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PMID: 11165500 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta.

Trends in biochemical sciences ·Vol. 26 ·No. 1 ·2001-01-00 ·Pages 7-9

Clissold PM, Ponting CP

Abstract

On the basis of significant sequence similarity, we have identified JmjC domains in more than 100 eukaryotic and bacterial sequences. These include human hairless, mutated in individuals with alopecia universalis, retinoblastoma-binding protein 2 and several putative chromatin-associated proteins. JmjC domains are predicted to be metalloenzymes that adopt the cupin fold, and are candidates for enzymes that regulate chromatin remodelling.

MeSH Terms
Amino Acid Motifs Amino Acid Sequence Animals Binding Sites Carrier Proteins/chemistry,metabolism Chromatin/metabolism DNA/metabolism Evolution, Molecular Group IV Phospholipases A2 Humans Intracellular Signaling Peptides and Proteins Molecular Sequence Data Nerve Tissue Proteins/chemistry,metabolism Phospholipases A/chemistry,metabolism Polycomb Repressive Complex 2 Protein Structure, Tertiary Proteins/chemistry,metabolism Retinoblastoma-Binding Protein 2 Transcription Factors Tumor Suppressor Proteins
Chemicals
Carrier Proteins Chromatin HR protein, human Intracellular Signaling Peptides and Proteins Jarid2 protein, mouse Nerve Tissue Proteins Proteins Transcription Factors Tumor Suppressor Proteins DNA KDM5A protein, human Retinoblastoma-Binding Protein 2 Polycomb Repressive Complex 2 Phospholipases A Group IV Phospholipases A2
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Clissold P M
MRC Functional Genetics Unit, Department of Human Anatomy and Genetics, University of Oxford, South Parks Road, OX1 3QX, Oxford, UK.
Ponting C P
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
2001-01-00
Pages
7-9
Language
English
Region
England
NLM ID
7610674
Subset
IM
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