Reversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function
Ontology highlight
ABSTRACT:
ORGANISM(S): Homo Sapiens
SUBMITTER: 
Ping Xu
PROVIDER: PXD016643 | iProX | Sun Dec 08 00:00:00 GMT 2019
REPOSITORIES: iProX
Publications
Reversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function.
Liu Xiaoyan X Xiao Weidi W Zhang Yanan Y Wiley Sandra E SE Zuo Tao T Zheng Yingying Y Chen Natalie N Chen Lu L Wang Xiaorong X Zheng Yawen Y Huang Lan L Lin Shixian S Murphy Anne N AN Dixon Jack E JE Xu Ping P Guo Xing X
Proceedings of the National Academy of Sciences of the United States of America 20191216 1
The fundamental importance of the 26S proteasome in health and disease suggests that its function must be finely controlled, and yet our knowledge about proteasome regulation remains limited. Posttranslational modifications, especially phosphorylation, of proteasome subunits have been shown to impact proteasome function through different mechanisms, although the vast majority of proteasome phosphorylation events have not been studied. Here, we have characterized 1 of the most frequently detected ...[more]
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PLoS One. 2008 Feb 6;3(2):e1555.
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In accordance with the authors due to typos in the original publication some initial conditions and parameters were slightly changed in the model:
article
model
[O-Mad2]
1.5e-7 M
1.3e-7 M
[BubR1:Bub3]
1.30e-7 M
1.27e-7 M
k -4
0.01 M -1
s -1
0.02 M -1
s -1
k -5
0.1 M -1
s -1
0.2 M -1
s -1
This model is hosted on BioModels Database
and identified by: MODEL6655578762
.
To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models
.
To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication
for more information.
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Ibrahim B, Diekmann S, Schmitt E, Dittrich P
PLoS One. 2008 Feb 6;3(2):e1555.
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article
model
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s -1
k -5
0.1 M -1
s -1
0.2 M -1
s -1
This model is hosted on BioModels Database
and identified by: MODEL6655615431
.
To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models
.
To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication
for more information.
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