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Identification
HMDB Protein ID HMDBP08710
Secondary Accession Numbers
  • 14432
Name m7GpppN-mRNA hydrolase
Synonyms
  1. Nucleoside diphosphate-linked moiety X motif 20
  2. Nudix motif 20
  3. hDpc
  4. mRNA-decapping enzyme 2
Gene Name DCP2
Protein Type Unknown
Biological Properties
General Function Involved in RNA binding
Specific Function 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.
Pathways
  • RNA degradation
Reactions
M(7)G5'ppp5'-mRNA + Water → m(7)GDP + 5'-phospho-mRNA details
GO Classification
Biological Process
exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay
gene expression
histone mRNA catabolic process
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Cellular Component
cytosol
cytoplasmic mRNA processing body
RNA-induced silencing complex
nucleus
Function
manganese ion binding
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
transition metal ion binding
nucleic acid binding
rna binding
Molecular Function
exoribonuclease activity, producing 5'-phosphomonoesters
m7G(5')pppN diphosphatase activity
manganese ion binding
RNA binding
Cellular Location
  1. Nucleus
  2. Cytoplasm
  3. P-body
Gene Properties
Chromosome Location 5
Locus 5q22.2
SNPs DCP2
Gene Sequence
>1263 bp
ATGGAGACCAAACGGGTGGAGATTCCCGGCAGCGTCCTGGACGATCTCTGCAGCCGATTT
ATTTTGCATATTCCCAGCGAGGAAAGAGACAATGCAATCCGAGTGTGTTTTCAGATTGAA
CTTGCCCATTGGTTTTACTTGGATTTCTACATGCAGAACACACCAGGATTACCTCAGTGT
GGGATAAGAGACTTTGCTAAAGCTGTCTTCAGTCATTGTCCGTTTTTGCTGCCTCAAGGT
GAAGATGTGGAAAAAGTTTTGGATGAATGGAAGGAATATAAAATGGGAGTACCAACATAT
GGTGCAATTATTCTTGATGAGACACTTGAAAATGTACTACTAGTTCAGGGGTACCTAGCA
AAATCAGGCTGGGGATTTCCAAAAGGAAAAGTAAATAAAGAAGAAGCTCCTCATGATTGT
GCTGCTAGAGAGGTCTTTGAAGAAACTGGTTTTGATATCAAAGACTATATTTGTAAGGAT
GATTACATTGAACTTCGAATCAATGACCAGCTTGCTCGTTTGTACATCATTCCAGGAATT
CCAAAAGACACAAAATTTAACCCAAAAACTAGAAGAGAAATTCGGAACATTGAGTGGTTC
TCTATTGAGAAATTGCCTTGTCATAGAAATGATATGACCCCCAAATCCAAACTTGGTTTG
GCACCTAACAAATTTTTTATGGCCATTCCCTTTATCAGACCATTAAGGGACTGGCTTTCT
CGAAGATTTGGCGATTCCTCAGACAGTGACAATGGATTTTCCTCAACTGGTAGCACGCCG
GCTAAACCCACTGTGGAAAAATTGAGTCGAACCAAATTCCGCCACAGTCAGCAGTTATTT
CCTGACGGTTCTCCTGGTGACCAGTGGGTAAAGCACAGGCAACCACTGCAGCAAAAGCCA
TATAATAATCATTCTGAAATGTCTGACCTTTTAAAAGGAAAGAATCAAAGTATGAGGGGA
AATGGCAGAAAACAGTATCAAGATTCACCTAATCAAAAGAAAAGAACAAATGGGCTTCAG
CCAGCAAAGCAGCAGAATTCTTTGATGAAGTGTGAAAAGAAACTTCATCCACGGAAACTT
CAGGATAATTTTGAAACAGATGCTGTATATGACTTGCCTAGCTCCAGTGAAGACCAGTTG
CTAGAACATGCTGAGGGACAGCCCGTGGCATGTAATGGACATTGCAAGTTCCCCTTTTCA
TCCAGAGCCTTTTTGAGTTTCAAGTTTGACCATAATGCTATAATGAAAATCTTGGACCTT
TGA
Protein Properties
Number of Residues 420
Molecular Weight 44408.25
Theoretical pI 6.936
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>mRNA-decapping enzyme 2
METKRVEIPGSVLDDFCSRFILHIPSEERDNAIRVCFQIELAHWFYLDFYMQNTPGLPQC
GIRDFAKAVFSHCPFLLPQGEDVEKVLDEWKEYKMGVPTYGAIILDETLENVLLVQGYLA
KSGWGFPKGKVNKEEAPHDCAAREVFEETGFDIKDYICKDDYIELRINDQLARLYIIPGI
PKDTKFNPKTRREIRNIEWFSIEKLPCHRNDMTPKSKLGLAPNKFFMAIPFIRPLRDWLS
RRFGDSSDSDNGFSSTGSTPAKPTVEKLSRTKFRHSQQLFPDGSPGDQWVKHRQPLQQKP
YNNHSEMSDLLKGKNQSMRGNGRKQYQDSPNQKKRTNGLQPAKQQNSLMKCEKKLHPRKL
QDNFETDAVYDLPSSSEDQLLEHAEGQPVACNGHCKFPFSSRAFLSFKFDHNAIMKILDL
GenBank ID Protein 31542498
UniProtKB/Swiss-Prot ID Q8IU60
UniProtKB/Swiss-Prot Entry Name DCP2_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_152624.4
GeneCard ID DCP2
GenAtlas ID DCP2
HGNC ID HGNC:24452
References
General References
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  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
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  8. Mullen TE, Marzluff WF: Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'. Genes Dev. 2008 Jan 1;22(1):50-65. doi: 10.1101/gad.1622708. [PubMed:18172165 ]
  9. Lehner B, Sanderson CM: A protein interaction framework for human mRNA degradation. Genome Res. 2004 Jul;14(7):1315-23. [PubMed:15231747 ]
  10. Lykke-Andersen J: Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Mol Cell Biol. 2002 Dec;22(23):8114-21. [PubMed:12417715 ]
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  12. Ingelfinger D, Arndt-Jovin DJ, Luhrmann R, Achsel T: The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA. 2002 Dec;8(12):1489-501. [PubMed:12515382 ]
  13. Lejeune F, Li X, Maquat LE: Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol Cell. 2003 Sep;12(3):675-87. [PubMed:14527413 ]
  14. Piccirillo C, Khanna R, Kiledjian M: Functional characterization of the mammalian mRNA decapping enzyme hDcp2. RNA. 2003 Sep;9(9):1138-47. [PubMed:12923261 ]
  15. Cougot N, Babajko S, Seraphin B: Cytoplasmic foci are sites of mRNA decay in human cells. J Cell Biol. 2004 Apr;165(1):31-40. Epub 2004 Apr 5. [PubMed:15067023 ]
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  17. Fenger-Gron M, Fillman C, Norrild B, Lykke-Andersen J: Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol Cell. 2005 Dec 22;20(6):905-15. [PubMed:16364915 ]
  18. Yamochi T, Ohnuma K, Hosono O, Tanaka H, Kanai Y, Morimoto C: SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity. Biochem Biophys Res Commun. 2008 May 23;370(1):195-9. doi: 10.1016/j.bbrc.2008.03.075. Epub 2008 Mar 24. [PubMed:18361920 ]