Molecular Target Synopsis
Overview
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Druggability
Chemistry
Ligand Efficiency Plot
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cid1 (O13833) - Overview - Molecular Target Synopsis

Protein


cid1, Terminal uridylyltransferase cid1
Enzyme Classification 2.7.7.19
UniProt O13833

Also Known as CID1_SCHPO, cid1

Cytoplasmic uridylyltransferase that mediates the terminal uridylation of mRNAs with short poly(A) tails such as such as act1, hcn1 and urg1 mRNAs, hence facilitating global mRNA decay (PubMed:17353264, PubMed:17449726, PubMed:19430462, PubMed:22751018, PubMed:22885303). Uridylates the 3' ends of actin mRNAs upon S-phase arrest (PubMed:17353264). Has also a weak poly(A) polymerase (PAP) activity (PubMed:22751018, PubMed:22885303). Residue His-336 is responsible for the specificity for UTP (PubMed:22751018, PubMed:22885303). Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis (PubMed:10757807).

4UD5
STRUCTURAL PLASTICITY OF CID1 PROVIDES A BASIS FOR ITS RNA TERMINAL URIDYLYL TRANSFERASE ACTIVITY
RCSB/PDB
Inspect Structure
See all 3D Structures for cid1

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform
405O13833-1

Sub-cellular localization


UniProt: cid1 is active in the following subcellular-locations: cytoplasm.
GO terms: cid1 is active in the following subcellular-locations: cytoplasm, cytosol.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project cid1 has gain in 0 cell-lines, loss in 0 cell-lines and no signal in 0 cell-lines. (see details)

3D Structures


For cid1 there are:
15 structures (27 chains) solved
9 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis