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Q12517

- DCP1_YEAST

UniProt

Q12517 - DCP1_YEAST

Protein

mRNA-decapping enzyme subunit 1

Gene

DCP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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 3 Publications
    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.

    GO - Cellular componenti

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

    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.
    Mutagenesisi29 – 313RYD → AYA in DCP1-2; strong loss of mRNA decapping activity at 36 degrees Celsius.
    Mutagenesisi32 – 343PKI → AKA: Partial loss of mRNA-decapping activity.
    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.
    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.
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12517.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DCP1 family.Curated

    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

    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: October 1, 2014
    This is version 107 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.1 Publication

    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