Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - P53550 (DCP2_YEAST)

Entry version 194 (25 May 2022)
Sequence version 1 (01 Oct 1996)
Previous versions | rss
Add a publicationFeedback
Protein

m7GpppN-mRNA hydrolase

Gene

DCP2

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

Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed:10508173, PubMed:11139489, PubMed:11741542).

Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:12554866).

Decapping is the major pathway of mRNA degradation in yeast and occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body (PubMed:10508173, PubMed:11139489, PubMed:11741542).

Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts (PubMed:19779198).

4 Publications

Miscellaneous

Present with 8530 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi149ManganeseBy similarity1
Metal bindingi153ManganeseBy similarity1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHydrolase, RNA-binding
Biological processmRNA processing, Nonsense-mediated mRNA decay
LigandManganese, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.1.62, 984

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%5Fand%5Ftaxonomy%5Fsection">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:
m7GpppN-mRNA hydrolaseCurated (EC:3.6.1.621 Publication)
Alternative name(s):
Protein PSU1
mRNA-decapping enzyme subunit 21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:DCP21 Publication
Synonyms:PSU1
Ordered Locus Names:YNL118CImported
ORF Names:N1917
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 XIV

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000005062, DCP2

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YNL118C

<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

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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Increases autophagy activity through accumulation of autophagy-related proteins in nutrient-replete conditions (PubMed:19779198).

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi60N → D in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with V-68 and V-142. 1 Publication1
Mutagenesisi68I → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-142. 1 Publication1
Mutagenesisi142D → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-68. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000570541 – 970m7GpppN-mRNA hydrolaseAdd BLAST970

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei116PhosphoserineCombined sources1
Modified residuei439PhosphoserineCombined sources1
Modified residuei677PhosphothreonineCombined sources1
Modified residuei679PhosphoserineCombined sources1
Modified residuei682PhosphoserineCombined sources1
Modified residuei751PhosphoserineCombined sources1
Modified residuei771PhosphoserineCombined sources1
Modified residuei773PhosphoserineCombined sources1
Modified residuei778PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P53550

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

More...PaxDbi		P53550

PRoteomics IDEntifications database

More...PRIDEi		P53550

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P53550

<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%5Fsection">'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%5Fsection">'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 (PubMed:10508173, PubMed:11741542, PubMed:14758354).

Interacts with mRNA, LSM2, LSM4 and LSM8 (PubMed:10900456).

Interacts with EDC3 (PubMed:18678652).

6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		35708, 662 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-969N

Protein interaction database and analysis system

More...IntActi		P53550, 45 interactors

Molecular INTeraction database

More...MINTi		P53550

STRING: functional protein association networks

More...STRINGi		4932.YNL118C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P53550, protein

<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

1970
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P53550

Biological Magnetic Resonance Data Bank

More...BMRBi		P53550

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

More...SMRi		P53550

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P53550

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini101 – 228Nudix hydrolasePROSITE-ProRule annotationAdd BLAST128

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni302 – 341DisorderedSequence analysisAdd BLAST40
Regioni417 – 465DisorderedSequence analysisAdd BLAST49
Regioni501 – 520DisorderedSequence analysisAdd BLAST20
Regioni528 – 692DisorderedSequence analysisAdd BLAST165
Regioni831 – 867DisorderedSequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi134 – 155Nudix boxAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi313 – 341Polar residuesSequence analysisAdd BLAST29
Compositional biasi432 – 464Polar residuesSequence analysisAdd BLAST33
Compositional biasi562 – 576Basic and acidic residuesSequence analysisAdd BLAST15
Compositional biasi577 – 614Polar residuesSequence analysisAdd BLAST38
Compositional biasi633 – 648Basic and acidic residuesSequence analysisAdd BLAST16
Compositional biasi649 – 663Polar residuesSequence analysisAdd BLAST15
Compositional biasi665 – 679Basic and acidic residuesSequence analysisAdd BLAST15
Compositional biasi840 – 867Polar residuesSequence analysisAdd BLAST28

<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 Nudix hydrolase family. DCP2 subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2937, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000018878

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_009571_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P53550

Identification of Orthologs from Complete Genome Data

More...OMAi		EPFANNK

Family and domain databases

Conserved Domains Database

More...CDDi		cd03672, Dcp2p, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.1050, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR007722, DCP2_BoxA
IPR036189, DCP2_BoxA_sf
IPR044099, Dcp2_NUDIX
IPR015797, NUDIX_hydrolase-like_dom_sf
IPR020084, NUDIX_hydrolase_CS
IPR000086, NUDIX_hydrolase_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF05026, DCP2, 1 hit
PF00293, NUDIX, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01125, DCP2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF140586, SSF140586, 1 hit
SSF55811, SSF55811, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51462, NUDIX, 1 hit
PS00893, NUDIX_BOX, 1 hit

