Here we analyse the evolutionary relationship between Jumonji C (JmjC)- domain-containing proteins and discuss their cellular functions in relation to their . Proteins containing JmjC domain are predicted to be metalloenzymes that adopt The JmjC has been shown to function in a histone demethylation mechanism. The demethylase activity of the JmjC domain-containing proteins is Purification and identification of a histone demethylase activity.a, Histone.
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Recommend FPrime to your librarian or information manager to request an extended free trial for all users at your institution. Proteins containing JmjC domain are predicted to be metalloenzymes demethylqtion adopt the cupin fold and are candidates for enzymes that regulate chromatin remodelling [ PMID: JmjC progeins histone demethylation protein 1 EC: PaxDb, a database of protein abundance averages across all three domains of life More References Publications referenced by this paper.
Institutional access Recommend FPrime to your librarian demethylatioon information manager to request an extended free trial for all users at your institution. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.
This family of proteins is broken up into seven distinct subgroups based on domain architecture and their ability to antagonize specific histone methylation marks.
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The cupin fold is a flattened beta-barrel structure containing two sheets of five antiparallel beta strands that form the walls of a zinc-binding cleft.
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Align Add to basket Added to basket This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.
Database of Orthologous Groups More Missing in isoform b. UCSC genome browser More Examples of ‘Non-Financial Competing Interests’ Within the past 4 years, you have held joint grants, published or collaborated with any of the authors of the selected paper.
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JmjC domain (IPR) < InterPro < EMBL-EBI
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JmjC-domain-containing proteins and histone demethylation – Semantic Scholar
Structure of factor-inhibiting hypoxia-inducible factor HIF reveals mechanism of oxidative modification of HIF-1 alpha. This paper has highly influenced 45 other papers.
March 7, Last sequence update: Select the link destinations: Evidence of domain swapping within the jumonji family of transcription factors. JmjC domain-containing histone deme Please consider upgrading your browser. The JmjC has been shown to function in a histone demethylation mechanism that is conserved from yeast to human [ PMID: Demeyhylation disclose any competing interests that might be construed to influence your judgment of the validity or importance of the article, or any recommendation or review.
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Chromatin regulatorDioxygenaseOxidoreductase. Bgee i WBGene Expressed in 5 organ shighest expression level in multi-cellular organism. Certain parts of this website offer the opportunity for users to post opinions, information and material including without limitation academic papers and data ‘Material’ in areas of the website. This is version of the entry and version 2 of the sequence. I would like to receive updates demethyllation further comments, recommendations, or dissenting opinions are publishing on this article.
Your basket is currently empty. The sequence of this isoform differs from the canonical sequence as follows: Priority is given to the annotation of physiological ligands. Additionally, this section gives relevant information on each alternative protein isoform.
Structural insights into histone demethylation by JMJD2 family members.
Histone demethylation by a family of JmjC domain-containing proteins.
In jmjv-domain-containing best studied JmjC-domain proteins, the JmjC barrel has a histone demethylase catalytic activity. Dissecting the biological roles of Kdm 3 b and Kdm 3 a lysine demethylases Ioannis Kasioulis Show all Align All Isoform a identifier: Encyclopedia of Proteome Dynamics More The algorithm is described in the ISO standard.