines (Tyr796 and Tyr805) at the C terminus of VCP have been reported to be the major sites of phosphorylation, with Tyr805 accounting for more than 90% of the tyrosine phosphorylation on the protein |The Y796F/Y805F VCP mutant was not associated with any of the PTPH1 constructs. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248461 |
Tyr805 |
EDNDDDLyG |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10364224 |
Identification of VCP as a substrate of PTPH1in vivo.|The tyrosines (Tyr796 and Tyr805) at the C terminus of VCP have been reported to be the major sites of phosphorylation, with Tyr805 accounting for more than 90% of the tyrosine phosphorylation on the protein |The Y796F/Y805F VCP mutant was not associated with any of the PTPH1 constructs. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
VCP | up-regulates activity
binding
|
DERL1 |
0.879 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261372 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
15215856 |
VIMP mediates p97 binding to hDerlin-1. these data suggest that Derlin-1 and VIMP form a membrane protein complex that serves as a receptor for p97. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
2-(2H-Benzo[b][1,4]oxazin-4(3H)-yl)-N-benzyl-5,6,7,8-tetrahydroquinazolin-4-amine | down-regulates activity
chemical inhibition
|
VCP |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261093 |
|
|
in vitro |
|
pmid |
sentence |
23316025 |
Inhibition of p97 by ML240 and ML241 is ATP competitive. To determine the mechanism by which ML240 and ML241 inhibited p97 ATPase, we evaluated rates of ATP hydrolysis at different concentrations of ATP. ML240 and ML241 inhibited p97competitively with respect to ATP with a Kivalues of 0.22 mm and 0.35 mm respectively. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
SELENOS | up-regulates activity
binding
|
VCP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261371 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
15215856 |
VIMP mediates p97 binding to hDerlin-1. these data suggest that Derlin-1 and VIMP form a membrane protein complex that serves as a receptor for p97. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
N2,N4-Dibenzylquinazoline-2,4-diamine | down-regulates activity
chemical inhibition
|
VCP |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261100 |
|
|
in vitro |
|
pmid |
sentence |
21383145 |
DBeQ (1) is a reversible and selective inhibitor of p97 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
VCP | up-regulates activity
binding
|
UFD1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252424 |
|
|
Homo sapiens |
|
pmid |
sentence |
20442859 |
These findings ascribe specific functions to each of the components of the VCP-UFD1L-NPL4 complex in Vpu-mediated CD4 degradation: VCP energizes the process through ATP binding and hydrolysis, UFD1L binds ubiquitinated CD4 through recognition of K48 Ub chains, and NPL4 stabilizes UFD1L. VCP is thus likely to provide the energy required for extraction of CD4 from membranes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VCP | up-regulates activity
binding
|
NGLY1 |
0.683 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261058 |
|
|
Homo sapiens |
|
pmid |
sentence |
15362974 |
PNGase is directed to polyubiquitinated MGPs via VCP and the adaptor protein SAKS1, allowing PNGase to deglycosylate MGPs, which can then be degraded by the proteasome. PNGase itself is reported to bind to the S4 component of the 19 S proteasome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VCPIP1 | up-regulates activity
binding
|
VCP |
0.568 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265039 |
|
|
|
|
pmid |
sentence |
23500464 |
Golgi biogenesis requires two distinct p97ATPase-mediated membrane fusion, the p97/p47 and p97/p37 pathways. |We clarified that VCIP135, an essential factor in both p97 membrane fusion pathways, is phosphorylated on Threonine-760 and Serine-767 by Cdc2 at mitosis and that this phosphorylated VCIP135 does not bind to p97. |
|
Publications: |
1 |
+ |
VCP | up-regulates activity
binding
|
NPLOC4 |
0.945 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252423 |
|
|
Homo sapiens |
|
pmid |
sentence |
20442859 |
These findings ascribe specific functions to each of the components of the VCP-UFD1L-NPL4 complex in Vpu-mediated CD4 degradation: VCP energizes the process through ATP binding and hydrolysis, UFD1L binds ubiquitinated CD4 through recognition of K48 Ub chains, and NPL4 stabilizes UFD1L. VCP is thus likely to provide the energy required for extraction of CD4 from membranes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VCP | down-regulates activity
binding
|
AURKA |
0.319 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265044 |
|
|
Caenorhabditis elegans |
|
pmid |
sentence |
23649807 |
The UBXN-2/p37/p47 adaptors of CDC-48/p97 regulate mitosis by limiting the centrosomal recruitment of Aurora A.|We found that UBXN-2 and CDC-48 coimmunoprecipitated with AIR-1 from embryonic extracts |
|
Publications: |
1 |
Organism: |
Caenorhabditis Elegans |
+ |
ELF2 | up-regulates quantity by expression
transcriptional regulation
|
VCP |
0.369 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254283 |
|
|
Homo sapiens |
MCF-7 Cell |
pmid |
sentence |
18544453 |
These findings indicate that ELF2 transactivates VCP promoter through binding to two motifs, with a predominant contribution of the upstream one. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ML240 | down-regulates activity
chemical inhibition
|
VCP |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261066 |
|
|
in vitro |
|
pmid |
sentence |
23316025 |
Inhibition of p97 by ML240 and ML241 is ATP competitive. To determine the mechanism by which ML240 and ML241 inhibited p97 ATPase, we evaluated rates of ATP hydrolysis at different concentrations of ATP. ML240 and ML241 inhibited p97competitively with respect to ATP with a Kivalues of 0.22 mm and 0.35 mm respectively. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CB-5083 | down-regulates activity
chemical inhibition
|
VCP |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260189 |
|
|
in vitro |
|
pmid |
sentence |
26565666 |
Herein we describe our lead optimization efforts focused on in vitro potency, ADME, and pharmaceutical properties that led to the discovery of a potent, ATP-competitive, D2-selective, and orally bioavailable p97 inhibitor 71, CB-5083. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
UBXN8 | down-regulates quantity
relocalization
|
VCP |
0.535 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261002 |
|
|
Homo sapiens |
|
pmid |
sentence |
21949850 |
The human protein named Rep8 or Ubxd6 as a new cofactor of p97. Rep8 tethers p97 to the ER membrane for efficient ER-associated degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPRO | down-regulates activity
dephosphorylation
|
VCP |
0.433 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277063 |
|
|
Homo sapiens |
|
pmid |
sentence |
23533167 |
An important aspect of this study is that tyrosine dephosphorylation of VCP by PTPRO sensitizes HepG2 cells to Doxorubicin, a chemotherapeutic drug commonly used for a variety of cancers. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VCP | form complex
binding
|
RQC complex |
0.595 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277695 |
|
|
|
|
pmid |
sentence |
28528489 |
The ribosome-bound quality control (RQC) complex is a multi-protein complex conserved throughout eukaryotes and composed of the E3 ubiquitin ligase Ltn1/Listerin, the ATPase Cdc48/p97 with its co-factors Ufd1/UFD1L and Npl4/NPLOC4, as well as the factors Rqc1/TCF25 and Rqc2/NEMF (Fig. 1). |
|
Publications: |
1 |