<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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P53550-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLPLRHALE NVTSVDRILE DLLVRFIINC PNEDLSSVER ELFHFEEASW 
        60         70         80         90        100
FYTDFIKLMN PTLPSLKIKS FAQLIIKLCP LVWKWDIRVD EALQQFSKYK 
       110        120        130        140        150
KSIPVRGAAI FNENLSKILL VQGTESDSWS FPRGKISKDE NDIDCCIREV 
       160        170        180        190        200
KEEIGFDLTD YIDDNQFIER NIQGKNYKIF LISGVSEVFN FKPQVRNEID 
       210        220        230        240        250
KIEWFDFKKI SKTMYKSNIK YYLINSMMRP LSMWLRHQRQ IKNEDQLKSY 
       260        270        280        290        300
AEEQLKLLLG ITKEEQIDPG RELLNMLHTA VQANSNNNAV SNGQVPSSQE 
       310        320        330        340        350
LQHLKEQSGE HNQQKDQQSS FSSQQQPSIF PSLSEPFANN KNVIPPTMPM 
       360        370        380        390        400
ANVFMSNPQL FATMNGQPFA PFPFMLPLTN NSNSANPIPT PVPPNFNAPP 
       410        420        430        440        450
NPMAFGVPNM HNLSGPAVSQ PFSLPPAPLP RDSGYSSSSP GQLLDILNSK 
       460        470        480        490        500
KPDSNVQSSK KPKLKILQRG TDLNSIKQNN NDETAHSNSQ ALLDLLKKPT 
       510        520        530        540        550
SSQKIHASKP DTSFLPNDSV SGIQDAEYED FESSSDEEVE TARDERNSLN 
       560        570        580        590        600
VDIGVNVMPS EKDSRRSQKE KPRNDASKTN LNASAESNSV EWGPGKSSPS 
       610        620        630        640        650
TQSKQNSSVG MQNKYRQEIH IGDSDAYEVF ESSSDEEDGK KLEELEQTQD 
       660        670        680        690        700
NSKLISQDIL KENNFQDGEV PHRDMPTESN KSINETVGLS STTNTVKKVP 
       710        720        730        740        750
KVKILKRGET FASLANDKKA FDSSSNVSSS KDLLQMLRNP ISSTVSSNQQ 
       760        770        780        790        800
SPKSQHLSGD EEIMMMLKRN SVSKPQNSEE NASTSSINDA NASELLGMLK 
       810        820        830        840        850
QKEKDITAPK QPYNVDSYSQ KNSAKGLLNI LKKNDSTGYP RTEGGPSSEM 
       860        870        880        890        900
STSMKRNDAT NNQELDKNST ELLNYLKPKP LNDGYENISN KDSSHELLNI 
       910        920        930        940        950
LHGNKNSSAF NNNVYATDGY SLASDNNENS SNKLLNMLQN RSSAINEPNF 
       960        970
DVRSNGTSGS NELLSILHRK
Length:970
Mass (Da):108,667
Last modified:October 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:iD53CA2C5A546FA4A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti425P → L in AAA68866 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti188V → A in strain: YJM339. 1 Publication1
Natural varianti288Missing in strain: V1-09, YJM269, YJM270, YJM326, YJM339, YJM627 and YJM1129. 1 Publication1
Natural varianti301L → H in strain: YJM280, YJM 20 and YJM339. 1 Publication1
Natural varianti319S → P in strain: YJM627. 1 Publication1
Natural varianti494D → N in strain: YJM339. 1 Publication1
Natural varianti505I → T in strain: SK1, V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129. 1 Publication1
Natural varianti522G → D in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication1
Natural varianti547N → T in strain: YJM280 and YJM320. 1 Publication1
Natural varianti567S → R in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication1
Natural varianti574N → S in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. 1 Publication1
Natural varianti577S → N in strain: V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339 and YJM1129. 1 Publication1
Natural varianti622G → S in strain: V1-09 and YJM339. 1 Publication1
Natural varianti650D → G in strain: YJM280 and YJM320. 1 Publication1
Natural varianti740P → S in strain: YJM269 and YJM270. 1 Publication1
Natural varianti807T → A in strain: YJM 69, YJM270, YJM326 and YJM1129. 1 Publication1
Natural varianti823S → P in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. 1 Publication1
Natural varianti835D → N in strain: YJM280 and YJM320. 1 Publication1
Natural varianti844G → V in strain: V1-09. 1 Publication1
Natural varianti851S → P in strain: YJM280, YJM320 and YJM627. 1 Publication1
Natural varianti854M → I in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication1
Natural varianti864E → Q in strain: YJM269 and YJM270. 1 Publication1
Natural varianti865L → S in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication1
Natural varianti866D → A in strain: YJM627. 1
Natural varianti909A → T in strain: YJM280 and YJM320. 1 Publication1
Natural varianti945I → L in strain: YJM627. 1 Publication1
Natural varianti951D → E in strain: V1-09. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U31377 Genomic DNA Translation: AAC99860.1
L43065 Genomic DNA Translation: AAA68866.1
EF125216 Genomic DNA Translation: ABN58539.1
EF125217 Genomic DNA Translation: ABN58548.1
EF125218 Genomic DNA Translation: ABN58557.1
EF125219 Genomic DNA Translation: ABN58566.1
EF125220 Genomic DNA Translation: ABN58578.1
EF125221 Genomic DNA Translation: ABN58584.1
EF125222 Genomic DNA Translation: ABN58593.1
EF125223 Genomic DNA Translation: ABN58602.1
EF125224 Genomic DNA Translation: ABN58611.1
EF125225 Genomic DNA Translation: ABN58620.1
EF125226 Genomic DNA Translation: ABN58629.1
EF125228 Genomic DNA Translation: ABN58647.1
Z69382 Genomic DNA Translation: CAA93389.1
Z71394 Genomic DNA Translation: CAA95998.1
BK006947 Genomic DNA Translation: DAA10430.1

Protein sequence database of the Protein Information Resource

More...PIRi		S63059

NCBI Reference Sequences

More...RefSeqi		NP_014281.1, NM_001182956.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YNL118C_mRNA; YNL118C; YNL118C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		855605

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YNL118C

<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
U31377 Genomic DNA Translation: AAC99860.1
L43065 Genomic DNA Translation: AAA68866.1
EF125216 Genomic DNA Translation: ABN58539.1
EF125217 Genomic DNA Translation: ABN58548.1
EF125218 Genomic DNA Translation: ABN58557.1
EF125219 Genomic DNA Translation: ABN58566.1
EF125220 Genomic DNA Translation: ABN58578.1
EF125221 Genomic DNA Translation: ABN58584.1
EF125222 Genomic DNA Translation: ABN58593.1
EF125223 Genomic DNA Translation: ABN58602.1
EF125224 Genomic DNA Translation: ABN58611.1
EF125225 Genomic DNA Translation: ABN58620.1
EF125226 Genomic DNA Translation: ABN58629.1
EF125228 Genomic DNA Translation: ABN58647.1
Z69382 Genomic DNA Translation: CAA93389.1
Z71394 Genomic DNA Translation: CAA95998.1
BK006947 Genomic DNA Translation: DAA10430.1
PIRiS63059
RefSeqiNP_014281.1, NM_001182956.1

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
2JVBNMR-A100-245[»]
4K6EX-ray2.10A102-245[»]
4KG3X-ray1.70A/B/C100-245[»]
4KG4X-ray1.80A/B100-245[»]
5LM5X-ray2.60C/D437-450[»]
5LMFX-ray2.15C/D484-500[»]
5LMGX-ray1.89C/D957-970[»]
6Y3ZX-ray3.49A1-271[»]
AlphaFoldDBiP53550
BMRBiP53550
SMRiP53550
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi35708, 662 interactors
ComplexPortaliCPX-1628, Decapping complex, DCP1-DCP2
DIPiDIP-969N
IntActiP53550, 45 interactors
MINTiP53550
STRINGi4932.YNL118C

PTM databases

iPTMnetiP53550

Proteomic databases

MaxQBiP53550
PaxDbiP53550
PRIDEiP53550

Genome annotation databases

EnsemblFungiiYNL118C_mRNA; YNL118C; YNL118C
GeneIDi855605
KEGGisce:YNL118C

Organism-specific databases

SGDiS000005062, DCP2
VEuPathDBiFungiDB:YNL118C

Phylogenomic databases

eggNOGiKOG2937, Eukaryota
GeneTreeiENSGT00390000018878
HOGENOMiCLU_009571_0_0_1
InParanoidiP53550
OMAiEPFANNK

Enzyme and pathway databases

BRENDAi3.6.1.62, 984
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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		DCP2, yeast
EvolutionaryTraceiP53550

Protein Ontology

More...PROi		PR:P53550
RNActiP53550, protein

Family and domain databases

CDDicd03672, Dcp2p, 1 hit
Gene3Di1.10.10.1050, 1 hit
InterProiView protein in InterPro
IPR007722, DCP2_BoxA
IPR036189, DCP2_BoxA_sf
IPR044099, Dcp2_NUDIX
IPR015797, NUDIX_hydrolase-like_dom_sf
IPR020084, NUDIX_hydrolase_CS
IPR000086, NUDIX_hydrolase_dom
PfamiView protein in Pfam
PF05026, DCP2, 1 hit
PF00293, NUDIX, 1 hit
SMARTiView protein in SMART
SM01125, DCP2, 1 hit
SUPFAMiSSF140586, SSF140586, 1 hit
SSF55811, SSF55811, 1 hit
PROSITEiView protein in PROSITE
PS51462, NUDIX, 1 hit
PS00893, NUDIX_BOX, 1 hit

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 nameiDCP2_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: P53550
Secondary accession number(s): B0KZS6
, B0KZU4, B0KZW2, B0KZY0, B0KZY9, B0KZZ8, B0L007, D6W164, Q6LCS6
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 25, 2022
This is version 194 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, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again