SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q12517

- DCP1_YEAST

UniProt

Q12517 - DCP1_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

mRNA-decapping enzyme subunit 1

Gene
DCP1, YOL149W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.16 Publications

GO - Molecular functioni

  1. enzyme activator activity Source: SGD
  2. mRNA binding Source: SGD
  3. protein binding Source: IntAct

GO - Biological processi

  1. deadenylation-dependent decapping of nuclear-transcribed mRNA Source: SGD
  2. mRNA processing Source: UniProtKB-KW
  3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
  4. positive regulation of catalytic activity Source: GOC
Complete GO annotation...

Keywords - Biological processi

mRNA processing, Nonsense-mediated mRNA decay

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33539-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-decapping enzyme subunit 1
Gene namesi
Name:DCP1
Ordered Locus Names:YOL149W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOL149w.
SGDiS000005509. DCP1.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. cytoplasmic mRNA processing body Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 205EFYRK → AFYAA in DCP1-17; partial loss of mRNA-decapping activity. 1 Publication
Mutagenesisi29 – 313RYD → AYA in DCP1-2; strong loss of mRNA decapping activity at 36 degrees Celsius. 2 Publications
Mutagenesisi32 – 343PKI → AKA: Partial loss of mRNA-decapping activity. 1 Publication
Mutagenesisi37 – 382LL → AA: Strong loss of mRNA-decapping activity; when associated with A-217 and A-221.
Mutagenesisi47 – 471Y → A in DCP1-32; partial loss of mRNA decapping activity. 1 Publication
Mutagenesisi47 – 471Y → F in DCP1-35; partial loss of mRNA decapping activity. 1 Publication
Mutagenesisi48 – 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. 1 Publication
Mutagenesisi56 – 561W → A in DCP1-31; partial loss of mRNA decapping activity. 3 Publications
Mutagenesisi70 – 701R → A in DCP1-33; strong loss of mRNA decapping activity. 2 Publications
Mutagenesisi156 – 1561G → D in DCP1-1; strong loss of mRNA decapping activity. 1 Publication
Mutagenesisi187 – 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.
Mutagenesisi204 – 2041W → A in DCP1-33; partial loss of mRNA decapping activity. 1 Publication
Mutagenesisi216 – 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. 1 Publication
Mutagenesisi217 – 2171L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-221. 1 Publication
Mutagenesisi221 – 2211L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-217. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231mRNA-decapping enzyme subunit 1PRO_0000232998Add
BLAST

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12517.
PaxDbiQ12517.
PeptideAtlasiQ12517.

Expressioni

Gene expression databases

GenevestigatoriQ12517.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DCP2P535505EBI-38519,EBI-270
EDC3P399985EBI-38519,EBI-22300

Protein-protein interaction databases

BioGridi34268. 65 interactions.
DIPiDIP-1288N.
IntActiQ12517. 24 interactions.
MINTiMINT-390330.
STRINGi4932.YOL149W.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 307
Beta strandi34 – 5017
Turni51 – 544
Beta strandi55 – 7016
Beta strandi139 – 15012
Beta strandi152 – 1576
Helixi160 – 16910
Helixi171 – 1766
Beta strandi183 – 1875
Beta strandi190 – 1945
Beta strandi200 – 2078
Helixi208 – 22316

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q67X-ray2.30A/B1-231[»]
ProteinModelPortaliQ12517.
SMRiQ12517. Positions 17-231.

Miscellaneous databases

EvolutionaryTraceiQ12517.

Family & Domainsi

Sequence similaritiesi

Belongs to the DCP1 family.

Phylogenomic databases

eggNOGiNOG240628.
HOGENOMiHOG000246588.
KOiK12612.
OMAiGLWVFNE.
OrthoDBiEOG74BK4D.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR010334. DCP1.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR16290. PTHR16290. 1 hit.
PfamiPF06058. DCP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12517-1 [UniParc]FASTAAdd to Basket

« Hide

MTGAATAAEN SATQLEFYRK ALNFNVIGRY DPKIKQLLFH TPHASLYKWD    50
FKKDEWNKLE YQGVLAIYLR DVSQNTNLLP VSPQEVDIFD SQNGSNNIQV 100
NNGSDNSNRN SSGNGNSYKS NDSLTYNCGK TLSGKDIYNY GLIILNRINP 150
DNFSMGIVPN SVVNKRKVFN AEEDTLNPLE CMGVEVKDEL VIIKNLKHEV 200
YGIWIHTVSD RQNIYELIKY LLENEPKDSF A 231
Length:231
Mass (Da):26,266
Last modified:November 1, 1996 - v1
Checksum:i8456B1C96C121C4D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48239 Genomic DNA. Translation: CAA88278.1.
Z74891 Genomic DNA. Translation: CAA99170.1.
AY558431 Genomic DNA. Translation: AAS56757.1.
BK006948 Genomic DNA. Translation: DAA10636.1.
PIRiS60387.
RefSeqiNP_014492.1. NM_001183403.1.

Genome annotation databases

EnsemblFungiiYOL149W; YOL149W; YOL149W.
GeneIDi854016.
KEGGisce:YOL149W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48239 Genomic DNA. Translation: CAA88278.1 .
Z74891 Genomic DNA. Translation: CAA99170.1 .
AY558431 Genomic DNA. Translation: AAS56757.1 .
BK006948 Genomic DNA. Translation: DAA10636.1 .
PIRi S60387.
RefSeqi NP_014492.1. NM_001183403.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q67 X-ray 2.30 A/B 1-231 [» ]
ProteinModelPortali Q12517.
SMRi Q12517. Positions 17-231.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34268. 65 interactions.
DIPi DIP-1288N.
IntActi Q12517. 24 interactions.
MINTi MINT-390330.
STRINGi 4932.YOL149W.

Proteomic databases

MaxQBi Q12517.
PaxDbi Q12517.
PeptideAtlasi Q12517.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOL149W ; YOL149W ; YOL149W .
GeneIDi 854016.
KEGGi sce:YOL149W.

Organism-specific databases

CYGDi YOL149w.
SGDi S000005509. DCP1.

Phylogenomic databases

eggNOGi NOG240628.
HOGENOMi HOG000246588.
KOi K12612.
OMAi GLWVFNE.
OrthoDBi EOG74BK4D.

Enzyme and pathway databases

BioCyci YEAST:G3O-33539-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q12517.
NextBioi 975538.
PROi Q12517.

Gene expression databases

Genevestigatori Q12517.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
InterProi IPR010334. DCP1.
IPR011993. PH_like_dom.
[Graphical view ]
PANTHERi PTHR16290. PTHR16290. 1 hit.
Pfami PF06058. DCP1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  23. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  24. 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. 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.

Entry informationi

Entry nameiDCP1_YEAST
AccessioniPrimary (citable) accession number: Q12517
Secondary accession number(s): D6W1S0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

Similar proteinsi