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Q12517 (DCP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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 subunit 1
Gene names
Name:DCP1
Ordered Locus Names:YOL149W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the decapping complex 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. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body. DCP1 is activated by the DEAD-box helicase DHH1 and destabilizes the eIF-4F cap-binding complex from the mRNA. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.20 Ref.21 Ref.24 Ref.26

Subunit structure

Component of the decapping complex composed of DCP1 and DCP2. Interacts with mRNAs, DHH1, LSM1, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, and the cap-binding proteins PAB1 and TIF4632/eIF-4G. Ref.9 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.28

Subcellular location

CytoplasmP-body. Note: Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. Ref.15 Ref.22 Ref.25

Post-translational modification

Phosphorylated. Ref.7

Miscellaneous

Present with 2880 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the DCP1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DCP2P535505EBI-38519,EBI-270
EDC3P399985EBI-38519,EBI-22300

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 231231mRNA-decapping enzyme subunit 1
PRO_0000232998

Experimental info

Mutagenesis16 – 205EFYRK → AFYAA in DCP1-17; partial loss of mRNA-decapping activity. Ref.10
Mutagenesis29 – 313RYD → AYA in DCP1-2; strong loss of mRNA decapping activity at 36 degrees Celsius. Ref.10 Ref.28
Mutagenesis32 – 343PKI → AKA: Partial loss of mRNA-decapping activity. Ref.28
Mutagenesis37 – 382LL → AA: Strong loss of mRNA-decapping activity; when associated with A-217 and A-221.
Mutagenesis471Y → A in DCP1-32; partial loss of mRNA decapping activity. Ref.10
Mutagenesis471Y → F in DCP1-35; partial loss of mRNA decapping activity. Ref.10
Mutagenesis48 – 503KWD → AWA in DCP1-4; partial loss of mRNA decapping activity. In DCP1-43; strong loss of mRNA-decapping activity; when associated with A-187 and A-188. In DCP1-44; strong loss of mRNA-decapping activity; when associated with A-216 and A-219. Ref.10
Mutagenesis561W → A in DCP1-31; partial loss of mRNA decapping activity. Ref.5 Ref.10 Ref.28
Mutagenesis701R → A in DCP1-33; strong loss of mRNA decapping activity. Ref.10 Ref.28
Mutagenesis1561G → D in DCP1-1; strong loss of mRNA decapping activity. Ref.10
Mutagenesis187 – 1882KD → AA in DCP1-19; partial loss of mRNA decapping activity. In DCP1-43; strong loss of mRNA-decapping activity; when associated with A-48 and A-50.
Mutagenesis2041W → A in DCP1-33; partial loss of mRNA decapping activity. Ref.10
Mutagenesis216 – 2194ELIK → ALIA in DCP1-25; partial loss of mRNA-decapping activity. In DCP1-44; strong loss of mRNA-decapping activity; when associated with A-48 and A-50. Ref.10
Mutagenesis2171L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-221. Ref.28
Mutagenesis2211L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-217. Ref.28

Secondary structure

...................... 231
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12517 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8456B1C96C121C4D

FASTA23126,266
        10         20         30         40         50         60 
MTGAATAAEN SATQLEFYRK ALNFNVIGRY DPKIKQLLFH TPHASLYKWD FKKDEWNKLE 

        70         80         90        100        110        120 
YQGVLAIYLR DVSQNTNLLP VSPQEVDIFD SQNGSNNIQV NNGSDNSNRN SSGNGNSYKS 

       130        140        150        160        170        180 
NDSLTYNCGK TLSGKDIYNY GLIILNRINP DNFSMGIVPN SVVNKRKVFN AEEDTLNPLE 

