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Entry version 147 (31 Jul 2019)
Sequence version 1 (01 Nov 1996)
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Protein

mRNA-decapping enzyme subunit 1

Gene

DCP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

Present with 2880 molecules/cell in log phase SD medium.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • enzyme activator activity Source: SGD
  • mRNA binding Source: SGD

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing, Nonsense-mediated mRNA decay

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33539-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-430039 mRNA decay by 5' to 3' exoribonuclease
R-SCE-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-SCE-450513 Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
mRNA-decapping enzyme subunit 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DCP1
Ordered Locus Names:YOL149W
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YOL149W

Saccharomyces Genome Database

More...
SGDi
S000005509 DCP1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi16 – 20EFYRK → AFYAA in DCP1-17; partial loss of mRNA-decapping activity. 1 Publication5
Mutagenesisi29 – 31RYD → AYA in DCP1-2; strong loss of mRNA decapping activity at 36 degrees Celsius. 2 Publications3
Mutagenesisi32 – 34PKI → AKA: Partial loss of mRNA-decapping activity. 1 Publication3
Mutagenesisi37 – 38LL → AA: Strong loss of mRNA-decapping activity; when associated with A-217 and A-221. 1 Publication2
Mutagenesisi47Y → A in DCP1-32; partial loss of mRNA decapping activity. 1 Publication1
Mutagenesisi47Y → F in DCP1-35; partial loss of mRNA decapping activity. 1 Publication1
Mutagenesisi48 – 50KWD → 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 Publication3
Mutagenesisi56W → A in DCP1-31; partial loss of mRNA decapping activity. 3 Publications1
Mutagenesisi70R → A in DCP1-33; strong loss of mRNA decapping activity. 2 Publications1
Mutagenesisi156G → D in DCP1-1; strong loss of mRNA decapping activity. 1 Publication1
Mutagenesisi187 – 188KD → 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. 1 Publication2
Mutagenesisi204W → A in DCP1-33; partial loss of mRNA decapping activity. 1 Publication1
Mutagenesisi216 – 219ELIK → 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 Publication4
Mutagenesisi217L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-221. 1 Publication1
Mutagenesisi221L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-217. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002329981 – 231mRNA-decapping enzyme subunit 1Add BLAST231

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q12517

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q12517

PRoteomics IDEntifications database

More...
PRIDEi
Q12517

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34268, 394 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1628 Decapping complex, DCP1-DCP2

Database of interacting proteins

More...
DIPi
DIP-1288N

Protein interaction database and analysis system

More...
IntActi
Q12517, 25 interactors

Molecular INTeraction database

More...
MINTi
Q12517

STRING: functional protein association networks

More...
STRINGi
4932.YOL149W

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q12517

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q12517

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DCP1 family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000246588

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q12517

KEGG Orthology (KO)

More...
KOi
K12612

Identification of Orthologs from Complete Genome Data

More...
OMAi
LLCHTSH

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.29.30, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010334 Dcp1
IPR011993 PH-like_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR16290 PTHR16290, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06058 DCP1, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q12517-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTGAATAAEN SATQLEFYRK ALNFNVIGRY DPKIKQLLFH TPHASLYKWD
60 70 80 90 100
FKKDEWNKLE YQGVLAIYLR DVSQNTNLLP VSPQEVDIFD SQNGSNNIQV
110 120 130 140 150
NNGSDNSNRN SSGNGNSYKS NDSLTYNCGK TLSGKDIYNY GLIILNRINP
160 170 180 190 200
DNFSMGIVPN SVVNKRKVFN AEEDTLNPLE CMGVEVKDEL VIIKNLKHEV
210 220 230
YGIWIHTVSD RQNIYELIKY LLENEPKDSF A
Length:231
Mass (Da):26,266
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8456B1C96C121C4D
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S60387

NCBI Reference Sequences

More...
RefSeqi
NP_014492.1, NM_001183403.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YOL149W_mRNA; YOL149W_mRNA; YOL149W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854016

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YOL149W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q67X-ray2.30A/B1-231[»]
SMRiQ12517
ModBaseiSearch...

Protein-protein interaction databases

BioGridi34268, 394 interactors
ComplexPortaliCPX-1628 Decapping complex, DCP1-DCP2
DIPiDIP-1288N
IntActiQ12517, 25 interactors
MINTiQ12517
STRINGi4932.YOL149W

Proteomic databases

MaxQBiQ12517
PaxDbiQ12517
PRIDEiQ12517

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL149W_mRNA; YOL149W_mRNA; YOL149W
GeneIDi854016
KEGGisce:YOL149W

Organism-specific databases

EuPathDBiFungiDB:YOL149W
SGDiS000005509 DCP1

Phylogenomic databases

HOGENOMiHOG000246588
InParanoidiQ12517
KOiK12612
OMAiLLCHTSH

Enzyme and pathway databases

BioCyciYEAST:G3O-33539-MONOMER
ReactomeiR-SCE-430039 mRNA decay by 5' to 3' exoribonuclease
R-SCE-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-SCE-450513 Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA

Miscellaneous databases

EvolutionaryTraceiQ12517

Protein Ontology

More...
PROi
PR:Q12517

Family and domain databases

Gene3Di2.30.29.30, 2 hits
InterProiView protein in InterPro
IPR010334 Dcp1
IPR011993 PH-like_dom_sf
PANTHERiPTHR16290 PTHR16290, 1 hit
PfamiView protein in Pfam
PF06058 DCP1, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDCP1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q12517
Secondary accession number(s): D6W1S0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1996
Last modified: July 31, 2019
This is version 147 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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