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Entry version 203 (16 Oct 2019)
Sequence version 2 (01 Mar 1992)
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Protein

ATP-dependent RNA helicase DED1

Gene

DED1

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

ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes. Has weak ATP-dependent affinity for dsRNA, but strong ATP-dependent affinity for ssRNA. Acts as a virus host factor involved in the replication of the MBV and the L-A viruses by promoting the negative-strand RNA synthesis. May be involved in recognition of the preinitiation complex and DNA binding of the RNA polymerase III and play a role in mRNA splicing.12 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.34 mM for ATP2 Publications

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi186 – 193ATP8

    <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

    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 functionHelicase, Hydrolase, Initiation factor, RNA-binding
    Biological processProtein biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:G3O-33708-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.6.4.13 984

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SCE-6798695 Neutrophil degranulation

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P06634

    <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:
    ATP-dependent RNA helicase DED1 (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 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:DED1
    Synonyms:SPP81
    Ordered Locus Names:YOR204W
    <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:YOR204W

    Saccharomyces Genome Database

    More...
    SGDi
    S000005730 DED1

    <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>Mutagenesisi108G → D in DED1-120; impairs protein synthesis at 15 degrees Celsius; when associated with D-494. 1 Publication1
    Mutagenesisi144F → A: Slow growth at 18 and 30 degrees Celsius and no growth at 16 degrees Celsius. 1 Publication1
    Mutagenesisi144F → D or E: Lethal. 1 Publication1
    Mutagenesisi162F → A: Lethal in vivo and inhibits ATPase and helicase activities in vitro. 1 Publication1
    Mutagenesisi162F → C: Slow growth at 18 degrees Celsius. 1 Publication1
    Mutagenesisi162F → L: Reduces RNA-helicase activity about 5-fold in vitro. 1 Publication1
    Mutagenesisi166T → A: Reduces RNA-helicase activity about 2.5-fold in vitro. 1 Publication1
    Mutagenesisi166T → S: Slow growth at 18 and 36 degrees Celsius in vivo, and reduces RNA-helicase activity about 5-fold in vitro. 1 Publication1
    Mutagenesisi169Q → A or E: Lethal in vivo and impairs ATPase and RNA-helicase activities in vitro. 1 Publication1
    Mutagenesisi169Q → C, D, F, G, H, K, L, M, N, S or T: Lethal. 1 Publication1
    Mutagenesisi192K → A: Impairs RNA-helicase activity in vitro. 1 Publication1
    Mutagenesisi237L → M in DED1-18; impairs BMV RNA synthesis; when associated with D-317. 1 Publication1
    Mutagenesisi307E → A: Lethal in vivo and impairs ATPase and RNA-helicase activities in vitro. 1 Publication1
    Mutagenesisi317E → D in DED1-18; impairs BMV RNA synthesis; when associated with M-237. 1 Publication1
    Mutagenesisi368G → D in DED1-199; impairs protein synthesis at 15 degrees Celsius. 1 Publication1
    Mutagenesisi405F → Y, M, L, A or W: Reduces strongly ATPase activity and strand displacement activity. 1 Publication1
    Mutagenesisi486R → A: Reduces ATPase activity. 1 Publication1
    Mutagenesisi494G → D in DED1-120; impairs protein synthesis at 15 degrees Celsius; when associated with D-108. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
    <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_00000550432 – 604ATP-dependent RNA helicase DED1Add BLAST603

    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 residuei2N-acetylalanineCombined sources1
    Modified residuei62Dimethylated arginine1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei215PhosphoserineCombined sources1
    Modified residuei218PhosphoserineCombined sources1
    Modified residuei263PhosphoserineCombined sources1
    Modified residuei535PhosphoserineCombined sources1
    Modified residuei539PhosphoserineCombined sources1
    Modified residuei543PhosphoserineCombined sources1
    Modified residuei572PhosphoserineCombined sources1
    Modified residuei576PhosphoserineCombined sources1
    Modified residuei598PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P06634

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

    More...
    PaxDbi
    P06634

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P06634

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P06634

    <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

    Interacts with the L-A virus GAG protein and the whole L-A virus particles.

    1 Publication

    <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

    WithEntry#Exp.IntActNotes
    DBP1P247843EBI-5744,EBI-5596

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    34599, 602 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-5820N

    Protein interaction database and analysis system

    More...
    IntActi
    P06634, 91 interactors

    Molecular INTeraction database

    More...
    MINTi
    P06634

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YOR204W

    <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

    3D structure databases

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

    More...
    SMRi
    P06634

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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_and_domains_section">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>Domaini173 – 362Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST190
    Domaini373 – 533Helicase C-terminalPROSITE-ProRule annotationAdd BLAST161

    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>Motifi142 – 170Q motifAdd BLAST29
    Motifi306 – 309DEAD box4

    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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi10 – 75Asn-richAdd BLAST66

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

    <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

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000268804

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P06634

    KEGG Orthology (KO)

    More...
    KOi
    K11594

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    GPDWWGQ

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011545 DEAD/DEAH_box_helicase_dom
    IPR014001 Helicase_ATP-bd
    IPR001650 Helicase_C
    IPR027417 P-loop_NTPase
    IPR000629 RNA-helicase_DEAD-box_CS
    IPR014014 RNA_helicase_DEAD_Q_motif

