DCP1A

mRNA-decapping enzyme 1A is a protein that in humans is encoded by the DCP1A gene.[5]

DCP1A
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDCP1A, HSA275986, Nbla00360, SMAD4IP1, SMIF, decapping mRNA 1A
External IDsOMIM: 607010 MGI: 1923151 HomoloGene: 10178 GeneCards: DCP1A
Gene location (Human)
Chr.Chromosome 3 (human)[1]
Band3p21.1Start53,283,429 bp[1]
End53,347,586 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

55802

75901

Ensembl

ENSG00000272886

ENSMUSG00000021962

UniProt

Q9NPI6

Q91YD3

RefSeq (mRNA)

NM_018403
NM_001290204
NM_001290205
NM_001290206
NM_001290207

NM_133761

RefSeq (protein)

NP_001277133
NP_001277134
NP_001277135
NP_001277136
NP_060873

NP_598522

Location (UCSC)Chr 3: 53.28 – 53.35 MbChr 14: 30.48 – 30.53 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Decapping is a key step in general and regulated mRNA decay. The protein encoded by this gene is a decapping enzyme. This protein and another decapping enzyme form a decapping complex, which interacts with the nonsense-mediated decay factor hUpf1 and may be recruited to mRNAs containing premature termination codons. This protein also participates in the TGF-beta signaling pathway.[5]

Interactions

DCP1A has been shown to interact with DCP2[6] and UPF1.[6] It has also been shown to colocalize with GW182, and other markers of P-body.[7] Human DCP1A is heterotrimeric,[8] and makes contacts with the scaffold EDC3/4.[9]

References

  1. GRCh38: Ensembl release 89: ENSG00000272886 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000021962 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: DCP1A DCP1 decapping enzyme homolog A (S. cerevisiae)".
  6. Lykke-Andersen J (December 2002). "Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay". Molecular and Cellular Biology. 22 (23): 8114–21. doi:10.1128/MCB.22.23.8114-8121.2002. PMC 134073. PMID 12417715.
  7. Eystathioy T, Jakymiw A, Chan EK, Séraphin B, Cougot N, Fritzler MJ (October 2003). "The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies". RNA. 9 (10): 1171–3. doi:10.1261/rna.5810203. PMC 1370480. PMID 13130130.
  8. Tritschler F, Braun JE, Motz C, Igreja C, Haas G, Truffault V, Izaurralde E, Weichenrieder O (December 2009). "DCP1 forms asymmetric trimers to assemble into active mRNA decapping complexes in metazoa". Proceedings of the National Academy of Sciences of the United States of America. 106 (51): 21591–6. Bibcode:2009PNAS..10621591T. doi:10.1073/pnas.0909871106. PMC 2789166. PMID 19966221.
  9. Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O (December 2007). "A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting". Molecular and Cellular Biology. 27 (24): 8600–11. doi:10.1128/MCB.01506-07. PMC 2169425. PMID 17923697.

Further reading

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