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Systematic name YNL118C
Gene name DCP2
Aliases PSU1
Feature type ORF, Verified
Coordinates Chr XIV:405564..402652
Primary SGDID S000005062

Description of YNL118C: Catalytic subunit of the Dcp1p-Dcp2p decapping enzyme complex, which removes the 5' cap structure from mRNAs prior to their degradation; member of the Nudix hydrolase family[1][2][3]


Community Commentary

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DNA and RNA Details

RNA Degradation

Yeast Dcp2 is catalitically active to cleave the cap structure of mRNAs [4] [5]


Two Hybrid

Two Hybrid interaction with NAM7
Yeast Two-Hybrid screen with Upf1p as bait identified several interacting proteins [6] [7]

Protein Details

Nucleic Acid Binding

YNL118C binds RNA Interacts with substrate mRNA to cleave cap structure but not with free cap. [4] [5]

Other Protein Details

Other Topic: Motif

Contains a MUT T/NUDIX motif as well as other specific conserved regions [4] [5]

Techniques and Reagents

Protein Purification

Recombinant protein (truncated) [4] [5]



See Help:References on how to add references

  1. Dunckley T, et al. (2001) Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae. Genetics 157(1):27-37 SGD PMID 11139489
  2. Gaudon C, et al. (1999) Role of the essential yeast protein PSU1 in p6anscriptional enhancement by the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J 18(8):2229-40 SGD PMID 10205176
  3. She M, et al. (2006) Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe. Nat Struct Mol Biol 13(1):63-70 SGD PMID 16341225
  4. 4.0 4.1 4.2 4.3 van Dijk E, et al. (2002) Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J 21(24):6915-24 SGD PMID 12486012
  5. 5.0 5.1 5.2 5.3 submitted by Bertrand Seraphin on 2003-09-03
  6. He F and Jacobson A (1995) Identification of a novel component of the nonsense-mediated mRNA decay pathway by use of an interacting protein screen. Genes Dev 9(4):437-54 SGD PMID 7883168
  7. submitted by Jurgen Wittmann on 2003-04-30

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