DCP2

Protein found in humans
DCP2
Identifiers
AliasesDCP2, NUDT20, decapping mRNA 2
External IDsOMIM: 609844; MGI: 1917890; HomoloGene: 13968; GeneCards: DCP2; OMA:DCP2 - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for DCP2
Genomic location for DCP2
Band5q22.2Start112,976,702 bp[1]
End113,022,195 bp[1]
Gene location (Mouse)
Chromosome 18 (mouse)
Chr.Chromosome 18 (mouse)[2]
Chromosome 18 (mouse)
Genomic location for DCP2
Genomic location for DCP2
Band18|18 B3Start44,513,569 bp[2]
End44,558,036 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • oocyte

  • secondary oocyte

  • trabecular bone

  • sperm

  • parietal pleura

  • placenta

  • monocyte

  • bone marrow

  • visceral pleura

  • endothelial cell
Top expressed in
  • hand

  • otolith organ

  • utricle

  • primitive streak

  • superior cervical ganglion

  • vas deferens

  • condyle

  • abdominal wall

  • trigeminal ganglion

  • renal corpuscle
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • m7G(5')pppN diphosphatase activity
  • manganese ion binding
  • metal ion binding
  • protein binding
  • exoribonuclease activity, producing 5'-phosphomonoesters
  • RNA binding
  • hydrolase activity
  • 5'-3' exoribonuclease activity
  • telomerase RNA binding
Cellular component
  • cytoplasm
  • RISC complex
  • cytosol
  • P-body
  • nucleoplasm
  • cell junction
  • nucleus
  • cytoplasmic ribonucleoprotein granule
Biological process
  • mRNA catabolic process
  • regulation of mRNA stability
  • deadenylation-dependent decapping of nuclear-transcribed mRNA
  • exonucleolytic catabolism of deadenylated mRNA
  • histone mRNA catabolic process
  • RNA phosphodiester bond hydrolysis, exonucleolytic
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
  • negative regulation of telomere maintenance via telomerase
  • regulation of telomerase RNA localization to Cajal body
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

167227

70640

Ensembl

ENSG00000172795

ENSMUSG00000024472

UniProt

Q8IU60

Q9CYC6

RefSeq (mRNA)

NM_001242377
NM_152624

NM_027490

RefSeq (protein)

NP_001229306
NP_689837

NP_081766

Location (UCSC)Chr 5: 112.98 – 113.02 MbChr 18: 44.51 – 44.56 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

mRNA-decapping enzyme 2 is a protein that in humans is encoded by the DCP2 gene.[5][6][7]

DCP2 is a key component of an mRNA-decapping complex required for removal of the 5-prime cap from mRNA prior to its degradation from the 5-prime end (Fenger-Gron et al., 2005).[supplied by OMIM][7]

Interactions

DCP2 has been shown to interact with DCP1A[8] and UPF1.[6][9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172795 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024472 – 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. ^ Wang Z, Jiao X, Carr-Schmid A, Kiledjian M (October 2002). "The hDcp2 protein is a mammalian mRNA decapping enzyme". Proceedings of the National Academy of Sciences of the United States of America. 99 (20): 12663–12668. Bibcode:2002PNAS...9912663W. doi:10.1073/pnas.192445599. PMC 130517. PMID 12218187.
  6. ^ a b 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): 8114–8121. doi:10.1128/MCB.22.23.8114-8121.2002. PMC 134073. PMID 12417715.
  7. ^ a b "Entrez Gene: DCP2 DCP2 decapping enzyme homolog (S. cerevisiae)".
  8. ^ 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): 8114–8121. doi:10.1128/MCB.22.23.8114-8121.2002. PMC 134073. PMID 12417715.
  9. ^ Lejeune F, Li X, Maquat LE (September 2003). "Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities". Molecular Cell. 12 (3): 675–687. doi:10.1016/S1097-2765(03)00349-6. PMID 14527413.

Further reading

  • Ueno K, Kumagai T, Kijima T, Kishimoto T, Hosoe S (January 1998). "Cloning and tissue expression of cDNAs from chromosome 5q21-22 which is frequently deleted in advanced lung cancer". Human Genetics. 102 (1): 63–68. doi:10.1007/s004390050655. PMID 9490301. S2CID 36201527.
  • van Dijk E, Cougot N, Meyer S, Babajko S, Wahle E, Séraphin B (December 2002). "Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures". The EMBO Journal. 21 (24): 6915–6924. doi:10.1093/emboj/cdf678. PMC 139098. PMID 12486012.
  • 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): 1489–1501. doi:10.1017/S1355838202021726. PMC 1370355. PMID 12515382.
  • Grzymski EC (June 2003). "Visualizing an mRNA destruction line". Nature Structural Biology. 10 (6): 416. doi:10.1038/nsb0603-416. PMID 12768200. S2CID 40900780.
  • Piccirillo C, Khanna R, Kiledjian M (September 2003). "Functional characterization of the mammalian mRNA decapping enzyme hDcp2". RNA. 9 (9): 1138–1147. doi:10.1261/rna.5690503. PMC 1370477. PMID 12923261.
  • Lejeune F, Li X, Maquat LE (September 2003). "Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities". Molecular Cell. 12 (3): 675–687. doi:10.1016/S1097-2765(03)00349-6. PMID 14527413.
  • Cougot N, Babajko S, Séraphin B (April 2004). "Cytoplasmic foci are sites of mRNA decay in human cells". The Journal of Cell Biology. 165 (1): 31–40. doi:10.1083/jcb.200309008. PMC 2172085. PMID 15067023.
  • Lehner B, Sanderson CM (July 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–1323. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
  • Liu SW, Jiao X, Liu H, Gu M, Lima CD, Kiledjian M (September 2004). "Functional analysis of mRNA scavenger decapping enzymes". RNA. 10 (9): 1412–1422. doi:10.1261/rna.7660804. PMC 1370627. PMID 15273322.
  • 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): 719–723. doi:10.1038/ncb1274. PMC 1855297. PMID 15937477.
  • 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): 905–915. doi:10.1016/j.molcel.2005.10.031. PMID 16364915.
  • Wichroski MJ, Robb GB, Rana TM (May 2006). "Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies". PLOS Pathogens. 2 (5): e41. doi:10.1371/journal.ppat.0020041. PMC 1458959. PMID 16699599.
  • Chu CY, Rana TM (July 2006). "Translation repression in human cells by microRNA-induced gene silencing requires RCK/p54". PLOS Biology. 4 (7): e210. doi:10.1371/journal.pbio.0040210. PMC 1475773. PMID 16756390.
  • 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): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
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