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Journal article

Biochemical and structural investigations clarify the substrate selectivity of the 2-oxoglutarate oxygenase JMJD6.

Abstract:

JmjC domain-containing protein 6 (JMJD6) is a 2-oxoglutarate (2OG)-dependent oxygenase linked to various cellular processes, including splicing regulation, histone modification, transcriptional pause release, hypoxia sensing, and cancer. JMJD6 is reported to catalyze hydroxylation of lysine residue(s) of histones, the tumor-suppressor protein p53, and splicing regulatory proteins, including u2 small nuclear ribonucleoprotein auxiliary factor 65-kDa subunit (U2AF65). JMJD6 is also reported to ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1074/jbc.RA119.008693

Authors


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Role:
Author
ORCID:
0000-0001-9842-0676
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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
ORCID:
0000-0003-4664-6942
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
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Publisher:
American Society for Biochemistry and Molecular Biology Publisher's website
Journal:
Journal of Biological Chemistry Journal website
Volume:
294
Issue:
30
Pages:
11637-11652
Publication date:
2019-07-26
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Pmid:
31147442
Source identifiers:
1007748

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