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mRNA-decapping enzyme 1A

 
Known also as: Smad4-interacting transcriptional co-activator, Transcription factor SMIF

Known abbreviations: DCP1A, SMIF

 

FUNCTION:
 
Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1. 
 
SUBUNIT STRUCTURE:
 
Forms a complex with EDC3, DCP2, DDX6 and EDC4/HEDLS, within this complex directly interacts with EDC3. Binds DCP1B, UPF1 and SMAD4. Part of a cytoplasmic complex containing proteins involved in mRNA decay, including XRN1 and LSM1. Interacts with PNRC2.
 
CELLULAR LOCALIZATION:
 
Cytoplasm › P-body. Nucleus. Note: Co-localizes with NANOS3 in the processing bodies (By similarity.) Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4. 
 
TISSUE SPECIFICITY:
 
Detected in heart, brain, placenta, lung, skeletal muscle, liver, kidney and pancreas. 



This protein can be a part of a given complexes: Activities in which mRNA-decapping enzyme 1A is involved: Pathways in which mRNA-decapping enzyme 1A is involved:

NCBI GI number(s): 291327466
291327465
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q9NPI6 Q9NPI6
BRENDA - -
KEGG hsa:55802 hsa:55802
PFAM: PF06058
PF06058
InterPro: IPR010334
IPR010334
CATH: - -
SCOP: - -
Solved crystal structures: 2WX3
[PDB] [details]


Protein sequence:
MEALSRAGQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDI
EGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQLHEPFLLYRNA
SLSIYSIWFYDKNDCHRIAKLMADVVEEETRRSQQAARDKQSPSQANGCS
DHRPIDILEMLSRAKDEYERNQMGDSNISSPGLQPSTQLSNLGSTETLEE
MPSGSQDKSAPSGHKHLTVEELFGTSLPKEQPAVVGLDSEEMERLPGDAS
QKEPNSFLPFPFEQLGGAPQSETLGVPSAAHHSVQPEITTPVLITPASIT
QSNEKHAPTYTIPLSPVLSPTLPAEAPTAQVPPSLPRNSTMMQAVKTTPR
QRSPLLNQPVPELSHASLIANQSPFRAPLNVTNTAGTSLPSVDLLQKLRL
TPQHDQIQTQPLGKGAMVASFSPAAGQLATPESFIEPPSKTAAARVAASA
SLSNMVLAPLQSMQQNQDPEVFVQPKVLSSAIQVAGAPLVTATTTAVSSV
LLAPSVFQQTVTRSSDLERKASSPSPLTIGTPESQRKPSIILSKSQLQDT
LIHLIKNDSSFLSTLHEVYLQVLTKNKDNHNL

MRNA-decapping enzyme 1A (Homo sapiens) is product of expression of DCP1A gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
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
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
Human proline-rich nuclear receptor coregulatory protein 2 mediates an interaction between mRNA surveillance machinery and decapping complex. Cho H, Kim KM, Kim YK Mol Cell 2009-02-16 (33) 19150429
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
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem 2009-06-01 (81) 19413330
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
The DNA sequence, annotation and analysis of human chromosome 3. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y Nature 2006-04-27 (440) 16641997
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
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M Mol Cell 2008-08-08 (31) 18691976
Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd J Proteome Res 2008-03-01 (7) 18220336
Large-scale characterization of HeLa cell nuclear phosphoproteins. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP Proc Natl Acad Sci U S A 2004-08-17 (101) 15302935
Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y Anal Sci 2008-02-01 (24) 18187866
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
SMIF, a Smad4-interacting protein that functions as a co-activator in TGFbeta signalling. Bai RY, Koester C, Ouyang T, Hahn SA, Hammerschmidt M, Peschel C, Duyster J Nat Cell Biol 2002-03-01 (4) 11836524



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

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