Journal article
Phosphorylation of <i>Schizosaccharomyces pombe</i> Dss1 mediates direct binding to the ubiquitin‐ligase Dma1 in vitro
- Abstract:
-
Intrinsically disordered proteins (IDPs) are often multifunctional and frequently posttranslationally modified. Deleted in split hand/split foot 1 (Dss1—Sem1 in budding yeast) is a highly multifunctional IDP associated with a range of protein complexes. However, it remains unknown if the different functions relate to different modified states. In this work, we show that Schizosaccharomyces pombe Dss1 is a substrate for casein kinase 2 in vitro, and we identify three phosphorylated threonines ...
Expand abstract
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
-
(Preview, Version of record, pdf, 3.1MB, Terms of use)
-
- Publisher copy:
- 10.1002/pro.4733
Authors
- Publisher:
- Wiley
- Journal:
- Protein Science More from this journal
- Volume:
- 32
- Issue:
- 9
- Pages:
- e4733-e4733
- Publication date:
- 2023-07-18
- DOI:
- EISSN:
-
1469-896X
- ISSN:
-
0961-8368
- Language:
-
English
- Keywords:
- Pubs id:
-
2370906
- Local pid:
-
pubs:2370906
- Source identifiers:
-
W4384627181
- Deposit date:
-
2026-02-13
- ARK identifier:
This ORA record was generated from metadata provided by an external service. It has not been edited by the ORA Team.
Terms of use
- Copyright date:
- 2023
- Licence:
- Other
If you are the owner of this record, you can report an update to it here: Report update to this record