Q9NPI6 (DCP1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
mRNA-decapping enzyme 1A
EC=3.-.-.-

Alternative name(s):
Smad4-interacting transcriptional co-activator
Transcription factor SMIF

Gene names

Name:	DCP1A
Synonyms:	SMIF

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.2 Ref.6 Ref.8 Ref.15
Subcellular location	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. Ref.1 Ref.2 Ref.6 Ref.8
Tissue specificity	Detected in heart, brain, placenta, lung, skeletal muscle, liver, kidney and pancreas. Ref.2
Sequence similarities	Belongs to the DCP1 family.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Traceable author statement. Source: Reactome nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasmic mRNA processing body Inferred from sequence or structural similarity. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction Ref.8. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-374238,EBI-374238
DCP2	Q8IU60	6	EBI-374238,EBI-521577
DDX6	P26196	4	EBI-374238,EBI-351257
UPF1	Q92900	13	EBI-374238,EBI-373471
ZFP36	P26651	2	EBI-374238,EBI-374248

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.13

Modified residue

180

1

Phosphoserine Ref.16

Modified residue

315

1

Phosphoserine Ref.11 Ref.12 Ref.13 Ref.16

Modified residue

319

1

Phosphoserine Ref.11 Ref.12 Ref.13 Ref.16

Modified residue

334

1

Phosphoserine Ref.11 Ref.13

Modified residue

353

1

Phosphoserine Ref.9 Ref.12 Ref.16

Modified residue

401

1

Phosphothreonine Ref.12 Ref.13

Modified residue

522

1

Phosphoserine Ref.13 Ref.14 Ref.16

Modified residue

523

1

Phosphoserine Ref.7 Ref.13 Ref.14 Ref.16

Modified residue

525

1

Phosphoserine Ref.7 Ref.10 Ref.13 Ref.14 Ref.16

Modified residue

531

1

Phosphothreonine Ref.11 Ref.13 Ref.14 Ref.16

Experimental info

Mutagenesis

20

1

D → A: Lowers decapping activity. Ref.1

Mutagenesis

59

1

R → A: Lowers decapping activity. Ref.1

Sequence conflict

483

1

Q → P in AAN62763. Ref.1

Sequence conflict

483

1

Q → P in CAB77023. Ref.2

Sequence conflict

483

1

Q → P in BAA92008. Ref.3

Sequence conflict

483

1

Q → P in AAH07439. Ref.5

Secondary structure

1

.

.

.

.

.

582

Helix Strand Turn

Details...

Helix

539 – 557

19

Helix

559 – 571

13

Sequences

	Sequence		Length	Mass (Da)
	Q9NPI6 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: D218180ABA7FD768	FASTA	582	63,309
	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

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. , 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: 14702039] [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. , 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: 16641997] [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: 15489334] [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: 12515382] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH A COMPLEX CONTAINING ENZYMES INVOLVED IN MRNA DECAY.
[7]	"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: Cervix carcinoma.
[8]	"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.
[9]	"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: Cervix carcinoma.
[10]	"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. Tissue: Cervix carcinoma.
[11]	"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. Tissue: Cervix carcinoma.
[12]	"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. Tissue: Cervix carcinoma.
[13]	"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. Tissue: Cervix carcinoma.
[14]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-523; SER-525 AND THR-531, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-315; SER-319; SER-353; SER-522; SER-523; SER-525 AND THR-531, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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: 21269460] [Abstract] Cited for: 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.

IPI

IPI00164672.

RefSeq

NP_060873.4. NM_018403.5.

UniGene

Hs.476353.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WX3	X-ray	2.31	A/B/C	539-582	[»]

ProteinModelPortal

Q9NPI6.

SMR

Q9NPI6. Positions 1-126, 539-582.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31292N.

IntAct

Q9NPI6. 16 interactions.

MINT

MINT-5005647.

STRING

Q9NPI6.

Protein family/group databases

TCDB

3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.

PTM databases

PhosphoSite

Q9NPI6.

Polymorphism databases

DMDM

296434475.

Proteomic databases

PRIDE

Q9NPI6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000294241; ENSP00000294241; ENSG00000162290.

GeneID

55802.

KEGG

hsa:55802.

Organism-specific databases

CTD

55802.

GeneCards

GC03M053319.

H-InvDB

HIX0003376.

HGNC

HGNC:18714. DCP1A.

MIM

607010. gene.

neXtProt

NX_Q9NPI6.

PharmGKB

PA134931379.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG714471.

HOVERGEN

HBG051320.

InParanoid

Q9NPI6.

OMA

PSGHKHL.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q9NPI6.

CleanEx

HS_DCP1A.

Genevestigator

Q9NPI6.

GermOnline

ENSG00000162290. Homo sapiens.

Family and domain databases

InterPro

IPR010334. DCP1.
[Graphical view]

KO

K12610.

PANTHER

PTHR16290. DCP1. 1 hit.

Pfam

PF06058. DCP1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

60947.

SOURCE

Search...

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:	May 18, 2010
Last modified:	December 14, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.