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Entry version 189 (02 Jun 2021)
Sequence version 1 (01 Nov 1997)
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Protein

ATP-dependent RNA helicase HAS1

Gene

HAS1

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-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.

3 Publications

Miscellaneous

Transcription depends partially on SET1.

<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 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=450 µM for ATP1 Publication

    pH dependencei

    Optimum pH is 6.5. Active from pH 5 to 8.1 Publication

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi86 – 93ATP8

    <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, RNA-binding
    Biological processRibosome biogenesis, rRNA processing
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q03532

    <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:
    ATP-dependent RNA helicase HAS1 (EC:3.6.4.13)
    Alternative name(s):
    Helicase associated with SET1 protein 1
    <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:HAS1
    Ordered Locus Names:YMR290C
    <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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <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 XIII

    Organism-specific databases

    Saccharomyces Genome Database

    More...
    SGDi
    S000004903, HAS1

    Eukaryotic Pathogen, Vector and Host Database Resources

    More...
    VEuPathDBi
    FungiDB:YMR290C

    <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

    Nucleus

    <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%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>Mutagenesisi92K → A: Lethal in vivo and impairs ATPase with 2-5% of wild-type ATPase activity, a 20-fold higher KM for ATP and unables RNA/DNA heteroduplexes unwinding activity in vitro. Leads to 13% of wild-type ATPase activity and higher RNA/DNA heteroduplexes unwinding activity in vitro; when associated with A-389. 2 Publications1
    Mutagenesisi105H → Y: Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius; when associated with S-315 and S-393. 1 Publication1
    Mutagenesisi228S → A: Slow growth at 18 and 16 degrees Celsius, no growth at 14 degrees Celsius and drastic decrease of the amount of 40S ribosomal subunits at 30 degrees Celsius in vivo. Leads to 70-80% of wild-type ATPase activity, a 2-fold lower KM for ATP and a slightly reduced RNA/DNA heteroduplexes unwinding activity in vitro. 1 Publication1
    Mutagenesisi230T → A: Lethal in vivo and leads to 70-80% of wild-type ATPase activity, a 2-fold lower KM for ATP and a reduced RNA/DNA heteroduplexes unwinding activity in vitro. 1 Publication1
    Mutagenesisi315P → S: Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius; when associated with Y-105 and S-393. 1 Publication1
    Mutagenesisi375H → E: Lethal in vivo and leads to 70-80% of wild-type ATPase activity, a 2-fold lower KM for ATP and a reduced RNA/DNA heteroduplexes unwinding activity in vitro. 1 Publication1
    Mutagenesisi376R → A: Lethal in vivo and leads to less than 30% of wild-type ATPase activity and a 2-fold lower KM for ATP in vitro. 1 Publication1
    Mutagenesisi389K → A: Increases 3-fold the ATPase activity and a higher RNA/DNA heteroduplexes unwinding activity in vitro. Leads to 13% of wild-type ATPase activity and lower RNA/DNA heteroduplexes unwinding activity in vitro; when associated with A-92. 1 Publication1
    Mutagenesisi393F → S: Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius; when associated with Y-105 and S-315. 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_00000550461 – 505ATP-dependent RNA helicase HAS1Add BLAST505

    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 residuei12PhosphoserineCombined sources1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 by CDK1.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q03532

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

    More...
    PaxDbi
    Q03532

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q03532

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q03532

    <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

    Interacts with RRP1. Associates in the nucleolus with the 60S and pre-60S ribosomal subunits. It has also been isolated with the nuclear pore complex.

    2 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

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    35470, 354 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-1604, Small ribosomal subunit processome, variant 1
    CPX-1607, Small ribosomal subunit processome, variant 2
    CPX-1608, Small ribosomal subunit processome, variant 3

    Database of interacting proteins

    More...
    DIPi
    DIP-4396N

    Protein interaction database and analysis system

    More...
    IntActi
    Q03532, 68 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q03532

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YMR290C

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    Q03532, 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

    1505
    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
    Q03532

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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%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>Domaini73 – 249Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST177
    Domaini263 – 433Helicase C-terminalPROSITE-ProRule annotationAdd BLAST171

    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>Regioni1 – 37DisorderedSequence 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>Motifi42 – 70Q motifAdd BLAST29
    Motifi196 – 199DEAD box4
    Motifi275 – 291Bipartite nuclear localization signalCuratedAdd BLAST17

    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 biasi9 – 23Basic and acidic residuesSequence analysisAdd BLAST15

    <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

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0342, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00680000100037

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_003041_26_5_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q03532

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    AHHSQTY

    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
    IPR025313, DUF4217
    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
    PF13959, DUF4217, 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
    SM01178, DUF4217, 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%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.