       190        200        210        220        230 
CMGVEVKDEL VIIKNLKHEV YGIWIHTVSD RQNIYELIKY LLENEPKDSF A 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence analysis of a 13 kbp fragment of the left arm of yeast chromosome XV containing seven new open reading frames."
Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J., Gancedo C., Arino J.
Yeast 11:1281-1288(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"An essential component of the decapping enzyme required for normal rates of mRNA turnover."
Beelman C.A., Stevens A., Caponigro G., LaGrandeur T.E., Hatfield L., Fortner D.M., Parker R.
Nature 382:642-646(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-14, FUNCTION, MUTAGENESIS OF TRP-56.
[6]"Mutations in trans-acting factors affecting mRNA decapping in Saccharomyces cerevisiae."
Hatfield L., Beelman C.A., Stevens A., Parker R.
Mol. Cell. Biol. 16:5830-5838(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Isolation and characterization of Dcp1p, the yeast mRNA decapping enzyme."
LaGrandeur T.E., Parker R.
EMBO J. 17:1487-1496(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[8]"The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complex."
Anderson J.S.J., Parker R.P.
EMBO J. 17:1497-1506(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif."
Dunckley T., Parker R.
EMBO J. 18:5411-5422(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DCP2.
[10]"Analysis of mutations in the yeast mRNA decapping enzyme."
Tharun S., Parker R.
Genetics 151:1273-1285(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 16-GLU--LYS-20; 29-ARG--ASP-31; TYR-47; 48-LYS--ASP-50; TRP-56; ARG-70; GLY-156; 187-LYS-ASP-188; TRP-204 AND 216-GLU--LYS-219.
[11]"Monitoring mRNA decapping activity."
Zhang S., Williams C.J., Wormington M., Stevens A., Peltz S.W.
Methods 17:46-51(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Recognition of yeast mRNAs as 'nonsense containing' leads to both inhibition of mRNA translation and mRNA degradation: implications for the control of mRNA decapping."
Muhlrad D., Parker R.
Mol. Biol. Cell 10:3971-3978(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae."
Schwartz D.C., Parker R.
Mol. Cell. Biol. 19:5247-5256(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex."
Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G.
EMBO J. 19:4372-4382(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PAB1 AND TIF4632.
[15]"Yeast Sm-like proteins function in mRNA decapping and decay."
Tharun S., He W., Mayes A.E., Lennertz P., Beggs J.D., Parker R.
Nature 404:515-518(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LSM1; LSM2; LSM3; LSM4; LSM5; LSM6 AND LSM7, SUBCELLULAR LOCATION.
[16]"Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins."
Fromont-Racine M., Mayes A.E., Brunet-Simon A., Rain J.-C., Colley A., Dix I., Decourty L., Joly N., Ricard F., Beggs J.D., Legrain P.
Yeast 17:95-110(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LSM4.
[17]"Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae."
Dunckley T., Tucker M., Parker R.
Genetics 157:27-37(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EDC1.
[18]"Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs."
Tharun S., Parker R.
Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MRNA, FUNCTION OF THE DCP1-DCP2 COMPLEX.
[19]"The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes."
Coller J.M., Tucker M., Sheth U., Valencia-Sanchez M.A., Parker R.
RNA 7:1717-1727(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DHH1.
[20]"The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1."
Fischer N., Weis K.
EMBO J. 21:2788-2797(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACTIVATION BY DHH1.
[21]"Modulation of eukaryotic mRNA stability via the cap-binding translation complex eIF4F."
Ramirez C.V., Vilela C., Berthelot K., McCarthy J.E.G.
J. Mol. Biol. 318:951-962(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[23]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[24]"Analysis of recombinant yeast decapping enzyme."
Steiger M., Carr-Schmid A., Schwartz D.C., Kiledjian M., Parker R.
RNA 9:231-238(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE DCP1-DCP2 COMPLEX.
[25]"Decapping and decay of messenger RNA occur in cytoplasmic processing bodies."
Sheth U., Parker R.
Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[26]"Loss of translational control in yeast compromised for the major mRNA decay pathway."
Holmes L.E.A., Campbell S.G., De Long S.K., Sachs A.B., Ashe M.P.
Mol. Cell. Biol. 24:2998-3010(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[27]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Crystal structure of Dcp1p and its functional implications in mRNA decapping."
She M., Decker C.J., Sundramurthy K., Liu Y., Chen N., Parker R., Song H.
Nat. Struct. Mol. Biol. 11:249-256(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), INTERACTION WITH DCP2, MUTAGENESIS OF 29-ARG--ASP-31; 32-PRO--ILE-34; 37-LEU-LEU-38; TRP-56; ARG-70; LEU-217 AND LEU-221.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z48239 Genomic DNA. Translation: CAA88278.1.
Z74891 Genomic DNA. Translation: CAA99170.1.
AY558431 Genomic DNA. Translation: AAS56757.1.
BK006948 Genomic DNA. Translation: DAA10636.1.
PIRS60387.
RefSeqNP_014492.1. NM_001183403.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q67X-ray2.30A/B1-231[»]
ProteinModelPortalQ12517.
SMRQ12517. Positions 17-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34268. 65 interactions.
DIPDIP-1288N.
IntActQ12517. 24 interactions.
MINTMINT-390330.
STRING4932.YOL149W.

Proteomic databases

PaxDbQ12517.
PeptideAtlasQ12517.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL149W; YOL149W; YOL149W.
GeneID854016.
KEGGsce:YOL149W.

Organism-specific databases

CYGDYOL149w.
SGDS000005509. DCP1.

Phylogenomic databases

eggNOGNOG240628.
HOGENOMHOG000246588.
KOK12612.
OMAGLWVFNE.
OrthoDBEOG74BK4D.

Enzyme and pathway databases

BioCycYEAST:G3O-33539-MONOMER.

Gene expression databases

GenevestigatorQ12517.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR010334. DCP1.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERPTHR16290. PTHR16290. 1 hit.
PfamPF06058. DCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ12517.
NextBio975538.
PROQ12517.

Entry information

Entry nameDCP1_YEAST
AccessionPrimary (citable) accession number: Q12517
Secondary accession number(s): D6W1S0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references