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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: -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

Miscellaneous

Transcription depends partially on SET1.

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)DescriptionActionsGraphical viewLength
    Nucleotide bindingi86 – 93ATP8

    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

    Keywordsi

    Molecular functionHelicase, Hydrolase, RNA-binding
    Biological processRibosome biogenesis, rRNA processing
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32960-MONOMER
    SABIO-RKiQ03532

    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

    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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000550461 – 505ATP-dependent RNA helicase HAS1Add BLAST505

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei12PhosphoserineCombined sources1

    Post-translational modificationi

    Phosphorylated by CDK1.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ03532
    PaxDbiQ03532
    PRIDEiQ03532

    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

    Show more details

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi35470, 310 interactors
    DIPiDIP-4396N
    IntActiQ03532, 85 interactors
    MINTiQ03532
    STRINGi4932.YMR290C

    Structurei

    Secondary structure

    1505
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi276 – 286Combined sources11
    Beta strandi292 – 297Combined sources6
    Helixi301 – 309Combined sources9
    Turni310 – 313Combined sources4
    Beta strandi316 – 318Combined sources3
    Helixi325 – 336Combined sources12
    Beta strandi342 – 346Combined sources5
    Turni347 – 352Combined sources6
    Beta strandi360 – 363Combined sources4
    Beta strandi368 – 370Combined sources3
    Turni371 – 377Combined sources7
    Beta strandi389 – 391Combined sources3
    Helixi419 – 421Combined sources3
    Helixi426 – 432Combined sources7
    Turni433 – 435Combined sources3
    Helixi438 – 455Combined sources18
    Beta strandi460 – 464Combined sources5
    Helixi468 – 474Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    6C0Felectron microscopy3.70p1-505[»]
    6ELZelectron microscopy3.30D1-505[»]
    6EM1electron microscopy3.60D1-505[»]
    6EM3electron microscopy3.20D1-505[»]
    6EM4electron microscopy4.10D1-505[»]
    6EM5electron microscopy4.30D1-505[»]
    ProteinModelPortaliQ03532
    SMRiQ03532
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini73 – 249Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST177
    Domaini263 – 433Helicase C-terminalPROSITE-ProRule annotationAdd BLAST171

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi42 – 70Q motifAdd BLAST29
    Motifi196 – 199DEAD box4
    Motifi275 – 291Bipartite nuclear localization signalCuratedAdd BLAST17

    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

    Phylogenomic databases

    GeneTreeiENSGT00680000100037
    HOGENOMiHOG000268799
    InParanoidiQ03532
    KOiK13179
    OMAiEMRQIVK
    OrthoDBiEOG092C1VLP

    Family and domain databases

    CDDicd00079 HELICc, 1 hit
    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

    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

    Similar proteinsi

    Entry informationi

    Entry nameiHAS1_YEAST
    AccessioniPrimary (citable) accession number: Q03532
    Secondary accession number(s): D6W0B7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: April 25, 2018
    This is version 165 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health