DCP1A

From Wikipedia, the free encyclopedia

DCP1 decapping enzyme homolog A (S. cerevisiae)

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2WX3, 4B6H

Identifiers

Symbols

DCP1A; HSA275986; Nbla00360; SMAD4IP1; SMIF

External IDs

OMIM: 607010 MGI: 1923151 HomoloGene: 10178 GeneCards: DCP1A Gene

Gene Ontology
Molecular function	• protein binding • hydrolase activity • identical protein binding
Cellular component	• cytoplasmic mRNA processing body • nucleus • cytosol
Biological process	• nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay • gene expression • RNA metabolic process • mRNA metabolic process • exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
53.3 – 53.36 Mb

Chr 14:
30.48 – 30.53 Mb

PubMed search

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

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.^[1]

Interactions

DCP1A has been shown to interact with DCP2^[2] and UPF1.^[2]

References

↑ 1.0 1.1 "Entrez Gene: DCP1A DCP1 decapping enzyme homolog A (S. cerevisiae)".
↑ 2.0 2.1 Lykke-Andersen, Jens (Dec 2002). "Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay". Mol. Cell. Biol. (United States) 22 (23): 8114–21. doi:10.1128/MCB.22.23.8114-8121.2002. ISSN 0270-7306. PMC 134073. PMID 12417715.

Bai RY, Koester C, Ouyang T, et al. (2002). "SMIF, a Smad4-interacting protein that functions as a co-activator in TGFbeta signalling.". Nat. Cell Biol. 4 (3): 181–90. doi:10.1038/ncb753. PMID 11836524.
Callebaut I (2002). "An EVH1/WH1 domain as a key actor in TGFbeta signalling.". FEBS Lett. 519 (1-3): 178–80. doi:10.1016/S0014-5793(02)02751-5. PMID 12023040.
Lykke-Andersen J (2003). "Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay.". Mol. Cell. Biol. 22 (23): 8114–21. doi:10.1128/MCB.22.23.8114-8121.2002. PMC 134073. PMID 12417715.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ingelfinger D, Arndt-Jovin DJ, Lührmann R, Achsel T (2003). "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci.". RNA 8 (12): 1489–501. PMC 1370355. PMID 12515382.
Leonard D, Ajuh P, Lamond AI, Legerski RJ (2003). "hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing.". Biochem. Biophys. Res. Commun. 308 (4): 793–801. doi:10.1016/S0006-291X(03)01486-4. PMID 12927788.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Liu J, Valencia-Sanchez MA, Hannon GJ, Parker R (2005). "MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies.". Nat. Cell Biol. 7 (7): 719–23. doi:10.1038/ncb1274. PMC 1855297. PMID 15937477.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Fenger-Grøn M, Fillman C, Norrild B, Lykke-Andersen J (2006). "Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping.". Mol. Cell 20 (6): 905–15. doi:10.1016/j.molcel.2005.10.031. PMID 16364915.
Olsen JV, Blagoev B, Gnad F, et al. (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.

v t e Post-transcriptional modification

Nuclear	Precursor mRNA 5′ cap formation Polyadenylation CPSF CstF PAP PAB2 CFI CFII Poly(A)-binding protein RNA splicing: intron/exon snRNP spliceosome minor spliceosome U1 alternative splicing pre-mRNA processing factor PLRG1 PRPF3 PRPF4 PRPF4B PRPF6 PRPF8 PRPF18 PRPF19 PRPF31 PRPF38A PRPF38B PRPF39 PRPF40A PRPF40B RNA editing Polyuridylation

Cytosolic	5′ cap methylation Messenger RNA decapping: DCP1A DCP1B DCP2 DCPS EDC3 EDC4

see also: disorders of transcription and post transcriptional modification, Transcription B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

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DCP1A

Interactions

References

Further reading