    Q03532-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MATPSNKRSR DSESTEEPVV DEKSTSKQNN AAPEGEQTTC VEKFEELKLS
    60 70 80 90 100
    QPTLKAIEKM GFTTMTSVQA RTIPPLLAGR DVLGAAKTGS GKTLAFLIPA
    110 120 130 140 150
    IELLHSLKFK PRNGTGIIVI TPTRELALQI FGVARELMEF HSQTFGIVIG
    160 170 180 190 200
    GANRRQEAEK LMKGVNMLIA TPGRLLDHLQ NTKGFVFKNL KALIIDEADR
    210 220 230 240 250
    ILEIGFEDEM RQIIKILPNE DRQSMLFSAT QTTKVEDLAR ISLRPGPLFI
    260 270 280 290 300
    NVVPETDNST ADGLEQGYVV CDSDKRFLLL FSFLKRNQKK KIIVFLSSCN
    310 320 330 340 350
    SVKYYAELLN YIDLPVLELH GKQKQQKRTN TFFEFCNAER GILICTDVAA
    360 370 380 390 400
    RGLDIPAVDW IIQFDPPDDP RDYIHRVGRT ARGTKGKGKS LMFLTPNELG
    410 420 430 440 450
    FLRYLKASKV PLNEYEFPEN KIANVQSQLE KLIKSNYYLH QTAKDGYRSY
    460 470 480 490 500
    LQAYASHSLK TVYQIDKLDL AKVAKSYGFP VPPKVNITIG ASGKTPNTKR

    RKTHK
    Length:505
    Mass (Da):56,717
    Last modified:November 1, 1997 - 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:iEE15D51A7F6BE1A2
    GO

    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
    X80836 Genomic DNA Translation: CAA56799.1
    BK006946 Genomic DNA Translation: DAA10191.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S47451

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_014017.1, NM_001182797.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YMR290C_mRNA; YMR290C; YMR290C

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    855335

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YMR290C

    <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
    X80836 Genomic DNA Translation: CAA56799.1
    BK006946 Genomic DNA Translation: DAA10191.1
    PIRiS47451
    RefSeqiNP_014017.1, NM_001182797.1

    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
    5Z3Gelectron microscopy3.65Y1-505[»]
    6C0Felectron microscopy3.70p1-505[»]
    6CB1electron microscopy4.60p1-505[»]
    6ELZelectron microscopy3.30D1-505[»]
    6EM1electron microscopy3.60D1-505[»]
    6EM3electron microscopy3.20D1-505[»]
    6EM4electron microscopy4.10D1-505[»]
    6EM5electron microscopy4.30D1-505[»]
    SMRiQ03532
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi35470, 354 interactors
    ComplexPortaliCPX-1604, Small ribosomal subunit processome, variant 1
    CPX-1607, Small ribosomal subunit processome, variant 2
    CPX-1608, Small ribosomal subunit processome, variant 3
    DIPiDIP-4396N
    IntActiQ03532, 68 interactors
    MINTiQ03532
    STRINGi4932.YMR290C

    PTM databases

    iPTMnetiQ03532

    Proteomic databases

    MaxQBiQ03532
    PaxDbiQ03532
    PRIDEiQ03532

    Genome annotation databases

    EnsemblFungiiYMR290C_mRNA; YMR290C; YMR290C
    GeneIDi855335
    KEGGisce:YMR290C

    Organism-specific databases

    SGDiS000004903, HAS1
    VEuPathDBiFungiDB:YMR290C

    Phylogenomic databases

    eggNOGiKOG0342, Eukaryota
    GeneTreeiENSGT00680000100037
    HOGENOMiCLU_003041_26_5_1
    InParanoidiQ03532
    OMAiAHHSQTY

    Enzyme and pathway databases

    SABIO-RKiQ03532

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:Q03532
    RNActiQ03532, protein

    Family and domain databases

    InterProiView protein in InterPro
    IPR011545, DEAD/DEAH_box_helicase_dom
    IPR025313, DUF4217
    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
    PF13959, DUF4217, 1 hit
    PF00271, Helicase_C, 1 hit
    SMARTiView protein in SMART
    SM00487, DEXDc, 1 hit
    SM01178, DUF4217, 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

    MobiDB: a database of protein disorder and mobility annotations

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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 nameiHAS1_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: Q03532
    Secondary accession number(s): D6W0B7
    <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: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: June 2, 2021
    This is version 189 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: 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
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