DCP1A

DCP1A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2WX3, 4B6H
Identifiers
Aliases	DCP1A , HSA275986, Nbla00360, SMAD4IP1, SMIF, decapping mRNA 1A
External IDs	OMIM: 607010; MGI: 1923151; HomoloGene: 10178; GeneCards: DCP1A; OMA:DCP1A - orthologs
Gene location (Human) Chr. Chromosome 3 (human) [1] Band 3p21.1 Start 53,283,429 bp [1] End 53,347,586 bp [1]
Gene location (Mouse) Chr. Chromosome 14 (mouse) [2] Band 14 B|14 18.75 cM Start 30,201,492 bp [2] End 30,249,020 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte secondary oocyte cartilage tissue testicle Achilles tendon gonad sural nerve tibialis anterior muscle buccal mucosa cell islet of Langerhans Top expressed in secondary oocyte zygote primary oocyte medullary collecting duct tail of embryo saccule otic vesicle genital tubercle otic placode cumulus cell More reference expression data BioGPS More reference expression data
Gene ontology Molecular function enzyme regulator activity enzyme activator activity protein binding mRNA binding hydrolase activity identical protein binding kinesin binding Cellular component cytoplasm cytosol membrane nucleus P-body cytoplasmic ribonucleoprotein granule Biological process positive regulation of catalytic activity deadenylation-independent decapping of nuclear-transcribed mRNA protein localization to cytoplasmic stress granule regulation of mRNA stability deadenylation-dependent decapping of nuclear-transcribed mRNA exonucleolytic catabolism of deadenylated mRNA nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 55802 75901 Ensembl ENSG00000272886 ENSMUSG00000021962 UniProt Q9NPI6 Q91YD3 RefSeq (mRNA) NM_018403 NM_001290204 NM_001290205 NM_001290206 NM_001290207 NM_133761 RefSeq (protein) NP_001277133 NP_001277134 NP_001277135 NP_001277136 NP_060873 NP_598522 Location (UCSC) Chr 3: 53.28 – 53.35 Mb Chr 14: 30.2 – 30.25 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

mRNA-decapping enzyme 1A is a protein that in humans is encoded by the DCP1A gene. ^[5]

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. ^[5]

Interactions

DCP1A has been shown to interact with DCP2 ^[6] and UPF1. ^[6] It has also been shown to colocalize with GW182, and other markers of P-body. ^[7] Human DCP1A is heterotrimeric, ^[8] and makes contacts with the scaffold EDC3/4. ^[9] The Arabidopsis thaliana homolog interacts with the plant specific type XI myosin motor protein. ^[10]

References

1. GRCh38: Ensembl release 89: ENSG00000272886 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021962 – 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. "Entrez Gene: DCP1A DCP1 decapping enzyme homolog A (S. cerevisiae)".
6. 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. Eystathioy T, Jakymiw A, Chan EK, Séraphin B, Cougot N, Fritzler MJ (October 2003). "The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies". RNA. 9 (10): 1171–1173. doi:10.1261/rna.5810203. PMC   1370480 . PMID   13130130.
8. Tritschler F, Braun JE, Motz C, Igreja C, Haas G, Truffault V, et al. (December 2009). "DCP1 forms asymmetric trimers to assemble into active mRNA decapping complexes in metazoa". Proceedings of the National Academy of Sciences of the United States of America. 106 (51): 21591–21596. Bibcode:2009PNAS..10621591T. doi: 10.1073/pnas.0909871106 . PMC   2789166 . PMID   19966221.
9. Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, et al. (December 2007). "A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting". Molecular and Cellular Biology. 27 (24): 8600–8611. doi:10.1128/MCB.01506-07. PMC   2169425 . PMID   17923697.
10. Steffens A, Jaegle B, Tresch A, Hülskamp M, Jakoby M (April 2014). "Processing-body movement in Arabidopsis depends on an interaction between myosins and DECAPPING PROTEIN1". Plant Physiology. 164 (4): 1879–1892. doi: 10.1104/pp.113.233031 . PMC   3982750 . PMID   24525673.

Further reading

• Bai RY, Koester C, Ouyang T, Hahn SA, Hammerschmidt M, Peschel C, Duyster J (March 2002). "SMIF, a Smad4-interacting protein that functions as a co-activator in TGFbeta signalling". Nature Cell Biology. 4 (3): 181–190. doi:10.1038/ncb753. PMID   11836524. S2CID   19938060.
• Callebaut I (May 2002). "An EVH1/WH1 domain as a key actor in TGFbeta signalling". FEBS Letters. 519 (1–3): 178–180. doi: 10.1016/S0014-5793(02)02751-5 . PMID   12023040. S2CID   84499961.
• 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.
• 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.
• Leonard D, Ajuh P, Lamond AI, Legerski RJ (September 2003). "hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing". Biochemical and Biophysical Research Communications. 308 (4): 793–801. CiteSeerX   10.1.1.539.8359 . doi:10.1016/S0006-291X(03)01486-4. PMID   12927788.
• 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.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, et al. (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–12135. Bibcode:2004PNAS..10112130B. doi: 10.1073/pnas.0404720101 . PMC   514446 . PMID   15302935.
• 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.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• 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.
• 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.