<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Lee HT</submitter><funding>National Research Foundation of Korea</funding><pagination>3418</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8304009</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13(14)</volume><pubmed_abstract>2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1 (OGFOD1) expression is upregulated in a variety of cancers and has been related to poor prognosis. However, despite this significance to cancer progression, the precise oncogenic mechanism of OGFOD1 is not understood. We demonstrated that OGFOD1 plays a role in enhancing the transcriptional activity of RNA polymerase II in breast cancer cells. OGFOD1 directly binds to the C-terminal domain of RNA polymerase II to alter phosphorylation status. The elimination of OGFOD1 resulted in decreased tumor development. Additionally, cell cycle-dependent kinase 7 and cell cycle-dependent kinase 9, critical enzymes for activating RNA polymerase II, phosphorylated serine 256 of OGFOD1, whereas a non-phosphorylated mutant OGFOD1 fail</pubmed_abstract><journal>Cancers</journal><pubmed_title>Phosphorylation of OGFOD1 by Cell Cycle-Dependent Kinase 7/9 Enhances the Transcriptional Activity of RNA Polymerase II in Breast Cancer Cells.</pubmed_title><pmcid>PMC8304009</pmcid><funding_grant_id>2012R1A3A2048767</funding_grant_id><funding_grant_id>2021R1A2C3006559</funding_grant_id><pubmed_authors>Kang BG</pubmed_authors><pubmed_authors>Lee S</pubmed_authors><pubmed_authors>Suh MY</pubmed_authors><pubmed_authors>Lee SE</pubmed_authors><pubmed_authors>Choi J</pubmed_authors><pubmed_authors>Lee HT</pubmed_authors><pubmed_authors>Lee BI</pubmed_authors><pubmed_authors>Roe JS</pubmed_authors><pubmed_authors>Hwang IY</pubmed_authors><pubmed_authors>Kim JH</pubmed_authors><pubmed_authors>Cho EJ</pubmed_authors><pubmed_authors>Youn HD</pubmed_authors><pubmed_authors>Lee IH</pubmed_authors><pubmed_authors>Cha SS</pubmed_authors><pubmed_authors>Kwak S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Phosphorylation of OGFOD1 by Cell Cycle-Dependent Kinase 7/9 Enhances the Transcriptional Activity of RNA Polymerase II in Breast Cancer Cells.</name><description>2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1 (OGFOD1) expression is upregulated in a variety of cancers and has been related to poor prognosis. However, despite this significance to cancer progression, the precise oncogenic mechanism of OGFOD1 is not understood. We demonstrated that OGFOD1 plays a role in enhancing the transcriptional activity of RNA polymerase II in breast cancer cells. OGFOD1 directly binds to the C-terminal domain of RNA polymerase II to alter phosphorylation status. The elimination of OGFOD1 resulted in decreased tumor development. Additionally, cell cycle-dependent kinase 7 and cell cycle-dependent kinase 9, critical enzymes for activating RNA polymerase II, phosphorylated serine 256 of OGFOD1, whereas a non-phosphorylated mutant OGFOD1 fail</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Jul</publication><modification>2026-04-08T06:55:29.05Z</modification><creation>2022-02-11T00:12:21.862Z</creation></dates><accession>S-EPMC8304009</accession><cross_references><pubmed>34298635</pubmed><doi>10.3390/cancers13143418</doi></cross_references></HashMap>