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DCP2

From Wikipedia, the free encyclopedia

Protein found in humans

This article is about the gene and encoded protein. For the Disease Control Priorities in Developing Countries Report (2nd edition), seeDisease Control Priorities Project.

DCP2

Identifiers

Aliases

DCP2, NUDT20, decapping mRNA 2

External IDs

OMIM:609844;MGI:1917890;HomoloGene:13968;GeneCards:DCP2;OMA:DCP2 - orthologs

Gene location (Human)

Chr.	Chromosome 5 (human)^[1]

Band	5q22.2	Start	112,976,702bp^[1]
Band	5q22.2	End	113,022,195bp^[1]

Gene location (Mouse)

Chr.	Chromosome 18 (mouse)^[2]

Band	18\|18 B3	Start	44,513,569bp^[2]
Band	18\|18 B3	End	44,558,036bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

oocyte

secondary oocyte

trabecular bone

sperm

parietal pleura

placenta

monocyte

bone marrow

visceral pleura

epithelium of nasopharynx

Top expressed in

hand

otolith organ

utricle

primitive streak

superior cervical ganglion

vas deferens

condyle

vestibular membrane of cochlear duct

abdominal wall

trigeminal ganglion

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

Species

Human

Mouse

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 Mb

Chr 18: 44.51 – 44.56 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

mRNA-decapping enzyme 2 is aprotein that in humans is encoded by theDCP2gene.^[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

[edit]

DCP2 has been shown tointeract withDCP1A^[8] andUPF1.^[6]^[9]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000172795 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000024472 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.
^^a ^bLykke-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.
^^a ^b"Entrez Gene: DCP2 DCP2 decapping enzyme homolog (S. cerevisiae)".
^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.
^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.

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.

Post-transcriptional modification

Nuclear

RNA splicing

Intron / Exon snRNP Spliceosome minor U1 Alternative splicing
pre-mRNA factors	PLRG1 PRPF3 PRPF4 PRPF4B PRPF6 PRPF8 PRPF18 PRPF19 PRPF31 PRPF38A PRPF38B PRPF39 PRPF40A PRPF40B

Cytosolic

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References

Further reading