DCP1A

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

DCP1A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2WX3, 4B6H
Identifiers
Aliases	DCP1A, HSA275986, Nbla00360, SMAD4IP1, SMIF, decapping mRNA 1A
External IDs	OMIM: 607010 MGI: 1923151 HomoloGene: 10178 GeneCards: DCP1A
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3p21.1 Start 53,283,429 bp[1] End 53,347,586 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14 B|14 18.75 cM Start 30,479,535 bp[2] End 30,527,063 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0010576 enzyme regulator activity • GO:0010577 enzyme activator activity • GO:0001948 protein binding • mRNA binding • hydrolase activity • identical protein binding • kinesin binding Cellular component • cytoplasm • cytosol • membrane • cell nucleus • P-body • cytoplasmic ribonucleoprotein granule Biological process • GO:0048554 positive regulation of catalytic activity • deadenylation-independent decapping of nuclear-transcribed mRNA • protein localization to cytoplasmic stress granule • regulation of mRNA stability • deadenylation-dependent decapping of nuclear-transcribed mRNA • exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
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 Mb	Chr 14: 30.48 – 30.53 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/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

• Bai RY, Koester C, Ouyang T, Hahn SA, Hammerschmidt M, Peschel C, Duyster J (March 2002). "SMIF, a Smad4-interacting protein that functions as a co-activator in TGFbeta signalling". Nature Cell Biology. 4 (3): 181–90. doi:10.1038/ncb753. PMID 11836524.
• Callebaut I (May 2002). "An EVH1/WH1 domain as a key actor in TGFbeta signalling". FEBS Letters. 519 (1–3): 178–80. doi:10.1016/S0014-5793(02)02751-5. PMID 12023040.
• 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.
• Ingelfinger D, Arndt-Jovin DJ, Lührmann R, Achsel T (December 2002). "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci". RNA. 8 (12): 1489–501. doi:10.1017/S1355838202021726 (inactive 2020-01-22). PMC 1370355. PMID 12515382.
• Leonard D, Ajuh P, Lamond AI, Legerski RJ (September 2003). "hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing". Biochemical and Biophysical Research Communications. 308 (4): 793–801. CiteSeerX 10.1.1.539.8359. doi:10.1016/S0006-291X(03)01486-4. PMID 12927788.
• Lehner B, Sanderson CM (July 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Liu J, Valencia-Sanchez MA, Hannon GJ, Parker R (July 2005). "MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies". Nature Cell Biology. 7 (7): 719–23. doi:10.1038/ncb1274. PMC 1855297. PMID 15937477.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
• Fenger-Grøn M, Fillman C, Norrild B, Lykke-Andersen J (December 2005). "Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping". Molecular Cell. 20 (6): 905–15. doi:10.1016/j.molcel.2005.10.031. PMID 16364915.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.