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mRNA-decapping enzyme 2

Known also as: Nucleoside diphosphate-linked moiety X motif 20, Nudix motif 20

Known abbreviations: DCP2, NUDT20


Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking a RNA moiety. 
Manganese. Required for highest activity. Can also utilize magnesium ions. 
Found in a mRNA decay complex with LSM1, LSM3, LSM4, EXOSC2, EXOSC4, EXOSC10, PARN, XRN1, CNOT6, UPF1, UPF2 and UPF3B. Forms a complex with DCP1A, EDC3, DDX6 and EDC4/HEDLS, within this complex directly interacts with EDC4/HEDLS. Interacts with DPC1B, UPF1, UPF2 and UPF3B. Interacts (via N-terminus and C-terminus) with TRIM21 (via N-terminus and C-terminus). Associates with polysomes. Interacts with LIMD1, WTIP and AJUBA. 
Cytoplasm › P-body. Nucleus. Note: Predominantly cytoplasmic, in processing bodies (PB). A minor amount is nuclear.
Phosphorylated upon DNA damage, probably by ATM or ATR. 

This protein can be a part of a given complexes: Activities in which mRNA-decapping enzyme 2 is involved: Pathways in which mRNA-decapping enzyme 2 is involved:

NCBI GI number(s): 334688848
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q8IU60 Q8IU60
KEGG hsa:167227 hsa:167227
PFAM: PF05026
InterPro: IPR007722
CATH: - -
SCOP: - -

Protein sequence:

MRNA-decapping enzyme 2 (Homo sapiens) is product of expression of DCP2 gene.


Title Authors Journal Publication date (Issue) PubMed ID
A protein interaction framework for human mRNA degradation. Lehner B, Sanderson CM Genome Res 2004-07-01 (14) 15231747
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, K Genome Res 2004-10-01 (14) 15489334
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K Nat Genet 2004-02-01 (36) 14702039
Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. van Dijk E, Cougot N, Meyer S, Babajko S, Wahle E, Seraphin B EMBO J 2002-12-16 (21) 12486012
Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'. Mullen TE, Marzluff WF Genes Dev 2008-02-01 (22) 18172165
Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Fenger-Gron M, Fillman C, Norrild B, Lykke-Andersen J Mol Cell 2005-12-22 (20) 16364915
Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Lykke-Andersen J Mol Cell Biol 2002-12-01 (22) 12417715
SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity. Yamochi T, Ohnuma K, Hosono O, Tanaka H, Kanai Y, Morimoto C Biochem Biophys Res Commun 2008-05-23 (370) 18361920
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell 2006-11-03 (127) 17081983
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science 2007-05-25 (316) 17525332
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A 2008-08-05 (105) 18669648
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal 2009-01-01 (2) 19690332
Functional analysis of mRNA scavenger decapping enzymes. Liu SW, Jiao X, Liu H, Gu M, Lima CD, Kiledjian M RNA 2004-09-01 (10) 15273322
Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Lejeune F, Li X, Maquat LE Mol Cell 2003-09-01 (12) 14527413
The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. Ingelfinger D, Arndt-Jovin DJ, Luhrmann R, Achsel T RNA 2002-12-01 (8) 12515382
LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing. James V, Zhang Y, Foxler DE, de Moor CH, Kong YW, Webb TM, Self TJ, Feng Y, Lagos D, Chu CY, Rana TM, Morley SJ, Longmore GD, Bushell M, Sharp TV Proc Natl Acad Sci U S A 2010-07-13 (107) 20616046
The hDcp2 protein is a mammalian mRNA decapping enzyme. Wang Z, Jiao X, Carr-Schmid A, Kiledjian M Proc Natl Acad Sci U S A 2002-10-01 (99) 12218187
The DNA sequence and comparative analysis of human chromosome 5. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W Nature 2004-09-16 (431) 15372022
Functional characterization of the mammalian mRNA decapping enzyme hDcp2. Piccirillo C, Khanna R, Kiledjian M RNA 2003-09-01 (9) 12923261
Cytoplasmic foci are sites of mRNA decay in human cells. Cougot N, Babajko S, Seraphin B J Cell Biol 2004-04-01 (165) 15067023

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Last modification of this entry: Sept. 25, 2012.

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