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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-Experimental evidence at protein leveli

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

Catalytic activityi

ATP + H2O = ADP + phosphate.

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)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi86 – 938ATP

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • ATP-dependent RNA helicase activity Source: SGD
    • identical protein binding Source: IntAct
    • RNA binding Source: SGD
    • RNA-dependent ATPase activity Source: SGD

    GO - Biological processi

    • maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
    • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
    • ribosomal large subunit biogenesis Source: SGD
    • ribosomal small subunit biogenesis Source: SGD
    • RNA secondary structure unwinding Source: GO_Central
    • rRNA processing Source: SGD
    • snoRNA release from pre-rRNA Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Ribosome biogenesis, rRNA processing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32960-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent RNA helicase HAS1 (EC:3.6.4.13)
    Alternative name(s):
    Helicase associated with SET1 protein 1
    Gene namesi
    Name:HAS1
    Ordered Locus Names:YMR290C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XIII

    Organism-specific databases

    EuPathDBiFungiDB:YMR290C.
    SGDiS000004903. HAS1.

    Subcellular locationi

    GO - Cellular componenti

    • nuclear envelope Source: SGD
    • nucleolus Source: SGD
    • preribosome, large subunit precursor Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi92 – 921K → 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 Publications
    Mutagenesisi105 – 1051H → Y: Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius; when associated with S-315 and S-393. 1 Publication
    Mutagenesisi228 – 2281S → 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 Publication
    Mutagenesisi230 – 2301T → 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 Publication
    Mutagenesisi315 – 3151P → S: Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius; when associated with Y-105 and S-393. 1 Publication
    Mutagenesisi375 – 3751H → 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 Publication
    Mutagenesisi376 – 3761R → 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 Publication
    Mutagenesisi389 – 3891K → 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 Publication
    Mutagenesisi393 – 3931F → S: Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius; when associated with Y-105 and S-315. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 505505ATP-dependent RNA helicase HAS1PRO_0000055046Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121PhosphoserineCombined sources

    Post-translational modificationi

    Phosphorylated by CDK1.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ03532.

    PTM databases

    iPTMnetiQ03532.

    Interactioni

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-8170,EBI-8170
    DBP10Q123894EBI-8170,EBI-5644
    ERB1Q046604EBI-8170,EBI-28098
    LOC1P435865EBI-8170,EBI-22906
    MAK21Q121764EBI-8170,EBI-10944
    MAK5P381125EBI-8170,EBI-10394
    NOC2P397443EBI-8170,EBI-29259
    NOG1Q028922EBI-8170,EBI-12105
    NOP15P539275EBI-8170,EBI-28853
    NOP4P378385EBI-8170,EBI-12122
    NSA2P400784EBI-8170,EBI-22681
    RLP7P406933EBI-8170,EBI-15415

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi35470. 125 interactions.
    DIPiDIP-4396N.
    IntActiQ03532. 50 interactions.
    MINTiMINT-8285404.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03532.
    SMRiQ03532. Positions 36-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini73 – 249177Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini263 – 433171Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi42 – 7029Q motifAdd
    BLAST
    Motifi196 – 1994DEAD box
    Motifi275 – 29117Bipartite nuclear localization signalCuratedAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00680000100037.
    HOGENOMiHOG000268799.
    InParanoidiQ03532.
    KOiK13179.
    OMAiAVELMYK.
    OrthoDBiEOG7FR7R5.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. 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.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF13959. DUF4217. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM01178. DUF4217. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequencei

    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
    Checksum:iEE15D51A7F6BE1A2
    GO

    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.

    Genome annotation databases

    EnsemblFungiiYMR290C; YMR290C; YMR290C.
    GeneIDi855335.
    KEGGisce:YMR290C.

    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

    ProteinModelPortaliQ03532.
    SMRiQ03532. Positions 36-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35470. 125 interactions.
    DIPiDIP-4396N.
    IntActiQ03532. 50 interactions.
    MINTiMINT-8285404.

    PTM databases

    iPTMnetiQ03532.

    Proteomic databases

    MaxQBiQ03532.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYMR290C; YMR290C; YMR290C.
    GeneIDi855335.
    KEGGisce:YMR290C.

    Organism-specific databases

    EuPathDBiFungiDB:YMR290C.
    SGDiS000004903. HAS1.

    Phylogenomic databases

    GeneTreeiENSGT00680000100037.
    HOGENOMiHOG000268799.
    InParanoidiQ03532.
    KOiK13179.
    OMAiAVELMYK.
    OrthoDBiEOG7FR7R5.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32960-MONOMER.

    Miscellaneous databases

    PROiQ03532.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. 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.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF13959. DUF4217. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM01178. DUF4217. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "SET1, a yeast member of the Trithorax family, functions in transcriptional silencing and diverse cellular processes."
      Nislow C., Ray E., Pillus L.
      Mol. Biol. Cell 8:2421-2436(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SET1 DEPENDENT EXPRESSION.
    4. "The yeast nuclear pore complex: composition, architecture, and transport mechanism."
      Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.
      J. Cell Biol. 148:635-651(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH NUCLEAR PORE.
    5. Cited for: PHOSPHORYLATION.
    6. "Has1p, a member of the DEAD-box family, is required for 40S ribosomal subunit biogenesis in Saccharomyces cerevisiae."
      Emery B., de la Cruz J., Rocak S., Deloche O., Linder P.
      Mol. Microbiol. 52:141-158(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-92; HIS-105; PRO-315 AND PHE-393.
    7. Cited for: FUNCTION.
    8. "Role of the yeast Rrp1 protein in the dynamics of pre-ribosome maturation."
      Horsey E.W., Jakovljevic J., Miles T.D., Harnpicharnchai P., Woolford J.L. Jr.
      RNA 10:813-827(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RRP1, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Characterization of the ATPase and unwinding activities of the yeast DEAD-box protein Has1p and the analysis of the roles of the conserved motifs."
      Rocak S., Emery B., Tanner N.K., Linder P.
      Nucleic Acids Res. 33:999-1009(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-92; SER-228; THR-230; HIS-375; ARG-376 AND LYS-389.
    10. "Rrp15p, a novel component of pre-ribosomal particles required for 60S ribosome subunit maturation."
      De Marchis M.L., Giorgi A., Schinina M.E., Bozzoni I., Fatica A.
      RNA 11:495-502(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RRP15, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHAS1_YEAST
    AccessioniPrimary (citable) accession number: Q03532
    Secondary accession number(s): D6W0B7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: July 6, 2016
    This is version 150 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Transcription depends partially on SET1.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.