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00270 DEAD, 1 hit
    PF00271 Helicase_C, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00487 DEXDc, 1 hit
    SM00490 HELICc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52540 SSF52540, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00039 DEAD_ATP_HELICASE, 1 hit
    PS51192 HELICASE_ATP_BIND_1, 1 hit
    PS51194 HELICASE_CTER, 1 hit
    PS51195 Q_MOTIF, 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_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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P06634-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAELSEQVQN LSINDNNENG YVPPHLRGKP RSARNNSSNY NNNNGGYNGG
    60 70 80 90 100
    RGGGSFFSNN RRGGYGNGGF FGGNNGGSRS NGRSGGRWID GKHVPAPRNE
    110 120 130 140 150
    KAEIAIFGVP EDPNFQSSGI NFDNYDDIPV DASGKDVPEP ITEFTSPPLD
    160 170 180 190 200
    GLLLENIKLA RFTKPTPVQK YSVPIVANGR DLMACAQTGS GKTGGFLFPV
    210 220 230 240 250
    LSESFKTGPS PQPESQGSFY QRKAYPTAVI MAPTRELATQ IFDEAKKFTY
    260 270 280 290 300
    RSWVKACVVY GGSPIGNQLR EIERGCDLLV ATPGRLNDLL ERGKISLANV
    310 320 330 340 350
    KYLVLDEADR MLDMGFEPQI RHIVEDCDMT PVGERQTLMF SATFPADIQH
    360 370 380 390 400
    LARDFLSDYI FLSVGRVGST SENITQKVLY VENQDKKSAL LDLLSASTDG
    410 420 430 440 450
    LTLIFVETKR MADQLTDFLI MQNFRATAIH GDRTQSERER ALAAFRSGAA
    460 470 480 490 500
    TLLVATAVAA RGLDIPNVTH VINYDLPSDV DDYVHRIGRT GRAGNTGLAT
    510 520 530 540 550
    AFFNSENSNI VKGLHEILTE ANQEVPSFLK DAMMSAPGSR SNSRRGGFGR
    560 570 580 590 600
    NNNRDYRKAG GASAGGWGSS RSRDNSFRGG SGWGSDSKSS GWGNSGGSNN

    SSWW
    Length:604
    Mass (Da):65,553
    Last modified:March 1, 1992 - v2
    <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:iB6722D94C03BFA4B
    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 conflicti37S → M in CAA27004 (PubMed:9169874).Curated1

    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
    X57278 Genomic DNA Translation: CAA40546.1
    Z75110 Genomic DNA Translation: CAA99419.1
    X03245 Genomic DNA Translation: CAA27004.1
    BK006948 Genomic DNA Translation: DAA10976.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S13653

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_014847.3, NM_001183623.3

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YOR204W_mRNA; YOR204W; YOR204W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    854379

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YOR204W

    <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
    X57278 Genomic DNA Translation: CAA40546.1
    Z75110 Genomic DNA Translation: CAA99419.1
    X03245 Genomic DNA Translation: CAA27004.1
    BK006948 Genomic DNA Translation: DAA10976.1
    PIRiS13653
    RefSeqiNP_014847.3, NM_001183623.3

    3D structure databases

    SMRiP06634
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi34599, 602 interactors
    DIPiDIP-5820N
    IntActiP06634, 91 interactors
    MINTiP06634
    STRINGi4932.YOR204W

    PTM databases

    iPTMnetiP06634

    Proteomic databases

    MaxQBiP06634
    PaxDbiP06634
    PRIDEiP06634

    Genome annotation databases

    EnsemblFungiiYOR204W_mRNA; YOR204W; YOR204W
    GeneIDi854379
    KEGGisce:YOR204W

    Organism-specific databases

    EuPathDBiFungiDB:YOR204W
    SGDiS000005730 DED1

    Phylogenomic databases

    HOGENOMiHOG000268804
    InParanoidiP06634
    KOiK11594
    OMAiGPDWWGQ

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33708-MONOMER
    BRENDAi3.6.4.13 984
    ReactomeiR-SCE-6798695 Neutrophil degranulation
    SABIO-RKiP06634

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P06634

    Family and domain databases

    InterProiView protein in InterPro
    IPR011545 DEAD/DEAH_box_helicase_dom
    IPR014001 Helicase_ATP-bd
    IPR001650 Helicase_C
    IPR027417 P-loop_NTPase
    IPR000629 RNA-helicase_DEAD-box_CS
    IPR014014 RNA_helicase_DEAD_Q_motif
    PfamiView protein in Pfam
    PF00270 DEAD, 1 hit
    PF00271 Helicase_C, 1 hit
    SMARTiView protein in SMART
    SM00487 DEXDc, 1 hit
    SM00490 HELICc, 1 hit
    SUPFAMiSSF52540 SSF52540, 1 hit
    PROSITEiView protein in PROSITE
    PS00039 DEAD_ATP_HELICASE, 1 hit
    PS51192 HELICASE_ATP_BIND_1, 1 hit
    PS51194 HELICASE_CTER, 1 hit
    PS51195 Q_MOTIF, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <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 nameiDED1_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: P06634
    Secondary accession number(s): D6W2R0
    <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: January 1, 1988
    Last sequence update: March 1, 1992
    Last modified: October 16, 2019
    This is version 203 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

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