mRNA-decapping enzyme 1A - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    mRNA-decapping enzyme 1A
    EC=3.-.-.-
Alternative name(s):
    Transcription factor SMIF
    Smad4-interacting transcriptional co-activator

Gene names

Name:	DCP1A
Synonyms:	SMIF

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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. Ref.1 Ref.2
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. Ref.1 Ref.2 Ref.5 Ref.7
Subcellular location	Cytoplasm › P-body. Nucleus. Note: Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4. Ref.1 Ref.2 Ref.5 Ref.7
Tissue specificity	Detected in heart, brain, placenta, lung, skeletal muscle, liver, kidney and pancreas. Ref.2
Sequence similarities	Belongs to the DCP1 family.

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Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasmic mRNA processing body Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.1 Ref.7 Ref.14 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
DCP2	Q8IU60	2	EBI-374238,EBI-521577
DDX6	P26196	1	EBI-374238,EBI-351257
LSM8	O95777	1	EBI-374238,EBI-347779
UPF1	Q92900	2	EBI-374238,EBI-373471
ZFP36	P26651	1	EBI-374238,EBI-374248

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 582

582

mRNA-decapping enzyme 1A

PRO_0000189632

Amino acid modifications

Modified residue

142

1

Phosphoserine Ref.12

Modified residue

315

1

Phosphoserine Ref.12 Ref.10 Ref.11

Modified residue

319

1

Phosphoserine Ref.12 Ref.10 Ref.11

Modified residue

334

1

Phosphoserine Ref.12 Ref.10

Modified residue

353

1

Phosphoserine Ref.11 Ref.8

Modified residue

401

1

Phosphothreonine Ref.12 Ref.11

Modified residue

522

1

Phosphoserine Ref.12

Modified residue

523

1

Phosphoserine Ref.12 Ref.6

Modified residue

525

1

Phosphoserine Ref.12 Ref.6 Ref.9

Modified residue

531

1

Phosphothreonine Ref.12 Ref.10

Experimental info

Mutagenesis

20

1

D → A: Lowers decapping activity. Ref.1

Mutagenesis

59

1

R → A: Lowers decapping activity. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9NPI6-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 26480D0B10CE7C72
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FASTA

582

63,278

        10         20         30         40         50         60 
MEALSRAGQE MSLAALKQHD PYITSIADLT GQVALYTFCP KANQWEKTDI EGTLFVYRRS 

        70         80         90        100        110        120 
ASPYHGFTIV NRLNMHNLVE PVNKDLEFQL HEPFLLYRNA SLSIYSIWFY DKNDCHRIAK 

       130        140        150        160        170        180 
LMADVVEEET RRSQQAARDK QSPSQANGCS DHRPIDILEM LSRAKDEYER NQMGDSNISS 

       190        200        210        220        230        240 
PGLQPSTQLS NLGSTETLEE MPSGSQDKSA PSGHKHLTVE ELFGTSLPKE QPAVVGLDSE 

       250        260        270        280        290        300 
EMERLPGDAS QKEPNSFLPF PFEQLGGAPQ SETLGVPSAA HHSVQPEITT PVLITPASIT 

       310        320        330        340        350        360 
QSNEKHAPTY TIPLSPVLSP TLPAEAPTAQ VPPSLPRNST MMQAVKTTPR QRSPLLNQPV 

       370        380        390        400        410        420 
PELSHASLIA NQSPFRAPLN VTNTAGTSLP SVDLLQKLRL TPQHDQIQTQ PLGKGAMVAS 

       430        440        450        460        470        480 
FSPAAGQLAT PESFIEPPSK TAAARVAASA SLSNMVLAPL QSMQQNQDPE VFVQPKVLSS 

       490        500        510        520        530        540 
AIPVAGAPLV TATTTAVSSV LLAPSVFQQT VTRSSDLERK ASSPSPLTIG TPESQRKPSI 

       550        560        570        580 
ILSKSQLQDT LIHLIKNDSS FLSTLHEVYL QVLTKNKDNH NL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay." Lykke-Andersen J. Mol. Cell. Biol. 22:8114-8121(2002) [PubMed: 12417715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF ASP-20 AND ARG-59, INTERACTION WITH DCP1B AND DCP2, SUBCELLULAR LOCATION.
[2]	"SMIF, a Smad4-interacting protein that functions as a co-activator in TGFbeta signalling." Bai R.-Y., Koester C., Ouyang T., Hahn S.A., Hammerschmidt M., Peschel C., Duyster J. Nat. Cell Biol. 4:181-190(2002) [PubMed: 11836524] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SMAD4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Pancreas.
[3]	"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., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[5]	"The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci." Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T. RNA 8:1489-1501(2002) [PubMed: 12515382] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH A COMPLEX CONTAINING ENZYMES INVOLVED IN MRNA DECAY.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND SER-525, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping." Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J. Mol. Cell 20:905-915(2005) [PubMed: 16364915] [Abstract] Cited for: INTERACTION WITH EDC3; DCP2; EDC4 AND DDX6, SUBCELLULAR LOCATION.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"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. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, MASS SPECTROMETRY.
[10]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-334 AND THR-531, MASS SPECTROMETRY.
[11]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-353 AND THR-401, MASS SPECTROMETRY.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-315; SER-319; SER-334; THR-401; SER-522; SER-523; SER-525 AND THR-531, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"Human proline-rich nuclear receptor coregulatory protein 2 mediates an interaction between mRNA surveillance machinery and decapping complex." Cho H., Kim K.M., Kim Y.K. Mol. Cell 33:75-86(2009) [PubMed: 19150429] [Abstract] Cited for: INTERACTION WITH PNRC2.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AY146651 mRNA. Translation: AAN62763.1. AJ275986 mRNA. Translation: CAB77023.1. AK001969 mRNA. Translation: BAA92008.1. BC007439 mRNA. Translation: AAH07439.1.
IPI	IPI00871439.
RefSeq	NP_060873.3.
UniGene	Hs.476353
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NPI6. 13 interactions.
Protein family/group databases
TCDB	3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.
PTM databases
PhosphoSite	Q9NPI6.
Proteomic databases
PRIDE	Q9NPI6.
Genome annotation databases
Ensembl	ENSG00000162290. Homo sapiens. [Contig view]
GeneID	55802.
KEGG	hsa:55802.
Organism-specific databases
GeneCards	GC03M053297.
H-InvDB	HIX0003376.
HGNC	HGNC:18714. DCP1A.
HPA	HPA013202.
MIM	607010. gene.
PharmGKB	PA134931379.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9NPI6.
HOVERGEN	Q9NPI6.
Enzyme and pathway databases
Pathway_Interaction_DB	smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
Gene expression databases
ArrayExpress	Q9NPI6.
Bgee	Q9NPI6.
CleanEx	HS_DCP1A.
GermOnline	ENSG00000162290. Homo sapiens.
Family and domain databases
InterPro	IPR010334. DCP1. [Graphical view]
PANTHER	PTHR16290. DCP1. 1 hit.
Pfam	PF06058. DCP1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	60947.
SOURCE	Search...

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Entry information

Entry name

DCP1A_HUMAN

Accession

Primary (citable) accession number: Q9NPI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	October 1, 2000
Last modified:	July 7, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents