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IPR009349

Description

IPR009349 is a TRIP4/RQT4, C2HC5-type zinc finger.

<p>This entry represents a C2HC5-type zinc finger found in human activating signal cointegrator 1 (ASC-1, also known as TRIP4) and its orthologue from yeast RQC trigger complex subunit RQT4 which function as part of the RQC trigger (RQT) complex that activates the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation [[cite:PUB00151150], [cite:PUB00151151], [cite:PUB00151152]]. TRIP4 has also been described as a transcription coactivator which associates with nuclear receptors and transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription [[cite:PUB00071531], [cite:PUB00088961]].</p> <p>Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [[cite:PUB00035807], [cite:PUB00035805], [cite:PUB00035806], [cite:PUB00035804], [cite:PUB00014077]]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [[cite:PUB00035812]]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Cellular component Nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
Biological process Regulation of transcription, DNA-templated Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
Molecular function Zinc ion binding Interacting selectively and non-covalently with zinc (Zn) ions.

Associated Lotus transcripts 2

Transcript Name Description Predicted domains Domain count
PREDICTED: activating signal cointegrator 1-like [Glycine max] gi|356562832|ref|XP_003549672.1| 6
Activating signal cointegrator 1; TAIR: AT3G47610.1 transcription regulator/ zinc ion binding protein; Swiss-Prot: sp|Q15650|TRIP4_HUMAN Activating signal cointegrator 1; TrEMBL-Plants: tr|V7CDE8|V7CDE8_PHAVU Uncharacterized protein; Found in the gene: LotjaGi4g1v0248600 7

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space:

Predicted domain Source Observations Saturation (%)
mobidb-lite MobiDBLite 1 50.00