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Q9NPI6 (DCP1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
mRNA-decapping enzyme 1A

EC=3.-.-.-
Alternative name(s):
Smad4-interacting transcriptional co-activator
Transcription factor SMIF
Gene names
Name:DCP1A
Synonyms:SMIF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length582 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Interacts with DDX17 in an RNA-independent manner. Interacts with ZC3HAV1. Ref.1 Ref.2 Ref.6 Ref.7 Ref.13 Ref.17

Subcellular location

CytoplasmP-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. Ref.1 Ref.2 Ref.6 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 582582mRNA-decapping enzyme 1A
PRO_0000189632

Amino acid modifications

Modified residue1421Phosphoserine Ref.11
Modified residue1801Phosphoserine Ref.14
Modified residue3151Phosphoserine Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.18
Modified residue3191Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue3341Phosphoserine Ref.9 Ref.11
Modified residue3531Phosphoserine Ref.8 Ref.10 Ref.11 Ref.15
Modified residue4011Phosphothreonine Ref.11
Modified residue4221Phosphoserine Ref.15
Modified residue5221Phosphoserine Ref.11 Ref.14
Modified residue5231Phosphoserine Ref.11 Ref.14
Modified residue5251Phosphoserine Ref.11 Ref.14
Modified residue5311Phosphothreonine Ref.9 Ref.11 Ref.14

Experimental info

Mutagenesis201D → A: Lowers decapping activity. Ref.1
Mutagenesis591R → A: Lowers decapping activity. Ref.1
Sequence conflict4831Q → P in AAN62763. Ref.1
Sequence conflict4831Q → P in CAB77023. Ref.2
Sequence conflict4831Q → P in BAA92008. Ref.3
Sequence conflict4831Q → P in AAH07439. Ref.5

Secondary structure

..................... 582
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NPI6 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: D218180ABA7FD768

FASTA58263,309
        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 
AIQVAGAPLV TATTTAVSSV LLAPSVFQQT VTRSSDLERK ASSPSPLTIG TPESQRKPSI 

       550        560        570        580 
ILSKSQLQDT LIHLIKNDSS FLSTLHEVYL QVLTKNKDNH NL 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[6]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH A COMPLEX CONTAINING ENZYMES INVOLVED IN MRNA DECAY.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-334 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-315; SER-319; SER-334; SER-353; THR-401; SER-522; SER-523; SER-525 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PNRC2.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-315; SER-319; SER-522; SER-523; SER-525 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-353 AND SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZC3HAV1 AND DDX17.
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY146651 mRNA. Translation: AAN62763.1.
AJ275986 mRNA. Translation: CAB77023.1.
AK001969 mRNA. Translation: BAA92008.1.
AC097015 Genomic DNA. No translation available.
AC112218 Genomic DNA. No translation available.
BC007439 mRNA. Translation: AAH07439.1.
RefSeqNP_001277134.1. NM_001290205.1.
NP_001277135.1. NM_001290206.1.
NP_060873.4. NM_018403.6.
UniGeneHs.476353.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WX3X-ray2.31A/B/C539-582[»]
4B6HX-ray2.60A/B1-130[»]
ProteinModelPortalQ9NPI6.
SMRQ9NPI6. Positions 1-129, 539-582.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120914. 17 interactions.
DIPDIP-31292N.
IntActQ9NPI6. 15 interactions.
MINTMINT-5005647.
STRING9606.ENSP00000294241.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteQ9NPI6.

Polymorphism databases

DMDM296434475.

Proteomic databases

MaxQBQ9NPI6.
PaxDbQ9NPI6.
PRIDEQ9NPI6.

Protocols and materials databases

DNASU55802.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID55802.
KEGGhsa:55802.
UCSCuc021wzi.1. human.

Organism-specific databases

CTD55802.
GeneCardsGC03M053319.
HGNCHGNC:18714. DCP1A.
HPAHPA013202.
MIM607010. gene.
neXtProtNX_Q9NPI6.
PharmGKBPA134931379.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314415.
HOVERGENHBG051320.
InParanoidQ9NPI6.
KOK12610.
PhylomeDBQ9NPI6.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

CleanExHS_DCP1A.
GenevestigatorQ9NPI6.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR010334. DCP1.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERPTHR16290. PTHR16290. 1 hit.
PfamPF06058. DCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCP1A. human.
EvolutionaryTraceQ9NPI6.
GeneWikiDCP1A.
GenomeRNAi55802.
NextBio60947.
PROQ9NPI6.
SOURCESearch...

Entry information

Entry nameDCP1A_HUMAN
AccessionPrimary (citable) accession number: Q9NPI6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: May 18, 2010
Last modified: June 11, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 3

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