DCP1A

Protein found in humans
DCP1A
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2WX3, 4B6H

Identifiers
AliasesDCP1A, HSA275986, Nbla00360, SMAD4IP1, SMIF, decapping mRNA 1A
External IDsOMIM: 607010; MGI: 1923151; HomoloGene: 10178; GeneCards: DCP1A; OMA:DCP1A - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for DCP1A
Genomic location for DCP1A
Band3p21.1Start53,283,429 bp[1]
End53,347,586 bp[1]
Gene location (Mouse)
Chromosome 14 (mouse)
Chr.Chromosome 14 (mouse)[2]
Chromosome 14 (mouse)
Genomic location for DCP1A
Genomic location for DCP1A
Band14 B|14 18.75 cMStart30,201,492 bp[2]
End30,249,020 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 14: 30.2 – 30.25 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000272886 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "Entrez Gene: DCP1A DCP1 decapping enzyme homolog A (S. cerevisiae)".
  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. ^ 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.
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